InterPro : IPR000980

Name  SH2 domain Short Name  SH2
Type  Domain Description  The Src homology 2 (SH2) domain is a protein domain of about 100 amino-acid residues first identified as a conserved sequence region between the oncoproteins Src and Fps []. Similar sequences were later found in many other intracellular signal-transducing proteins []. SH2 domains function as regulatory modules of intracellular signalling cascades by interacting with high affinity to phosphotyrosine-containing target peptides in a sequence-specific, SH2 domains recognise between 3-6 residues C-terminal to the phosphorylated tyrosine in a fashion that differs from one SH2 domain to another, and strictly phosphorylation-dependent manner [, , , ]. They are found in a wide variety of protein contexts e.g., in association with catalytic domains of phospholipase Cy (PLCy) and the non-receptor protein tyrosine kinases; within structural proteins such as fodrin and tensin; and in a group of small adaptor molecules, i.e Crk and Nck. The domains are frequently found as repeats in a single protein sequence and will then often bind both mono- and di-phosphorylated substrates. The structure of the SH2 domain belongs to the alpha+beta class, its overall shape forming a compact flattened hemisphere. The core structural elements comprise a central hydrophobic anti-parallel beta-sheet, flanked by 2 short alpha-helices. The loop between strands 2 and 3 provides many of the binding interactions with the phosphate group of its phosphopeptide ligand, and is hence designated the phosphate binding loop, the phosphorylated ligand binds perpendicular to the beta-sheet and typically interacts with the phosphate binding loop and a hydrophobic binding pocket that interacts with a pY+3 side chain. The N- and C-termini of the domain are close together in space and on the opposite face from the phosphopeptide binding surface and it has been speculated that this has facilitated their integration into surface-exposed regions of host proteins [].
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

Other

1 Child Features

Id Name Short Name Type
IPR014742 Adaptor protein Cbl, SH2-like Adaptor_Cbl_SH2-like Domain

0 Contains

14 Found In

Id Name Short Name Type
IPR001217 Transcription factor STAT STAT Family
IPR017072 Transcription elongation factor Spt6 TF_Spt6 Family
IPR017304 Cytoplasmic protein NCK NCK Family
IPR001720 PI3 kinase, P85 regulatory subunit PI3kinase_P85 Family
IPR016250 Tyrosine-protein kinase, Fes/Fps type Tyr-prot_kinase_Fes/Fps Family
IPR016045 Tyrosine-protein kinase, non-receptor, TYK2, N-terminal Tyr_kinase_non-rcpt_TYK2_N Domain
IPR016251 Tyrosine-protein kinase, non-receptor Jak/Tyk2 Tyr_kinase_non-rcpt_Jak/Tyk2 Family
IPR012152 Protein-tyrosine phosphatase, non-receptor type-6, -11 Tyr_Pase_non-rcpt_typ-6/11 Family
IPR016279 Phosphatidylinositol-4, 5-bisphosphate phosphodiesterase gamma PLC-gamma Family
IPR020693 Tyrosine-protein kinase, non-receptor Jak2 Tyr_kinase_non-rcpt_Jak2 Family
IPR020775 Tyrosine-protein kinase, non-receptor Jak3 Tyr_kinase_non-rcpt_Jak3 Family
IPR020776 Tyrosine-protein kinase, non-receptor Jak1 Tyr_kinase_non-rcpt_Jak1 Family
IPR017356 N-chimaerin N-chimaerin Family
IPR012234 Tyrosine-protein kinase, non-receptor SYK/ZAP-70 Tyr_kinase_non-rcpt_SYK/ZAP70 Family

0 Parent Features

7 Publications

First Author Title Year Journal Volume Pages
Pawson T SH2 and SH3 domains. 1993 Curr Biol 3 434-42
Russell RB Conservation analysis and structure prediction of the SH2 family of phosphotyrosine binding domains. 1992 FEBS Lett 304 15-20
Marengere LE Structure and function of SH2 domains. 1994 J Cell Sci Suppl 18 97-104
Sadowski I A noncatalytic domain conserved among cytoplasmic protein-tyrosine kinases modifies the kinase function and transforming activity of Fujinami sarcoma virus P130gag-fps. 1986 Mol Cell Biol 6 4396-408
Pawson T Protein modules and signalling networks. 1995 Nature 373 573-80
Mayer BJ Signalling through SH2 and SH3 domains. 1993 Trends Cell Biol 3 8-13
Pawson T Interaction domains: from simple binding events to complex cellular behavior. 2002 FEBS Lett 513 2-10



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)