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8ACO

Crystal structure of WT p38alpha

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0000077biological_processDNA damage checkpoint signaling
AAA0000165biological_processMAPK cascade
AAA0000902biological_processcell morphogenesis
AAA0000922cellular_componentspindle pole
AAA0001502biological_processcartilage condensation
AAA0001525biological_processangiogenesis
AAA0001649biological_processosteoblast differentiation
AAA0001890biological_processplacenta development
AAA0002021biological_processresponse to dietary excess
AAA0002062biological_processchondrocyte differentiation
AAA0004672molecular_functionprotein kinase activity
AAA0004674molecular_functionprotein serine/threonine kinase activity
AAA0004707molecular_functionMAP kinase activity
AAA0005515molecular_functionprotein binding
AAA0005524molecular_functionATP binding
AAA0005634cellular_componentnucleus
AAA0005654cellular_componentnucleoplasm
AAA0005737cellular_componentcytoplasm
AAA0005739cellular_componentmitochondrion
AAA0005829cellular_componentcytosol
AAA0006006biological_processglucose metabolic process
AAA0006355biological_processregulation of DNA-templated transcription
AAA0006357biological_processregulation of transcription by RNA polymerase II
AAA0006366biological_processtranscription by RNA polymerase II
AAA0006468biological_processprotein phosphorylation
AAA0006915biological_processapoptotic process
AAA0006974biological_processDNA damage response
AAA0007178biological_processcell surface receptor protein serine/threonine kinase signaling pathway
AAA0007519biological_processskeletal muscle tissue development
AAA0010628biological_processpositive regulation of gene expression
AAA0010831biological_processpositive regulation of myotube differentiation
AAA0016301molecular_functionkinase activity
AAA0016607cellular_componentnuclear speck
AAA0018105biological_processpeptidyl-serine phosphorylation
AAA0019395biological_processfatty acid oxidation
AAA0019899molecular_functionenzyme binding
AAA0019903molecular_functionprotein phosphatase binding
AAA0030278biological_processregulation of ossification
AAA0030316biological_processosteoclast differentiation
AAA0031098biological_processstress-activated protein kinase signaling cascade
AAA0031663biological_processlipopolysaccharide-mediated signaling pathway
AAA0032495biological_processresponse to muramyl dipeptide
AAA0032496biological_processresponse to lipopolysaccharide
AAA0032735biological_processpositive regulation of interleukin-12 production
AAA0032868biological_processresponse to insulin
AAA0035331biological_processnegative regulation of hippo signaling
AAA0035556biological_processintracellular signal transduction
AAA0035924biological_processcellular response to vascular endothelial growth factor stimulus
AAA0035994biological_processresponse to muscle stretch
AAA0038066biological_processp38MAPK cascade
AAA0042307biological_processpositive regulation of protein import into nucleus
AAA0042770biological_processsignal transduction in response to DNA damage
AAA0043229cellular_componentintracellular organelle
AAA0045648biological_processpositive regulation of erythrocyte differentiation
AAA0045663biological_processpositive regulation of myoblast differentiation
AAA0045944biological_processpositive regulation of transcription by RNA polymerase II
AAA0046323biological_processglucose import
AAA0046326biological_processpositive regulation of glucose import
AAA0048010biological_processvascular endothelial growth factor receptor signaling pathway
AAA0048273molecular_functionmitogen-activated protein kinase p38 binding
AAA0048863biological_processstem cell differentiation
AAA0051146biological_processstriated muscle cell differentiation
AAA0051403biological_processstress-activated MAPK cascade
AAA0051525molecular_functionNFAT protein binding
AAA0060045biological_processpositive regulation of cardiac muscle cell proliferation
AAA0060348biological_processbone development
AAA0071222biological_processcellular response to lipopolysaccharide
AAA0071223biological_processcellular response to lipoteichoic acid
AAA0071356biological_processcellular response to tumor necrosis factor
AAA0071479biological_processcellular response to ionizing radiation
AAA0071493biological_processcellular response to UV-B
AAA0090090biological_processnegative regulation of canonical Wnt signaling pathway
AAA0090336biological_processpositive regulation of brown fat cell differentiation
AAA0090400biological_processstress-induced premature senescence
AAA0098586biological_processcellular response to virus
AAA0098978cellular_componentglutamatergic synapse
AAA0099179biological_processregulation of synaptic membrane adhesion
AAA0106310molecular_functionprotein serine kinase activity
AAA1900015biological_processregulation of cytokine production involved in inflammatory response
AAA1901741biological_processpositive regulation of myoblast fusion
AAA2000379biological_processpositive regulation of reactive oxygen species metabolic process
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGSGAYGSVCaAfdtktghrv.........AVKK
ChainResidueDetails
AAAVAL30-LYS54

site_idPS01351
Number of Residues104
DetailsMAPK MAP kinase signature. FqsiihakrtyRElrllkhmkhenviglldvftparsleefndvylvthlmgadlnnivkcqkltddhvqfliyqilrglkyihsadiih.........RDlKpsnlavnedC
ChainResidueDetails
AAAPHE59-CYS162

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AAAASP168

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AAAVAL30
AAALYS53

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q16539
ChainResidueDetails
AAASER2

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q16539
ChainResidueDetails
AAATHR16

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q16539
ChainResidueDetails
AAALYS53
AAALYS152

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by MAP2K3, MAP2K4, MAP2K6 and autocatalysis => ECO:0000250
ChainResidueDetails
AAATHR180

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by MAP2K3, MAP2K4, MAP2K6 and autocatalysis => ECO:0000250
ChainResidueDetails
AAATYR182

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by ZAP70 => ECO:0000250|UniProtKB:Q16539
ChainResidueDetails
AAATYR323

219869

PDB entries from 2024-05-15

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