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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 to 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei409 – 4091ATP
Active sitei504 – 5041Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri159 – 20951Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri231 – 28151Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi386 – 3949ATPPROSITE-ProRule annotation

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

BRENDAi2.7.11.13. 2681.
ReactomeiREACT_107. Apoptotic cleavage of cellular proteins.
REACT_12555. Downstream TCR signaling.
REACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_163994. FCERI mediated NF-kB activation.
REACT_19333. G alpha (z) signalling events.
REACT_2202. Effects of PIP2 hydrolysis.
REACT_22237. Netrin-1 signaling.
SignaLinkiQ04759.

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
ProteomesiUP000005640 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi90 – 901Y → F: Loss of function in T-cells proliferation. No effect on kinase activity. 1 Publication
Mutagenesisi148 – 1481A → E: Constitutively active form. 1 Publication
Mutagenesisi219 – 2191T → A: Loss of transactivation of the IL2 promoter and translocation to the plasma membrane. No effect on kinase activity. 1 Publication
Mutagenesisi409 – 4091K → A or E: Loss of kinase activity. 1 Publication
Mutagenesisi538 – 5381T → A: Loss of kinase activity. 2 Publications
Mutagenesisi676 – 6761S → A: Reduction in kinase activity. 1 Publication
Mutagenesisi695 – 6951S → A: Reduction in kinase activity. 2 Publications

Organism-specific databases

PharmGKBiPA33773.

Chemistry

DrugBankiDB00675. Tamoxifen.

Polymorphism and mutation databases

BioMutaiPRKCQ.
DMDMi20141582.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 706706Protein kinase C theta typePRO_0000055708Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei90 – 901Phosphotyrosine; by LCK1 Publication
Modified residuei219 – 2191Phosphothreonine; by autocatalysis1 Publication
Modified residuei348 – 3481Phosphoserine1 Publication
Modified residuei538 – 5381Phosphothreonine; by PDPK13 Publications
Modified residuei676 – 6761Phosphoserine4 Publications
Modified residuei685 – 6851Phosphoserine3 Publications
Modified residuei695 – 6951Phosphoserine8 Publications

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

MaxQBiQ04759.
PaxDbiQ04759.
PRIDEiQ04759.

PTM databases

PhosphoSiteiQ04759.

Miscellaneous databases

PMAP-CutDBQ04759.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ04759.
CleanExiHS_PRKCQ.
ExpressionAtlasiQ04759. baseline and differential.
GenevisibleiQ04759. HS.

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 interactions.
IntActiQ04759. 18 interactions.
MINTiMINT-4649766.
STRINGi9606.ENSP00000263125.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 139Combined sources
Beta strandi28 – 3912Combined sources
Beta strandi42 – 5211Combined sources
Beta strandi56 – 627Combined sources
Beta strandi69 – 757Combined sources
Beta strandi83 – 897Combined sources
Helixi90 – 989Combined sources
Turni99 – 1013Combined sources
Beta strandi103 – 1086Combined sources
Beta strandi110 – 1123Combined sources
Beta strandi114 – 1218Combined sources
Beta strandi155 – 1595Combined sources
Beta strandi161 – 1655Combined sources
Beta strandi174 – 1763Combined sources
Beta strandi187 – 1893Combined sources
Beta strandi191 – 1933Combined sources
Beta strandi196 – 1994Combined sources
Helixi200 – 2023Combined sources
Beta strandi234 – 2363Combined sources
Beta strandi246 – 2483Combined sources
Beta strandi255 – 2573Combined sources
Beta strandi259 – 2657Combined sources
Turni271 – 2766Combined sources
Turni281 – 2833Combined sources
Helixi377 – 3793Combined sources
Beta strandi380 – 3889Combined sources
Beta strandi390 – 39910Combined sources
Turni400 – 4023Combined sources
Beta strandi405 – 4128Combined sources
Helixi413 – 4186Combined sources
Helixi422 – 43514Combined sources
Beta strandi444 – 4496Combined sources
Beta strandi451 – 4599Combined sources
Helixi466 – 4738Combined sources
Helixi478 – 49720Combined sources
Helixi507 – 5093Combined sources
Beta strandi510 – 5123Combined sources
Beta strandi518 – 5203Combined sources
Helixi543 – 5453Combined sources
Helixi548 – 5514Combined sources
Helixi559 – 57416Combined sources
Helixi584 – 59310Combined sources
Helixi604 – 61310Combined sources
Helixi618 – 6203Combined sources
Helixi628 – 6303Combined sources
Helixi632 – 6343Combined sources
Helixi639 – 6435Combined sources
Turni667 – 6704Combined sources
Helixi680 – 6856Combined sources
Turni690 – 6934Combined sources
Helixi701 – 7066Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ04759.
SMRiQ04759. Positions 3-126, 144-281, 375-706.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04759.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 123116C2Add
BLAST
Domaini380 – 634255Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini635 – 70672AGC-kinase C-terminalAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri159 – 20951Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri231 – 28151Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00770000120449.
HOGENOMiHOG000233022.
HOVERGENiHBG108317.
InParanoidiQ04759.
KOiK18052.
OMAiREPQGIS.
OrthoDBiEOG77M8QM.
PhylomeDBiQ04759.
TreeFamiTF102004.

Family and domain databases

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.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24352:SF43. PTHR24352:SF43. 1 hit.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti700 – 7001G → R in AAA75571 (PubMed:7686153).Curated
Sequence conflicti700 – 7001G → R in AAU29340 (Ref. 4) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti240 – 2401K → N in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_042319
Natural varianti306 – 3061D → V.1 Publication
Corresponds to variant rs45590231 [ dbSNP | Ensembl ].
VAR_042320
Natural varianti330 – 3301P → L.3 Publications
Corresponds to variant rs2236379 [ dbSNP | Ensembl ].
VAR_020401
Natural varianti354 – 3541D → N.1 Publication
Corresponds to variant rs34524148 [ dbSNP | Ensembl ].
VAR_042321

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2 – 126125Missing in isoform 3. 1 PublicationVSP_054550Add
BLAST
Alternative sequencei550 – 61263Missing in isoform 2. 1 PublicationVSP_017294Add
BLAST

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_006248.1. NM_006257.4. [Q04759-1]
XP_006717528.1. XM_006717465.2. [Q04759-1]
UniGeneiHs.498570.

Genome annotation databases

EnsembliENST00000263125; ENSP00000263125; ENSG00000065675. [Q04759-1]
ENST00000397176; ENSP00000380361; ENSG00000065675. [Q04759-2]
ENST00000539722; ENSP00000441752; ENSG00000065675. [Q04759-3]
GeneIDi5588.
KEGGihsa:5588.
UCSCiuc001iji.1. human. [Q04759-1]
uc009xim.2. human. [Q04759-2]
uc010qax.2. human.

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_006248.1. NM_006257.4. [Q04759-1]
XP_006717528.1. XM_006717465.2. [Q04759-1]
UniGeneiHs.498570.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ04759.
SMRiQ04759. Positions 3-126, 144-281, 375-706.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111574. 30 interactions.
IntActiQ04759. 18 interactions.
MINTiMINT-4649766.
STRINGi9606.ENSP00000263125.

Chemistry

BindingDBiQ04759.
ChEMBLiCHEMBL3920.
DrugBankiDB00675. Tamoxifen.
GuidetoPHARMACOLOGYi1488.

PTM databases

PhosphoSiteiQ04759.

Polymorphism and mutation databases

BioMutaiPRKCQ.
DMDMi20141582.

Proteomic databases

MaxQBiQ04759.
PaxDbiQ04759.
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.
UCSCiuc001iji.1. human. [Q04759-1]
uc009xim.2. human. [Q04759-2]
uc010qax.2. human.

Organism-specific databases

CTDi5588.
GeneCardsiGC10M006509.
HGNCiHGNC:9410. PRKCQ.
MIMi600448. gene.
neXtProtiNX_Q04759.
PharmGKBiPA33773.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00770000120449.
HOGENOMiHOG000233022.
HOVERGENiHBG108317.
InParanoidiQ04759.
KOiK18052.
OMAiREPQGIS.
OrthoDBiEOG77M8QM.
PhylomeDBiQ04759.
TreeFamiTF102004.

Enzyme and pathway databases

BRENDAi2.7.11.13. 2681.
ReactomeiREACT_107. Apoptotic cleavage of cellular proteins.
REACT_12555. Downstream TCR signaling.
REACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_163994. FCERI mediated NF-kB activation.
REACT_19333. G alpha (z) signalling events.
REACT_2202. Effects of PIP2 hydrolysis.
REACT_22237. Netrin-1 signaling.
SignaLinkiQ04759.

Miscellaneous databases

ChiTaRSiPRKCQ. human.
EvolutionaryTraceiQ04759.
GeneWikiiPRKCQ.
GenomeRNAii5588.
NextBioi21674.
PMAP-CutDBQ04759.
PROiQ04759.
SOURCEiSearch...

Gene expression databases

BgeeiQ04759.
CleanExiHS_PRKCQ.
ExpressionAtlasiQ04759. baseline and differential.
GenevisibleiQ04759. HS.

Family and domain databases

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.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24352:SF43. PTHR24352:SF43. 1 hit.
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.
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Publicationsi

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  1. "Molecular cloning and expression of a cDNA encoding a novel isoenzyme of protein kinase C (nPKC). A new member of the nPKC family expressed in skeletal muscle, megakaryoblastic cells, and platelets."
    Chang J.D., Xu Y., Raychowdhury M.K., Ware J.A.
    J. Biol. Chem. 268:14208-14214(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT LEU-330.
  2. Erratum
    Chang J.D., Xu Y., Raychowdhury M.K., Ware J.A.
    J. Biol. Chem. 269:31322-31322(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  3. "Molecular cloning and characterization of PKC theta, a novel member of the protein kinase C (PKC) gene family expressed predominantly in hematopoietic cells."
    Baier G., Telford D., Giampa L., Coggeshall K.M., Baier-Bitterlich G., Isakov N., Altman A.
    J. Biol. Chem. 268:4997-5004(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Blood.
  4. Li H., Ke R., Zhou G., Shen C., Zhong G., Lin L., Yang S.
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT LEU-330.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Cerebellum.
  6. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  8. "Protein kinase C-theta isoenzyme selective stimulation of the transcription factor complex AP-1 in T lymphocytes."
    Baier-Bitterlich G., Uberall F., Bauer B., Fresser F., Wachter H., Grunicke H., Utermann G., Altman A., Baier G.
    Mol. Cell. Biol. 16:1842-1850(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACTIVATION OF JUN.
  9. "Inhibition of the c-Jun N-terminal kinase/AP-1 and NF-kappaB pathways by PICOT, a novel protein kinase C-interacting protein with a thioredoxin homology domain."
    Witte S., Villalba M., Bi K., Liu Y., Isakov N., Altman A.
    J. Biol. Chem. 275:1902-1909(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GLRX3.
  10. "Regulation of protein kinase Ctheta function during T cell activation by Lck-mediated tyrosine phosphorylation."
    Liu Y., Witte S., Liu Y.C., Doyle M., Elly C., Altman A.
    J. Biol. Chem. 275:3603-3609(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-90, MUTAGENESIS OF TYR-90; ALA-148 AND LYS-409.
  11. "Protein kinase C-theta mediates a selective T cell survival signal via phosphorylation of BAD."
    Villalba M., Bushway P., Altman A.
    J. Immunol. 166:5955-5963(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF BAD.
  12. "Phosphorylation of the protein kinase C-theta activation loop and hydrophobic motif regulates its kinase activity, but only activation loop phosphorylation is critical to in vivo nuclear-factor-kappaB induction."
    Liu Y., Graham C., Li A., Fisher R.J., Shaw S.
    Biochem. J. 361:255-265(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-538; SER-676 AND SER-695, MUTAGENESIS OF THR-538 AND SER-695.
  13. "SPAK kinase is a substrate and target of PKCtheta in T-cell receptor-induced AP-1 activation pathway."
    Li Y., Hu J., Vita R., Sun B., Tabata H., Altman A.
    EMBO J. 23:1112-1122(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF STK39/SPAK.
  14. "Protein kinase C Theta inhibits insulin signaling by phosphorylating IRS1 at Ser(1101)."
    Li Y., Soos T.J., Li X., Wu J., Degennaro M., Sun X., Littman D.R., Birnbaum M.J., Polakiewicz R.D.
    J. Biol. Chem. 279:45304-45307(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF IRS1.
  15. "Nucleotide exchange factor ECT2 interacts with the polarity protein complex Par6/Par3/protein kinase Czeta (PKCzeta) and regulates PKCzeta activity."
    Liu X.F., Ishida H., Raziuddin R., Miki T.
    Mol. Cell. Biol. 24:6665-6675(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ECT2.
  16. "Critical role of novel Thr-219 autophosphorylation for the cellular function of PKCtheta in T lymphocytes."
    Thuille N., Heit I., Fresser F., Krumbock N., Bauer B., Leuthaeusser S., Dammeier S., Graham C., Copeland T.D., Shaw S., Baier G.
    EMBO J. 24:3869-3880(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT THR-219; THR-538; SER-676 AND SER-695, MUTAGENESIS OF THR-219; THR-538; SER-676 AND SER-695.
  17. Cited for: FUNCTION IN PHOSPHORYLATION OF CARD11, SUBUNIT.
  18. "Protein kinase C-theta-mediated signals enhance CD4+ T cell survival by up-regulating Bcl-xL."
    Manicassamy S., Gupta S., Huang Z., Sun Z.
    J. Immunol. 176:6709-6716(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACTIVATION OF BCL-X(L)/BCL2L1.
  19. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348; SER-685 AND SER-695, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-676 AND SER-695, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "PKC-theta modulates the strength of T cell responses by targeting Cbl-b for ubiquitination and degradation."
    Gruber T., Hermann-Kleiter N., Hinterleitner R., Fresser F., Schneider R., Gastl G., Penninger J.M., Baier G.
    Sci. Signal. 2:RA30-RA30(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CBLB.
  22. "Protein kinase C(theta) in T cell activation."
    Isakov N., Altman A.
    Annu. Rev. Immunol. 20:761-794(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  23. "Protein kinase C-theta (PKC theta): a key enzyme in T cell life and death."
    Altman A., Villalba M.
    J. Biochem. 132:841-846(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  24. Cited for: REVIEW.
  25. "Selective function of PKC-theta in T cells."
    Manicassamy S., Gupta S., Sun Z.
    Cell. Mol. Immunol. 3:263-270(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  26. "Protein kinase C theta (PKCtheta): a key player in T cell life and death."
    Hayashi K., Altman A.
    Pharmacol. Res. 55:537-544(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  27. "T-cell fate and function: PKC-theta and beyond."
    Marsland B.J., Kopf M.
    Trends Immunol. 29:179-185(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  28. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-685, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "Protein kinase C-theta in platelet activation."
    Cohen S., Braiman A., Shubinsky G., Isakov N.
    FEBS Lett. 585:3208-3215(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION IN PLATELET ACTIVATION.
  31. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-685 AND SER-695, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  33. Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 362-706, PHOSPHORYLATION AT THR-538 AND SER-695.
  34. "The crystal structure of the kinase domain of the protein kinase C theta in complex with Nvp-Xaa228."
    Stark W., Bitsch F., Berner A., Buelens F., Graff P., Depersin H., Fendrich G., Geiser M., Knecht R., Rahuel J., Rummel G., Schlaeppi J.M., Schmitz R., Strauss A., Wagner J.
    Submitted (JAN-2007) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 361-706, PHOSPHORYLATION AT SER-676 AND SER-695.
  35. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASN-240; VAL-306; LEU-330 AND ASN-354.

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: June 24, 2015
This is version 176 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

External Data

Dasty 3

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 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.