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Conserved domains on  [gi|1958682645|ref|XP_038950014|]
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hematopoietic SH2 domain-containing protein isoform X2 [Rattus norvegicus]

Protein Classification

SH2 domain-containing protein( domain architecture ID 61889)

SH2 (Src homology 2) domain-containing protein may act as an intracellular signal-transducing protein

CATH:  3.30.505.10
Gene Ontology:  GO:0007165|GO:0035591|GO:0005515
SCOP:  4001650

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SH2 super family cl15255
Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they ...
1-47 4.23e-22

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.


The actual alignment was detected with superfamily member cd09946:

Pssm-ID: 472789  Cd Length: 102  Bit Score: 87.64  E-value: 4.23e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1958682645   1 MVKLSEDGTFVFAGDHVTHASLDALVTFHQQNPIRPYGELLTRACGQ 47
Cdd:cd09946    56 MVKLLDDGTFMIPGEKVAHTSLHALVTFHQQKPIEPRRELLTQACRQ 102
 
Name Accession Description Interval E-value
SH2_HSH2_like cd09946
Src homology 2 domain found in hematopoietic SH2 (HSH2) protein; HSH2 is thought to function ...
1-47 4.23e-22

Src homology 2 domain found in hematopoietic SH2 (HSH2) protein; HSH2 is thought to function as an adapter protein involved in tyrosine kinase signaling. It may also be involved in regulating cytokine signaling and cytoskeletal reorganization in hematopoietic cells. HSH2 contains several putative protein-binding motifs, SH3-binding proline-rich regions, and phosphotyrosine sites, but lacks enzymatic motifs. HSH2 was found to interact with cytokine-regulated tyrosine kinase c-FES and an activated Cdc42-associated tyrosine kinase ACK1. HSH2 binds c-FES through both its C-terminal region and its N-terminal region including the SH2 domain and binds ACK1 via its N-terminal proline-rich region. Both kinases bound and tyrosine-phosphorylated HSH2 in mammalian cells. 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: 198199  Cd Length: 102  Bit Score: 87.64  E-value: 4.23e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1958682645   1 MVKLSEDGTFVFAGDHVTHASLDALVTFHQQNPIRPYGELLTRACGQ 47
Cdd:cd09946    56 MVKLLDDGTFMIPGEKVAHTSLHALVTFHQQKPIEPRRELLTQACRQ 102
 
Name Accession Description Interval E-value
SH2_HSH2_like cd09946
Src homology 2 domain found in hematopoietic SH2 (HSH2) protein; HSH2 is thought to function ...
1-47 4.23e-22

Src homology 2 domain found in hematopoietic SH2 (HSH2) protein; HSH2 is thought to function as an adapter protein involved in tyrosine kinase signaling. It may also be involved in regulating cytokine signaling and cytoskeletal reorganization in hematopoietic cells. HSH2 contains several putative protein-binding motifs, SH3-binding proline-rich regions, and phosphotyrosine sites, but lacks enzymatic motifs. HSH2 was found to interact with cytokine-regulated tyrosine kinase c-FES and an activated Cdc42-associated tyrosine kinase ACK1. HSH2 binds c-FES through both its C-terminal region and its N-terminal region including the SH2 domain and binds ACK1 via its N-terminal proline-rich region. Both kinases bound and tyrosine-phosphorylated HSH2 in mammalian cells. 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: 198199  Cd Length: 102  Bit Score: 87.64  E-value: 4.23e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1958682645   1 MVKLSEDGTFVFAGDHVTHASLDALVTFHQQNPIRPYGELLTRACGQ 47
Cdd:cd09946    56 MVKLLDDGTFMIPGEKVAHTSLHALVTFHQQKPIEPRRELLTQACRQ 102
SH2_SH2D7 cd10417
Src homology 2 domain found in the SH2 domain containing protein 7 (SH2D7); SH2D7 contains a ...
6-45 3.24e-05

Src homology 2 domain found in the SH2 domain containing protein 7 (SH2D7); SH2D7 contains a single SH2 domain. 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: 199832  Cd Length: 102  Bit Score: 41.80  E-value: 3.24e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1958682645   6 EDGTFVFAGDHVTHASLDALVTFHQQNPIRPYGELLTRAC 45
Cdd:cd10417    61 RNRRYLISGDTSSHSTLAELVRHYQEVQLEPFGETLTAAC 100
SH2_SH2D4A cd10350
Src homology 2 domain found in the SH2 domain containing protein 4A (SH2D4A); SH2D4A contains ...
4-47 5.18e-03

Src homology 2 domain found in the SH2 domain containing protein 4A (SH2D4A); SH2D4A contains a single SH2 domain. 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: 198213  Cd Length: 103  Bit Score: 35.68  E-value: 5.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958682645   4 LSEDG-----------TFVFAG-DHVTHASLDALVTFHQQNPIRPYG-ELLTRACGQ 47
Cdd:cd10350    47 LSEEGckhflidasadSYSFLGvDQLQHATLADLVEYHKEEPITSLGkELLLYPCGQ 103
 
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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