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Protein

Protein kinase C zeta type

Gene

PRKCZ

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

Functioni

Calcium- and diacylglycerol-independent serine/threonine-protein kinase that functions in phosphatidylinositol 3-kinase (PI3K) pathway and mitogen-activated protein (MAP) kinase cascade, and is involved in NF-kappa-B activation, mitogenic signaling, cell proliferation, cell polarity, inflammatory response and maintenance of long-term potentiation (LTP). Upon lipopolysaccharide (LPS) treatment in macrophages, or following mitogenic stimuli, functions downstream of PI3K to activate MAP2K1/MEK1-MAPK1/ERK2 signaling cascade independently of RAF1 activation. Required for insulin-dependent activation of AKT3, but may function as an adapter rather than a direct activator. Upon insulin treatment may act as a downstream effector of PI3K and contribute to the activation of translocation of the glucose transporter SLC2A4/GLUT4 and subsequent glucose transport in adipocytes. In EGF-induced cells, binds and activates MAP2K5/MEK5-MAPK7/ERK5 independently of its kinase activity and can activate JUN promoter through MEF2C. Through binding with SQSTM1/p62, functions in interleukin-1 signaling and activation of NF-kappa-B with the specific adapters RIPK1 and TRAF6. Participates in TNF-dependent transactivation of NF-kappa-B by phosphorylating and activating IKBKB kinase, which in turn leads to the degradation of NF-kappa-B inhibitors. In migrating astrocytes, forms a cytoplasmic complex with PARD6A and is recruited by CDC42 to function in the establishment of cell polarity along with the microtubule motor and dynein. In association with FEZ1, stimulates neuronal differentiation in PC12 cells. In the inflammatory response, is required for the T-helper 2 (Th2) differentiation process, including interleukin production, efficient activation of JAK1 and the subsequent phosphorylation and nuclear translocation of STAT6. May be involved in development of allergic airway inflammation (asthma), a process dependent on Th2 immune response. In the NF-kappa-B-mediated inflammatory response, can relieve SETD6-dependent repression of NF-kappa-B target genes by phosphorylating the RELA subunit at 'Ser-311'. Necessary and sufficient for LTP maintenance in hippocampal CA1 pyramidal cells. In vein endothelial cells treated with the oxidant peroxynitrite, phosphorylates STK11 leading to nuclear export of STK11, subsequent inhibition of PI3K/Akt signaling, and increased apoptosis. Phosphorylates VAMP2 in vitro (PubMed:17313651).7 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Atypical PKCs (PRKCI and PRKCZ) exhibit an elevated basal enzymatic activity (that may be due to the interaction with SMG1 or SQSTM1) and are not regulated by diacylglycerol, phosphatidylserine, phorbol esters or calcium ions. Two specific sites, Thr-410 (activation loop of the kinase domain) and Thr-560 (turn motif), need to be phosphorylated for its full activation. Phosphatidylinositol 3,4,5-trisphosphate might be a physiological activator (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei281ATPPROSITE-ProRule annotation1
Active sitei376Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri130 – 180Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST51
Nucleotide bindingi258 – 266ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • insulin receptor substrate binding Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • potassium channel regulator activity Source: Ensembl
  • protein kinase activity Source: UniProtKB
  • protein kinase C activity Source: Reactome
  • protein serine/threonine kinase activity Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Inflammatory response

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciZFISH:HS00913-MONOMER.
BRENDAi2.7.11.13. 2681.
ReactomeiR-HSA-114604. GPVI-mediated activation cascade.
R-HSA-2173791. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
R-HSA-5218921. VEGFR2 mediated cell proliferation.
SignaLinkiQ05513.
SIGNORiQ05513.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein kinase C zeta type (EC:2.7.11.13)
Alternative name(s):
nPKC-zeta
Gene namesi
Name:PRKCZ
Synonyms:PKC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:9412. PRKCZ.

Subcellular locationi

GO - Cellular componenti

  • apical cortex Source: Ensembl
  • apical plasma membrane Source: Ensembl
  • axon hillock Source: Ensembl
  • bicellular tight junction Source: Ensembl
  • cell-cell junction Source: UniProtKB
  • cell junction Source: Reactome
  • cell leading edge Source: Ensembl
  • cytoplasm Source: ProtInc
  • cytosol Source: Reactome
  • endosome Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • filamentous actin Source: Ensembl
  • membrane Source: ProtInc
  • membrane raft Source: Ensembl
  • microtubule organizing center Source: Ensembl
  • myelin sheath abaxonal region Source: Ensembl
  • nuclear envelope Source: Ensembl
  • nuclear matrix Source: Ensembl
  • perinuclear region of cytoplasm Source: Ensembl
  • plasma membrane Source: ProtInc
  • vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Endosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi19K → A: No effect on interaction with SQSTM1 and PARD6B. 1 Publication1
Mutagenesisi62D → A: Loss of interaction with SQSTM1 and PARD6B. 1 Publication1
Mutagenesisi66D → A: Loss of interaction with SQSTM1 and PARD6B. 1 Publication1

Organism-specific databases

DisGeNETi5590.
OpenTargetsiENSG00000067606.
PharmGKBiPA33775.

Chemistry databases

ChEMBLiCHEMBL3438.
DrugBankiDB00675. Tamoxifen.
GuidetoPHARMACOLOGYi1491.

Polymorphism and mutation databases

BioMutaiPRKCZ.
DMDMi68067736.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000557011 – 592Protein kinase C zeta typeAdd BLAST592

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei410Phosphothreonine; by PDPK1 and PI3K3 Publications1
Modified residuei560PhosphothreonineCombined sources1
Modified residuei591PhosphoserineBy similarity1

Post-translational modificationi

CDH5 is required for its phosphorylation at Thr-410. Phosphorylated by protein kinase PDPK1; phosphorylation is inhibited by the apoptotic C-terminal cleavage product of PKN2. Phosphorylation at Thr-410 by PI3K activates the kinase.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ05513.
MaxQBiQ05513.
PaxDbiQ05513.
PeptideAtlasiQ05513.
PRIDEiQ05513.

PTM databases

iPTMnetiQ05513.
PhosphoSitePlusiQ05513.

Miscellaneous databases

PMAP-CutDBQ05513.

Expressioni

Tissue specificityi

Expressed in brain, and to a lesser extent in lung, kidney and testis.

Gene expression databases

BgeeiENSG00000067606.
CleanExiHS_PRKCZ.
ExpressionAtlasiQ05513. baseline and differential.
GenevisibleiQ05513. HS.

Organism-specific databases

HPAiCAB004533.
HPA021851.

Interactioni

Subunit structurei

Forms a ternary complex with SQSTM1 and KCNAB2. Forms another ternary complex with SQSTM1 and GABRR3. Forms a complex with SQSTM1 and MAP2K5 (By similarity). Interacts with PARD6A, PARD6B, PARD6G and SQSTM1. Part of a complex with PARD3, PARD6A or PARD6B or PARD6G and CDC42 or RAC1. Interacts with ADAP1/CENTA1. Forms a ternary complex composed of SQSTM1 and PAWR. Interacts directly with SQSTM1 (Probable). Interacts with IKBKB. Interacts (via the protein kinase domain) with WWC1. Forms a tripartite complex with WWC1 and DDR1, but predominantly in the absence of collagen. Component of the Par polarity complex, composed of at least phosphorylated PRKCZ, PARD3 and TIAM1. Interacts with PDPK1 (via N-terminal region). Interacts with WDFY2 (via WD repeats 1-3) (PubMed:16792529). Interacts with VAMP2 (PubMed:17313651). Forms a complex with WDFY2 and VAMP2 (PubMed:17313651).By similarityCurated12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AKT1P317492EBI-295351,EBI-296087
BCL10O959993EBI-295351,EBI-958922
C1QBPQ070212EBI-295351,EBI-347528
F11RQ9Y6242EBI-295351,EBI-742600
HSP90AB1P082382EBI-295351,EBI-352572
NCF1P145983EBI-295351,EBI-395044
NUMBP49757-14EBI-295351,EBI-7199607
numbP165542EBI-295351,EBI-429581From a different organism.
PARD6AQ9NPB68EBI-295351,EBI-81876
PARD6BQ9BYG59EBI-295351,EBI-295391
PARD6GQ9BYG43EBI-295351,EBI-295417
PRKCIP417434EBI-295351,EBI-286199
PRKCQQ047593EBI-295351,EBI-374762
VHLP403373EBI-295351,EBI-301246

GO - Molecular functioni

  • insulin receptor substrate binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi111576. 85 interactors.
IntActiQ05513. 36 interactors.
MINTiMINT-5004464.
STRINGi9606.ENSP00000367830.

Chemistry databases

BindingDBiQ05513.

Structurei

3D structure databases

ProteinModelPortaliQ05513.
SMRiQ05513.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini15 – 98PB1PROSITE-ProRule annotationAdd BLAST84
Domaini252 – 518Protein kinasePROSITE-ProRule annotationAdd BLAST267
Domaini519 – 590AGC-kinase C-terminalAdd BLAST72

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni79 – 145Interaction with SQSTM1By similarityAdd BLAST67

Domaini

The PB1 domain mediate mutually exclusive interactions with SQSTM1 and PARD6B.1 Publication
The C1 domain does not bind the diacylglycerol (DAG).1 Publication

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 PB1 domain.PROSITE-ProRule annotation
Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri130 – 180Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST51

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0695. Eukaryota.
ENOG410ZMG2. LUCA.
GeneTreeiENSGT00820000126964.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiQ05513.
KOiK18952.
OMAiRCHVLVP.
OrthoDBiEOG091G03Q9.
PhylomeDBiQ05513.
TreeFamiTF102004.

Family and domain databases

CDDicd00029. C1. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR000270. PB1_dom.
IPR002219. PE/DAG-bd.
IPR012233. PKC.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00130. C1_1. 1 hit.
PF00564. PB1. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000554. PKC_zeta. 1 hit.
PRINTSiPR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 1 hit.
SM00666. PB1. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS51745. PB1. 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. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q05513-1) [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
MPSRTGPKME GSGGRVRLKA HYGGDIFITS VDAATTFEEL CEEVRDMCRL
60 70 80 90 100
HQQHPLTLKW VDSEGDPCTV SSQMELEEAF RLARQCRDEG LIIHVFPSTP
110 120 130 140 150
EQPGLPCPGE DKSIYRRGAR RWRKLYRANG HLFQAKRFNR RAYCGQCSER
160 170 180 190 200
IWGLARQGYR CINCKLLVHK RCHGLVPLTC RKHMDSVMPS QEPPVDDKNE
210 220 230 240 250
DADLPSEETD GIAYISSSRK HDSIKDDSED LKPVIDGMDG IKISQGLGLQ
260 270 280 290 300
DFDLIRVIGR GSYAKVLLVR LKKNDQIYAM KVVKKELVHD DEDIDWVQTE
310 320 330 340 350
KHVFEQASSN PFLVGLHSCF QTTSRLFLVI EYVNGGDLMF HMQRQRKLPE
360 370 380 390 400
EHARFYAAEI CIALNFLHER GIIYRDLKLD NVLLDADGHI KLTDYGMCKE
410 420 430 440 450
GLGPGDTTST FCGTPNYIAP EILRGEEYGF SVDWWALGVL MFEMMAGRSP
460 470 480 490 500
FDIITDNPDM NTEDYLFQVI LEKPIRIPRF LSVKASHVLK GFLNKDPKER
510 520 530 540 550
LGCRPQTGFS DIKSHAFFRS IDWDLLEKKQ ALPPFQPQIT DDYGLDNFDT
560 570 580 590
QFTSEPVQLT PDDEDAIKRI DQSEFEGFEY INPLLLSTEE SV
Length:592
Mass (Da):67,660
Last modified:June 21, 2005 - v4
Checksum:i88CCD0577E6A596C
GO
Isoform 2 (identifier: Q05513-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-183: Missing.

Show »
Length:409
Mass (Da):46,622
Checksum:i21C316A4A2B418BD
GO
Isoform 3 (identifier: Q05513-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-112: MPSRTGPKME...PGLPCPGEDK → MLTPRTDE

Note: No experimental confirmation available.
Show »
Length:488
Mass (Da):56,136
Checksum:i219A7C60FCEF0905
GO

Sequence cautioni

The sequence CAA78813 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti6G → D in AAA36488 (PubMed:8224878).Curated1
Sequence conflicti198K → R in BAF83684 (PubMed:14702039).Curated1
Sequence conflicti262S → T in AAA36488 (PubMed:8224878).Curated1
Sequence conflicti281K → R in BAH11883 (PubMed:14702039).Curated1
Sequence conflicti366F → L in BAF83684 (PubMed:14702039).Curated1
Sequence conflicti500R → G in BAF83684 (PubMed:14702039).Curated1
Sequence conflicti522D → G in BAF83684 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05056049R → H.Corresponds to variant rs35271800dbSNPEnsembl.1
Natural variantiVAR_04231084R → H.1 PublicationCorresponds to variant rs56017162dbSNPEnsembl.1
Natural variantiVAR_035467514S → F in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_042311519R → C in a colorectal adenocarcinoma sample; somatic mutation. 1 PublicationCorresponds to variant rs376894109dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0419041 – 183Missing in isoform 2. 1 PublicationAdd BLAST183
Alternative sequenceiVSP_0463471 – 112MPSRT…PGEDK → MLTPRTDE in isoform 3. 1 PublicationAdd BLAST112

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14283 mRNA. Translation: AAA36488.1.
BT007082 mRNA. Translation: AAP35745.1.
AK290995 mRNA. Translation: BAF83684.1.
AK294649 mRNA. Translation: BAH11833.1.
AK294782 mRNA. Translation: BAH11883.1.
AL162271 Genomic DNA. No translation available.
AL391845, AL590822, AL645703 Genomic DNA. Translation: CAI15438.1.
AL645703, AL391845, AL590822 Genomic DNA. Translation: CAI21535.1.
BC008058 mRNA. Translation: AAH08058.1.
BC014270 mRNA. Translation: AAH14270.1.
Z15108 mRNA. Translation: CAA78813.1. Different initiation.
CCDSiCCDS37.1. [Q05513-1]
CCDS41229.1. [Q05513-2]
CCDS55563.1. [Q05513-3]
PIRiJN0877.
RefSeqiNP_001028753.1. NM_001033581.1. [Q05513-2]
NP_001028754.1. NM_001033582.1. [Q05513-2]
NP_001229803.1. NM_001242874.1. [Q05513-3]
NP_002735.3. NM_002744.4. [Q05513-1]
XP_016857288.1. XM_017001799.1. [Q05513-2]
UniGeneiHs.496255.

Genome annotation databases

EnsembliENST00000378567; ENSP00000367830; ENSG00000067606. [Q05513-1]
ENST00000400921; ENSP00000383712; ENSG00000067606. [Q05513-2]
ENST00000461106; ENSP00000426412; ENSG00000067606. [Q05513-3]
GeneIDi5590.
KEGGihsa:5590.
UCSCiuc001aiq.3. human. [Q05513-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14283 mRNA. Translation: AAA36488.1.
BT007082 mRNA. Translation: AAP35745.1.
AK290995 mRNA. Translation: BAF83684.1.
AK294649 mRNA. Translation: BAH11833.1.
AK294782 mRNA. Translation: BAH11883.1.
AL162271 Genomic DNA. No translation available.
AL391845, AL590822, AL645703 Genomic DNA. Translation: CAI15438.1.
AL645703, AL391845, AL590822 Genomic DNA. Translation: CAI21535.1.
BC008058 mRNA. Translation: AAH08058.1.
BC014270 mRNA. Translation: AAH14270.1.
Z15108 mRNA. Translation: CAA78813.1. Different initiation.
CCDSiCCDS37.1. [Q05513-1]
CCDS41229.1. [Q05513-2]
CCDS55563.1. [Q05513-3]
PIRiJN0877.
RefSeqiNP_001028753.1. NM_001033581.1. [Q05513-2]
NP_001028754.1. NM_001033582.1. [Q05513-2]
NP_001229803.1. NM_001242874.1. [Q05513-3]
NP_002735.3. NM_002744.4. [Q05513-1]
XP_016857288.1. XM_017001799.1. [Q05513-2]
UniGeneiHs.496255.

3D structure databases

ProteinModelPortaliQ05513.
SMRiQ05513.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111576. 85 interactors.
IntActiQ05513. 36 interactors.
MINTiMINT-5004464.
STRINGi9606.ENSP00000367830.

Chemistry databases

BindingDBiQ05513.
ChEMBLiCHEMBL3438.
DrugBankiDB00675. Tamoxifen.
GuidetoPHARMACOLOGYi1491.

PTM databases

iPTMnetiQ05513.
PhosphoSitePlusiQ05513.

Polymorphism and mutation databases

BioMutaiPRKCZ.
DMDMi68067736.

Proteomic databases

EPDiQ05513.
MaxQBiQ05513.
PaxDbiQ05513.
PeptideAtlasiQ05513.
PRIDEiQ05513.

Protocols and materials databases

DNASUi5590.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000378567; ENSP00000367830; ENSG00000067606. [Q05513-1]
ENST00000400921; ENSP00000383712; ENSG00000067606. [Q05513-2]
ENST00000461106; ENSP00000426412; ENSG00000067606. [Q05513-3]
GeneIDi5590.
KEGGihsa:5590.
UCSCiuc001aiq.3. human. [Q05513-1]

Organism-specific databases

CTDi5590.
DisGeNETi5590.
GeneCardsiPRKCZ.
H-InvDBHIX0000049.
HIX0029201.
HGNCiHGNC:9412. PRKCZ.
HPAiCAB004533.
HPA021851.
MIMi176982. gene.
neXtProtiNX_Q05513.
OpenTargetsiENSG00000067606.
PharmGKBiPA33775.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0695. Eukaryota.
ENOG410ZMG2. LUCA.
GeneTreeiENSGT00820000126964.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiQ05513.
KOiK18952.
OMAiRCHVLVP.
OrthoDBiEOG091G03Q9.
PhylomeDBiQ05513.
TreeFamiTF102004.

Enzyme and pathway databases

BioCyciZFISH:HS00913-MONOMER.
BRENDAi2.7.11.13. 2681.
ReactomeiR-HSA-114604. GPVI-mediated activation cascade.
R-HSA-2173791. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
R-HSA-5218921. VEGFR2 mediated cell proliferation.
SignaLinkiQ05513.
SIGNORiQ05513.

Miscellaneous databases

ChiTaRSiPRKCZ. human.
GeneWikiiProtein_kinase_M_zeta/Protein_kinase_C_zeta.
GenomeRNAii5590.
PMAP-CutDBQ05513.
PROiQ05513.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000067606.
CleanExiHS_PRKCZ.
ExpressionAtlasiQ05513. baseline and differential.
GenevisibleiQ05513. HS.

Family and domain databases

CDDicd00029. C1. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR000270. PB1_dom.
IPR002219. PE/DAG-bd.
IPR012233. PKC.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00130. C1_1. 1 hit.
PF00564. PB1. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000554. PKC_zeta. 1 hit.
PRINTSiPR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 1 hit.
SM00666. PB1. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS51745. PB1. 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. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKPCZ_HUMAN
AccessioniPrimary (citable) accession number: Q05513
Secondary accession number(s): A8K4N0
, A8MU64, B7Z2J7, E9PCW2, Q15207, Q5SYT5, Q969S4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: June 21, 2005
Last modified: November 30, 2016
This is version 196 of the entry and version 4 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. 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.