PRKCH

Protein identityUniProt · HPA

UniProt accession

P24723

Gene

PRKCH

Ensembl

ENSG00000027075

Chromosome

14

Canonical length

683 aa

Protein class

Cancer-related genes, Disease related genes, Enzymes, Potential drug targets, Predicted intracellular proteins

Subcellular location

Plasma membrane,Cytosol

OverviewNCBI Gene

Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and the second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. The protein encoded by this gene is one of the PKC family members. It is a calcium-independent and phospholipids-dependent protein kinase. It is predominantly expressed in epithelial tissues and has been shown to reside specifically in the cell nucleus. This protein kinase can regulate keratinocyte differentiation by activating the MAP kinase MAPK13 (p38delta)-activated protein kinase cascade that targets CCAAT/enhancer-binding protein alpha (CEBPA). It is also found to mediate the transcription activation of the transglutaminase 1 (TGM1) gene. Mutations in this gene are associated with susceptibility to cerebral infarction. [provided by RefSeq, Sep 2015]

Canonical amino-acid sequenceUniProt

683 residues, UniProt reviewed canonical sequence.

>P24723|PRKCH
     1  MSSGTMKFNG YLRVRIGEAV GLQPTRWSLR HSLFKKGHQL LDPYLTVSVD QVRVGQTSTK
    61  QKTNKPTYNE EFCANVTDGG HLELAVFHET PLGYDHFVAN CTLQFQELLR TTGASDTFEG
   121  WVDLEPEGKV FVVITLTGSF TEATLQRDRI FKHFTRKRQR AMRRRVHQIN GHKFMATYLR
   181  QPTYCSHCRE FIWGVFGKQG YQCQVCTCVV HKRCHHLIVT ACTCQNNINK VDSKIAEQRF
   241  GINIPHKFSI HNYKVPTFCD HCGSLLWGIM RQGLQCKICK MNVHIRCQAN VAPNCGVNAV
   301  ELAKTLAGMG LQPGNISPTS KLVSRSTLRR QGKESSKEGN GIGVNSSNRL GIDNFEFIRV
   361  LGKGSFGKVM LARVKETGDL YAVKVLKKDV ILQDDDVECT MTEKRILSLA RNHPFLTQLF
   421  CCFQTPDRLF FVMEFVNGGD LMFHIQKSRR FDEARARFYA AEIISALMFL HDKGIIYRDL
   481  KLDNVLLDHE GHCKLADFGM CKEGICNGVT TATFCGTPDY IAPEILQEML YGPAVDWWAM
   541  GVLLYEMLCG HAPFEAENED DLFEAILNDE VVYPTWLHED ATGILKSFMT KNPTMRLGSL
   601  TQGGEHAILR HPFFKEIDWA QLNHRQIEPP FRPRIKSRED VSNFDPDFIK EEPVLTPIDE
   661  GHLPMINQDE FRNFSYVSPE LQP

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against PRKCH can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Intracellular

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.3

Highest tissue expression

60 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about PRKCH.

Disease | AllUniProt

Conditions PRKCH is implicated in, by any mechanism.

• Ischemic stroke (ISCHSTR) MIM:601367

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.39

gnomAD pLI

0.43

gnomAD missense Z

2.19

DepMap mean gene effect

0.07

DepMap dependency class

none

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 3% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• cell differentiation
• intracellular signal transduction
• negative regulation of glial cell apoptotic process
• phospholipase C/protein kinase C signal transduction
• positive regulation of B cell receptor signaling pathway
• positive regulation of glial cell proliferation
• positive regulation of keratinocyte differentiation
• positive regulation of macrophage derived foam cell differentiation
• positive regulation of NF-kappaB transcription factor activity
• positive regulation of protein localization to plasma membrane
• protein phosphorylation
• regulation of bicellular tight junction assembly
• signal transduction

Molecular functions

• ATP binding
• diacylglycerol-dependent serine/threonine kinase activity
• diacylglycerol-dependent, calcium-independent serine/threonine kinase activity
• enzyme binding
• protein kinase activity
• protein serine kinase activity
• protein serine/threonine kinase activity
• small GTPase binding
• zinc ion binding

Cellular components

• cell-cell junction
• cytoplasm
• cytosol
• extracellular exosome
• plasma membrane

Protein domainsUniProt · Pfam · InterPro

• C2 domain
• Protein kinase domain
• AGC-kinase, C-terminal
• Protein kinase C-like, phorbol ester/diacylglycerol-binding domain
• Serine/threonine-protein kinase, active site
• Protein kinase-like domain superfamily
• Protein kinase C, delta/epsilon/eta/theta types
• Protein kinase, ATP binding site
• Protein kinase, C-terminal
• Diacylglycerol/phorbol-ester binding
• C2 domain superfamily
• C1-like domain superfamily
• Protein kinase domain
• Phorbol esters/diacylglycerol binding domain (C1 domain)
• C2 domain
• Protein kinase C terminal domain
• Protein kinase C, eta
• Novel protein kinase C eta, catalytic domain

KeywordsUniProt

• ATP-binding
• Cytoplasm
• Differentiation
• Kinase
• Metal-binding
• Nucleotide-binding
• Phosphoprotein
• Repeat
• Serine/threonine-protein kinase
• Transferase
• Zinc
• Zinc-finger

InteractionsUniProt · HPA

Protein binding partners of PRKCH in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• DGKQ
• FYN
• RALA
• RBCK1