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Conserved domains on  [gi|295982523|pdb|3MAZ|A]
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Chain A, Signal-transducing adaptor protein 1

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SH2_STAP1 cd10403
Src homology 2 domain found in Signal-transducing adaptor protein 1 (STAP1); STAP1 is a ...
 16-109 3.26e-60

Src homology 2 domain found in Signal-transducing adaptor protein 1 (STAP1); STAP1 is a signal-transducing adaptor protein. It is composed of a Pleckstrin homology (PH) and SH2 domains along with several tyrosine phosphorylation sites. STAP-1 is an ortholog of BRDG1 (BCR downstream signaling 1). STAP1 protein functions as a docking protein acting downstream of Tec tyrosine kinase in B cell antigen receptor signaling. The protein is phosphorylated by Tec and participates in a positive feedback loop, increasing Tec activity. STAP1 has been shown to interact with C19orf2, an unconventional prefoldin RPB5 interactor. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


:

Pssm-ID: 198266  Cd Length: 94  Bit Score: 179.92  E-value: 3.26e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MAZ_A       16 PACFYTVSRKEATEMLQKNPSLGNMILRPGSDSRNYSITIRQEIDIPRIKHYKVMSVGQNYTIELEKPVTLPNLFSVIDY 95
Cdd:cd10403   1 PACFYKVSRKEAEELLERNPSCGNMLLRPGSDSSNYSITTRQEINKPRIKHYRVMSRGQGYTIELEKPVTCPTLHDVINY 80

                        90
                ....*....|....
3MAZ_A       96 FVKETRGNLRPFIA 109
Cdd:cd10403  81 FVEKTRGNLRPFIM 94
 
Name Accession Description Interval E-value
SH2_STAP1 cd10403
Src homology 2 domain found in Signal-transducing adaptor protein 1 (STAP1); STAP1 is a ...
 16-109 3.26e-60

Src homology 2 domain found in Signal-transducing adaptor protein 1 (STAP1); STAP1 is a signal-transducing adaptor protein. It is composed of a Pleckstrin homology (PH) and SH2 domains along with several tyrosine phosphorylation sites. STAP-1 is an ortholog of BRDG1 (BCR downstream signaling 1). STAP1 protein functions as a docking protein acting downstream of Tec tyrosine kinase in B cell antigen receptor signaling. The protein is phosphorylated by Tec and participates in a positive feedback loop, increasing Tec activity. STAP1 has been shown to interact with C19orf2, an unconventional prefoldin RPB5 interactor. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198266  Cd Length: 94  Bit Score: 179.92  E-value: 3.26e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MAZ_A       16 PACFYTVSRKEATEMLQKNPSLGNMILRPGSDSRNYSITIRQEIDIPRIKHYKVMSVGQNYTIELEKPVTLPNLFSVIDY 95
Cdd:cd10403   1 PACFYKVSRKEAEELLERNPSCGNMLLRPGSDSSNYSITTRQEINKPRIKHYRVMSRGQGYTIELEKPVTCPTLHDVINY 80

                        90
                ....*....|....
3MAZ_A       96 FVKETRGNLRPFIA 109
Cdd:cd10403  81 FVEKTRGNLRPFIM 94
SH2 pfam00017
SH2 domain;
22-74 1.46e-03

SH2 domain;


Pssm-ID: 425423 [Multi-domain]  Cd Length: 77  Bit Score: 34.88  E-value: 1.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
3MAZ_A         22 VSRKEATEMLQKNPSLGNMILRPgSDSR--NYSITIRQEidiPRIKHYKVMSVGQ 74
Cdd:pfam00017   6 ISRQEAERLLLNGKPDGTFLVRE-SESTpgGYTLSVRDD---GKVKHYKIQSTDN 56
 
Name Accession Description Interval E-value
SH2_STAP1 cd10403
Src homology 2 domain found in Signal-transducing adaptor protein 1 (STAP1); STAP1 is a ...
 16-109 3.26e-60

Src homology 2 domain found in Signal-transducing adaptor protein 1 (STAP1); STAP1 is a signal-transducing adaptor protein. It is composed of a Pleckstrin homology (PH) and SH2 domains along with several tyrosine phosphorylation sites. STAP-1 is an ortholog of BRDG1 (BCR downstream signaling 1). STAP1 protein functions as a docking protein acting downstream of Tec tyrosine kinase in B cell antigen receptor signaling. The protein is phosphorylated by Tec and participates in a positive feedback loop, increasing Tec activity. STAP1 has been shown to interact with C19orf2, an unconventional prefoldin RPB5 interactor. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198266  Cd Length: 94  Bit Score: 179.92  E-value: 3.26e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MAZ_A       16 PACFYTVSRKEATEMLQKNPSLGNMILRPGSDSRNYSITIRQEIDIPRIKHYKVMSVGQNYTIELEKPVTLPNLFSVIDY 95
Cdd:cd10403   1 PACFYKVSRKEAEELLERNPSCGNMLLRPGSDSSNYSITTRQEINKPRIKHYRVMSRGQGYTIELEKPVTCPTLHDVINY 80

                        90
                ....*....|....
3MAZ_A       96 FVKETRGNLRPFIA 109
Cdd:cd10403  81 FVEKTRGNLRPFIM 94
SH2_STAP_family cd09939
Src homology 2 domain found in Signal-transducing adaptor protein (STAP) family; STAP1 and ...
 16-109 2.89e-58

Src homology 2 domain found in Signal-transducing adaptor protein (STAP) family; STAP1 and STAP2 are signal-transducing adaptor proteins. They are composed of a Pleckstrin homology (PH) and SH2 domains along with several tyrosine phosphorylation sites. STAP-1 is an ortholog of BRDG1 (BCR downstream signaling 1). STAP1 protein functions as a docking protein acting downstream of Tec tyrosine kinase in B cell antigen receptor signaling. The protein is phosphorylated by Tec and participates in a positive feedback loop, increasing Tec activity. STAP1 has been shown to interact with C19orf2, an unconventional prefoldin RPB5 interactor. The STAP2 protein is the substrate of breast tumor kinase, an Src-type non-receptor tyrosine kinase that mediates the interactions linking proteins involved in signal transduction pathways. STAP2 has alternative splicing variants. STAP2 has been shown to interact with tyrosine-protein kinase 6 (PTK6). In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198192  Cd Length: 94  Bit Score: 175.04  E-value: 2.89e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MAZ_A       16 PACFYTVSRKEATEMLQKNPSLGNMILRPGSDSRNYSITIRQEIDIPRIKHYKVMSVGQNYTIELEKPVTLPNLFSVIDY 95
Cdd:cd09939   1 PACFYTVSRKEATELLERNPSCGNMLLRPGSDSRNYSVTTRQEINIPVIRHYKVMSVGQNYTIELEKPVTCPNLFSVINY 80

                        90
                ....*....|....
3MAZ_A       96 FVKETRGNLRPFIA 109
Cdd:cd09939  81 FVKETRGNLRPFIL 94
SH2_STAP2 cd10404
Src homology 2 domain found in Signal-transducing adaptor protein 2 (STAP2); STAP2 is a ...
 16-108 1.97e-21

Src homology 2 domain found in Signal-transducing adaptor protein 2 (STAP2); STAP2 is a signal-transducing adaptor protein. It is composed of a Pleckstrin homology (PH) and SH2 domains along with several tyrosine phosphorylation sites. The STAP2 protein is the substrate of breast tumor kinase, an Src-type non-receptor tyrosine kinase that mediates the interactions linking proteins involved in signal transduction pathways. STAP2 has alternative splicing variants. STAP2 has been shown to interact with tyrosine-protein kinase 6 (PTK6). In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198267  Cd Length: 97  Bit Score: 81.87  E-value: 1.97e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MAZ_A       16 PACFYTVSRKEATEMLQKNPSLGNMILRPGSDSRN-YSITIRQEID-IPRIKHYKVMSVGQNYTIELEKPVTLPNLFSVI 93
Cdd:cd10404   1 PSCFLKVSRLEAQLLLERYPECGNLLLRPGGDGADgVSVTTRQMLNgTPVVRHYKVKREGPKYVIDVEEPFSCTSLDAVV 80

                        90
                ....*....|....*
3MAZ_A       94 DYFVKETRGNLRPFI 108
Cdd:cd10404  81 NYFVSHTKKALVPFL 95
SH2 cd00173
Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they ...
 22-96 1.70e-09

Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they bind pTyr-containing polypeptide ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. They are present in a wide array of proteins including: adaptor proteins (Nck1, Crk, Grb2), scaffolds (Slp76, Shc, Dapp1), kinases (Src, Syk, Fps, Tec), phosphatases (Shp-1, Shp-2), transcription factors (STAT1), Ras signaling molecules (Ras-Gap), ubiquitination factors (c-Cbl), cytoskeleton regulators (Tensin), signal regulators (SAP), and phospholipid second messengers (PLCgamma), amongst others.


Pssm-ID: 198173 [Multi-domain]  Cd Length: 79  Bit Score: 50.53  E-value: 1.70e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
3MAZ_A       22 VSRKEATEMLQKNPSlGNMILRPGSDSRN-YSITIRQEIDipRIKHYKVMSVGQNYTIELEKPVTLPNLFSVIDYF 96
Cdd:cd00173   7 ISREEAERLLRGKPD-GTFLVRESSSEPGdYVLSVRSGDG--KVKHYLIERNEGGYYLLGGSGRTFPSLPELVEHY 79
SH2_C-SH2_PLC_gamma_like cd09932
C-terminal Src homology 2 (C-SH2) domain in Phospholipase C gamma; Phospholipase C gamma is a ...
 21-98 3.08e-06

C-terminal Src homology 2 (C-SH2) domain in Phospholipase C gamma; Phospholipase C gamma is a signaling molecule that is recruited to the C-terminal tail of the receptor upon autophosphorylation of a highly conserved tyrosine. PLCgamma is composed of a Pleckstrin homology (PH) domain followed by an elongation factor (EF) domain, 2 catalytic regions of PLC domains that flank 2 tandem SH2 domains (N-SH2, C-SH2), and ending with a SH3 domain and C2 domain. N-SH2 SH2 domain-mediated interactions represent a crucial step in transmembrane signaling by receptor tyrosine kinases. SH2 domains recognize phosphotyrosine (pY) in the context of particular sequence motifs in receptor phosphorylation sites. Both N-SH2 and C-SH2 have a very similar binding affinity to pY. But in growth factor stimulated cells these domains bind to different target proteins. N-SH2 binds to pY containing sites in the C-terminal tails of tyrosine kinases and other receptors. Recently it has been shown that this interaction is mediated by phosphorylation-independent interactions between a secondary binding site found exclusively on the N-SH2 domain and a region of the FGFR1 tyrosine kinase domain. This secondary site on the SH2 cooperates with the canonical pY site to regulate selectivity in mediating a specific cellular process. C-SH2 binds to an intramolecular site on PLCgamma itself which allows it to hydrolyze phosphatidylinositol-4,5-bisphosphate into diacylglycerol and inositol triphosphate. These then activate protein kinase C and release calcium. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198186  Cd Length: 104  Bit Score: 42.64  E-value: 3.08e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MAZ_A       21 TVSRKEATEMLQKNPSLGNMILRP-GSDSRNYSITIRQEidiPRIKHYKVMSVGQNYTI---ELEkpvtlpNLFSVIDYF 96
Cdd:cd09932  10 NLTREQAEEMLMRVPRDGAFLVRPsETDPNSFAISFRAE---GKIKHCRIKQEGRLFVIgtsQFE------SLVELVSYY 80


                ..
3MAZ_A       97 VK 98
Cdd:cd09932  81 EK 82
SH2_Nterm_SPT6_like cd09918
N-terminal Src homology 2 (SH2) domain found in Spt6; N-terminal SH2 domain in Spt6. Spt6 is ...
 19-82 1.50e-04

N-terminal Src homology 2 (SH2) domain found in Spt6; N-terminal SH2 domain in Spt6. Spt6 is an essential transcription elongation factor and histone chaperone that binds the C-terminal repeat domain (CTD) of RNA polymerase II. Spt6 contains a tandem SH2 domain with a novel structure and CTD-binding mode. The tandem SH2 domain binds to a serine 2-phosphorylated CTD peptide in vitro, whereas its N-terminal SH2 subdomain does not. CTD binding requires a positively charged crevice in the C-terminal SH2 subdomain, which lacks the canonical phospho-binding pocket of SH2 domains. The tandem SH2 domain is apparently required for transcription elongation in vivo as its deletion in cells is lethal in the presence of 6-azauracil. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198174  Cd Length: 85  Bit Score: 37.99  E-value: 1.50e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3MAZ_A       19 FYTVSRKEATEMLQKNPSlGNMILRPGSDSRNY-SITIR------QEIDIPRIKHYKVMSVGQNYTIELEK 82
Cdd:cd09918   5 FKNVNYKQAEAYLKSKDV-GEVVIRPSSKGVDHlTVTWKvadgvyQHIDIEELNKENPFSLGKELIIGGEE 74
SH2 pfam00017
SH2 domain;
22-74 1.46e-03

SH2 domain;


Pssm-ID: 425423 [Multi-domain]  Cd Length: 77  Bit Score: 34.88  E-value: 1.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
3MAZ_A         22 VSRKEATEMLQKNPSLGNMILRPgSDSR--NYSITIRQEidiPRIKHYKVMSVGQ 74
Cdd:pfam00017   6 ISRQEAERLLLNGKPDGTFLVRE-SESTpgGYTLSVRDD---GKVKHYKIQSTDN 56
 
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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