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Conserved domains on  [gi|163310753|ref|NP_001106192|]
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E3 ubiquitin-protein ligase UBR5 isoform 2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 2461-2789 4.17e-123

Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.


:

Pssm-ID: 214523  Cd Length: 328  Bit Score: 391.98  E-value: 4.17e-123
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753   2461 LDSSEKVQENRKRHGSSRSVVDMDLEDTddgddNAPLFYQPGKRGFY-TPRPGKNTEARLNCFRNIGRILGLCLLQNELC 2539
Cdd:smart00119   11 FEGEEGLDGGGVTREFFFLLSKELFNPD-----YGLFRYSPNDYLLYpNPRSGFANEEHLSYFRFIGRVLGKALYDNRLL 85

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753   2540 PITLNRHVIKVLLGRKVNWHDFAFFDPVMYESLRQLILASQSSDAdavfsaMDLAFAIDLCKEEGGG-QVELIPNGVNIP 2618
Cdd:smart00119   86 DLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEE------LDLTFSIVLTSEFGQVkVVELKPGGSNIP 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753   2619 VTPQNVYEYVRKYAEHRMLVVAEQPLHAMRKGLLDVLPKNSLEDLTAEDFRLLVNGCGEVNVQMLISFTSFNDESGENAE 2698
Cdd:smart00119  160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753   2699 KLlqfkRWFWSIVEKMSMTERQDLVYFWTSSPSLPAseEGFQPM-PSITIRP--PDDQHLPTANTCISRLYVPLYSSKQI 2775
Cdd:smart00119  240 TI----KWFWEVVESFTNEERRKLLQFVTGSSRLPV--GGFAALsPKFTIRKagSDDERLPTAHTCFNRLKLPPYSSKEI 313

                           330
                    ....*....|....*
gi 163310753   2776 LKQKLLLAIK-TKNF 2789
Cdd:smart00119  314 LREKLLLAINeGKGF 328
UBR-box_UBR5 cd19675
UBR-box found in HECT-type E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5 (EC 2.3. ...
 1165-1240 5.97e-58

UBR-box found in HECT-type E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5 (EC 2.3.2.26; also called E3 ubiquitin-protein ligase, HECT domain-containing 1, E3 ligase identified by differential display (EDD), hyperplastic discs protein homolog (HYD), progestin-induced protein, or N-recognin-5) is a HECT (homologous to E6-AP C-terminus)-type E3 ubiquitin-protein ligase that acts as a key regulator of the ubiquitin proteasome system in both cancer and developmental biology. It is required for Wnt signal responses in Drosophila and human cell lines downstream of activated Armadillo/beta-catenin. It also plays a key role in ciliogenesis by regulating centriolar satellite stability and primary cilia.


:

Pssm-ID: 439073  Cd Length: 76  Bit Score: 194.61  E-value: 5.97e-58
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 163310753 1165 YVLCCNDTCSFTWTGAEHINQDIFECRTCGLLESLCCCTECARVCHKGHDCKLKRTSPTAYCDCWEKCKCKTLIAG 1240
Cdd:cd19675     1 YVLCCNDTCSFTWTGAEHINQDIFECRTCGLVGSLCCCTECARVCHKGHDCKLKRTSPTAYCDCWEKCKCKALIAG 76
PolyA smart00517
C-terminal domain of Poly(A)-binding protein. Present also in Drosophila hyperplastics discs ...
 2383-2446 4.66e-26

C-terminal domain of Poly(A)-binding protein. Present also in Drosophila hyperplastics discs protein; Involved in homodimerisation (either directly or indirectly)


:

Pssm-ID: 197769 [Multi-domain]  Cd Length: 64  Bit Score: 103.13  E-value: 4.66e-26
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 163310753   2383 PLPAHRQALGERLYPRVQAMQPAFASKITGMLLELSPAQLLLLLASEDSLRARVDEAMELIIAH 2446
Cdd:smart00517    1 PPQEQKQALGERLYPKVQALEPELAGKITGMLLEMDNSELLHLLESPELLRAKVDEALEVLKSH 64
CUE_UBR5 cd14423
CUE domain found in E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5, also called ...
 184-230 4.68e-25

CUE domain found in E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5, also called E3 ubiquitin-protein ligase, HECT domain-containing 1, hyperplastic discs protein homolog (HYD), progestin-induced protein, EDD, or Rat100, belongs to the E3 protein family of HECT (homologous to E6-AP C-terminus) ligases. It is frequently overexpressed in breast and ovarian cancer, suggesting a role in cancer development. UBR5 is involved in DNA-damage signaling. It can ubiquitinate DNA topoisomerase II-binding protein 1 (TopBP1) in the presence of the E2 enzyme UBCH4. It also activates the DNA-damage checkpoint kinase CHK2. Moreover, UBR5 interacts with the calcium and integrin-binding protein (CIB) in a DNA-damage-dependent manner. It functions as the substrate of the extracellular signal-regulated kinases (ERKs) 1 and 2. It also acts as a ubiquitin ligase that controls the levels of poly(A)-binding protein-interacting protein 2. In addition, UBR5 ubiquitinates and up-regulates beta-catenin, regulates transcription, and activates smooth-muscle differentiation through its ability to stabilize myocardin. UBR5 contains an N-terminal CUE domain, a zinc-finger-like domain termed the ubiquitin-recognin (UBR) box, a MLLE (mademoiselle) domain, and a C-terminal catalytic HECT domain.


:

Pssm-ID: 270606  Cd Length: 47  Bit Score: 99.85  E-value: 4.68e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 163310753  184 VIPEELISQAQVVLQGKSRSVIIRELQRTNLDVNLAVNNLLSRDDED 230
Cdd:cd14423     1 VVPEELISQAQVVLQGKSRSVIIRELQRTNLDVNLAVNNLLSRDDED 47
 
Name Accession Description Interval E-value
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 2461-2789 4.17e-123

Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.


Pssm-ID: 214523  Cd Length: 328  Bit Score: 391.98  E-value: 4.17e-123
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753   2461 LDSSEKVQENRKRHGSSRSVVDMDLEDTddgddNAPLFYQPGKRGFY-TPRPGKNTEARLNCFRNIGRILGLCLLQNELC 2539
Cdd:smart00119   11 FEGEEGLDGGGVTREFFFLLSKELFNPD-----YGLFRYSPNDYLLYpNPRSGFANEEHLSYFRFIGRVLGKALYDNRLL 85

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753   2540 PITLNRHVIKVLLGRKVNWHDFAFFDPVMYESLRQLILASQSSDAdavfsaMDLAFAIDLCKEEGGG-QVELIPNGVNIP 2618
Cdd:smart00119   86 DLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEE------LDLTFSIVLTSEFGQVkVVELKPGGSNIP 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753   2619 VTPQNVYEYVRKYAEHRMLVVAEQPLHAMRKGLLDVLPKNSLEDLTAEDFRLLVNGCGEVNVQMLISFTSFNDESGENAE 2698
Cdd:smart00119  160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753   2699 KLlqfkRWFWSIVEKMSMTERQDLVYFWTSSPSLPAseEGFQPM-PSITIRP--PDDQHLPTANTCISRLYVPLYSSKQI 2775
Cdd:smart00119  240 TI----KWFWEVVESFTNEERRKLLQFVTGSSRLPV--GGFAALsPKFTIRKagSDDERLPTAHTCFNRLKLPPYSSKEI 313

                           330
                    ....*....|....*
gi 163310753   2776 LKQKLLLAIK-TKNF 2789
Cdd:smart00119  314 LREKLLLAINeGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 2494-2792 1.40e-86

HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.


Pssm-ID: 459880  Cd Length: 304  Bit Score: 286.04  E-value: 1.40e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753  2494 NAPLF-YQPGKRGFYTPRPGKNTEA---RLNCFRNIGRILGLCLLQNELCPITLNRHVIKVLLGRKVNWHDFAFFDPVMY 2569
Cdd:pfam00632   11 NYGLFeYETEDDRTYWFNPSSSESPdleLLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLEDLESIDPELY 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753  2570 ESLRQLILASQSSDADavfsaMDLAFAIDLCKEEGGgqVELIPNGVNIPVTPQNVYEYVRKYAEHRMLVVAEQPLHAMRK 2649
Cdd:pfam00632   91 KSLKSLLNMDNDDDED-----LGLTFTIPVFGESKT--IELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRK 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753  2650 GLLDVLPKNSLEDLTAEDFRLLVNGCGEVNVQMLISFTSFNDESGENAekllQFKRWFWSIVEKMSMTERQDLVYFWTSS 2729
Cdd:pfam00632  164 GFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNS----PTIQWFWEILEEFSPEQRRLFLKFVTGS 239

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 163310753  2730 PSLPASeeGFQPMPSITIRP---PDDQHLPTANTCISRLYVPLYSSKQILKQKLLLAIK-TKNFGFV 2792
Cdd:pfam00632  240 SRLPVG--GFKSLPKFTIVRkggDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEeGEGFGLS 304
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 2496-2790 3.49e-81

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 272.52  E-value: 3.49e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753 2496 PLFYQP--GKRGFYTPRPGKNTEARLNCFRNIGRILGLCLLQNELCPITLNRHVIKVLLGRKVNWHDFAFFDPVMYESLR 2573
Cdd:cd00078    63 GLFRYTpdDSGLLYPNPSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLK 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753 2574 QLIlasqssDADAVFSAMDLAFAIDL-CKEEGGGQVELIPNGVNIPVTPQNVYEYVRKYAEHRMLVVAEQPLHAMRKGLL 2652
Cdd:cd00078   143 ELL------DNDGDEDDLELTFTIELdSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFS 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753 2653 DVLPKNSLEDLTAEDFRLLVNGCGEVNVQMLISFTSFNDESGENAekllQFKRWFWSIVEKMSMTERQDLVYFWTSSPSL 2732
Cdd:cd00078   217 EVIPEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGYSSDS----PTIQWFWEVLESFTNEERKKFLQFVTGSSRL 292

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 163310753 2733 PAseEGFQPM-PSITIRPPD--DQHLPTANTCISRLYVPLYSSKQILKQKLLLAIK-TKNFG 2790
Cdd:cd00078   293 PV--GGFADLnPKFTIRRVGspDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINeGAGFG 352
UBR-box_UBR5 cd19675
UBR-box found in HECT-type E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5 (EC 2.3. ...
 1165-1240 5.97e-58

UBR-box found in HECT-type E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5 (EC 2.3.2.26; also called E3 ubiquitin-protein ligase, HECT domain-containing 1, E3 ligase identified by differential display (EDD), hyperplastic discs protein homolog (HYD), progestin-induced protein, or N-recognin-5) is a HECT (homologous to E6-AP C-terminus)-type E3 ubiquitin-protein ligase that acts as a key regulator of the ubiquitin proteasome system in both cancer and developmental biology. It is required for Wnt signal responses in Drosophila and human cell lines downstream of activated Armadillo/beta-catenin. It also plays a key role in ciliogenesis by regulating centriolar satellite stability and primary cilia.


Pssm-ID: 439073  Cd Length: 76  Bit Score: 194.61  E-value: 5.97e-58
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 163310753 1165 YVLCCNDTCSFTWTGAEHINQDIFECRTCGLLESLCCCTECARVCHKGHDCKLKRTSPTAYCDCWEKCKCKTLIAG 1240
Cdd:cd19675     1 YVLCCNDTCSFTWTGAEHINQDIFECRTCGLVGSLCCCTECARVCHKGHDCKLKRTSPTAYCDCWEKCKCKALIAG 76
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
2502-2791 2.39e-41

Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 166.87  E-value: 2.39e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753 2502 GKRGFYTPRPGKNTEARLNCFRNIGRILGLCLLQNELCPITLNRHVIKVLLGRKVNWHDFAFFDPVMYESLRQLIlasqs 2581
Cdd:COG5021   585 DLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLL----- 659

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753 2582 sDADAVFSAMDLAFAIDLCKEEGGGQVELIPNGVNIPVTPQNVYEYVRKYAEHRMLVVAEQPLHAMRKGLLDVLPKNSLE 2661
Cdd:COG5021   660 -NNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQ 738

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753 2662 DLTAEDFRLLVngCGEVNVQMLISFTSFNDESGENAE-KLLQfkrWFWSIVEKMSMTERQDLVYFWTSSPSLPASeeGFQ 2740
Cdd:COG5021   739 IFDESELELLI--GGIPEDIDIDDWKSNTAYHGYTEDsPIIV---WFWEIISEFDFEERAKLLQFVTGTSRIPIN--GFK 811

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753 2741 PMP------SITIRPP--DDQHLPTANTCISRLYVPLYSSKQILKQKLLLAI-KTKNFGF 2791
Cdd:COG5021   812 DLQgsdgvrKFTIEKGgtDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAInEGAGFGL 871
PolyA smart00517
C-terminal domain of Poly(A)-binding protein. Present also in Drosophila hyperplastics discs ...
 2383-2446 4.66e-26

C-terminal domain of Poly(A)-binding protein. Present also in Drosophila hyperplastics discs protein; Involved in homodimerisation (either directly or indirectly)


Pssm-ID: 197769 [Multi-domain]  Cd Length: 64  Bit Score: 103.13  E-value: 4.66e-26
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 163310753   2383 PLPAHRQALGERLYPRVQAMQPAFASKITGMLLELSPAQLLLLLASEDSLRARVDEAMELIIAH 2446
Cdd:smart00517    1 PPQEQKQALGERLYPKVQALEPELAGKITGMLLEMDNSELLHLLESPELLRAKVDEALEVLKSH 64
CUE_UBR5 cd14423
CUE domain found in E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5, also called ...
 184-230 4.68e-25

CUE domain found in E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5, also called E3 ubiquitin-protein ligase, HECT domain-containing 1, hyperplastic discs protein homolog (HYD), progestin-induced protein, EDD, or Rat100, belongs to the E3 protein family of HECT (homologous to E6-AP C-terminus) ligases. It is frequently overexpressed in breast and ovarian cancer, suggesting a role in cancer development. UBR5 is involved in DNA-damage signaling. It can ubiquitinate DNA topoisomerase II-binding protein 1 (TopBP1) in the presence of the E2 enzyme UBCH4. It also activates the DNA-damage checkpoint kinase CHK2. Moreover, UBR5 interacts with the calcium and integrin-binding protein (CIB) in a DNA-damage-dependent manner. It functions as the substrate of the extracellular signal-regulated kinases (ERKs) 1 and 2. It also acts as a ubiquitin ligase that controls the levels of poly(A)-binding protein-interacting protein 2. In addition, UBR5 ubiquitinates and up-regulates beta-catenin, regulates transcription, and activates smooth-muscle differentiation through its ability to stabilize myocardin. UBR5 contains an N-terminal CUE domain, a zinc-finger-like domain termed the ubiquitin-recognin (UBR) box, a MLLE (mademoiselle) domain, and a C-terminal catalytic HECT domain.


Pssm-ID: 270606  Cd Length: 47  Bit Score: 99.85  E-value: 4.68e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 163310753  184 VIPEELISQAQVVLQGKSRSVIIRELQRTNLDVNLAVNNLLSRDDED 230
Cdd:cd14423     1 VVPEELISQAQVVLQGKSRSVIIRELQRTNLDVNLAVNNLLSRDDED 47
ZnF_UBR1 smart00396
Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain ...
 1171-1238 2.34e-23

Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain is involved in recognition of N-end rule substrates in yeast Ubr1p


Pssm-ID: 197698  Cd Length: 71  Bit Score: 95.59  E-value: 2.34e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 163310753   1171 DTCSFTWTGAEHInqdiFECRTCGLLESLCCCTECAR-VCHKGHDCKLKRTSPTAYCDCWEK------CKCKTLI 1238
Cdd:smart00396    1 DVCGYKFTGGEVI----YRCKTCGLDPTCVLCSDCFRpSCHKGHDVSLKTSRGSGICDCGDKeawnedLKCKAHE 71
E3_UbLigase_EDD pfam11547
E3 ubiquitin ligase EDD; EDD, the ER ubiquitin ligase from the HECT ligases, contains an ...
 179-226 5.17e-22

E3 ubiquitin ligase EDD; EDD, the ER ubiquitin ligase from the HECT ligases, contains an N-terminal ubiquitin-associated domain which binds ubiquitin. Ubiquitin is recognized by helices alpha-1 and -3 in in the UBA domain. EDD is involved in DNA damage repair pathways and binds to mono-ubiquitinated proteins.


Pssm-ID: 431928  Cd Length: 52  Bit Score: 91.07  E-value: 5.17e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 163310753   179 VIPASVIPEELISQAQVVLQGKSRSVIIRELQRTNLDVNLAVNNLLSR 226
Cdd:pfam11547    1 VVPAALVPEELIEQVQGVLQGKSRQVIIRELQRTNLDVNLAVNNLLSR 48
PABP pfam00658
Poly-adenylate binding protein, unique domain; The region featured in this family is found ...
 2383-2443 4.43e-21

Poly-adenylate binding protein, unique domain; The region featured in this family is found towards the C-terminus of poly(A)-binding proteins (PABPs). These are eukaryotic proteins that, through their binding of the 3' poly(A) tail on mRNA, have very important roles in the pathways of gene expression. They seem to provide a scaffold on which other proteins can bind and mediate processes such as export, translation and turnover of the transcripts. Moreover, they may act as antagonists to the binding of factors that allow mRNA degradation, regulating mRNA longevity. PABPs are also involved in nuclear transport. PABPs interact with poly(A) tails via RNA-recognition motifs (pfam00076). Note that the PABP C-terminal region is also found in members of the hyperplastic discs protein (HYD) family of ubiquitin ligases that contain HECT domains - these are also included in this family.


Pssm-ID: 459893 [Multi-domain]  Cd Length: 66  Bit Score: 89.07  E-value: 4.43e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 163310753  2383 PLPAHRQALGERLYPRVQAMQPAFASKITGMLLELSPAQLLLLLASEDSLRARVDEAMELI 2443
Cdd:pfam00658    6 SPEQQKQMLGERLYPLVQAIQPELAGKITGMLLEMDNSELLHLLEDPEALKEKVDEALEVL 66
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 2368-2443 1.11e-12

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 73.69  E-value: 1.11e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753  2368 PFRPASEGNPSDDPDPLPA-----------------------HRQALGERLYPRVQAMQPAFASKITGMLLELSPAQLLL 2424
Cdd:TIGR01628  463 MYPPNYQSLPLSQDLPQPQstasqggqnkklaqvlasatpqmQKQVLGERLFPLVEAIEPALAAKITGMLLEMDNSELLH 542

                           90
                   ....*....|....*....
gi 163310753  2425 LLASEDSLRARVDEAMELI 2443
Cdd:TIGR01628  543 LLESPELLKSKVDEALEVL 561
zf-UBR pfam02207
Putative zinc finger in N-recognin (UBR box); This region is found in E3 ubiquitin ligases ...
 1173-1235 7.36e-11

Putative zinc finger in N-recognin (UBR box); This region is found in E3 ubiquitin ligases that recognize N-recognins.


Pssm-ID: 460491  Cd Length: 68  Bit Score: 60.00  E-value: 7.36e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753  1173 CSFTWTgaehINQDIFECRTCGLLESLCCCTECARVC-HKGHDCKLKRTSPTAYCDC-----W-EKCKCK 1235
Cdd:pfam02207    1 CGYVFK----KGQPVYRCLTCSLDPTCVICYSCFINCdHEGHDYELFTSRGGGCCDCgdpeaWkEEGFCK 66
 
Name Accession Description Interval E-value
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 2461-2789 4.17e-123

Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.


Pssm-ID: 214523  Cd Length: 328  Bit Score: 391.98  E-value: 4.17e-123
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753   2461 LDSSEKVQENRKRHGSSRSVVDMDLEDTddgddNAPLFYQPGKRGFY-TPRPGKNTEARLNCFRNIGRILGLCLLQNELC 2539
Cdd:smart00119   11 FEGEEGLDGGGVTREFFFLLSKELFNPD-----YGLFRYSPNDYLLYpNPRSGFANEEHLSYFRFIGRVLGKALYDNRLL 85

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753   2540 PITLNRHVIKVLLGRKVNWHDFAFFDPVMYESLRQLILASQSSDAdavfsaMDLAFAIDLCKEEGGG-QVELIPNGVNIP 2618
Cdd:smart00119   86 DLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLLLNNDTSEE------LDLTFSIVLTSEFGQVkVVELKPGGSNIP 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753   2619 VTPQNVYEYVRKYAEHRMLVVAEQPLHAMRKGLLDVLPKNSLEDLTAEDFRLLVNGCGEVNVQMLISFTSFNDESGENAE 2698
Cdd:smart00119  160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQ 239

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753   2699 KLlqfkRWFWSIVEKMSMTERQDLVYFWTSSPSLPAseEGFQPM-PSITIRP--PDDQHLPTANTCISRLYVPLYSSKQI 2775
Cdd:smart00119  240 TI----KWFWEVVESFTNEERRKLLQFVTGSSRLPV--GGFAALsPKFTIRKagSDDERLPTAHTCFNRLKLPPYSSKEI 313

                           330
                    ....*....|....*
gi 163310753   2776 LKQKLLLAIK-TKNF 2789
Cdd:smart00119  314 LREKLLLAINeGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 2494-2792 1.40e-86

HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.


Pssm-ID: 459880  Cd Length: 304  Bit Score: 286.04  E-value: 1.40e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753  2494 NAPLF-YQPGKRGFYTPRPGKNTEA---RLNCFRNIGRILGLCLLQNELCPITLNRHVIKVLLGRKVNWHDFAFFDPVMY 2569
Cdd:pfam00632   11 NYGLFeYETEDDRTYWFNPSSSESPdleLLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLEDLESIDPELY 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753  2570 ESLRQLILASQSSDADavfsaMDLAFAIDLCKEEGGgqVELIPNGVNIPVTPQNVYEYVRKYAEHRMLVVAEQPLHAMRK 2649
Cdd:pfam00632   91 KSLKSLLNMDNDDDED-----LGLTFTIPVFGESKT--IELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRK 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753  2650 GLLDVLPKNSLEDLTAEDFRLLVNGCGEVNVQMLISFTSFNDESGENAekllQFKRWFWSIVEKMSMTERQDLVYFWTSS 2729
Cdd:pfam00632  164 GFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNS----PTIQWFWEILEEFSPEQRRLFLKFVTGS 239

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 163310753  2730 PSLPASeeGFQPMPSITIRP---PDDQHLPTANTCISRLYVPLYSSKQILKQKLLLAIK-TKNFGFV 2792
Cdd:pfam00632  240 SRLPVG--GFKSLPKFTIVRkggDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEeGEGFGLS 304
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 2496-2790 3.49e-81

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 272.52  E-value: 3.49e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753 2496 PLFYQP--GKRGFYTPRPGKNTEARLNCFRNIGRILGLCLLQNELCPITLNRHVIKVLLGRKVNWHDFAFFDPVMYESLR 2573
Cdd:cd00078    63 GLFRYTpdDSGLLYPNPSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLK 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753 2574 QLIlasqssDADAVFSAMDLAFAIDL-CKEEGGGQVELIPNGVNIPVTPQNVYEYVRKYAEHRMLVVAEQPLHAMRKGLL 2652
Cdd:cd00078   143 ELL------DNDGDEDDLELTFTIELdSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFS 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753 2653 DVLPKNSLEDLTAEDFRLLVNGCGEVNVQMLISFTSFNDESGENAekllQFKRWFWSIVEKMSMTERQDLVYFWTSSPSL 2732
Cdd:cd00078   217 EVIPEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGYSSDS----PTIQWFWEVLESFTNEERKKFLQFVTGSSRL 292

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 163310753 2733 PAseEGFQPM-PSITIRPPD--DQHLPTANTCISRLYVPLYSSKQILKQKLLLAIK-TKNFG 2790
Cdd:cd00078   293 PV--GGFADLnPKFTIRRVGspDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINeGAGFG 352
UBR-box_UBR5 cd19675
UBR-box found in HECT-type E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5 (EC 2.3. ...
 1165-1240 5.97e-58

UBR-box found in HECT-type E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5 (EC 2.3.2.26; also called E3 ubiquitin-protein ligase, HECT domain-containing 1, E3 ligase identified by differential display (EDD), hyperplastic discs protein homolog (HYD), progestin-induced protein, or N-recognin-5) is a HECT (homologous to E6-AP C-terminus)-type E3 ubiquitin-protein ligase that acts as a key regulator of the ubiquitin proteasome system in both cancer and developmental biology. It is required for Wnt signal responses in Drosophila and human cell lines downstream of activated Armadillo/beta-catenin. It also plays a key role in ciliogenesis by regulating centriolar satellite stability and primary cilia.


Pssm-ID: 439073  Cd Length: 76  Bit Score: 194.61  E-value: 5.97e-58
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 163310753 1165 YVLCCNDTCSFTWTGAEHINQDIFECRTCGLLESLCCCTECARVCHKGHDCKLKRTSPTAYCDCWEKCKCKTLIAG 1240
Cdd:cd19675     1 YVLCCNDTCSFTWTGAEHINQDIFECRTCGLVGSLCCCTECARVCHKGHDCKLKRTSPTAYCDCWEKCKCKALIAG 76
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
2502-2791 2.39e-41

Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 166.87  E-value: 2.39e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753 2502 GKRGFYTPRPGKNTEARLNCFRNIGRILGLCLLQNELCPITLNRHVIKVLLGRKVNWHDFAFFDPVMYESLRQLIlasqs 2581
Cdd:COG5021   585 DLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLL----- 659

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753 2582 sDADAVFSAMDLAFAIDLCKEEGGGQVELIPNGVNIPVTPQNVYEYVRKYAEHRMLVVAEQPLHAMRKGLLDVLPKNSLE 2661
Cdd:COG5021   660 -NNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQ 738

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753 2662 DLTAEDFRLLVngCGEVNVQMLISFTSFNDESGENAE-KLLQfkrWFWSIVEKMSMTERQDLVYFWTSSPSLPASeeGFQ 2740
Cdd:COG5021   739 IFDESELELLI--GGIPEDIDIDDWKSNTAYHGYTEDsPIIV---WFWEIISEFDFEERAKLLQFVTGTSRIPIN--GFK 811

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753 2741 PMP------SITIRPP--DDQHLPTANTCISRLYVPLYSSKQILKQKLLLAI-KTKNFGF 2791
Cdd:COG5021   812 DLQgsdgvrKFTIEKGgtDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAInEGAGFGL 871
PolyA smart00517
C-terminal domain of Poly(A)-binding protein. Present also in Drosophila hyperplastics discs ...
 2383-2446 4.66e-26

C-terminal domain of Poly(A)-binding protein. Present also in Drosophila hyperplastics discs protein; Involved in homodimerisation (either directly or indirectly)


Pssm-ID: 197769 [Multi-domain]  Cd Length: 64  Bit Score: 103.13  E-value: 4.66e-26
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 163310753   2383 PLPAHRQALGERLYPRVQAMQPAFASKITGMLLELSPAQLLLLLASEDSLRARVDEAMELIIAH 2446
Cdd:smart00517    1 PPQEQKQALGERLYPKVQALEPELAGKITGMLLEMDNSELLHLLESPELLRAKVDEALEVLKSH 64
UBR-box_UBR4_5_6_7 cd19671
UBR-box found in UBR4, UBR5, UBR6/FBOX11, UBR7 and similar proteins; This family includes UBR4 ...
 1173-1235 1.79e-25

UBR-box found in UBR4, UBR5, UBR6/FBOX11, UBR7 and similar proteins; This family includes UBR4 (EC 2.3.2.27), UBR5 (EC 2.3.2.26), UBR6/FBOX11 and UBR7 (EC 2.3.2.27). Both UBR4 (also called 600 kDa retinoblastoma protein-associated factor, or N-recognin-4, or retinoblastoma-associated factor of 600 kDa, or RBAF600, or p600, or zinc finger UBR1-type protein 1) and UBR7 (also called N-recognin-7) are RING-type E3 ubiquitin ligases of the Arg/N-end rule degradation pathway. They recognize and bind to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. UBR5 (also called E3 ubiquitin-protein ligase, HECT domain-containing 1, E3 ligase identified by differential display (EDD), hyperplastic discs protein homolog (HYD), progestin-induced protein, or N-recognin-5) is a HECT (homologous to E6-AP C-terminus)-type E3 ubiquitin-protein ligase that acts as a key regulator of the ubiquitin proteasome system in both cancer and developmental biology. It is required for Wnt signal responses in Drosophila and human cell lines downstream of activated Armadillo/beta-catenin. It also plays a key role in ciliogenesis by regulating centriolar satellite stability and primary cilia. UBR6 (also called FBOX11, protein arginine N-methyltransferase 9 (PRMT9), or vitiligo-associated protein 1 (VIT-1)), is an E3 ubiquitin ligase and a type II methyltransferase, which functions as a key regulator of tumor initiation and progression. UBR6 is a substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. UBR6 does not bind N-terminal signals.


Pssm-ID: 439069  Cd Length: 67  Bit Score: 101.38  E-value: 1.79e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 163310753 1173 CSFTWTGAEHINQDIFECRTCGLLESLCCCTECARVCHKGHDCKLKRTSpTAYCDCW----EKCKCK 1235
Cdd:cd19671     1 CTFEKTGRKYIKQPWYHCYTCGLIDGLGVCEACARKCHKGHDLVYIGYS-NFYCDCGssgpGKCKCE 66
CUE_UBR5 cd14423
CUE domain found in E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5, also called ...
 184-230 4.68e-25

CUE domain found in E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5, also called E3 ubiquitin-protein ligase, HECT domain-containing 1, hyperplastic discs protein homolog (HYD), progestin-induced protein, EDD, or Rat100, belongs to the E3 protein family of HECT (homologous to E6-AP C-terminus) ligases. It is frequently overexpressed in breast and ovarian cancer, suggesting a role in cancer development. UBR5 is involved in DNA-damage signaling. It can ubiquitinate DNA topoisomerase II-binding protein 1 (TopBP1) in the presence of the E2 enzyme UBCH4. It also activates the DNA-damage checkpoint kinase CHK2. Moreover, UBR5 interacts with the calcium and integrin-binding protein (CIB) in a DNA-damage-dependent manner. It functions as the substrate of the extracellular signal-regulated kinases (ERKs) 1 and 2. It also acts as a ubiquitin ligase that controls the levels of poly(A)-binding protein-interacting protein 2. In addition, UBR5 ubiquitinates and up-regulates beta-catenin, regulates transcription, and activates smooth-muscle differentiation through its ability to stabilize myocardin. UBR5 contains an N-terminal CUE domain, a zinc-finger-like domain termed the ubiquitin-recognin (UBR) box, a MLLE (mademoiselle) domain, and a C-terminal catalytic HECT domain.


Pssm-ID: 270606  Cd Length: 47  Bit Score: 99.85  E-value: 4.68e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 163310753  184 VIPEELISQAQVVLQGKSRSVIIRELQRTNLDVNLAVNNLLSRDDED 230
Cdd:cd14423     1 VVPEELISQAQVVLQGKSRSVIIRELQRTNLDVNLAVNNLLSRDDED 47
ZnF_UBR1 smart00396
Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain ...
 1171-1238 2.34e-23

Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain is involved in recognition of N-end rule substrates in yeast Ubr1p


Pssm-ID: 197698  Cd Length: 71  Bit Score: 95.59  E-value: 2.34e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 163310753   1171 DTCSFTWTGAEHInqdiFECRTCGLLESLCCCTECAR-VCHKGHDCKLKRTSPTAYCDCWEK------CKCKTLI 1238
Cdd:smart00396    1 DVCGYKFTGGEVI----YRCKTCGLDPTCVLCSDCFRpSCHKGHDVSLKTSRGSGICDCGDKeawnedLKCKAHE 71
E3_UbLigase_EDD pfam11547
E3 ubiquitin ligase EDD; EDD, the ER ubiquitin ligase from the HECT ligases, contains an ...
 179-226 5.17e-22

E3 ubiquitin ligase EDD; EDD, the ER ubiquitin ligase from the HECT ligases, contains an N-terminal ubiquitin-associated domain which binds ubiquitin. Ubiquitin is recognized by helices alpha-1 and -3 in in the UBA domain. EDD is involved in DNA damage repair pathways and binds to mono-ubiquitinated proteins.


Pssm-ID: 431928  Cd Length: 52  Bit Score: 91.07  E-value: 5.17e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 163310753   179 VIPASVIPEELISQAQVVLQGKSRSVIIRELQRTNLDVNLAVNNLLSR 226
Cdd:pfam11547    1 VVPAALVPEELIEQVQGVLQGKSRQVIIRELQRTNLDVNLAVNNLLSR 48
PABP pfam00658
Poly-adenylate binding protein, unique domain; The region featured in this family is found ...
 2383-2443 4.43e-21

Poly-adenylate binding protein, unique domain; The region featured in this family is found towards the C-terminus of poly(A)-binding proteins (PABPs). These are eukaryotic proteins that, through their binding of the 3' poly(A) tail on mRNA, have very important roles in the pathways of gene expression. They seem to provide a scaffold on which other proteins can bind and mediate processes such as export, translation and turnover of the transcripts. Moreover, they may act as antagonists to the binding of factors that allow mRNA degradation, regulating mRNA longevity. PABPs are also involved in nuclear transport. PABPs interact with poly(A) tails via RNA-recognition motifs (pfam00076). Note that the PABP C-terminal region is also found in members of the hyperplastic discs protein (HYD) family of ubiquitin ligases that contain HECT domains - these are also included in this family.


Pssm-ID: 459893 [Multi-domain]  Cd Length: 66  Bit Score: 89.07  E-value: 4.43e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 163310753  2383 PLPAHRQALGERLYPRVQAMQPAFASKITGMLLELSPAQLLLLLASEDSLRARVDEAMELI 2443
Cdd:pfam00658    6 SPEQQKQMLGERLYPLVQAIQPELAGKITGMLLEMDNSELLHLLEDPEALKEKVDEALEVL 66
UBR-box cd19669
UBR-box found in UBR family of E3 ubiquitin ligases (UBR1-7) and similar proteins; The UBR-box ...
 1173-1235 1.72e-19

UBR-box found in UBR family of E3 ubiquitin ligases (UBR1-7) and similar proteins; The UBR-box is a 70-residue zinc finger domain present in the UBR family of E3 ubiquitin ligases (UBR1-7, also called N-recognins) that directly binds N-terminal degradation signals (N-degrons) in substrate proteins to facilitate substrate ubiquitination and proteasomal degradation via the ubiquitin-proteasome system (UPS). UBR1 and UBR2 bind all type-1 and type-2 N-degrons. They mediate ubiquitination and proteolysis of short-lived regulators and misfolded proteins. UBR4 binds both type-1 and type-2 N-degrons and is involved in proteome-wide turnover of cell surface proteins. UBR5 preferentially binds type-1 N-degrons and mediates ubiquitination of short-lived proteins. UBR3, UBR6 (also called FBXO11), and UBR7 may not bind efficiently to N-degrons. UBR3 is a RING-type E3 ubiquitin ligase with a function in olfactory and other sensory systems. UBR6 is an E3 ubiquitin ligase and a type II methyltransferase, which functions as a key regulator of tumor initiation and progression. It does not bind N-terminal signals. UBR7 is a RING-type E3 ubiquitin ligase that may play an important role in spermiogenesis and fertilization.


Pssm-ID: 439067  Cd Length: 66  Bit Score: 84.49  E-value: 1.72e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 163310753 1173 CSFTWTGaehINQDIFECRTCGLLESLCCCTECARVCHKGHDCKLKRTSpTAYCDCW----EKCKCK 1235
Cdd:cd19669     1 CTFSITG---INQVMYHCLTCSLDDNSGICEECAKKCHEGHDVVYIGSG-SGFCDCGdssaKSGFCK 63
UBR-box_UBR4_like cd19674
UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins; UBR4 (EC 2.3. ...
 1172-1234 7.74e-19

UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins; UBR4 (EC 2.3.2.27; also called 600 kDa retinoblastoma protein-associated factor, N-recognin-4, retinoblastoma-associated factor of 600 kDa, RBAF600, p600, or zinc finger UBR1-type protein 1) is a RING-type E3 ubiquitin ligase of the Arg/N-end rule degradation pathway. It recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. UBR4 acts as a multifunctional protein with roles in anoikis, viral transformation, and protein degradation, as well as in neurogenesis, neuronal migration, neuronal signaling, and survival. The family also includes Arabidopsis thaliana auxin transport protein BIG (also called protein attenuated shade avoidance 1, protein corymbosa1, protein dark over-expression of cab 1, protein low phosphate-resistant root 1, protein transport inhibitor response 3, or protein umbrella 1). It is a calossin-like protein required for auxin efflux and polar auxin transport (PAT) influencing auxin-mediated developmental responses in Arabidopsis.


Pssm-ID: 439072  Cd Length: 72  Bit Score: 82.78  E-value: 7.74e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 163310753 1172 TCSFTWTGAEHINQDIFECRTCGLLESLCCCTECARVCHKGHDCKLKRTSPtAYCDC-----WEKCKC 1234
Cdd:cd19674     2 VCTFASTGKNYARQHWYECYTCFLNGNEGVCEVCARVCHKGHDLVYSKTSS-FFCDCgagggPSKCKS 68
UBR-box_BIG_like cd19681
UBR-box found in Arabidopsis thaliana auxin transport protein BIG and similar proteins; BIG ...
 1173-1228 4.67e-13

UBR-box found in Arabidopsis thaliana auxin transport protein BIG and similar proteins; BIG (also called protein attenuated shade avoidance 1, protein corymbosa1, protein dark over-expression of cab 1, protein low phosphate-resistant root 1, protein transport inhibitor response 3, or protein umbrella 1) is a calossin-like protein required for auxin efflux and polar auxin transport (PAT) influencing auxin-mediated developmental responses in Arabidopsis.


Pssm-ID: 439079  Cd Length: 74  Bit Score: 66.28  E-value: 4.67e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 163310753 1173 CSFTWTGAEHINQDIFECRTCGLLESLCCCTECARVCHKGHDCKLKRTSpTAYCDC 1228
Cdd:cd19681     3 CTYVSSGSNFMEQHWYFCYTCGLVDSKGCCSVCAKVCHRGHDVVYSRYS-RFFCDC 57
UBR-box_UBR4 cd19680
UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins; UBR4 (EC 2.3. ...
 1173-1238 6.69e-13

UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins; UBR4 (EC 2.3.2.27; also called 600 kDa retinoblastoma protein-associated factor, N-recognin-4, retinoblastoma-associated factor of 600 kDa, RBAF600, p600, or zinc finger UBR1-type protein 1) is a RING-type E3 ubiquitin ligase of the Arg/N-end rule degradation pathway. It recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. UBR4 acts as a multifunctional protein with roles in anoikis, viral transformation, and protein degradation, as well as in neurogenesis, neuronal migration, neuronal signaling, and survival.


Pssm-ID: 439078  Cd Length: 71  Bit Score: 65.94  E-value: 6.69e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 163310753 1173 CSFTWTGAEHINQDIFECRTCGLLESLCCCTECARVCHKGHDCKLKRTSpTAYCDCW--EKCKCKTLI 1238
Cdd:cd19680     3 CTFTITQKEFMNQHWYHCHTCKMVDGVGVCSVCAKVCHKDHDLSYAKYG-SFFCDCGakEDGSCQALV 69
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 2368-2443 1.11e-12

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 73.69  E-value: 1.11e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753  2368 PFRPASEGNPSDDPDPLPA-----------------------HRQALGERLYPRVQAMQPAFASKITGMLLELSPAQLLL 2424
Cdd:TIGR01628  463 MYPPNYQSLPLSQDLPQPQstasqggqnkklaqvlasatpqmQKQVLGERLFPLVEAIEPALAAKITGMLLEMDNSELLH 542

                           90
                   ....*....|....*....
gi 163310753  2425 LLASEDSLRARVDEAMELI 2443
Cdd:TIGR01628  543 LLESPELLKSKVDEALEVL 561
zf-UBR pfam02207
Putative zinc finger in N-recognin (UBR box); This region is found in E3 ubiquitin ligases ...
 1173-1235 7.36e-11

Putative zinc finger in N-recognin (UBR box); This region is found in E3 ubiquitin ligases that recognize N-recognins.


Pssm-ID: 460491  Cd Length: 68  Bit Score: 60.00  E-value: 7.36e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310753  1173 CSFTWTgaehINQDIFECRTCGLLESLCCCTECARVC-HKGHDCKLKRTSPTAYCDC-----W-EKCKCK 1235
Cdd:pfam02207    1 CGYVFK----KGQPVYRCLTCSLDPTCVICYSCFINCdHEGHDYELFTSRGGGCCDCgdpeaWkEEGFCK 66
UBR-box_UBR1_2_3 cd19670
UBR-box found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), E3-alpha-3 ...
 1173-1228 8.71e-08

UBR-box found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), E3-alpha-3 (UBR3) and similar proteins; This family includes UBR1, UBR2, and UBR3 (all belonging to EC 2.3.2.27). Both UBR1 (also called E3alpha-I or N-recognin-1) and UBR2 (also called E3-alpha-II or N-recognin-2), are RING-type E3 ubiquitin ligases of the Arg/N-end rule degradation pathway. They recognize and bind to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Deficiency of UBR1 causes Johanson-Blizzard syndrome. UBR2 is associated with chromatin and controls chromatin dynamics and gene expression in both germ cells and somatic cells. It plays an important role in spermatogenesis. UBR3, also called ubiquitin-protein ligase E3-alpha-III (E3alpha-III), or N-recognin-3, or zinc finger protein 650, is a RING-type E3 ubiquitin ligase with a function in olfactory and other sensory systems. It negatively regulates the mono-ubiquitination of non-muscle Myosin II, a protein associated with hearing loss in humans. It acts as a positive regulator of Hedgehog (Hh) signaling in Drosophila and vertebrates. It also plays an important role for genome stability by controlling cellular levels of the essential DNA repair protein APE1.


Pssm-ID: 439068  Cd Length: 69  Bit Score: 51.21  E-value: 8.71e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 163310753 1173 CSFTWTgaehINQDIFECRTCGLLESLCCCTECARV-CHKGHDCKLKRTSPTAYCDC 1228
Cdd:cd19670     1 CGKSLK----KGELYYRCLDCSLDPSSCICEECFLNgNHEGHNYSLRTSSGGGVCDC 53
CUE_AUP1_AMFR_like cd14376
CUE domain found in ancient ubiquitous protein 1 (AUP1), autocrine motility factor receptor ...
 187-224 3.90e-07

CUE domain found in ancient ubiquitous protein 1 (AUP1), autocrine motility factor receptor (AMFR) and similar proteins; AUP1 is a component of the HRD1-SEL1L endoplasmic reticulum (ER) quality control complex and is essential for US11-mediated dislocation of class I MHC heavy chains. AMFR is an internalizing cell surface glycoprotein that is localized in both plasma membrane caveolae and the ER, and involves in the regulation of cellular adhesion, proliferation, motility and apoptosis, as well as in the process of learning and memory. Cue1p is an N-terminally membrane-anchored endoplasmic reticulum (ER) protein essential for the activity of the two major yeast RING finger ubiquitin ligases (E3s) implicated in ER-associated degradation (ERAD). This family also includes plant E3 ubiquitin protein ligases RIN2, RIN3, and similar proteins. Comparing with other CUE domain-containing proteins, some family members from higher eukaryotes do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains.


Pssm-ID: 270559  Cd Length: 37  Bit Score: 48.24  E-value: 3.90e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 163310753  187 EELISQAQVVLQGKSRSVIIRELQRTNlDVNLAVNNLL 224
Cdd:cd14376     1 EEMVEQVQEVFPHIPREAIRRDLQRTN-SVDLTINNIL 37
UBR-box_UBR6_FBXO11 cd19676
UBR-box found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11 (also called UBR6, ...
 1173-1228 1.11e-06

UBR-box found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11 (also called UBR6, protein arginine N-methyltransferase 9 (PRMT9), or vitiligo-associated protein 1 (VIT-1)) is an E3 ubiquitin ligase and a type II methyltransferase, which functions as a key regulator of tumor initiation and progression. FBXO11 is a substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. FBXO11 does not bind N-terminal signals.


Pssm-ID: 439074  Cd Length: 69  Bit Score: 48.27  E-value: 1.11e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 163310753 1173 CSFTWTG-AEHINQDIFECRTCGLLESLCCCTECARVCHKGHDCKLKRTSpTAYCDC 1228
Cdd:cd19676     1 CLYKISSyTSFPMHDFYRCLTCNTTDRNAICVNCIKKCHEGHDVEFIRHD-RFFCDC 56
UBR-box_UBR3 cd19673
UBR-box found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar proteins; UBR3 (EC 2.3. ...
 1172-1228 1.54e-06

UBR-box found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar proteins; UBR3 (EC 2.3.2.27), also called ubiquitin-protein ligase E3-alpha-III (E3alpha-III), or N-recognin-3, or zinc finger protein 650, is a RING-type E3 ubiquitin ligase with a function in olfactory and other sensory systems. It negatively regulates the mono-ubiquitination of non-muscle Myosin II, a protein associated with hearing loss in humans. It acts as a positive regulator of Hedgehog (Hh) signaling in Drosophila and vertebrates. It also plays an important role for genome stability by controlling cellular levels of the essential DNA repair protein APE1.


Pssm-ID: 439071  Cd Length: 72  Bit Score: 47.96  E-value: 1.54e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 163310753 1172 TCSFTWTgAEHInqdIFECRTCGLLESLCCCTECARVC-HKGHDCKLKRTSPTAYCDC 1228
Cdd:cd19673     3 VCGRVWK-AGDI---AYRCRTCGLDPTCVICADCFQAGdHEGHDYSMYRSSAGGCCDC 56
UBR-box_UBR7 cd19677
UBR-box found in RING-type E3 ubiquitin-protein ligase UBR7 and similar proteins; UBR7 (EC 2.3. ...
 1172-1228 3.91e-03

UBR-box found in RING-type E3 ubiquitin-protein ligase UBR7 and similar proteins; UBR7 (EC 2.3.2.27; also called N-recognin-7) is a RING-type E3 ubiquitin ligase of the Arg/N-end rule degradation pathway. It recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. UBR7 may play an important role in spermiogenesis and fertilization.


Pssm-ID: 439075  Cd Length: 71  Bit Score: 38.06  E-value: 3.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 163310753 1172 TCSFTwtgAEHINQDIFECRTC---GLLESLCCCTECARVCHKGHDCK---LKRtspTAYCDC 1228
Cdd:cd19677     1 ECTYS---KGYIRQAVYACLTCtpaGADQPAGICLACSLSCHEGHELEelyTKR---NFRCDC 57
 
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.
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