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8SE3

Structure of Full-length Human Protein Kinase C Beta 1 (PKCBI) in the Active Conformation

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0002250biological_processadaptive immune response
A0002376biological_processimmune system process
A0003682molecular_functionchromatin binding
A0003713molecular_functiontranscription coactivator activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004697molecular_functiondiacylglycerol-dependent serine/threonine kinase activity
A0004698molecular_functioncalcium,diacylglycerol-dependent serine/threonine kinase activity
A0005080molecular_functionprotein kinase C binding
A0005246molecular_functioncalcium channel regulator activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006325biological_processchromatin organization
A0006338biological_processchromatin remodeling
A0006357biological_processregulation of transcription by RNA polymerase II
A0006468biological_processprotein phosphorylation
A0006816biological_processcalcium ion transport
A0006874biological_processintracellular calcium ion homeostasis
A0006915biological_processapoptotic process
A0007077biological_processmitotic nuclear membrane disassembly
A0007165biological_processsignal transduction
A0007207biological_processphospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway
A0008091cellular_componentspectrin
A0008270molecular_functionzinc ion binding
A0010827biological_processregulation of D-glucose transmembrane transport
A0010829biological_processnegative regulation of D-glucose transmembrane transport
A0016020cellular_componentmembrane
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0030949biological_processpositive regulation of vascular endothelial growth factor receptor signaling pathway
A0032024biological_processpositive regulation of insulin secretion
A0035403molecular_functionhistone H3T6 kinase activity
A0035556biological_processintracellular signal transduction
A0042113biological_processB cell activation
A0042393molecular_functionhistone binding
A0042953biological_processlipoprotein transport
A0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
A0044305cellular_componentcalyx of Held
A0045766biological_processpositive regulation of angiogenesis
A0045893biological_processpositive regulation of DNA-templated transcription
A0046627biological_processnegative regulation of insulin receptor signaling pathway
A0046872molecular_functionmetal ion binding
A0050681molecular_functionnuclear androgen receptor binding
A0050853biological_processB cell receptor signaling pathway
A0051049biological_processregulation of transport
A0070062cellular_componentextracellular exosome
A0070528biological_processprotein kinase C signaling
A0071322biological_processcellular response to carbohydrate stimulus
A0099171biological_processpresynaptic modulation of chemical synaptic transmission
A0099523cellular_componentpresynaptic cytosol
A0106310molecular_functionprotein serine kinase activity
A2000300biological_processregulation of synaptic vesicle exocytosis
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGSFGKVMlSerkgtdel..........YAVK
ChainResidueDetails
ALEU348-LYS371

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiYrDLKldNVML
ChainResidueDetails
AILE462-LEU474

site_idPS00479
Number of Residues50
DetailsZF_DAG_PE_1 Zinc finger phorbol-ester/DAG-type signature. HkFtarffkqptf.CshCtdfIwgfgkqgfq.CqvCcfvvHkrChefvtfs..C
ChainResidueDetails
AHIS37-CYS86
AHIS102-CYS151

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues117
DetailsDomain: {"description":"C2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00041","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues50
DetailsZinc finger: {"description":"Phorbol-ester/DAG-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00226","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues50
DetailsZinc finger: {"description":"Phorbol-ester/DAG-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00226","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues21
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues12
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P68403","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by PDPK1","evidences":[{"source":"PubMed","id":"17115692","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"UniProtKB","id":"P68403","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17115692","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"17115692","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

245011

PDB entries from 2025-11-19

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