NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|198442873|ref|NP_001101188|]
View 

dual specificity protein phosphatase CDC14A isoform 2 [Rattus norvegicus]

Protein Classification

CDC14 family protein phosphatase( domain architecture ID 13026096)

cell division control 14 (CDC14) family protein phosphatase similar to human dual-specificity protein phosphatases CDC14A/B/C that may play a key role in cell cycle control in human cells

CATH:  3.90.190.10
EC:  3.1.3.-
Gene Ontology:  GO:0006470|GO:0004721|GO:0004725|GO:0004722
PubMed:  17057753|27514797|19228121|20720150
SCOP:  3000304

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 163-336 3.31e-138

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.


:

Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 399.91  E-value: 3.31e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 163 TFDADEYEHYERVENGDFNWIVPGKFLAFSGPHPKSKIENGYPLHAPEAYFPYFKKNNVTTIVRLNKKIYEAKRFTDAGF 242
Cdd:cd14499    1 TFDLEEYEHYERVENGDLNWIVPGKFLAFSGPHDTRKDENGYPTHTPEDYIPYFKKLGVTTVVRLNKKLYDAKRFTDAGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 243 EHYDLFFIDGSTPSDNIVRRFLNICENTEGAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPGSIIGPQQH 322
Cdd:cd14499   81 RHYDLYFPDGSTPSDDIVKKFLDICENEKGAIAVHCKAGLGRTGTLIACYLMKHYGFTAREAIAWLRICRPGSVIGPQQQ 160

                        170
                 ....*....|....
gi 198442873 323 FLEEKQASLWVQGD 336
Cdd:cd14499  161 FLEEKEARLWRAGD 174
CDC14_N cd17657
N-terminal domain pseudophosphatase domain of CDC14 family proteins; The cell division control ...
 10-154 2.60e-89

N-terminal domain pseudophosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif. The N-terminal pseudophosphatase domain lacks the catalytic residues.


:

Pssm-ID: 350495  Cd Length: 144  Bit Score: 273.22  E-value: 2.60e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873  10 GACEFMKDRLYFATLRNRPKSTINIHYFSIDEELVYENFYADFGPLNLAMVYRYCCKLNKKLKSYSLSRKKIVHYTSFDQ 89
Cdd:cd17657    1 SAIEIIPDRLYFASLRGPPKSTDNTHYFSIDDELVYEPFFADFGPLNLAQIYRFCCKLNKKLKSPSLASKKIVHYTSLDP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 198442873  90 RKRANAAFLIGAYAVIYLKKTPEEAYRALLSGSnPPYLPFRDASFGNCTYNLTVLDCLQGIRKGL 154
Cdd:cd17657   81 KKRANAAFLIGAYAVIYLGKTPEEAYRPLESGE-PPFLPFRDASYGPCTYELTVLDCLKGLEKAL 144
 
Name Accession Description Interval E-value
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 163-336 3.31e-138

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 399.91  E-value: 3.31e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 163 TFDADEYEHYERVENGDFNWIVPGKFLAFSGPHPKSKIENGYPLHAPEAYFPYFKKNNVTTIVRLNKKIYEAKRFTDAGF 242
Cdd:cd14499    1 TFDLEEYEHYERVENGDLNWIVPGKFLAFSGPHDTRKDENGYPTHTPEDYIPYFKKLGVTTVVRLNKKLYDAKRFTDAGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 243 EHYDLFFIDGSTPSDNIVRRFLNICENTEGAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPGSIIGPQQH 322
Cdd:cd14499   81 RHYDLYFPDGSTPSDDIVKKFLDICENEKGAIAVHCKAGLGRTGTLIACYLMKHYGFTAREAIAWLRICRPGSVIGPQQQ 160

                        170
                 ....*....|....
gi 198442873 323 FLEEKQASLWVQGD 336
Cdd:cd14499  161 FLEEKEARLWRAGD 174
CDC14_N cd17657
N-terminal domain pseudophosphatase domain of CDC14 family proteins; The cell division control ...
 10-154 2.60e-89

N-terminal domain pseudophosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif. The N-terminal pseudophosphatase domain lacks the catalytic residues.


Pssm-ID: 350495  Cd Length: 144  Bit Score: 273.22  E-value: 2.60e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873  10 GACEFMKDRLYFATLRNRPKSTINIHYFSIDEELVYENFYADFGPLNLAMVYRYCCKLNKKLKSYSLSRKKIVHYTSFDQ 89
Cdd:cd17657    1 SAIEIIPDRLYFASLRGPPKSTDNTHYFSIDDELVYEPFFADFGPLNLAQIYRFCCKLNKKLKSPSLASKKIVHYTSLDP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 198442873  90 RKRANAAFLIGAYAVIYLKKTPEEAYRALLSGSnPPYLPFRDASFGNCTYNLTVLDCLQGIRKGL 154
Cdd:cd17657   81 KKRANAAFLIGAYAVIYLGKTPEEAYRPLESGE-PPFLPFRDASYGPCTYELTVLDCLKGLEKAL 144
DSPn pfam14671
Dual specificity protein phosphatase, N-terminal half; The active core of the dual specificity ...
 13-153 2.53e-78

Dual specificity protein phosphatase, N-terminal half; The active core of the dual specificity protein phosphatase is made up of two globular domains both with the DSP-like fold. This family represents the N-terminal half of the core. These domains are arranged in tandem, and are associated via an extensive interface to form a single globular whole. The conserved PTP signature motif (Cys-[X]5-Arg) that defines the catalytic centre of all PTP-family members is located within the C-terminal domain, family DSPc, pfam00782. Although the centre of the catalytic site is formed from DSPc, two loops from the N-terminal domain, DSPn, also contribute to the catalytic site, facilitating peptide substrate specificity.


Pssm-ID: 464252  Cd Length: 140  Bit Score: 244.76  E-value: 2.53e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873   13 EFMKDRLYFATLRNRPKSTINIHYFSIDEELVYENFYADFGPLNLAMVYRYCCKLNKKLKSYSLSRKKIVHYTSFDQRKR 92
Cdd:pfam14671   1 EIIPDRLYFATLKSKPKNTPNYHYFSIDDELVYEPFYFDFGPLNLAHLYRFCIKLNKKLKSPELKKKKIVHYTSQDKQKR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 198442873   93 ANAAFLIGAYAVIYLKKTPEEAYRALLSGSnPPYLPFRDASFGNCTYNLTVLDCLQGIRKG 153
Cdd:pfam14671  81 ANAAFLIGAYMVLYLNMSPEEALSPLSSIS-PPFIPFRDASYGPCTYTLTLLDCLKGLEKA 140
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 187-326 1.84e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 85.84  E-value: 1.84e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 187 KFLAFSGPHPKSkiengypLHApeaYFPYFKKNNVTTIVRLNKKIYEAKRFTDAGFEHYDLFFIDGSTPSDNIVRRFLNI 266
Cdd:PTZ00242  17 KFLILDAPSPSN-------LPL---YIKELQRYNVTHLVRVCGPTYDAELLEKNGIEVHDWPFDDGAPPPKAVIDNWLRL 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 198442873 267 CENT-------EGAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPGSIIGPQQHFLEE 326
Cdd:PTZ00242  87 LDQEfakqstpPETIAVHCVAGLGRAPILVALALVEYGGMEPLDAVGFVREKRKGAINQTQLQFLKK 153
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
182-326 6.70e-16

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 74.62  E-value: 6.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 182 WIVPGKFlaFSGPHPKSKIEngyplhapeayfpYFKKNNVTTIVRLN-KKIYEAKRFTDAGFEHYDLFFIDGSTPSDNIV 260
Cdd:COG2453    2 WIIPGLL--AGGPLPGGGEA-------------DLKREGIDAVVSLTeEEELLLGLLEEAGLEYLHLPIPDFGAPDDEQL 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 261 RRFLN-ICENTE--GAIAVHCKAGLGRTGTLIACYVMKHyRFTHAEIIAWIRICRPGSIIGPQQH-FLEE 326
Cdd:COG2453   67 QEAVDfIDEALRegKKVLVHCRGGIGRTGTVAAAYLVLL-GLSAEEALARVRAARPGAVETPAQRaFLER 135
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 258-324 2.64e-10

Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The enzyme's tertiary fold is highly similar to that of tyrosine-specific phosphatases, except for a "recognition" region.


Pssm-ID: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 58.43  E-value: 2.64e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 198442873  258 NIVRRFLNICENTEGAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPGsiIGPQQHFL 324
Cdd:pfam00782  56 EEAVEFIDDARQKGGKVLVHCQAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRPG--ISPNFGFK 120
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
217-326 2.85e-10

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 58.45  E-value: 2.85e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873   217 KKNNVTTIVRL--NKKIYEAKRFTdagFEHYDLFFIDGSTPSD--NIVRRFLNICENTEGAIAVHCKAGLGRTGTLIACY 292
Cdd:smart00195  23 KKLGITHVINVtnEVPNYNGSDFT---YLGVPIDDNTETKISPyfPEAVEFIEDAESKGGKVLVHCQAGVSRSATLIIAY 99

                           90       100       110
                   ....*....|....*....|....*....|....
gi 198442873   293 VMKHYRFTHAEIIAWIRICRPgsIIGPQQHFLEE 326
Cdd:smart00195 100 LMKTRNMSLNDAYDFVKDRRP--IISPNFGFLRQ 131
 
Name Accession Description Interval E-value
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 163-336 3.31e-138

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 399.91  E-value: 3.31e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 163 TFDADEYEHYERVENGDFNWIVPGKFLAFSGPHPKSKIENGYPLHAPEAYFPYFKKNNVTTIVRLNKKIYEAKRFTDAGF 242
Cdd:cd14499    1 TFDLEEYEHYERVENGDLNWIVPGKFLAFSGPHDTRKDENGYPTHTPEDYIPYFKKLGVTTVVRLNKKLYDAKRFTDAGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 243 EHYDLFFIDGSTPSDNIVRRFLNICENTEGAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPGSIIGPQQH 322
Cdd:cd14499   81 RHYDLYFPDGSTPSDDIVKKFLDICENEKGAIAVHCKAGLGRTGTLIACYLMKHYGFTAREAIAWLRICRPGSVIGPQQQ 160

                        170
                 ....*....|....
gi 198442873 323 FLEEKQASLWVQGD 336
Cdd:cd14499  161 FLEEKEARLWRAGD 174
CDC14_N cd17657
N-terminal domain pseudophosphatase domain of CDC14 family proteins; The cell division control ...
 10-154 2.60e-89

N-terminal domain pseudophosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif. The N-terminal pseudophosphatase domain lacks the catalytic residues.


Pssm-ID: 350495  Cd Length: 144  Bit Score: 273.22  E-value: 2.60e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873  10 GACEFMKDRLYFATLRNRPKSTINIHYFSIDEELVYENFYADFGPLNLAMVYRYCCKLNKKLKSYSLSRKKIVHYTSFDQ 89
Cdd:cd17657    1 SAIEIIPDRLYFASLRGPPKSTDNTHYFSIDDELVYEPFFADFGPLNLAQIYRFCCKLNKKLKSPSLASKKIVHYTSLDP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 198442873  90 RKRANAAFLIGAYAVIYLKKTPEEAYRALLSGSnPPYLPFRDASFGNCTYNLTVLDCLQGIRKGL 154
Cdd:cd17657   81 KKRANAAFLIGAYAVIYLGKTPEEAYRPLESGE-PPFLPFRDASYGPCTYELTVLDCLKGLEKAL 144
DSPn pfam14671
Dual specificity protein phosphatase, N-terminal half; The active core of the dual specificity ...
 13-153 2.53e-78

Dual specificity protein phosphatase, N-terminal half; The active core of the dual specificity protein phosphatase is made up of two globular domains both with the DSP-like fold. This family represents the N-terminal half of the core. These domains are arranged in tandem, and are associated via an extensive interface to form a single globular whole. The conserved PTP signature motif (Cys-[X]5-Arg) that defines the catalytic centre of all PTP-family members is located within the C-terminal domain, family DSPc, pfam00782. Although the centre of the catalytic site is formed from DSPc, two loops from the N-terminal domain, DSPn, also contribute to the catalytic site, facilitating peptide substrate specificity.


Pssm-ID: 464252  Cd Length: 140  Bit Score: 244.76  E-value: 2.53e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873   13 EFMKDRLYFATLRNRPKSTINIHYFSIDEELVYENFYADFGPLNLAMVYRYCCKLNKKLKSYSLSRKKIVHYTSFDQRKR 92
Cdd:pfam14671   1 EIIPDRLYFATLKSKPKNTPNYHYFSIDDELVYEPFYFDFGPLNLAHLYRFCIKLNKKLKSPELKKKKIVHYTSQDKQKR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 198442873   93 ANAAFLIGAYAVIYLKKTPEEAYRALLSGSnPPYLPFRDASFGNCTYNLTVLDCLQGIRKG 153
Cdd:pfam14671  81 ANAAFLIGAYMVLYLNMSPEEALSPLSSIS-PPFIPFRDASYGPCTYTLTLLDCLKGLEKA 140
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 180-326 9.99e-24

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 96.26  E-value: 9.99e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 180 FNWIVPGKFLAFSGPHPKskiengyplhaPEAYFPYFKKNNVTTIVRLNKKIYEAkrftdagfehydlffidgstpsdni 259
Cdd:cd14494    1 FNWIDPLRLIAGALPLSP-----------LEADSRFLKQLGVTTIVDLTLAMVDR------------------------- 44

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 198442873 260 VRRFLNICENTEGAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPGSI--IGPQQHFLEE 326
Cdd:cd14494   45 FLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMSAEEAVRIVRLIRPGGIpqTIEQLDFLIK 113
PTP-IVa cd14500
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...
 206-326 2.55e-22

protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), also known as protein-tyrosine phosphatases of regenerating liver (PRLs) constitute a family of small, prenylated phosphatases that are the most oncogenic of all PTPs. They stimulate progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. They associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation. Vertebrates contain three members: PRL-1, PRL-2, and PRL-3.


Pssm-ID: 350350 [Multi-domain]  Cd Length: 156  Bit Score: 93.82  E-value: 2.55e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 206 LHAP-----EAYFPYFKKNNVTTIVRLNKKIYEAKRFTDAGFEHYDLFFIDGSTPSDNIVRRFLNICENT-------EGA 273
Cdd:cd14500   18 TDAPtdsnlPLYIKELKKYNVTDLVRVCEPTYDKEPLEKAGIKVHDWPFDDGSPPPDDVVDDWLDLLKTRfkeegkpGAC 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 198442873 274 IAVHCKAGLGRTGTLIACYVMKhYRFTHAEIIAWIRICRPGSIIGPQQHFLEE 326
Cdd:cd14500   98 IAVHCVAGLGRAPVLVAIALIE-LGMKPEDAVEFIRKKRRGAINSKQLQFLEK 149
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 180-334 2.03e-21

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP23 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin.


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 90.80  E-value: 2.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 180 FNWIVPGKFLAFSGPHPkskiengyplhapEAYFPYFKKNNVTTIVRLNKKIYEAKRFTDAGFEHYDLFFIDGSTPSDNI 259
Cdd:cd14504    1 FSWVIPGKLAGMAFPRL-------------PEHYAYLNENGIRHVVTLTEEPPPEHSDTCPGLRYHHIPIEDYTPPTLEQ 67

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 198442873 260 VRRFLNICE--NTEG-AIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPGSIIGPQQhfleEKQASLWVQ 334
Cdd:cd14504   68 IDEFLDIVEeaNAKNeAVLVHCLAGKGRTGTMLACYLVKTGKISAVDAINEIRRIRPGSIETSEQ----EKFVIQFAK 141
PTZ00242 PTZ00242
protein tyrosine phosphatase; Provisional
 187-326 1.84e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 185524 [Multi-domain]  Cd Length: 166  Bit Score: 85.84  E-value: 1.84e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 187 KFLAFSGPHPKSkiengypLHApeaYFPYFKKNNVTTIVRLNKKIYEAKRFTDAGFEHYDLFFIDGSTPSDNIVRRFLNI 266
Cdd:PTZ00242  17 KFLILDAPSPSN-------LPL---YIKELQRYNVTHLVRVCGPTYDAELLEKNGIEVHDWPFDDGAPPPKAVIDNWLRL 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 198442873 267 CENT-------EGAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPGSIIGPQQHFLEE 326
Cdd:PTZ00242  87 LDQEfakqstpPETIAVHCVAGLGRAPILVALALVEYGGMEPLDAVGFVREKRKGAINQTQLQFLKK 153
PTZ00393 PTZ00393
protein tyrosine phosphatase; Provisional
 195-326 1.15e-16

protein tyrosine phosphatase; Provisional


Pssm-ID: 240399  Cd Length: 241  Bit Score: 79.98  E-value: 1.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 195 HPkSKIENG----YPLHAPE-----AYFPYFKKNNVTTIVRLNKKIYEAKRFTDAGFEHYDLFFIDGSTPSDNIVRRFLN 265
Cdd:PTZ00393  83 HP-TKIEHGkikiLILDAPTndllpLYIKEMKNYNVTDLVRTCERTYNDGEITSAGINVHELIFPDGDAPTVDIVSNWLT 161

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 198442873 266 ICENT---EGAIAVHCKAGLGRTGTLIACyVMKHYRFTHAEIIAWIRICRPGSIIGPQQHFLEE 326
Cdd:PTZ00393 162 IVNNViknNRAVAVHCVAGLGRAPVLASI-VLIEFGMDPIDAIVFIRDRRKGAINKRQLQFLKA 224
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
182-326 6.70e-16

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 74.62  E-value: 6.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 182 WIVPGKFlaFSGPHPKSKIEngyplhapeayfpYFKKNNVTTIVRLN-KKIYEAKRFTDAGFEHYDLFFIDGSTPSDNIV 260
Cdd:COG2453    2 WIIPGLL--AGGPLPGGGEA-------------DLKREGIDAVVSLTeEEELLLGLLEEAGLEYLHLPIPDFGAPDDEQL 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 261 RRFLN-ICENTE--GAIAVHCKAGLGRTGTLIACYVMKHyRFTHAEIIAWIRICRPGSIIGPQQH-FLEE 326
Cdd:COG2453   67 QEAVDfIDEALRegKKVLVHCRGGIGRTGTVAAAYLVLL-GLSAEEALARVRAARPGAVETPAQRaFLER 135
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 216-339 3.81e-14

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine phosphatase domain-containing protein 1 (PTPDC1) is an uncharacterized non-receptor class protein-tyrosine phosphatase (PTP). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Small interfering RNA (siRNA) knockdown of the ptpdc1 gene is associated with elongated cilia.


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 71.61  E-value: 3.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 216 FKKNNVTTIVRLNKK----------------IYEAKRFTDAGFEHYDLFFIDGSTPSDNIVrrfLNICE------NTEGA 273
Cdd:cd14506   35 FKEKGIKTVINLQEPgehascgpglepesgfSYLPEAFMRAGIYFYNFGWKDYGVPSLTTI---LDIVKvmafalQEGGK 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 198442873 274 IAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPGSI-IGPQQHFLEEKQASLWVQGDIFR 339
Cdd:cd14506  112 VAVHCHAGLGRTGVLIACYLVYALRMSADQAIRLVRSKRPNSIqTRGQVLCVREFAQFLLPLRNVFA 178
PTPMT1 cd14524
protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or ...
 217-326 2.39e-13

protein-tyrosine phosphatase mitochondrial 1; Protein-tyrosine phosphatase mitochondrial 1 or PTP localized to the mitochondrion 1 (PTPMT1), also called phosphoinositide lipid phosphatase (PLIP), phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1, or PTEN-like phosphatase, is a lipid phosphatase or phosphatidylglycerophosphatase (EC 3.1.3.27) which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). It is targeted to the mitochondrion by an N-terminal signal sequence and is found anchored to the matrix face of the inner membrane. It is essential for the biosynthesis of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle. PTPMT1 also plays a crucial role in hematopoietic stem cell (HSC) function, and has been shown to display activity toward phosphoprotein substrates.


Pssm-ID: 350374 [Multi-domain]  Cd Length: 149  Bit Score: 67.67  E-value: 2.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 217 KKNNVTTIVRLNKKiYEAKRF-------TDAGFEHYDLFFID-GSTPSDNIVRR---FLNICENTEGAIAVHCKAGLGRT 285
Cdd:cd14524   25 AKENVRGVITMNEE-YETRFFcnskeewKALGVEQLRLPTVDfTGVPSLEDLEKgvdFILKHREKGKSVYVHCKAGRGRS 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 198442873 286 GTLIACYVMKHYRFTHAEIIAWIRICRPGSIIGP-QQHFLEE 326
Cdd:cd14524  104 ATIVACYLIQHKGWSPEEAQEFLRSKRPHILLRLsQREVLEE 145
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 235-321 1.99e-12

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function.


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 65.36  E-value: 1.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 235 KRFTDAGFEHYDLFFIDGSTPSDniVRRFLNICE------NTEGAIAVHCKAGLGRTGTLIACY-VMKHYRFTHAEIIAW 307
Cdd:cd14505   66 EQYQQAGITWHHLPIPDGGVPSD--IAQWQELLEellsalENGKKVLIHCKGGLGRTGLIAACLlLELGDTLDPEQAIAA 143

                         90
                 ....*....|....
gi 198442873 308 IRICRPGSIIGPQQ 321
Cdd:cd14505  144 VRALRPGAIQTPKQ 157
DSP cd14498
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ...
 214-325 8.50e-12

dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in typical and atypical dual-specificity phosphatases (DUSPs), which function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). Typical DUSPs, also called mitogen-activated protein kinase (MAPK) phosphatases (MKPs), deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain. Atypical DUSPs contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. Also included in this family are dual specificity phosphatase-like domains of catalytically inactive members such as serine/threonine/tyrosine-interacting protein (STYX) and serine/threonine/tyrosine interacting like 1 (STYXL1), as well as active phosphatases with substrates that are not phosphoproteins such as PTP localized to the mitochondrion 1 (PTPMT1), which is a lipid phosphatase, and laforin, which is a glycogen phosphatase.


Pssm-ID: 350348 [Multi-domain]  Cd Length: 135  Bit Score: 62.95  E-value: 8.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 214 PYFKKNNVTTIVRLNKKIYEAKRftDAGFEHYDLFFIDgsTPSDNIVR------RFLNICENTEGAIAVHCKAGLGRTGT 287
Cdd:cd14498   20 ELLKKLGITHILNVAGEPPPNKF--PDGIKYLRIPIED--SPDEDILShfeeaiEFIEEALKKGGKVLVHCQAGVSRSAT 95

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 198442873 288 LIACYVMKHYRFTHAEIIAWIRICRPgsIIGPQQHFLE 325
Cdd:cd14498   96 IVIAYLMKKYGWSLEEALELVKSRRP--IISPNPGFLK 131
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 258-324 2.64e-10

Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The enzyme's tertiary fold is highly similar to that of tyrosine-specific phosphatases, except for a "recognition" region.


Pssm-ID: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 58.43  E-value: 2.64e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 198442873  258 NIVRRFLNICENTEGAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPGsiIGPQQHFL 324
Cdd:pfam00782  56 EEAVEFIDDARQKGGKVLVHCQAGISRSATLIIAYLMKTRNLSLNEAYSFVKERRPG--ISPNFGFK 120
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
217-326 2.85e-10

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 58.45  E-value: 2.85e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873   217 KKNNVTTIVRL--NKKIYEAKRFTdagFEHYDLFFIDGSTPSD--NIVRRFLNICENTEGAIAVHCKAGLGRTGTLIACY 292
Cdd:smart00195  23 KKLGITHVINVtnEVPNYNGSDFT---YLGVPIDDNTETKISPyfPEAVEFIEDAESKGGKVLVHCQAGVSRSATLIIAY 99

                           90       100       110
                   ....*....|....*....|....*....|....
gi 198442873   293 VMKHYRFTHAEIIAWIRICRPgsIIGPQQHFLEE 326
Cdd:smart00195 100 LMKTRNMSLNDAYDFVKDRRP--IISPNFGFLRQ 131
PTP-IVa3 cd18535
protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), ...
 216-326 7.99e-10

protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), also known as protein-tyrosine phosphatase of regenerating liver 3 (PRL-3), stimulates progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. It exerts its oncogenic functions through activation of PI3K/Akt, which is a key regulator of the rapamycin-sensitive mTOR complex 1. PRL-3 is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation.


Pssm-ID: 350511 [Multi-domain]  Cd Length: 154  Bit Score: 57.73  E-value: 7.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 216 FKKNNVTTIVRLNKKIYEAKRFTDAGFEHYDLFFIDGSTPSDNIVRRFLNI-----CENTEGAIAVHCKAGLGRTGTLIA 290
Cdd:cd18535   33 LKKYGATTVVRVCEVTYDKTPLEKDGITVVDWPFDDGAPPPGKVVEDWLSLlktkfCEDPGCCVAVHCVAGLGRAPVLVA 112

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 198442873 291 CYVMKHyRFTHAEIIAWIRICRPGSIIGPQQHFLEE 326
Cdd:cd18535  113 LALIES-GMKYEDAIQFIRQKRRGAINSKQLTYLEK 147
PTP-IVa2 cd18536
protein tyrosine phosphatase type IVA 2; Protein tyrosine phosphatase type IVA 2 (PTP-IVa2), ...
 216-326 1.02e-09

protein tyrosine phosphatase type IVA 2; Protein tyrosine phosphatase type IVA 2 (PTP-IVa2), also known as protein-tyrosine phosphatase of regenerating liver 2 (PRL-2), stimulates progression from G1 into S phase during mitosis and promotes tumors. It regulates tumor cell migration and invasion through an ERK-dependent signaling pathway. Its overexpression correlates with breast tumor formation and progression. PRL-2 is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation.


Pssm-ID: 350512 [Multi-domain]  Cd Length: 155  Bit Score: 57.70  E-value: 1.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 216 FKKNNVTTIVRLNKKIYEAKRFTDAGFEHYDLFFIDGSTPSDNIVRRFLNIC-----ENTEGAIAVHCKAGLGRTGTLIA 290
Cdd:cd18536   34 LKKYGVTTLVRVCDATYDKAPVEKEGIQVLDWPFDDGAPPPNQIVDDWLNLLktkfrEEPGCCVAVHCVAGLGRAPVLVA 113

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 198442873 291 CYVMKhYRFTHAEIIAWIRICRPGSIIGPQQHFLEE 326
Cdd:cd18536  114 LALIE-CGMKYEDAVQFIRQKRRGAFNSKQLLYLEK 148
RNA_5'-triphosphatase cd14502
RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes ...
 183-326 1.18e-09

RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes baculovirus RNA 5'-triphosphatase, dual specificity protein phosphatase 11 (DUSP11), and the RNA triphosphatase domains of metazoan and plant mRNA capping enzymes. RNA/polynucleotide 5'-triphosphatase (EC 3.1.3.33) catalyzes the removal of the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end. mRNA capping enzyme is a bifunctional enzyme that catalyzes the first two steps of cap formation. DUSP11 has RNA 5'-triphosphatase and diphosphatase activity, but only poor protein-tyrosine phosphatase activity.


Pssm-ID: 350352 [Multi-domain]  Cd Length: 167  Bit Score: 57.67  E-value: 1.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 183 IVPGKFLAFSGP--HPKSKIENGYPLHAPEAYFPYFKK-NNVTTIVRLNK--KIYEAKRFTDAGFEHYDLFFIDGSTPSD 257
Cdd:cd14502   12 VGPTRFIPMKTPlsDDYEHLFAPEIRFTPSALAEKFRQdRKVGLVIDLTNtdRYYDPNDLDDDGYVYYKKVCVRKEPPDA 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 198442873 258 NIVRRFLNICE------NTEGAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPGSIIGPqqHFLEE 326
Cdd:cd14502   92 EEVNKFIELVDkflaedNPDKLIAVHCTHGFNRTGFMIVSYLVERLGLTVEQALEAFAQARPPGIYKP--HYIDE 164
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 251-322 6.51e-09

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 56.14  E-value: 6.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 251 DGSTPSD-----NIVRRFLNICENTEGAIAVHCKAGLGRTGTLIA-CYVMKHYRFTH----AEIIAWIRICRPGSIIGPQ 320
Cdd:cd00047  114 DHGVPSSpedllALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAiDILLERLEAEGevdvFEIVKALRKQRPGMVQTLE 193


                 ..
gi 198442873 321 QH 322
Cdd:cd00047  194 QY 195
PTP-IVa1 cd18537
protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), ...
 216-331 9.66e-09

protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), also known as protein-tyrosine phosphatase of regenerating liver 1 (PRL-1), stimulates progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. It may play a role in the development and maintenance of differentiating epithelial tissues. PRL-1 promotes cell growth and migration by activating both the ERK1/2 and RhoA pathways. It is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation.


Pssm-ID: 350513 [Multi-domain]  Cd Length: 167  Bit Score: 55.08  E-value: 9.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 216 FKKNNVTTIVRLNKKIYEAKRFTDAGFEHYDLFFIDGSTPSDNIVRRFLNIC-----ENTEGAIAVHCKAGLGRTGTLIA 290
Cdd:cd18537   37 LKKYGVTTVVRVCEATYDTTLVEKEGIQVLDWPFDDGAPPSNQIVDDWLNLLkvkfrEEPGCCIAVHCVAGLGRAPVLVA 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 198442873 291 CYVMKHyRFTHAEIIAWIRICRPGSIIGPQQHFLEEKQASL 331
Cdd:cd18537  117 LALIEC-GMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKM 156
DSP_fungal_YVH1 cd14518
dual specificity phosphatase domain of fungal YVH1-like dual specificity protein phosphatase; ...
 216-332 1.85e-08

dual specificity phosphatase domain of fungal YVH1-like dual specificity protein phosphatase; This family is composed of Saccharomyces cerevisiae dual specificity protein phosphatase Yvh1 and similar fungal proteins. Yvh1 could function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It regulates cell growth, sporulation, and glycogen accumulation. It plays an important role in ribosome assembly. Yvh1 associates transiently with late pre-60S particles and is required for the release of the nucleolar/nuclear pre-60S factor Mrt4, which is necessary to construct a translation-competent 60S subunit and mature ribosome stalk. Yvh1 contains an N-terminal catalytic dual specificity phosphatase domain and a C-terminal tail.


Pssm-ID: 350368 [Multi-domain]  Cd Length: 153  Bit Score: 53.86  E-value: 1.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 216 FKKNNVTTIVRLNKkiYEAKRFTDAGFEHYDLFFIDgsTPSDNIVR------RFLNIC-----------ENTEGAIAVHC 278
Cdd:cd14518   22 LKAENITHILSVIP--GDVPEEYFKGYEHKQIEIDD--VEDENILQhfpetnRFIDSAlfgngkdedeeKKHGGAVLVHC 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 198442873 279 KAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPgsIIGPQQHFLEekQASLW 332
Cdd:cd14518   98 AMGKSRSVTVVIAYLMYKYNLSVSQALHAVRRKRP--IAEPNDGFME--QLELY 147
DSP_STYX cd14522
dual specificity phosphatase-like domain of serine/threonine/tyrosine-interacting protein; ...
 183-324 4.31e-08

dual specificity phosphatase-like domain of serine/threonine/tyrosine-interacting protein; Serine/threonine/tyrosine-interacting protein (STYX), also called protein tyrosine phosphatase-like protein, is a catalytically inactive member of the protein tyrosine phosphatase family that plays an integral role in regulating pathways by competing with active phosphatases for binding to MAPKs. It acts as a nuclear anchor for MAPKs, affecting their nucleocytoplasmic shuttling.


Pssm-ID: 350372 [Multi-domain]  Cd Length: 151  Bit Score: 52.72  E-value: 4.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 183 IVPGKFLafsGPHP---KSKIENgyplhapeayfpyFKKNNVTTIVRLNKKIyEAkRFTDAGF-EHYDLFFID-GSTPSD 257
Cdd:cd14522    8 ILPGLYL---GPYSaamKSKLEV-------------LLKHGITHIVCVRQNI-EA-NFIKPNFpDHFRYLVLDvADNPTE 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 198442873 258 NIVR------RFLNICENTEGAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWI---RICrpgsiIGPQQHFL 324
Cdd:cd14522   70 NIIRhfptvkEFIDDCLQTGGKVLVHGNAGISRSAALVIAYIMETYGLSYRDAFAYVqqrRFC-----INPNEGFV 140
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
251-317 5.16e-08

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 54.71  E-value: 5.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 251 DGSTPSDNI-------VRRFLNICENTEGAIAVHCKAGLGRTGTLIACYVM-------KHYRFTHAEIIAWIRICRPGSI 316
Cdd:COG5599  179 DHGAISAEAlknladlIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALsksinalVQITLSVEEIVIDMRTSRNGGM 258


                 .
gi 198442873 317 I 317
Cdd:COG5599  259 V 259
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
258-316 1.24e-07

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 50.05  E-value: 1.24e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 198442873   258 NIVRRFLNICENTeGAIAVHCKAGLGRTGTLIACYVM------KHYRFTHAEIIAWIRICRPGSI 316
Cdd:smart00404  27 RAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDILlqqleaEAGEVDIFDTVKELRSQRPGMV 90
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 258-316 1.24e-07

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 50.05  E-value: 1.24e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 198442873   258 NIVRRFLNICENTeGAIAVHCKAGLGRTGTLIACYVM------KHYRFTHAEIIAWIRICRPGSI 316
Cdd:smart00012  27 RAVKKNLNQSESS-GPVVVHCSAGVGRTGTFVAIDILlqqleaEAGEVDIFDTVKELRSQRPGMV 90
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
251-316 1.49e-07

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 53.05  E-value: 1.49e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 198442873   251 DGSTPSD-----NIVRRFLNICENTEGAIAVHCKAGLGRTGTLIACYVM-----KHYRFTHAEIIAWIRICRPGSI 316
Cdd:smart00194 169 DHGVPESpesilDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILlqqleAGKEVDIFEIVKELRSQRPGMV 244
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 223-303 2.32e-07

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar proteins; Phosphatase and tensin homolog (PTEN) is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It dephosphorylates phosphoinositide trisphosphate. In addition to PTEN, this family includes tensins, voltage-sensitive phosphatases (VSPs), and auxilins. They all contain a protein tyrosine phosphatase-like domain although not all are active phosphatases. Tensins are intracellular proteins that act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility, and they may or may not have phosphatase activity. VSPs are phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. Auxilins are J domain-containing proteins that facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles, and they do not exhibit phosphatase activity.


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 50.66  E-value: 2.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 223 TIVRLNKKIYEAKRFTDAGFEHYDlfFIDGSTPSDNIVrrfLNICENTEG--------AIAVHCKAGLGRTGTLIACYVM 294
Cdd:cd14497   44 MIFNLSEEEYDDDSKFEGRVLHYG--FPDHHPPPLGLL---LEIVDDIDSwlsedpnnVAVVHCKAGKGRTGTVICAYLL 118


                 ....*....
gi 198442873 295 KHYRFTHAE 303
Cdd:cd14497  119 YYGQYSTAD 127
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 228-294 1.43e-06

protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; Phosphatase and tensin homolog (PTEN), also phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN or mutated in multiple advanced cancers 1 (MMAC1), is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It is a critical endogenous inhibitor of phosphoinositide signaling. It dephosphorylates phosphoinositide trisphosphate, and therefore, has the function of negatively regulating Akt. The PTEN/PI3K/AKT pathway regulates the signaling of multiple biological processes such as apoptosis, metabolism, cell proliferation, and cell growth. PTEN contains an N-terminal PIP-binding domain, a protein tyrosine phosphatase (PTP)-like catalytic domain, a regulatory C2 domain responsible for its cellular location, a C-tail containing phosphorylation sites, and a C-terminal PDZ domain.


Pssm-ID: 350359 [Multi-domain]  Cd Length: 158  Bit Score: 48.35  E-value: 1.43e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 198442873 228 NKKIYEAKRFtDAGFEHYDlfFIDGSTPSDNIVRRFLN-----ICENTEGAIAVHCKAGLGRTGTLIACYVM 294
Cdd:cd14509   49 SERSYDPSKF-NGRVAEYP--FDDHNPPPLELIKPFCEdvdewLKEDEKNVAAVHCKAGKGRTGVMICCYLL 117
DSP_DUSP11 cd17665
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ...
 181-294 1.64e-06

dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar proteins; dual specificity protein phosphatase 11 (DUSP11), also known as RNA/RNP complex-1-interacting phosphatase or phosphatase that interacts with RNA/RNP complex 1 (PIR1), has RNA 5'-triphosphatase and diphosphatase activity, but only poor protein-tyrosine phosphatase activity. It has activity for short RNAs but is less active toward mononucleotide triphosphates, suggesting that its primary function in vivo is to dephosphorylate RNA 5'-ends. It may play a role in nuclear mRNA metabolism. Also included in this subfamily is baculovirus RNA 5'-triphosphatase for Autographa californica nuclear polyhedrosis virus.


Pssm-ID: 350503  Cd Length: 169  Bit Score: 48.43  E-value: 1.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 181 NWIVPG-KFLAFSGPHPKSkIENGYPLH---APEAYFPYFKKNN--VTTIVRLN--KKIYEAKRFTDAGFEHYDLFFIDG 252
Cdd:cd17665    9 GQRIPGtRFIAFKVPLRKS-FFANLPPEqrfTPKDLVEQVEKRGekLGLVIDLTntTRYYDPRDLTNHGVYYKKITCPGH 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 198442873 253 STPSD-------NIVRRFLNICENTEGAIAVHCKAGLGRTGTLIaCYVM 294
Cdd:cd17665   88 QVPDDktiqsfkDAVKDFLEKNKDNDKLIGVHCTHGLNRTGYLI-CRYL 135
DUSP18_21 cd14573
dual specificity protein phosphatases 18 and 21; This subfamily contains dual specificity ...
 272-326 2.57e-06

dual specificity protein phosphatases 18 and 21; This subfamily contains dual specificity protein phosphatase 18 (DUSP18), dual specificity protein phosphatase 21 (DUSP21), and similar proteins. They function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48), and are atypical DUSPs. They contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP18, also called low molecular weight dual specificity phosphatase 20 (LMW-DSP20), is a catalytically active phosphatase with a preference for phosphotyrosine over phosphoserine/threonine oligopeptides in vitro. In vivo, it has been shown to interact and dephosphorylate SAPK/JNK, and may play a role in regulating the SAPK/JNK pathway. DUSP21 is also called low molecular weight dual specificity phosphatase 21 (LMW-DSP21). Its gene has been identified as a potential therapeutic target in human hepatocellular carcinoma. DUSP18 and DUSP21 target to opposing sides of the mitochondrial inner membrane.


Pssm-ID: 350421 [Multi-domain]  Cd Length: 158  Bit Score: 47.86  E-value: 2.57e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 198442873 272 GAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPgsIIGPQQHFLEE 326
Cdd:cd14573   80 GRTLLHCVAGVSRSATLCLAYLMKYHAMSLLDAHTWVKSCRP--IIRPNNGFWEQ 132
Mce1_N cd17664
N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as ...
 184-326 3.97e-06

N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as RNA guanylyltransferase and 5'-phosphatase (RNGTT) or mammalian mRNA capping enzyme (Mce1) in mammals, is a bifunctional enzyme that catalyzes the first two steps of cap formation: (1) by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end using the polynucleotide 5'-phosphatase activity (EC 3.1.3.33) of the N-terminal triphosphatase domain; and (2) by transferring the GMP moiety of GTP to the 5'-diphosphate terminus through the C-terminal mRNA guanylyltransferase domain (EC 2.7.7.50). The enzyme is also referred to as CEL-1 in Caenorhabditis elegans.


Pssm-ID: 350502  Cd Length: 167  Bit Score: 47.29  E-value: 3.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 184 VPGKFLAFsgphpKSKIENGYPLHAPEAY-------FPYFK--KNNVTTIVRLNKkiyeAKRFTD-AGFEHYDLFFID-- 251
Cdd:cd17664   12 VAGKFLPF-----KTPLGPRYDDQVPEENrfhpsmlFNYLKslKVKLGLWIDLTN----TNRFYDrNEVEKEGCKYIKlq 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 252 ----GSTPSDNIVRRFLNICEN------TEgAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPGSIIgpQQ 321
Cdd:cd17664   83 ckghGECPSPEQTETFIRLCENfieknpLE-LIGVHCTHGFNRTGFLICAYLVEKMDWSVEAAVATFAQARPPGIY--KG 159


                 ....*
gi 198442873 322 HFLEE 326
Cdd:cd17664  160 DYLKE 164
DUSP14 cd14572
dual specificity protein phosphatase 14; dual specificity protein phosphatase 14 (DUSP14), ...
 272-323 6.54e-06

dual specificity protein phosphatase 14; dual specificity protein phosphatase 14 (DUSP14), also called mitogen-activated protein kinase (MAPK) phosphatase 6 (MKP-6) or MKP-1-like protein tyrosine phosphatase (MKP-L), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP14 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP14 dephosphorylates JNK, ERK, and p38 in vitro. It also directly interacts and dephosphorylates TGF-beta-activated kinase 1 (TAK1)-binding protein 1 (TAB1) in T cells, and negatively regulates TCR signaling and immune responses.


Pssm-ID: 350420 [Multi-domain]  Cd Length: 150  Bit Score: 46.40  E-value: 6.54e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 198442873 272 GAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPgsIIGPQQHF 323
Cdd:cd14572   86 GATLVHCAAGVSRSATLCIAYLMKYHRVSLLEAYNWVKARRP--VIRPNVGF 135
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 55-131 1.10e-05

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 44.65  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873  55 LNLAMVYRYCCKLNKKLKSyslsRKKIVHYTSfdqRKRANAAFLIGAYAVIYLKKTPEEAY---RALLSGSNPPYLPFRD 131
Cdd:cd14494   37 LTLAMVDRFLEVLDQAEKP----GEPVLVHCK---AGVGRTGTLVACYLVLLGGMSAEEAVrivRLIRPGGIPQTIEQLD 109
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 251-316 1.93e-05

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness.


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 45.83  E-value: 1.93e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 198442873 251 DGSTPS--DNIVR--RFLNICENTeGAIAVHCKAGLGRTGTLIA-----CYVMKHYRFTHAEIIAWIRICRPGSI 316
Cdd:cd14538  117 DHGTPQsaDPLLRfiRYMRRIHNS-GPIVVHCSAGIGRTGVLITidvalGLIERDLPFDIQDIVKDLREQRQGMI 190
DSP_slingshot cd14513
dual specificity phosphatase domain of slingshot family phosphatases; The slingshot (SSH) ...
 217-326 2.19e-05

dual specificity phosphatase domain of slingshot family phosphatases; The slingshot (SSH) family of dual specificity protein phosphatases is composed of Drosophila slingshot phosphatase and its vertebrate homologs: SSH1, SSH2 and SSH3. Its members specifically dephosphorylate and reactivate Ser-3-phosphorylated cofilin (P-cofilin), an actin-binding protein that plays an essential role in actin filament dynamics. In Drosophila, loss of ssh gene function causes prominent elevation in the levels of P-cofilin and filamentous actin and disorganized epidermal cell morphogenesis, including bifurcation phenotypes of bristles and wing hairs. SSH family phosphatases contain an N-terminal, SSH family-specific non-catalytic (SSH-N) domain, followed by a short domain with similarity to the C-terminal domain of the chromatin-associated protein DEK, and a dual specificity phosphatase catalytic domain. In addition, many members contain a C-terminal tail. The SSH-N domain plays critical roles in P-cofilin recognition, F-actin-mediated activation, and subcellular localization of SSHs.


Pssm-ID: 350363 [Multi-domain]  Cd Length: 139  Bit Score: 44.69  E-value: 2.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 217 KKNNVTTIVRLNKKIyeaKRFTDAGFEHYDLFFIDGST----PSDNIVRRFLNICENTEGAIAVHCKAGLGRTGTLIACY 292
Cdd:cd14513   23 QNNGVKYILNVTREI---DNFFPGRFTYHNIRVWDEEStnllPYWNETYRFIKEARRKGSKVLVHCKMGVSRSASTVIAY 99

                         90       100       110
                 ....*....|....*....|....*....|....
gi 198442873 293 VMKHYRFTHAEIIAWIRICRpgSIIGPQQHFLEE 326
Cdd:cd14513  100 AMKEYGWSLEQALEHVKERR--SCIKPNPGFLRQ 131
DSP_slingshot_3 cd14571
dual specificity phosphatase domain of slingshot homolog 3; Dual specificity protein ...
 211-328 3.49e-05

dual specificity phosphatase domain of slingshot homolog 3; Dual specificity protein phosphatase slingshot homolog 3 (SSH3), also called SSH-like protein 3, is part of the slingshot (SSH) family, whose members specifically dephosphorylate and reactivate Ser-3-phosphorylated cofilin (P-cofilin), an actin-binding protein that plays an essential role in actin filament dynamics. The Xenopus homolog (xSSH) is involved in the gastrulation movement. Mouse SSH3 dephosphorylates actin-depolymerizing factor (ADF) and cofilin but is dispensable for development. There are at least two human SSH3 isoforms reported: hSSH-3L (long) and hSSH-3. As SSH family phosphatases, they contain an N-terminal, SSH family-specific non-catalytic (SSH-N) domain, followed by a short domain with similarity to the C-terminal domain of the chromatin-associated protein DEK, and a dual specificity phosphatase catalytic domain. In addition, hSSH-3L contains a C-terminal tail while hSSH-3 does not.


Pssm-ID: 350419 [Multi-domain]  Cd Length: 144  Bit Score: 44.08  E-value: 3.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 211 AYFPYFKKNNVTTIVRLNKKI--YEAKRFTDAGFEHYDLFFIDgSTPSDNIVRRFLNICENTEGAIAVHCKAGLGRTGTL 288
Cdd:cd14571   20 ANLEELQRNRVSHILNVTREIdnFFPERFTYMNIRVYDEEATQ-LLPHWKETHRFIEAARAQGTRVLVHCKMGVSRSAST 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 198442873 289 IACYVMKHYRFTHAEIIAWIRICRPgsIIGPQQHFLEEKQ 328
Cdd:cd14571   99 VIAYAMKQYGWTLEQALRHVRERRP--IVQPNPGFLRQLQ 136
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
221-316 4.03e-05

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 45.31  E-value: 4.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873  221 VTTIVRLNKKIYEAKRFTdagfEHYdlFFI---DGSTPSD-----NIVRRFLNIC-ENTEGAIAVHCKAGLGRTGTLIAC 291
Cdd:pfam00102 116 TVRTLEVSNGGSEETRTV----KHF--HYTgwpDHGVPESpnsllDLLRKVRKSSlDGRSGPIVVHCSAGIGRTGTFIAI 189

                          90       100       110
                  ....*....|....*....|....*....|.
gi 198442873  292 YVMkHYRFTH------AEIIAWIRICRPGSI 316
Cdd:pfam00102 190 DIA-LQQLEAegevdiFQIVKELRSQRPGMV 219
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 208-294 4.30e-05

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa TpbA; This subfamily contains bacterial protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DUSPs) related to Pseudomonas aeruginosa TpbA, a DUSP that negatively regulates biofilm formation by converting extracellular quorum sensing signals and to Mycobacterium tuberculosis PtpB, a PTP virulence factor that attenuates host immune defenses by interfering with signal transduction pathways in macrophages. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides, while DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and PTPs.


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 44.29  E-value: 4.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 208 APEAYFPYFKKNNVTTIVRLNKKIYEAKRF----TDAGFEHYDL-FFIDGSTPSDNIVRRFLNICENTEGAIAVHCKAGL 282
Cdd:cd14529   21 SPDEDRALLKKLGIKTVIDLRGADERAASEeaaaKIDGVKYVNLpLSATRPTESDVQSFLLIMDLKLAPGPVLIHCKHGK 100

                         90
                 ....*....|..
gi 198442873 283 GRTGTLIACYVM 294
Cdd:cd14529  101 DRTGLVSALYRI 112
DUSP14-like cd14514
dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is ...
 272-319 6.77e-05

dual specificity protein phosphatases 14, 18, 21, 28 and similar proteins; This family is composed of dual specificity protein phosphatase 14 (DUSP14, also known as MKP-6), 18 (DUSP18), 21 (DUSP21), 28 (DUSP28), and similar proteins. They function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48), and are atypical DUSPs. They contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP14 directly interacts and dephosphorylates TGF-beta-activated kinase 1 (TAK1)-binding protein 1 (TAB1) in T cells, and negatively regulates TCR signaling and immune responses. DUSP18 has been shown to interact and dephosphorylate SAPK/JNK, and may play a role in regulating the SAPK/JNK pathway. DUSP18 and DUSP21 target to opposing sides of the mitochondrial inner membrane. DUSP28 has been implicated in hepatocellular carcinoma progression and in migratory activity and drug resistance of pancreatic cancer cells.


Pssm-ID: 350364 [Multi-domain]  Cd Length: 133  Bit Score: 42.93  E-value: 6.77e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 198442873 272 GAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPgsIIGP 319
Cdd:cd14514   78 GRTLVHCVAGVSRSATLCLAYLMKYEGMTLREAYKHVKAARP--IIRP 123
PFA-DSP_unk cd18538
unknown subfamily of atypical dual-specificity phosphatases from fungi; This uncharacterized ...
 203-292 1.13e-04

unknown subfamily of atypical dual-specificity phosphatases from fungi; This uncharacterized subfamily belongs to the plant and fungi atypical dual-specificity phosphatases (PFA-DSPs) group of atypical DSPs that present in plants, fungi, kinetoplastids, and slime molds. They share structural similarity with atypical- and lipid phosphatase DSPs from mammals. The PFA-DSP group is composed of active as well as inactive phosphatases. This unknown subgroup contains the conserved the CxxxxxR catalytic motif present in active cysteine phosphatases.


Pssm-ID: 350514 [Multi-domain]  Cd Length: 145  Bit Score: 42.74  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 203 GYPLhaPEAyFPYFKKNNVTTIVRLNKKIY---EAKRFTDAGFEHYDLFfIDG------STPsDNIVRRFLNICENTEG- 272
Cdd:cd18538   17 SFPK--PEN-FGFLKSLGLRTILTLVQEEYspeFLNFLRENGIQHFHIA-MLGnkdpkvSIP-DHTMNRILRIILDKENh 91

                         90       100
                 ....*....|....*....|
gi 198442873 273 AIAVHCKAGLGRTGTLIACY 292
Cdd:cd18538   92 PILVHCNKGKHRTGCVIACF 111
DUSP26 cd14578
dual specificity protein phosphatase 26; Dual specificity protein phosphatase 26 (DUSP26), ...
 232-326 1.33e-04

dual specificity protein phosphatase 26; Dual specificity protein phosphatase 26 (DUSP26), also called mitogen-activated protein kinase (MAPK) phosphatase 8 (MKP-8) or low-molecular-mass dual-specificity phosphatase 4 (LDP-4), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP26 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is a brain phosphatase highly overexpressed in neuroblastoma and has also been identified as a p53 phosphatase, dephosphorylating phospho-Ser20 and phospho-Ser37 in the p53 transactivation domain.


Pssm-ID: 350426 [Multi-domain]  Cd Length: 144  Bit Score: 42.52  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 232 YEAKRFTDAGFEHYDLFFIDGST---PSDNIVRRFLNiceNTEGAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWI 308
Cdd:cd14578   45 YEGLNIRYLGIEAHDSPAFDMSIhfyPAADFIHRALS---QPGGKILVHCAVGVSRSATLVLAYLMIHHHMTLVEAIKTV 121

                         90
                 ....*....|....*...
gi 198442873 309 RICRPgsiIGPQQHFLEE 326
Cdd:cd14578  122 KDHRG---IIPNRGFLRQ 136
DUSP22 cd14581
dual specificity protein phosphatase 22; Dual specificity protein phosphatase 22 (DUSP22), ...
 254-328 1.57e-04

dual specificity protein phosphatase 22; Dual specificity protein phosphatase 22 (DUSP22), also called JNK-stimulatory phosphatase-1 (JSP-1), low molecular weight dual specificity phosphatase 2 (LMW-DSP2), mitogen-activated protein kinase phosphatase x (MKP-x) or VHR-related MKPx (VHX), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP22 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP22 negatively regulates the estrogen receptor-alpha-mediated signaling pathway and the IL6-leukemia inhibitory factor (LIF)-STAT3-mediated signaling pathway. It also regulates cell death by acting as a scaffold protein for the ASK1-MKK7-JNK signal transduction pathway independently of its phosphatase activity.


Pssm-ID: 350429 [Multi-domain]  Cd Length: 149  Bit Score: 42.48  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 254 TPSDNIVR------RFLNICENTEGAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRpgSIIGPQQHFLEEK 327
Cdd:cd14581   57 SPSQNLTQhfkesiKFIHECRLRGEGCLVHCLAGVSRSVTLVVAYIMTVTDFGWEDALSAVKAAR--SCANPNMGFQRQL 134


                 .
gi 198442873 328 Q 328
Cdd:cd14581  135 Q 135
DSP_DUSP10 cd14567
dual specificity phosphatase domain of dual specificity protein phosphatase 10; Dual ...
 276-324 1.63e-04

dual specificity phosphatase domain of dual specificity protein phosphatase 10; Dual specificity protein phosphatase 10 (DUSP10), also called mitogen-activated protein kinase (MAPK) phosphatase 5 (MKP-5), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class III subfamily and is a JNK/p38-selective cytoplasmic MKP. DUSP10/MKP-5 coordinates skeletal muscle regeneration by negatively regulating mitochondria-mediated apoptosis. It is also an important regulator of intestinal epithelial barrier function and a suppressor of colon tumorigenesis. DUSP10/MKP-5 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350415 [Multi-domain]  Cd Length: 152  Bit Score: 42.43  E-value: 1.63e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 198442873 276 VHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPgsIIGPQQHFL 324
Cdd:cd14567   85 VHCQAGVSRSATIVIAYLMKHTRMTMTDAYKFVKNKRP--IISPNLNFM 131
DSP_MKP_classIII cd14568
dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; ...
 263-324 2.50e-04

dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs and function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III). Class III MKPs consist of DUSP8, DUSP10/MKP-5 and DUSP16/MKP-7, and are JNK/p38-selective phosphatases, which are found in both the cell nucleus and cytoplasm. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350416 [Multi-domain]  Cd Length: 140  Bit Score: 41.63  E-value: 2.50e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 198442873 263 FLNICENTEGAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPgsIIGPQQHFL 324
Cdd:cd14568   71 FIEKARASNKRVLVHCLAGISRSATIAIAYIMKHMRMSLDDAYRFVKEKRP--TISPNFNFL 130
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 271-324 3.32e-04

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2).


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 42.51  E-value: 3.32e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 271 EGAIAVHCKAGLGRTGTLIACY-VMKHYRFTHA----EIIAWIRICRPGSIIGPQQ-HFL 324
Cdd:cd14554  174 EGPITVHCSAGVGRTGVFITLSiVLERMRYEGVvdvfQTVKLLRTQRPAMVQTEDQyQFC 233
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 260-303 3.57e-04

protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase/transmembrane phosphatase with tensin homology; Voltage-sensitive phosphatase (VSP) proteins comprise a family of phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. This family is conserved in deuterostomes; VSP was first identified as a sperm flagellar plasma membrane protein in Ciona intestinalis. Gene duplication events in primates resulted in the presence of paralogs, transmembrane phosphatase with tensin homology (TPTE) and TPTE2, that retain protein domain architecture but, in the case of TPTE, have lost catalytic activity. TPTE, also called cancer/testis antigen 44 (CT44), may play a role in the signal transduction pathways of the endocrine or spermatogenic function of the testis. TPTE2, also called TPTE and PTEN homologous inositol lipid phosphatase (TPIP), occurs in several differentially spliced forms; TPIP alpha displays phosphoinositide 3-phosphatase activity and is localized on the endoplasmic reticulum, while TPIP beta is cytosolic and lacks detectable phosphatase activity. VSP/TPTE proteins contain an N-terminal voltage sensor consisting of four transmembrane segments, a protein tyrosine phosphatase (PTP)-like phosphoinositide phosphatase catalytic domain, followed by a regulatory C2 domain.


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 41.96  E-value: 3.57e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 198442873 260 VRRFLNicENTEGAIAVHCKAGLGRTGTLIACYVMKHYRFTHAE 303
Cdd:cd14510   99 VREWMA--ADPKNVVAIHCKGGKGRTGTMVCAWLIYSGQFESAK 140
DSP_plant_IBR5-like cd18534
dual specificity phosphatase domain of plant IBR5-like protein phosphatases; This subfamily is ...
 263-319 4.76e-04

dual specificity phosphatase domain of plant IBR5-like protein phosphatases; This subfamily is composed of Arabidopsis thaliana INDOLE-3-BUTYRIC ACID (IBA) RESPONSE 5 (IBR5) and similar plant proteins. IBR5 protein is also called SKP1-interacting partner 33. The IBR5 gene encodes a dual-specificity phosphatase (DUSP) which acts as a positive regulator of plant responses to auxin and abscisic acid. DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). Typical DUSPs, also called mitogen-activated protein kinase (MAPK) phosphatases (MKPs), deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. IBR5 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs. It has been shown to target MPK12, which is a negative regulator of auxin signaling.


Pssm-ID: 350510 [Multi-domain]  Cd Length: 130  Bit Score: 40.59  E-value: 4.76e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 198442873 263 FLNICENTEGAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPGSIIGP 319
Cdd:cd18534   65 FIEQCRKDKARVLVHCMSGQSRSPAVVIAYLMKHKGWRLAESYQWVKERRPSINLSP 121
DUSP3-like cd14515
dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is ...
 270-325 4.81e-04

dual specificity protein phosphatases 3, 13, 26, 27, and similar domains; This family is composed of dual specificity protein phosphatase 3 (DUSP3, also known as VHR), 13B (DUSP13B, also known as TMDP), 26 (DUSP26, also known as MPK8), 13A (DUSP13A, also known as MDSP), dual specificity phosphatase and pro isomerase domain containing 1 (DUPD1), and inactive DUSP27. In general, DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). Members of this family are atypical DUSPs; they contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. Inactive DUSP27 contains a dual specificity phosphatase-like domain with the active site cysteine substituted to serine.


Pssm-ID: 350365 [Multi-domain]  Cd Length: 148  Bit Score: 41.04  E-value: 4.81e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 198442873 270 TEGAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPgsiIGPQQHFLE 325
Cdd:cd14515   87 PGGKVLVHCVEGVSRSATLVLAYLMIYQNMTLEEAIRTVRKKRE---IRPNRGFLQ 139
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 276-317 4.95e-04

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. YopH is an essential virulence determinant of the pathogenic bacterium by dephosphorylating several focal adhesion proteins including p130Cas in human epithelial cells, resulting in the disruption of focal adhesions and cell detachment from the extracellular matrix. It contains an N-terminal domain that contains signals required for TTSS-mediated delivery of YopH into host cells and a C-terminal catalytic PTP domain.


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 42.00  E-value: 4.95e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 198442873 276 VHCKAGLGRTGTLIACYVMKHYRFTHA--EIIAWIRICRPGSII 317
Cdd:cd14559  173 IHCRAGVGRTGQLAAAMELNKSPNNLSveDIVSDMRTSRNGKMV 216
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 251-316 5.08e-04

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 41.66  E-value: 5.08e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 198442873 251 DGSTP--SDNIVR--RFLNICENTeGAIAVHCKAGLGRTGTLIA-----CYVMKHYRFTHAEIIAWIRICRPGSI 316
Cdd:cd14596  116 DHGTPqsSDQLVKfiCYMRKVHNT-GPIVVHCSAGIGRAGVLICvdvllSLIEKDLSFNIKDIVREMRQQRYGMI 189
DSP_MKP cd14512
dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; ...
 263-324 7.72e-04

dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs, which are involved in gene regulation, cell proliferation, programmed cell death and stress responses, as an important feedback control mechanism that limits MAPK cascades. MKPs, also referred to as typical DUSPs, function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III).


Pssm-ID: 350362 [Multi-domain]  Cd Length: 136  Bit Score: 40.16  E-value: 7.72e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 198442873 263 FLNICENTEGAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPgsIIGPQQHFL 324
Cdd:cd14512   71 FIEEAKASNGGVLVHCLAGISRSATIAIAYLMKRMRMSLDEAYDFVKEKRP--TISPNFNFM 130
DSP_MKP_classI cd14565
dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase; ...
 263-324 8.79e-04

dual specificity phosphatase domain of class I mitogen-activated protein kinase phosphatase; Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs and function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III). Class I MKPs consist of DUSP1/MKP-1, DUSP2 (PAC1), DUSP4/MKP-2 and DUSP5. They are all mitogen- and stress-inducible nuclear MKPs. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350413 [Multi-domain]  Cd Length: 138  Bit Score: 40.06  E-value: 8.79e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 198442873 263 FLNICENTEGAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPgsIIGPQQHFL 324
Cdd:cd14565   70 FIDKVKASGGRVLVHCQAGISRSATICLAYLMTTRRVRLNEAFDYVKQRRS--VISPNFNFM 129
DSP_DUSP4 cd14640
dual specificity phosphatase domain of dual specificity protein phosphatase 4; Dual ...
 263-324 1.10e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 4; Dual specificity protein phosphatase 4 (DUSP4), also called mitogen-activated protein kinase (MAPK) phosphatase 2 (MKP-2), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class I subfamily and is a mitogen- and stress-inducible nuclear MKP. DUSP4 regulates either ERK or c-JUN N-terminal kinase (JNK), depending on the cell type. It dephosphorylates nuclear JNK and induces apoptosis in diffuse large B cell lymphoma (DLBCL) cells. It acts as a negative regulator of macrophage M1 activation and inhibits inflammation during macrophage-adipocyte interaction. It has been linked to different aspects of cancer: it may have a role in the development of ovarian cancers, oesophagogastric rib metastasis, and pancreatic tumours; it may also be a candidate tumor suppressor gene, with its deletion implicated in breast cancer, prostate cancer, and gliomas. DUSP4/MKP-2 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350488 [Multi-domain]  Cd Length: 141  Bit Score: 39.63  E-value: 1.10e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 198442873 263 FLNICENTEGAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRpgSIIGPQQHFL 324
Cdd:cd14640   70 YIDSVKDCNGRVLVHCQAGISRSATICLAYLMMKKRVRLEEAFEFVKQRR--SIISPNFSFM 129
DSP_DUSP15 cd14582
dual specificity phosphatase domain of dual specificity protein phosphatase 15; Dual ...
 254-326 1.31e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 15; Dual specificity protein phosphatase 15 (DUSP15), also called Vaccinia virus VH1-related dual-specific protein phosphatase Y (VHY) or VH1-related member Y, functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). DUSP15 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is highly expressed in the testis and is located in the plasma membrane in a myristoylation-dependent manner. It may be involved in the regulation of meiotic signal transduction in testis cells. It is also expressed in the brain and has been identified as a regulator of oligodendrocyte differentiation. DUSP15 contains an N-terminal catalytic dual specificity phosphatase domain and a short C-terminal tail.


Pssm-ID: 350430 [Multi-domain]  Cd Length: 146  Bit Score: 39.55  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 254 TPSDNIVRRF------LNICENTEGAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPgsIIGPQQHF---L 324
Cdd:cd14582   58 TPEAPIKKHFkecisfIHQCRLNGGNCLVHCLAGISRSTTIVVAYVMAVTELSWQEVLEAIRAVRP--IANPNPGFkqqL 135


                 ..
gi 198442873 325 EE 326
Cdd:cd14582  136 EE 137
DSP_fungal_PPS1 cd14516
dual specificity phosphatase domain of fungal dual specificity protein phosphatase PPS1-like; ...
 194-326 1.38e-03

dual specificity phosphatase domain of fungal dual specificity protein phosphatase PPS1-like; This subfamily contains fungal proteins with similarity to dual specificity protein phosphatase PPS1 from Saccharomyces cerevisiae, which has a role in the DNA synthesis phase of the cell cycle. As a dual specificity protein phosphatase, PPS1 functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It contains a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350366 [Multi-domain]  Cd Length: 177  Bit Score: 39.95  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 194 PHPKSKIENGYPLHAPEAYFPYFKKNNVTTIVRLNKKIYEAKRFTDAGfehydlffIDGSTPSDNIVRRFLNICENTEGA 273
Cdd:cd14516   47 SNLKIKYIFDFSLQDLSNLDSNSEGSLWAAEYKGLISVLYIHNLKDDG--------IDSLLPQLTDALDFIQKARLLGGK 118

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 198442873 274 IAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPGSIIGPQQHFLEE 326
Cdd:cd14516  119 TLVHCRVGVSRSATVVIAEVMKHLRMSLVDAYLFVRVRRLNIIIQPNLRFFYE 171
DSP_DUSP19 cd14523
dual specificity phosphatase domain of dual specificity protein phosphatase 19; Dual ...
 217-326 1.43e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 19; Dual specificity protein phosphatase 19 (DUSP19), also called low molecular weight dual specificity phosphatase 3 (LMW-DSP3) or stress-activated protein kinase (SAPK) pathway-regulating phosphatase 1 (SKRP1), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP19 interacts with the MAPK kinase MKK7, a JNK activator, and inactivates the JNK MAPK pathway.


Pssm-ID: 350373 [Multi-domain]  Cd Length: 137  Bit Score: 39.26  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 217 KKNNVTTIVRLNKKIYEA--KRFTDAGFEHYDLffidgstPSDNIVR------RFLNICENTEGAIAVHCKAGLGRTGTL 288
Cdd:cd14523   24 KKHKVTHILNVAYGVENAfpDDFTYKTISILDL-------PETDITSyfpecfEFIDEAKSQDGVVLVHCNAGVSRSASI 96

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 198442873 289 IACYVMKHYRFTHAEIIAWIRICRPGsiIGPQQHFLEE 326
Cdd:cd14523   97 VIGYLMATENLSFEDAFSLVKNARPS--IRPNPGFMEQ 132
PTPlike_phytase pfam14566
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ...
 231-294 1.62e-03

Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in abundance in seeds and acting as an inorganic phosphate reservoir. Phytases are phosphatases that hydrolyze phytate to less-phosphorylated myo-inositol derivatives and inorganic phosphate. The active-site sequence (HCXXGXGR) of the phytase identified from the gut micro-organizm Selenomonas ruminantium forms a loop (P loop) at the base of a substrate binding pocket that is characteriztic of protein tyrosine phosphatases (PTPs). The depth of this pocket is an important determinant of the substrate specificity of PTPs. In humans this enzyme is thought to aid bone mineralization and salvage the inositol moiety prior to apoptosis.


Pssm-ID: 464208 [Multi-domain]  Cd Length: 157  Bit Score: 39.60  E-value: 1.62e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 198442873  231 IYEAKRFTDAGFEHYDLFFIDGSTPSDNIVRRFLNICENT--EGAIAVHCKAGLGRTGTLIACYVM 294
Cdd:pfam14566  90 VYERLKAEGPGVDYRRIPITDEKAPLEEDFDALISIVKDApeDTALVFNCQMGRGRTTTAMVIADL 155
DSP_DUSP5 cd14639
dual specificity phosphatase domain of dual specificity protein phosphatase 5; Dual ...
 263-324 1.89e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 5; Dual specificity protein phosphatase 5 (DUSP5) functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other mitogen-activated protein kinase (MAPK) phosphatases (MKPs), it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class I subfamily and is a mitogen- and stress-inducible nuclear MKP. DUSP5 preferentially dephosphorylates extracellular signal-regulated kinase (ERK), and is involved in ERK signaling and ERK-dependent inflammatory gene expression in adipocytes. It also plays a role in regulating pressure-dependent myogenic cerebral arterial constriction, which is crucial for the maintenance of constant cerebral blood flow to the brain. DUSP5 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350487 [Multi-domain]  Cd Length: 138  Bit Score: 39.13  E-value: 1.89e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 198442873 263 FLNICENTEGAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRpgSIIGPQQHFL 324
Cdd:cd14639   70 FIDCVRRAGGKVLVHCEAGISRSPTICMAYLMKTKRFRLEEAFDYIKQRR--SLISPNFGFM 129
DUSP13A cd14580
dual specificity protein phosphatase 13 isoform A; Dual specificity protein phosphatase 13 ...
 269-326 2.12e-03

dual specificity protein phosphatase 13 isoform A; Dual specificity protein phosphatase 13 isoform A (DUSP13A), also called branching-enzyme interacting DSP or muscle-restricted DSP (MDSP), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP13A is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. DUSP13A also functions as a regulator of apoptosis signal-regulating kinase 1 (ASK1), a MAPK kinase kinase, by interacting with its N-terminal domain and inducing ASK1-mediated apoptosis through the activation of caspase-3. This function is independent of phosphatase activity.


Pssm-ID: 350428 [Multi-domain]  Cd Length: 145  Bit Score: 38.97  E-value: 2.12e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 198442873 269 NTEGA-IAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRpgsIIGPQQHFLEE 326
Cdd:cd14580   82 NTPGAkVLVHCAVGVSRSATLVLAYLMIYHQLSLVQAIKTVKERR---WIFPNRGFLKQ 137
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 251-290 2.35e-03

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 39.92  E-value: 2.35e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 198442873 251 DGSTPSD-----NIVR--RFLNICENTEGAIAVHCKAGLGRTGTLIA 290
Cdd:cd18533  115 DFGVPDSpedllTLIKlkRELNDSASLDPPIIVHCSAGVGRTGTFIA 161
DSP_DUSP22_15 cd14519
dual specificity phosphatase domain of dual specificity protein phosphatase 22, 15, and ...
 254-328 2.88e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 22, 15, and similar proteins; Dual specificity protein phosphatase 22 (DUSP22, also known as VHX) and 15 (DUSP15, also known as VHY) function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). They are atypical DUSPs; they contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. The both contain N-terminal myristoylation recognition sequences and myristoylation regulates their subcellular location. DUSP22 negatively regulates the estrogen receptor-alpha-mediated signaling pathway and the IL6-leukemia inhibitory factor (LIF)-STAT3-mediated signaling pathway. DUSP15 has been identified as a regulator of oligodendrocyte differentiation. DUSP22 is a single domain protein containing only the catalytic dual specificity phosphatase domain while DUSP15 contains a short C-terminal tail.


Pssm-ID: 350369 [Multi-domain]  Cd Length: 136  Bit Score: 38.50  E-value: 2.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 254 TPSDNIVR------RFLNICENTEGAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPgsIIGPQQHFLEEK 327
Cdd:cd14519   54 TPEQNISQhfreciNFIHEARLNGGNVLVHCLAGVSRSVTIVAAYLMTVTDLGWRDALKAVRAARP--CANPNFGFQRQL 131


                 .
gi 198442873 328 Q 328
Cdd:cd14519  132 Q 132
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 270-298 3.04e-03

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 39.87  E-value: 3.04e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 198442873 270 TEGAIAVHCKAGLGRTGTLIAC-YVMKHYR 298
Cdd:cd14614  178 SKGPMIIHCSAGVGRTGTFIALdRLLQHIR 207
DSP_STYXL1 cd14517
dual specificity phosphatase-like domain of serine/threonine/tyrosine interacting like 1; ...
 263-332 4.11e-03

dual specificity phosphatase-like domain of serine/threonine/tyrosine interacting like 1; Serine/threonine/tyrosine interacting like 1 (STYXL1), also known as DUSP24 and MK-STYX, is a catalytically inactive phosphatase with homology to the mitogen-activated protein kinase (MAPK) phosphatases (MKPs). STYXL1 plays a role in regulating pathways by competing with active phosphatases for binding to MAPKs. Similar to MKPs, STYXL1 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, however its C-terminal dual specificity phosphatase-like domain is a pseudophosphatase missing the catalytic cysteine.


Pssm-ID: 350367 [Multi-domain]  Cd Length: 155  Bit Score: 38.41  E-value: 4.11e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198442873 263 FLNICENTEGAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPGsiIGPQQHFLeeKQASLW 332
Cdd:cd14517   82 FIDKHKNNGSRVLVFSTLGISRSVAVAIAYLMYHYKWSLKDAWKYLLKCKNN--MRPNRGFV--KQLSEW 147
DSP_DUSP12 cd14520
dual specificity phosphatase domain of dual specificity protein phosphatase 12 and similar ...
 271-325 4.20e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 12 and similar proteins; Dual specificity protein phosphatase 12 (DUSP12), also called YVH1, functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP12 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It targets p38 MAPK to regulate macrophage response to bacterial infection. It also ameliorates cardiac hypertrophy in response to pressure overload through c-Jun N-terminal kinase (JNK) inhibition. DUSP12 has been identified as a modulator of cell cycle progression, a function independent of phosphatase activity and mediated by its C-terminal zinc-binding domain.


Pssm-ID: 350370 [Multi-domain]  Cd Length: 144  Bit Score: 38.00  E-value: 4.20e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 198442873 271 EGAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPGsiIGPQQHFLE 325
Cdd:cd14520   79 EGAVLVHCHAGVSRSAAVVTAYLMKTEQLSFEEALASLRECKPD--VKPNDGFLK 131
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 258-294 5.69e-03

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRH is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility.


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 38.72  E-value: 5.69e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 198442873 258 NIVRRFLNICENTeGAIAVHCKAGLGRTGTLIACYVM 294
Cdd:cd14619  154 RLLRQWLDQTMSG-GPTVVHCSAGVGRTGTLIALDVL 189
DSP_DUSP1 cd14638
dual specificity phosphatase domain of dual specificity protein phosphatase 1; Dual ...
 263-324 6.05e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 1; Dual specificity protein phosphatase 1 (DUSP1), also called mitogen-activated protein kinase (MAPK) phosphatase 1 (MKP-1), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class I subfamily and is a mitogen- and stress-inducible nuclear MKP. Human MKP-1 dephosphorylates MAPK1/ERK2, regulating its activity during the meiotic cell cycle. Although initially MKP-1 was considered to be ERK-specific, it has been shown that MKP-1 also dephosphorylates both JNK and p38 MAPKs. DUSP1/MKP-1 is involved in various functions, including proliferation, differentiation, and apoptosis in normal cells. It is a central regulator of a variety of functions in the immune, metabolic, cardiovascular, and nervous systems. It contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350486 [Multi-domain]  Cd Length: 151  Bit Score: 37.74  E-value: 6.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 198442873 263 FLNICENTEGAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRpgSIIGPQQHFL 324
Cdd:cd14638   70 FIDSVKNAGGRVFVHCQAGISRSATICLAYLMRTNRVKLDEAFEFVKQRR--SIISPNFSFM 129
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 269-289 7.77e-03

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 38.60  E-value: 7.77e-03
                         10        20
                 ....*....|....*....|.
gi 198442873 269 NTEGAIAVHCKAGLGRTGTLI 289
Cdd:cd14544  177 PHAGPIVVHCSAGIGRTGTFI 197
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 272-294 8.56e-03

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 38.10  E-value: 8.56e-03
                         10        20
                 ....*....|....*....|...
gi 198442873 272 GAIAVHCKAGLGRTGTLIACYVM 294
Cdd:cd14549  144 GPIVVHCSAGVGRTGTYIVIDSM 166
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 258-290 9.78e-03

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2.


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 38.26  E-value: 9.78e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 198442873 258 NIVRRFLNICEnTEGAIAVHCKAGLGRTGTLIA 290
Cdd:cd14615  152 HLVREYMKQNP-PNSPILVHCSAGVGRTGTFIA 183
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH