PRKCQ

Protein identityUniProt · HPA

UniProt accession

Q04759

Gene

PRKCQ

Ensembl

ENSG00000065675

Chromosome

10

Canonical length

706 aa

Protein class

Cancer-related genes, Enzymes, FDA approved drug targets, Plasma proteins, Predicted intracellular proteins

Subcellular location

Centriolar satellite

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. The protein encoded by this gene is one of the PKC family members. It is a calcium-independent and phospholipid-dependent protein kinase. This kinase is important for T-cell activation. It is required for the activation of the transcription factors NF-kappaB and AP-1, and may link the T cell receptor (TCR) signaling complex to the activation of the transcription factors. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

706 residues, UniProt reviewed canonical sequence.

>Q04759|PRKCQ
     1  MSPFLRIGLS NFDCGSCQSC QGEAVNPYCA VLVKEYVESE NGQMYIQKKP TMYPPWDSTF
    61  DAHINKGRVM QIIVKGKNVD LISETTVELY SLAERCRKNN GKTEIWLELK PQGRMLMNAR
   121  YFLEMSDTKD MNEFETEGFF ALHQRRGAIK QAKVHHVKCH EFTATFFPQP TFCSVCHEFV
   181  WGLNKQGYQC RQCNAAIHKK CIDKVIAKCT GSAINSRETM FHKERFKIDM PHRFKVYNYK
   241  SPTFCEHCGT LLWGLARQGL KCDACGMNVH HRCQTKVANL CGINQKLMAE ALAMIESTQQ
   301  ARCLRDTEQI FREGPVEIGL PCSIKNEARP PCLPTPGKRE PQGISWESPL DEVDKMCHLP
   361  EPELNKERPS LQIKLKIEDF ILHKMLGKGS FGKVFLAEFK KTNQFFAIKA LKKDVVLMDD
   421  DVECTMVEKR VLSLAWEHPF LTHMFCTFQT KENLFFVMEY LNGGDLMYHI QSCHKFDLSR
   481  ATFYAAEIIL GLQFLHSKGI VYRDLKLDNI LLDKDGHIKI ADFGMCKENM LGDAKTNTFC
   541  GTPDYIAPEI LLGQKYNHSV DWWSFGVLLY EMLIGQSPFH GQDEEELFHS IRMDNPFYPR
   601  WLEKEAKDLL VKLFVREPEK RLGVRGDIRQ HPLFREINWE ELERKEIDPP FRPKVKSPFD
   661  CSNFDKEFLN EKPRLSFADR ALINSMDQNM FRNFSFMNPG MERLIS

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against PRKCQ 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

Cell surface

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.32

Highest tissue expression

115 nTPM

Expression across tissuesHPA

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

0.3

gnomAD missense Z

2.36

DepMap mean gene effect

-0.03

DepMap dependency class

none

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• axon guidance
• CD4-positive, alpha-beta T cell proliferation
• cell chemotaxis
• Fc-epsilon receptor signaling pathway
• inflammatory response
• intracellular signal transduction
• membrane protein ectodomain proteolysis
• negative regulation of insulin receptor signaling pathway
• negative regulation of T cell apoptotic process
• positive regulation of CD4-positive, alpha-beta T cell proliferation
• positive regulation of interleukin-17 production
• positive regulation of interleukin-2 production
• positive regulation of interleukin-4 production
• positive regulation of NF-kappaB transcription factor activity
• positive regulation of T cell activation
• positive regulation of T-helper 17 type immune response
• positive regulation of telomere maintenance
• regulation of cell growth
• regulation of DNA-templated transcription
• regulation of platelet aggregation
• positive regulation of T-helper 2 cell activation

Molecular functions

• ATP binding
• diacylglycerol-dependent serine/threonine kinase activity
• protein kinase activity
• protein serine kinase activity
• protein serine/threonine kinase activity
• zinc ion binding

Cellular components

• aggresome
• centriolar satellite
• cytosol
• immunological synapse
• 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)
• Protein kinase C terminal domain
• Protein kinase C delta/epsilon/eta/theta, C2 domain
• Protein kinase C, theta
• Novel protein kinase C theta, catalytic domain

KeywordsUniProt

• ATP-binding
• Cell membrane
• Cytoplasm
• Immunity
• Inflammatory response
• Kinase
• Magnesium
• Membrane
• Metal-binding
• Nucleotide-binding
• Phosphoprotein
• Repeat
• Serine/threonine-protein kinase
• Transferase
• Zinc
• Zinc-finger

InteractionsUniProt · HPA

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

• CD28
• ECT2
• GLRX3
• FYN