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Protein

Protein kinase C theta type

Gene

PRKCQ

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that mediates non-redundant functions in T-cell receptor (TCR) signaling, including T-cells activation, proliferation, differentiation and survival, by mediating activation of multiple transcription factors such as NF-kappa-B, JUN, NFATC1 and NFATC2. In TCR-CD3/CD28-co-stimulated T-cells, is required for the activation of NF-kappa-B and JUN, which in turn are essential for IL2 production, and participates in the calcium-dependent NFATC1 and NFATC2 transactivation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11 on several serine residues, inducing CARD11 association with lipid rafts and recruitment of the BCL10-MALT1 complex, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. May also play an indirect role in activation of the non-canonical NF-kappa-B (NFKB2) pathway. In the signaling pathway leading to JUN activation, acts by phosphorylating the mediator STK39/SPAK and may not act through MAP kinases signaling. Plays a critical role in TCR/CD28-induced NFATC1 and NFATC2 transactivation by participating in the regulation of reduced inositol 1,4,5-trisphosphate generation and intracellular calcium mobilization. After costimulation of T-cells through CD28 can phosphorylate CBLB and is required for the ubiquitination and subsequent degradation of CBLB, which is a prerequisite for the activation of TCR. During T-cells differentiation, plays an important role in the development of T-helper 2 (Th2) cells following immune and inflammatory responses, and, in the development of inflammatory autoimmune diseases, is necessary for the activation of IL17-producing Th17 cells. May play a minor role in Th1 response. Upon TCR stimulation, mediates T-cell protective survival signal by phosphorylating BAD, thus protecting T-cells from BAD-induced apoptosis, and by up-regulating BCL-X(L)/BCL2L1 levels through NF-kappa-B and JUN pathways. In platelets, regulates signal transduction downstream of the ITGA2B, CD36/GP4, F2R/PAR1 and F2RL3/PAR4 receptors, playing a positive role in 'outside-in' signaling and granule secretion signal transduction. May relay signals from the activated ITGA2B receptor by regulating the uncoupling of WASP and WIPF1, thereby permitting the regulation of actin filament nucleation and branching activity of the Arp2/3 complex. May mediate inhibitory effects of free fatty acids on insulin signaling by phosphorylating IRS1, which in turn blocks IRS1 tyrosine phosphorylation and downstream activation of the PI3K/AKT pathway. Phosphorylates MSN (moesin) in the presence of phosphatidylglycerol or phosphatidylinositol. Phosphorylates PDPK1 at 'Ser-504' and 'Ser-532' and negatively regulates its ability to phosphorylate PKB/AKT1.8 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Enzyme regulationi

Novel PKCs (PRKCD, PRKCE, PRKCH and PRKCQ) are calcium-insensitive, but activated by diacylglycerol (DAG) and phosphatidylserine. Three specific sites; Thr-538 (activation loop of the kinase domain), Ser-676 (turn motif) and Ser-695 (hydrophobic region), need to be phosphorylated for its full activation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei409ATP1
Active sitei504Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri159 – 209Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri231 – 281Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd BLAST51
Nucleotide bindingi386 – 394ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Immunity, Inflammatory response

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:HS00853-MONOMER.
BRENDAi2.7.11.13. 2681.
ReactomeiR-HSA-111465. Apoptotic cleavage of cellular proteins.
R-HSA-114508. Effects of PIP2 hydrolysis.
R-HSA-202424. Downstream TCR signaling.
R-HSA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-373752. Netrin-1 signaling.
R-HSA-418597. G alpha (z) signalling events.
SABIO-RKQ04759.
SignaLinkiQ04759.
SIGNORiQ04759.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein kinase C theta type (EC:2.7.11.13)
Alternative name(s):
nPKC-theta
Gene namesi
Name:PRKCQ
Synonyms:PRKCT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:9410. PRKCQ.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi90Y → F: Loss of function in T-cells proliferation. No effect on kinase activity. 1 Publication1
Mutagenesisi148A → E: Constitutively active form. 1 Publication1
Mutagenesisi219T → A: Loss of transactivation of the IL2 promoter and translocation to the plasma membrane. No effect on kinase activity. 1 Publication1
Mutagenesisi409K → A or E: Loss of kinase activity. 1 Publication1
Mutagenesisi538T → A: Loss of kinase activity. 2 Publications1
Mutagenesisi676S → A: Reduction in kinase activity. 1 Publication1
Mutagenesisi695S → A: Reduction in kinase activity. 2 Publications1

Organism-specific databases

DisGeNETi5588.
OpenTargetsiENSG00000065675.
PharmGKBiPA33773.

Chemistry databases

ChEMBLiCHEMBL3920.
DrugBankiDB00675. Tamoxifen.
GuidetoPHARMACOLOGYi1488.

Polymorphism and mutation databases

BioMutaiPRKCQ.
DMDMi20141582.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000557081 – 706Protein kinase C theta typeAdd BLAST706

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei90Phosphotyrosine; by LCK1 Publication1
Modified residuei219Phosphothreonine; by autocatalysis1 Publication1
Modified residuei348PhosphoserineCombined sources1
Modified residuei538Phosphothreonine; by PDPK13 Publications1
Modified residuei676PhosphoserineCombined sources3 Publications1
Modified residuei685PhosphoserineCombined sources1
Modified residuei695PhosphoserineCombined sources4 Publications1

Post-translational modificationi

Autophosphorylation at Thr-219 is required for targeting to the TCR and cellular function of PRKCQ upon antigen receptor ligation. Following TCR stimulation, phosphorylated at Tyr-90 and Ser-685.5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ04759.
MaxQBiQ04759.
PaxDbiQ04759.
PeptideAtlasiQ04759.
PRIDEiQ04759.

PTM databases

iPTMnetiQ04759.
PhosphoSitePlusiQ04759.

Miscellaneous databases

PMAP-CutDBQ04759.

Expressioni

Tissue specificityi

Expressed in skeletal muscle, T-cells, megakaryoblastic cells and platelets.1 Publication

Gene expression databases

BgeeiENSG00000065675.
CleanExiHS_PRKCQ.
ExpressionAtlasiQ04759. baseline and differential.
GenevisibleiQ04759. HS.

Organism-specific databases

HPAiCAB020789.

Interactioni

Subunit structurei

Interacts with GLRX3 (via N-terminus). Interacts with ECT2. Part of a lipid raft complex composed at least of BCL10, CARD11, MALT1 and IKBKB.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BTKQ061872EBI-374762,EBI-624835
FYNP062417EBI-374762,EBI-515315
GLRX3O760035EBI-374762,EBI-374781
HSF1Q006132EBI-374762,EBI-719620
Irs1P355702EBI-374762,EBI-520230From a different organism.
LCKP062392EBI-374762,EBI-1348
MAP4K3Q8IVH84EBI-374762,EBI-1758170
PRKCZQ055133EBI-374762,EBI-295351

Protein-protein interaction databases

BioGridi111574. 30 interactors.
IntActiQ04759. 19 interactors.
MINTiMINT-4649766.
STRINGi9606.ENSP00000263125.

Chemistry databases

BindingDBiQ04759.

Structurei

Secondary structure

1706
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 13Combined sources9
Beta strandi28 – 39Combined sources12
Beta strandi42 – 52Combined sources11
Beta strandi56 – 62Combined sources7
Beta strandi69 – 75Combined sources7
Beta strandi83 – 89Combined sources7
Helixi90 – 98Combined sources9
Turni99 – 101Combined sources3
Beta strandi103 – 108Combined sources6
Beta strandi110 – 112Combined sources3
Beta strandi114 – 121Combined sources8
Beta strandi155 – 159Combined sources5
Beta strandi161 – 165Combined sources5
Beta strandi174 – 176Combined sources3
Beta strandi187 – 189Combined sources3
Beta strandi191 – 193Combined sources3
Beta strandi196 – 199Combined sources4
Helixi200 – 202Combined sources3
Beta strandi234 – 236Combined sources3
Beta strandi246 – 248Combined sources3
Beta strandi255 – 257Combined sources3
Beta strandi259 – 265Combined sources7
Turni271 – 276Combined sources6
Turni281 – 283Combined sources3
Helixi377 – 379Combined sources3
Beta strandi380 – 388Combined sources9
Beta strandi390 – 399Combined sources10
Turni400 – 402Combined sources3
Beta strandi405 – 412Combined sources8
Helixi413 – 418Combined sources6
Helixi422 – 435Combined sources14
Beta strandi444 – 449Combined sources6
Beta strandi451 – 459Combined sources9
Beta strandi463 – 465Combined sources3
Helixi466 – 473Combined sources8
Helixi478 – 497Combined sources20
Helixi507 – 509Combined sources3
Beta strandi510 – 512Combined sources3
Beta strandi518 – 520Combined sources3
Helixi543 – 545Combined sources3
Helixi548 – 551Combined sources4
Helixi559 – 574Combined sources16
Helixi584 – 593Combined sources10
Helixi604 – 613Combined sources10
Helixi618 – 620Combined sources3
Helixi628 – 630Combined sources3
Helixi632 – 634Combined sources3
Helixi639 – 643Combined sources5
Helixi666 – 669Combined sources4
Helixi680 – 685Combined sources6
Turni690 – 693Combined sources4
Helixi699 – 706Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XJDX-ray2.00A362-706[»]
2ENJNMR-A1-125[»]
2ENNNMR-A144-213[»]
2ENZNMR-A227-284[»]
2JEDX-ray2.32A/B361-706[»]
4Q9ZX-ray2.60A/B374-706[»]
4RA5X-ray2.61A/B374-706[»]
5F9EX-ray2.00A/B361-706[»]
ProteinModelPortaliQ04759.
SMRiQ04759.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04759.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini8 – 123C2Add BLAST116
Domaini380 – 634Protein kinasePROSITE-ProRule annotationAdd BLAST255
Domaini635 – 706AGC-kinase C-terminalAdd BLAST72

Domaini

The C1 domain, containing the phorbol ester/DAG-type region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor and the C2 domain is a non-calcium binding domain.

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 C2 domain.Curated
Contains 2 phorbol-ester/DAG-type zinc fingers.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri159 – 209Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri231 – 281Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd BLAST51

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0694. Eukaryota.
ENOG410XNPH. LUCA.
GeneTreeiENSGT00820000126964.
HOGENOMiHOG000233022.
HOVERGENiHBG108317.
InParanoidiQ04759.
KOiK18052.
OMAiREPQGIS.
OrthoDBiEOG091G0QRS.
PhylomeDBiQ04759.
TreeFamiTF102004.

Family and domain databases

CDDicd00029. C1. 2 hits.
Gene3Di2.60.40.150. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR027264. PKC_theta.
IPR017892. Pkinase_C.
IPR014376. Prot_kin_PKC_delta.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00130. C1_1. 2 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000551. PKC_delta. 1 hit.
PIRSF501105. Protein_kin_C_theta. 1 hit.
PRINTSiPR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 2 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00479. ZF_DAG_PE_1. 2 hits.
PS50081. ZF_DAG_PE_2. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q04759-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSPFLRIGLS NFDCGSCQSC QGEAVNPYCA VLVKEYVESE NGQMYIQKKP
60 70 80 90 100
TMYPPWDSTF DAHINKGRVM QIIVKGKNVD LISETTVELY SLAERCRKNN
110 120 130 140 150
GKTEIWLELK PQGRMLMNAR YFLEMSDTKD MNEFETEGFF ALHQRRGAIK
160 170 180 190 200
QAKVHHVKCH EFTATFFPQP TFCSVCHEFV WGLNKQGYQC RQCNAAIHKK
210 220 230 240 250
CIDKVIAKCT GSAINSRETM FHKERFKIDM PHRFKVYNYK SPTFCEHCGT
260 270 280 290 300
LLWGLARQGL KCDACGMNVH HRCQTKVANL CGINQKLMAE ALAMIESTQQ
310 320 330 340 350
ARCLRDTEQI FREGPVEIGL PCSIKNEARP PCLPTPGKRE PQGISWESPL
360 370 380 390 400
DEVDKMCHLP EPELNKERPS LQIKLKIEDF ILHKMLGKGS FGKVFLAEFK
410 420 430 440 450
KTNQFFAIKA LKKDVVLMDD DVECTMVEKR VLSLAWEHPF LTHMFCTFQT
460 470 480 490 500
KENLFFVMEY LNGGDLMYHI QSCHKFDLSR ATFYAAEIIL GLQFLHSKGI
510 520 530 540 550
VYRDLKLDNI LLDKDGHIKI ADFGMCKENM LGDAKTNTFC GTPDYIAPEI
560 570 580 590 600
LLGQKYNHSV DWWSFGVLLY EMLIGQSPFH GQDEEELFHS IRMDNPFYPR
610 620 630 640 650
WLEKEAKDLL VKLFVREPEK RLGVRGDIRQ HPLFREINWE ELERKEIDPP
660 670 680 690 700
FRPKVKSPFD CSNFDKEFLN EKPRLSFADR ALINSMDQNM FRNFSFMNPG

MERLIS
Length:706
Mass (Da):81,865
Last modified:March 27, 2002 - v3
Checksum:iB3C53AB892D5210A
GO
Isoform 2 (identifier: Q04759-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     550-612: Missing.

Show »
Length:643
Mass (Da):74,287
Checksum:iA3B688EBE8809B9E
GO
Isoform 3 (identifier: Q04759-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-126: Missing.

Note: No experimental confirmation available.
Show »
Length:581
Mass (Da):67,560
Checksum:iABB524BD5B3E2898
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti700G → R in AAA75571 (PubMed:7686153).Curated1
Sequence conflicti700G → R in AAU29340 (Ref. 4) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_042319240K → N in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_042320306D → V.1 PublicationCorresponds to variant rs45590231dbSNPEnsembl.1
Natural variantiVAR_020401330P → L.3 PublicationsCorresponds to variant rs2236379dbSNPEnsembl.1
Natural variantiVAR_042321354D → N.1 PublicationCorresponds to variant rs34524148dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0545502 – 126Missing in isoform 3. 1 PublicationAdd BLAST125
Alternative sequenceiVSP_017294550 – 612Missing in isoform 2. 1 PublicationAdd BLAST63

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01087 mRNA. Translation: AAA75571.1.
L07032 mRNA. Translation: AAA60101.1.
AY702977 mRNA. Translation: AAU29340.1.
AK293935 mRNA. Translation: BAG57313.1.
AL158043 Genomic DNA. Translation: CAC12904.2.
AL137145 Genomic DNA. Translation: CAC10200.2.
BC101465 mRNA. Translation: AAI01466.1.
BC113359 mRNA. Translation: AAI13360.1.
CCDSiCCDS55701.1. [Q04759-2]
CCDS60482.1. [Q04759-3]
CCDS7079.1. [Q04759-1]
PIRiA45416.
RefSeqiNP_001229342.1. NM_001242413.2. [Q04759-2]
NP_001269573.1. NM_001282644.1.
NP_001269574.1. NM_001282645.1. [Q04759-3]
NP_001310194.1. NM_001323265.1. [Q04759-1]
NP_001310195.1. NM_001323266.1. [Q04759-3]
NP_006248.1. NM_006257.4. [Q04759-1]
XP_006717528.1. XM_006717465.3. [Q04759-1]
XP_016871899.1. XM_017016410.1. [Q04759-1]
XP_016871900.1. XM_017016411.1. [Q04759-3]
UniGeneiHs.498570.

Genome annotation databases

EnsembliENST00000263125; ENSP00000263125; ENSG00000065675. [Q04759-1]
ENST00000397176; ENSP00000380361; ENSG00000065675. [Q04759-2]
ENST00000539722; ENSP00000441752; ENSG00000065675. [Q04759-3]
GeneIDi5588.
KEGGihsa:5588.
UCSCiuc001ijj.3. human. [Q04759-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01087 mRNA. Translation: AAA75571.1.
L07032 mRNA. Translation: AAA60101.1.
AY702977 mRNA. Translation: AAU29340.1.
AK293935 mRNA. Translation: BAG57313.1.
AL158043 Genomic DNA. Translation: CAC12904.2.
AL137145 Genomic DNA. Translation: CAC10200.2.
BC101465 mRNA. Translation: AAI01466.1.
BC113359 mRNA. Translation: AAI13360.1.
CCDSiCCDS55701.1. [Q04759-2]
CCDS60482.1. [Q04759-3]
CCDS7079.1. [Q04759-1]
PIRiA45416.
RefSeqiNP_001229342.1. NM_001242413.2. [Q04759-2]
NP_001269573.1. NM_001282644.1.
NP_001269574.1. NM_001282645.1. [Q04759-3]
NP_001310194.1. NM_001323265.1. [Q04759-1]
NP_001310195.1. NM_001323266.1. [Q04759-3]
NP_006248.1. NM_006257.4. [Q04759-1]
XP_006717528.1. XM_006717465.3. [Q04759-1]
XP_016871899.1. XM_017016410.1. [Q04759-1]
XP_016871900.1. XM_017016411.1. [Q04759-3]
UniGeneiHs.498570.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XJDX-ray2.00A362-706[»]
2ENJNMR-A1-125[»]
2ENNNMR-A144-213[»]
2ENZNMR-A227-284[»]
2JEDX-ray2.32A/B361-706[»]
4Q9ZX-ray2.60A/B374-706[»]
4RA5X-ray2.61A/B374-706[»]
5F9EX-ray2.00A/B361-706[»]
ProteinModelPortaliQ04759.
SMRiQ04759.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111574. 30 interactors.
IntActiQ04759. 19 interactors.
MINTiMINT-4649766.
STRINGi9606.ENSP00000263125.

Chemistry databases

BindingDBiQ04759.
ChEMBLiCHEMBL3920.
DrugBankiDB00675. Tamoxifen.
GuidetoPHARMACOLOGYi1488.

PTM databases

iPTMnetiQ04759.
PhosphoSitePlusiQ04759.

Polymorphism and mutation databases

BioMutaiPRKCQ.
DMDMi20141582.

Proteomic databases

EPDiQ04759.
MaxQBiQ04759.
PaxDbiQ04759.
PeptideAtlasiQ04759.
PRIDEiQ04759.

Protocols and materials databases

DNASUi5588.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263125; ENSP00000263125; ENSG00000065675. [Q04759-1]
ENST00000397176; ENSP00000380361; ENSG00000065675. [Q04759-2]
ENST00000539722; ENSP00000441752; ENSG00000065675. [Q04759-3]
GeneIDi5588.
KEGGihsa:5588.
UCSCiuc001ijj.3. human. [Q04759-1]

Organism-specific databases

CTDi5588.
DisGeNETi5588.
GeneCardsiPRKCQ.
HGNCiHGNC:9410. PRKCQ.
HPAiCAB020789.
MIMi600448. gene.
neXtProtiNX_Q04759.
OpenTargetsiENSG00000065675.
PharmGKBiPA33773.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0694. Eukaryota.
ENOG410XNPH. LUCA.
GeneTreeiENSGT00820000126964.
HOGENOMiHOG000233022.
HOVERGENiHBG108317.
InParanoidiQ04759.
KOiK18052.
OMAiREPQGIS.
OrthoDBiEOG091G0QRS.
PhylomeDBiQ04759.
TreeFamiTF102004.

Enzyme and pathway databases

BioCyciZFISH:HS00853-MONOMER.
BRENDAi2.7.11.13. 2681.
ReactomeiR-HSA-111465. Apoptotic cleavage of cellular proteins.
R-HSA-114508. Effects of PIP2 hydrolysis.
R-HSA-202424. Downstream TCR signaling.
R-HSA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-373752. Netrin-1 signaling.
R-HSA-418597. G alpha (z) signalling events.
SABIO-RKQ04759.
SignaLinkiQ04759.
SIGNORiQ04759.

Miscellaneous databases

ChiTaRSiPRKCQ. human.
EvolutionaryTraceiQ04759.
GeneWikiiPRKCQ.
GenomeRNAii5588.
PMAP-CutDBQ04759.
PROiQ04759.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000065675.
CleanExiHS_PRKCQ.
ExpressionAtlasiQ04759. baseline and differential.
GenevisibleiQ04759. HS.

Family and domain databases

CDDicd00029. C1. 2 hits.
Gene3Di2.60.40.150. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR027264. PKC_theta.
IPR017892. Pkinase_C.
IPR014376. Prot_kin_PKC_delta.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00130. C1_1. 2 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000551. PKC_delta. 1 hit.
PIRSF501105. Protein_kin_C_theta. 1 hit.
PRINTSiPR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 2 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00479. ZF_DAG_PE_1. 2 hits.
PS50081. ZF_DAG_PE_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKPCT_HUMAN
AccessioniPrimary (citable) accession number: Q04759
Secondary accession number(s): B4DF52
, Q14DH6, Q3MJF1, Q64FY5, Q9H508, Q9H549
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: March 27, 2002
Last modified: November 30, 2016
This is version 191 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.