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8YGW

The Crystal Structure of MAPK11 from Biortus

Functional Information from GO Data
ChainGOidnamespacecontents
A0000165biological_processMAPK cascade
A0001649biological_processosteoblast differentiation
A0004674molecular_functionprotein serine/threonine kinase activity
A0004707molecular_functionMAP kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0010628biological_processpositive regulation of gene expression
A0031098biological_processstress-activated protein kinase signaling cascade
A0032735biological_processpositive regulation of interleukin-12 production
A0035556biological_processintracellular signal transduction
A0038066biological_processp38MAPK cascade
A0045648biological_processpositive regulation of erythrocyte differentiation
A0051149biological_processpositive regulation of muscle cell differentiation
A0051403biological_processstress-activated MAPK cascade
A0060038biological_processcardiac muscle cell proliferation
A0060043biological_processregulation of cardiac muscle cell proliferation
A0060044biological_processnegative regulation of cardiac muscle cell proliferation
A0060348biological_processbone development
A0071347biological_processcellular response to interleukin-1
A0071493biological_processcellular response to UV-B
A0090398biological_processcellular senescence
A0098586biological_processcellular response to virus
A0106310molecular_functionprotein serine kinase activity
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGSGAYGSVCsAydarlrqkv.........AVKK
ChainResidueDetails
AVAL30-LYS54

site_idPS01351
Number of Residues104
DetailsMAPK MAP kinase signature. FqsliharrtyRElrllkhlkhenviglldvftpatsiedfsevylvttlmgadlnnivkcqalsdehvqflvyqllrglkyihsagiih.........RDlKpsnvavnedC
ChainResidueDetails
APHE59-CYS162

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AASP150

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AVAL30
ALYS53

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AGLU71

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by MAP2K3, MAP2K4 and MAP2K6 => ECO:0000305|PubMed:15356147
ChainResidueDetails
ATHR180

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by MAP2K3, MAP2K4 and MAP2K6 => ECO:0000305|PubMed:15356147
ChainResidueDetails
ATYR182

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by ZAP70 => ECO:0000250
ChainResidueDetails
ATYR323

220113

PDB entries from 2024-05-22

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