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Conserved domains on  [gi|56788401|ref|NP_001006619|]
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target of rapamycin complex 2 subunit MAPKAP1 isoform 5 [Homo sapiens]

Protein Classification

Sin1 family protein( domain architecture ID 11157408)

Sin1 (SAPK-interacting protein 1) family protein containing CRIM and PH (Pleckstrin homology) domains; lacks the N-terminal SIN1 domain present in Sin1 protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CRIM pfam16978
SAPK-interacting protein 1 (Sin1), middle CRIM domain; CRIM is a domain in the middle of Sin1 ...
 140-266 5.35e-51

SAPK-interacting protein 1 (Sin1), middle CRIM domain; CRIM is a domain in the middle of Sin1 that is important in the substrate recognition of TORC2. It is conserved from yeast to humans. TOR is a serine/threonine-specific protein kinase and forms functionally distinct protein complexes referred to as TORC1 and TORC2.


:

Pssm-ID: 465326  Cd Length: 137  Bit Score: 165.37  E-value: 5.35e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788401   140 SILSVRLEQCPLQLNNPFNEYSKFDGKGHVGTTAtkKIDVYLPlhSSQDRLLPMTVVTMASARVQDLIGLICWQYTSEGR 219
Cdd:pfam16978   2 SLLSALLKAKKKSPSNPLEYYAFLSGKGEPSNPL--KIKIYFP--FSTSPSKPFEVKVRKDATVAEVIGLILWRYSEEKR 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 56788401   220 EPKLND---NVSAYCLHIAEDDGEVDTDFPPLDSNEPIHKFGFSTLALVE 266
Cdd:pfam16978  78 EPPLDEeklNPNRWTLRIVEEDGEVDEDFPALDRTRPISKFGFDEFALVE 127
SIN1 pfam05422
Stress-activated map kinase interacting protein 1 (SIN1); SIN1 is the N-terminus of ...
 18-129 3.50e-48

Stress-activated map kinase interacting protein 1 (SIN1); SIN1 is the N-terminus of stress-activated map kinase interacting protein 1 (MAPKAP1 OR SIN1) sequences. This domain is likely to be the Ras-binding domain. The fission yeast Sty1/Spc1 mitogen-activated protein (MAP) kinase is a member of the eukaryotic stress-activated MAP kinase (SAPK) family. Sin1 interacts with Sty1/Spc1. Cells lacking Sin1 display many, but not all, of the phenotypes of cells lacking the Sty1/Spc1 MAP kinase including sterility, multiple stress sensitivity and a cell-cycle delay. Sin1 is phosphorylated after stress but this is not Sty1/Spc1-dependent. The separate CRIM and PH, pleckstrin-homology domains of the full-length SIN1 proteins have been separated into distinct families.


:

Pssm-ID: 461648  Cd Length: 136  Bit Score: 158.01  E-value: 3.50e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788401    18 HVTSDDTGMCEMVLIDHDV-------------DLEKIHPPSMPGDSGSEIQGSNGETQGY-----------VYAQSVDIT 73
Cdd:pfam05422   1 FITSDDTGLCETVMLDDDVskhylrkandtvsDLRKPSDKKQVGGSGGDFRHSNADFSDYpgldlsdseddGLDQSYDIQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 56788401    74 SSWDFGIRRRSNTAQRLERLRKERQNQIKCKNIQWKERNSKQSAQELKSLFEKKSL 129
Cdd:pfam05422  81 SYWDFGIHRRSNTAQKLERLDKAKQKAAKIKNIKWEDRSSELSAEDLSELFEKKEV 136
 
Name Accession Description Interval E-value
CRIM pfam16978
SAPK-interacting protein 1 (Sin1), middle CRIM domain; CRIM is a domain in the middle of Sin1 ...
 140-266 5.35e-51

SAPK-interacting protein 1 (Sin1), middle CRIM domain; CRIM is a domain in the middle of Sin1 that is important in the substrate recognition of TORC2. It is conserved from yeast to humans. TOR is a serine/threonine-specific protein kinase and forms functionally distinct protein complexes referred to as TORC1 and TORC2.


Pssm-ID: 465326  Cd Length: 137  Bit Score: 165.37  E-value: 5.35e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788401   140 SILSVRLEQCPLQLNNPFNEYSKFDGKGHVGTTAtkKIDVYLPlhSSQDRLLPMTVVTMASARVQDLIGLICWQYTSEGR 219
Cdd:pfam16978   2 SLLSALLKAKKKSPSNPLEYYAFLSGKGEPSNPL--KIKIYFP--FSTSPSKPFEVKVRKDATVAEVIGLILWRYSEEKR 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 56788401   220 EPKLND---NVSAYCLHIAEDDGEVDTDFPPLDSNEPIHKFGFSTLALVE 266
Cdd:pfam16978  78 EPPLDEeklNPNRWTLRIVEEDGEVDEDFPALDRTRPISKFGFDEFALVE 127
SIN1 pfam05422
Stress-activated map kinase interacting protein 1 (SIN1); SIN1 is the N-terminus of ...
 18-129 3.50e-48

Stress-activated map kinase interacting protein 1 (SIN1); SIN1 is the N-terminus of stress-activated map kinase interacting protein 1 (MAPKAP1 OR SIN1) sequences. This domain is likely to be the Ras-binding domain. The fission yeast Sty1/Spc1 mitogen-activated protein (MAP) kinase is a member of the eukaryotic stress-activated MAP kinase (SAPK) family. Sin1 interacts with Sty1/Spc1. Cells lacking Sin1 display many, but not all, of the phenotypes of cells lacking the Sty1/Spc1 MAP kinase including sterility, multiple stress sensitivity and a cell-cycle delay. Sin1 is phosphorylated after stress but this is not Sty1/Spc1-dependent. The separate CRIM and PH, pleckstrin-homology domains of the full-length SIN1 proteins have been separated into distinct families.


Pssm-ID: 461648  Cd Length: 136  Bit Score: 158.01  E-value: 3.50e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788401    18 HVTSDDTGMCEMVLIDHDV-------------DLEKIHPPSMPGDSGSEIQGSNGETQGY-----------VYAQSVDIT 73
Cdd:pfam05422   1 FITSDDTGLCETVMLDDDVskhylrkandtvsDLRKPSDKKQVGGSGGDFRHSNADFSDYpgldlsdseddGLDQSYDIQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 56788401    74 SSWDFGIRRRSNTAQRLERLRKERQNQIKCKNIQWKERNSKQSAQELKSLFEKKSL 129
Cdd:pfam05422  81 SYWDFGIHRRSNTAQKLERLDKAKQKAAKIKNIKWEDRSSELSAEDLSELFEKKEV 136
 
Name Accession Description Interval E-value
CRIM pfam16978
SAPK-interacting protein 1 (Sin1), middle CRIM domain; CRIM is a domain in the middle of Sin1 ...
 140-266 5.35e-51

SAPK-interacting protein 1 (Sin1), middle CRIM domain; CRIM is a domain in the middle of Sin1 that is important in the substrate recognition of TORC2. It is conserved from yeast to humans. TOR is a serine/threonine-specific protein kinase and forms functionally distinct protein complexes referred to as TORC1 and TORC2.


Pssm-ID: 465326  Cd Length: 137  Bit Score: 165.37  E-value: 5.35e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788401   140 SILSVRLEQCPLQLNNPFNEYSKFDGKGHVGTTAtkKIDVYLPlhSSQDRLLPMTVVTMASARVQDLIGLICWQYTSEGR 219
Cdd:pfam16978   2 SLLSALLKAKKKSPSNPLEYYAFLSGKGEPSNPL--KIKIYFP--FSTSPSKPFEVKVRKDATVAEVIGLILWRYSEEKR 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 56788401   220 EPKLND---NVSAYCLHIAEDDGEVDTDFPPLDSNEPIHKFGFSTLALVE 266
Cdd:pfam16978  78 EPPLDEeklNPNRWTLRIVEEDGEVDEDFPALDRTRPISKFGFDEFALVE 127
SIN1 pfam05422
Stress-activated map kinase interacting protein 1 (SIN1); SIN1 is the N-terminus of ...
 18-129 3.50e-48

Stress-activated map kinase interacting protein 1 (SIN1); SIN1 is the N-terminus of stress-activated map kinase interacting protein 1 (MAPKAP1 OR SIN1) sequences. This domain is likely to be the Ras-binding domain. The fission yeast Sty1/Spc1 mitogen-activated protein (MAP) kinase is a member of the eukaryotic stress-activated MAP kinase (SAPK) family. Sin1 interacts with Sty1/Spc1. Cells lacking Sin1 display many, but not all, of the phenotypes of cells lacking the Sty1/Spc1 MAP kinase including sterility, multiple stress sensitivity and a cell-cycle delay. Sin1 is phosphorylated after stress but this is not Sty1/Spc1-dependent. The separate CRIM and PH, pleckstrin-homology domains of the full-length SIN1 proteins have been separated into distinct families.


Pssm-ID: 461648  Cd Length: 136  Bit Score: 158.01  E-value: 3.50e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788401    18 HVTSDDTGMCEMVLIDHDV-------------DLEKIHPPSMPGDSGSEIQGSNGETQGY-----------VYAQSVDIT 73
Cdd:pfam05422   1 FITSDDTGLCETVMLDDDVskhylrkandtvsDLRKPSDKKQVGGSGGDFRHSNADFSDYpgldlsdseddGLDQSYDIQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 56788401    74 SSWDFGIRRRSNTAQRLERLRKERQNQIKCKNIQWKERNSKQSAQELKSLFEKKSL 129
Cdd:pfam05422  81 SYWDFGIHRRSNTAQKLERLDKAKQKAAKIKNIKWEDRSSELSAEDLSELFEKKEV 136
 
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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