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1A81

CRYSTAL STRUCTURE OF THE TANDEM SH2 DOMAIN OF THE SYK KINASE BOUND TO A DUALLY TYROSINE-PHOSPHORYLATED ITAM

Functional Information from GO Data
ChainGOidnamespacecontents
A0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
B0004888molecular_functiontransmembrane signaling receptor activity
B0007166biological_processcell surface receptor signaling pathway
B0016020cellular_componentmembrane
C0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
D0004888molecular_functiontransmembrane signaling receptor activity
D0007166biological_processcell surface receptor signaling pathway
D0016020cellular_componentmembrane
E0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
F0004888molecular_functiontransmembrane signaling receptor activity
F0007166biological_processcell surface receptor signaling pathway
F0016020cellular_componentmembrane
G0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
H0004888molecular_functiontransmembrane signaling receptor activity
H0007166biological_processcell surface receptor signaling pathway
H0016020cellular_componentmembrane
I0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
J0004888molecular_functiontransmembrane signaling receptor activity
J0007166biological_processcell surface receptor signaling pathway
J0016020cellular_componentmembrane
K0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
L0004888molecular_functiontransmembrane signaling receptor activity
L0007166biological_processcell surface receptor signaling pathway
L0016020cellular_componentmembrane
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsMOD_RES: Phosphotyrosine => ECO:0000255|PROSITE-ProRule:PRU00379, ECO:0000269|PubMed:9698567, ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:19690332
ChainResidueDetails
BPTR170
DPTR170
FPTR170
HPTR170
JPTR170
LPTR170

site_idSWS_FT_FI2
Number of Residues6
DetailsMOD_RES: Phosphotyrosine => ECO:0000255|PROSITE-ProRule:PRU00379, ECO:0000269|PubMed:9698567
ChainResidueDetails
GSER44
GSER202
ISER44
ISER202
KSER44
KSER202
BPTR181
DPTR181
FPTR181
HPTR181
JPTR181
LPTR181

site_idSWS_FT_FI3
Number of Residues12
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:21469132
ChainResidueDetails
ATYR47
ATYR131
GTYR47
GTYR131
ITYR47
ITYR131
KTYR47
KTYR131
CTYR47
CTYR131
ETYR47
ETYR131

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:21469132
ChainResidueDetails
ATHR256
CTHR256
ETHR256
GTHR256
ITHR256
KTHR256

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PDB entries from 2024-06-12

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