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Q05513

- KPCZ_HUMAN

UniProt

Q05513 - KPCZ_HUMAN

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Protein

Protein kinase C zeta type

Gene

PRKCZ

Organism
Homo sapiens (Human)
Status
Reviewed - 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.6 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei281 – 2811ATPPROSITE-ProRule annotation
Active sitei376 – 3761Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri130 – 18051Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi258 – 2669ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. insulin receptor substrate binding Source: BHF-UCL
  3. potassium channel regulator activity Source: Ensembl
  4. protein kinase activity Source: UniProtKB
  5. protein kinase C activity Source: UniProtKB-EC
  6. protein serine/threonine kinase activity Source: BHF-UCL
  7. zinc ion binding Source: InterPro

GO - Biological processi

  1. actin cytoskeleton reorganization Source: Ensembl
  2. activation of phospholipase D activity Source: Ensembl
  3. activation of protein kinase B activity Source: Ensembl
  4. blood coagulation Source: Reactome
  5. cell migration Source: Ensembl
  6. establishment of cell polarity Source: UniProtKB
  7. inflammatory response Source: UniProtKB-KW
  8. insulin receptor signaling pathway Source: Ensembl
  9. long-term memory Source: Ensembl
  10. long-term synaptic potentiation Source: UniProtKB
  11. membrane hyperpolarization Source: Ensembl
  12. microtubule cytoskeleton organization Source: Ensembl
  13. negative regulation of apoptotic process Source: ProtInc
  14. negative regulation of hydrolase activity Source: Ensembl
  15. negative regulation of insulin receptor signaling pathway Source: BHF-UCL
  16. negative regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  17. negative regulation of protein complex assembly Source: BHF-UCL
  18. neuron projection extension Source: Ensembl
  19. peptidyl-serine phosphorylation Source: BHF-UCL
  20. platelet activation Source: Reactome
  21. positive regulation of cell-matrix adhesion Source: Ensembl
  22. positive regulation of cell proliferation Source: Ensembl
  23. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  24. positive regulation of excitatory postsynaptic membrane potential Source: UniProtKB
  25. positive regulation of glucose import Source: Ensembl
  26. positive regulation of insulin receptor signaling pathway Source: UniProtKB
  27. positive regulation of interleukin-10 secretion Source: UniProtKB
  28. positive regulation of interleukin-13 secretion Source: UniProtKB
  29. positive regulation of interleukin-4 production Source: UniProtKB
  30. positive regulation of interleukin-5 secretion Source: UniProtKB
  31. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  32. positive regulation of T-helper 2 cell cytokine production Source: UniProtKB
  33. positive regulation of T-helper 2 cell differentiation Source: UniProtKB
  34. protein heterooligomerization Source: Ensembl
  35. protein kinase C signaling Source: Ensembl
  36. protein localization to plasma membrane Source: Ensembl
  37. protein phosphorylation Source: UniProtKB
  38. signal transduction Source: ProtInc
  39. transforming growth factor beta receptor signaling pathway Source: Reactome
  40. vesicle transport along microtubule Source: Ensembl
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

BRENDAi2.7.11.13. 2681.
ReactomeiREACT_120726. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
REACT_1695. GPVI-mediated activation cascade.
REACT_228024. VEGFR2 mediated cell proliferation.
SignaLinkiQ05513.

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
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:9412. PRKCZ.

Subcellular locationi

Cytoplasm. Endosome. Cell junction
Note: In the retina, localizes in the terminals of the rod bipolar cells (By similarity). Associates with endosomes. Presence of KRIT1, CDH5 and RAP1B is required for its localization to the cell junction.By similarity

GO - Cellular componenti

  1. apical cortex Source: Ensembl
  2. apical plasma membrane Source: Ensembl
  3. axon hillock Source: Ensembl
  4. cell-cell junction Source: UniProtKB
  5. cell junction Source: Reactome
  6. cell leading edge Source: Ensembl
  7. cytoplasm Source: ProtInc
  8. cytosol Source: Ensembl
  9. endosome Source: UniProtKB-KW
  10. extracellular vesicular exosome Source: UniProt
  11. membrane Source: ProtInc
  12. membrane raft Source: Ensembl
  13. microtubule organizing center Source: Ensembl
  14. myelin sheath abaxonal region Source: Ensembl
  15. nuclear envelope Source: Ensembl
  16. nuclear matrix Source: Ensembl
  17. perinuclear region of cytoplasm Source: Ensembl
  18. plasma membrane Source: ProtInc
  19. protein complex Source: Ensembl
  20. tight junction Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Endosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi19 – 191K → A: No effect on interaction with SQSTM1 and PARD6B. 1 Publication
Mutagenesisi62 – 621D → A: Loss of interaction with SQSTM1 and PARD6B. 1 Publication
Mutagenesisi66 – 661D → A: Loss of interaction with SQSTM1 and PARD6B. 1 Publication

Organism-specific databases

PharmGKBiPA33775.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 592592Protein kinase C zeta typePRO_0000055701Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei410 – 4101Phosphothreonine; by PDPK1 and PI3K3 Publications
Modified residuei560 – 5601Phosphothreonine1 Publication

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.5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ05513.
PaxDbiQ05513.
PRIDEiQ05513.

PTM databases

PhosphoSiteiQ05513.

Miscellaneous databases

PMAP-CutDBQ05513.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ05513.
CleanExiHS_PRKCZ.
ExpressionAtlasiQ05513. baseline and differential.
GenevestigatoriQ05513.

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).By similarity10 PublicationsCurated

Binary interactionsi

WithEntry#Exp.IntActNotes
AKT1P317492EBI-295351,EBI-296087
F11RQ9Y6242EBI-295351,EBI-742600
HSP90AB1P082382EBI-295351,EBI-352572
NUMBP49757-14EBI-295351,EBI-7199607
numbP165542EBI-295351,EBI-429581From a different organism.
PARD6AQ9NPB66EBI-295351,EBI-81876
PARD6BQ9BYG54EBI-295351,EBI-295391
PARD6GQ9BYG42EBI-295351,EBI-295417
PRKCIP417432EBI-295351,EBI-286199
PRKCQQ047593EBI-295351,EBI-374762
VHLP403373EBI-295351,EBI-301246

Protein-protein interaction databases

BioGridi111576. 75 interactions.
IntActiQ05513. 28 interactions.
MINTiMINT-5004464.
STRINGi9606.ENSP00000367830.

Structurei

3D structure databases

ProteinModelPortaliQ05513.
SMRiQ05513. Positions 15-182, 216-584.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 9884OPRAdd
BLAST
Domaini252 – 518267Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini519 – 59072AGC-kinase C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni79 – 14567Interaction with SQSTM1By similarityAdd
BLAST

Domaini

The OPR domain mediates 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 OPR domain.Curated
Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri130 – 18051Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00770000120449.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiQ05513.
KOiK06069.
OMAiRCHVLVP.
OrthoDBiEOG7HF1J3.
PhylomeDBiQ05513.
TreeFamiTF102004.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR000270. OPR_PB1.
IPR002219. PE/DAG-bd.
IPR012233. PKC_zeta.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24357:SF60. PTHR24357:SF60. 1 hit.
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.
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. Align

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 CAA78813.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61G → D in AAA36488. (PubMed:8224878)Curated
Sequence conflicti198 – 1981K → R in BAF83684. (PubMed:14702039)Curated
Sequence conflicti262 – 2621S → T in AAA36488. (PubMed:8224878)Curated
Sequence conflicti281 – 2811K → R in BAH11883. (PubMed:14702039)Curated
Sequence conflicti366 – 3661F → L in BAF83684. (PubMed:14702039)Curated
Sequence conflicti500 – 5001R → G in BAF83684. (PubMed:14702039)Curated
Sequence conflicti522 – 5221D → G in BAF83684. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti49 – 491R → H.
Corresponds to variant rs35271800 [ dbSNP | Ensembl ].
VAR_050560
Natural varianti84 – 841R → H.1 Publication
Corresponds to variant rs56017162 [ dbSNP | Ensembl ].
VAR_042310
Natural varianti514 – 5141S → F in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035467
Natural varianti519 – 5191R → C in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_042311

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 183183Missing in isoform 2. 1 PublicationVSP_041904Add
BLAST
Alternative sequencei1 – 112112MPSRT…PGEDK → MLTPRTDE in isoform 3. 1 PublicationVSP_046347Add
BLAST

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_006710830.1. XM_006710767.1. [Q05513-2]
UniGeneiHs.496255.

Genome annotation databases

EnsembliENST00000378567; ENSP00000367830; ENSG00000067606. [Q05513-1]
ENST00000400920; ENSP00000383711; ENSG00000067606. [Q05513-2]
ENST00000400921; ENSP00000383712; ENSG00000067606. [Q05513-2]
ENST00000461106; ENSP00000426412; ENSG00000067606. [Q05513-3]
GeneIDi5590.
KEGGihsa:5590.
UCSCiuc001aiq.3. human. [Q05513-1]
uc001ait.3. human. [Q05513-2]

Polymorphism databases

DMDMi68067736.

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.
CCDSi CCDS37.1. [Q05513-1 ]
CCDS41229.1. [Q05513-2 ]
CCDS55563.1. [Q05513-3 ]
PIRi JN0877.
RefSeqi NP_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_006710830.1. XM_006710767.1. [Q05513-2 ]
UniGenei Hs.496255.

3D structure databases

ProteinModelPortali Q05513.
SMRi Q05513. Positions 15-182, 216-584.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111576. 75 interactions.
IntActi Q05513. 28 interactions.
MINTi MINT-5004464.
STRINGi 9606.ENSP00000367830.

Chemistry

BindingDBi Q05513.
ChEMBLi CHEMBL3438.
DrugBanki DB00675. Tamoxifen.
GuidetoPHARMACOLOGYi 1491.

PTM databases

PhosphoSitei Q05513.

Polymorphism databases

DMDMi 68067736.

Proteomic databases

MaxQBi Q05513.
PaxDbi Q05513.
PRIDEi Q05513.

Protocols and materials databases

DNASUi 5590.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000378567 ; ENSP00000367830 ; ENSG00000067606 . [Q05513-1 ]
ENST00000400920 ; ENSP00000383711 ; ENSG00000067606 . [Q05513-2 ]
ENST00000400921 ; ENSP00000383712 ; ENSG00000067606 . [Q05513-2 ]
ENST00000461106 ; ENSP00000426412 ; ENSG00000067606 . [Q05513-3 ]
GeneIDi 5590.
KEGGi hsa:5590.
UCSCi uc001aiq.3. human. [Q05513-1 ]
uc001ait.3. human. [Q05513-2 ]

Organism-specific databases

CTDi 5590.
GeneCardsi GC01P001982.
H-InvDB HIX0000049.
HIX0029201.
HGNCi HGNC:9412. PRKCZ.
HPAi CAB004533.
HPA021851.
MIMi 176982. gene.
neXtProti NX_Q05513.
PharmGKBi PA33775.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00770000120449.
HOGENOMi HOG000233033.
HOVERGENi HBG108317.
InParanoidi Q05513.
KOi K06069.
OMAi RCHVLVP.
OrthoDBi EOG7HF1J3.
PhylomeDBi Q05513.
TreeFami TF102004.

Enzyme and pathway databases

BRENDAi 2.7.11.13. 2681.
Reactomei REACT_120726. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
REACT_1695. GPVI-mediated activation cascade.
REACT_228024. VEGFR2 mediated cell proliferation.
SignaLinki Q05513.

Miscellaneous databases

ChiTaRSi PRKCZ. human.
GeneWikii Protein_kinase_M_zeta/Protein_kinase_C_zeta.
GenomeRNAii 5590.
NextBioi 21684.
PMAP-CutDB Q05513.
PROi Q05513.
SOURCEi Search...

Gene expression databases

Bgeei Q05513.
CleanExi HS_PRKCZ.
ExpressionAtlasi Q05513. baseline and differential.
Genevestigatori Q05513.

Family and domain databases

InterProi IPR000961. AGC-kinase_C.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR000270. OPR_PB1.
IPR002219. PE/DAG-bd.
IPR012233. PKC_zeta.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
PANTHERi PTHR24357:SF60. PTHR24357:SF60. 1 hit.
Pfami PF00130. C1_1. 1 hit.
PF00564. PB1. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF000554. PKC_zeta. 1 hit.
PRINTSi PR00008. DAGPEDOMAIN.
SMARTi SM00109. C1. 1 hit.
SM00666. PB1. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS51285. 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. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
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Publicationsi

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  1. "The cDNA sequence encoding human protein kinase C-zeta."
    Barbee J.L., Loomis C.R., Deutscher S.L., Burns D.J.
    Gene 132:305-306(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Frontal cortex.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "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] (ISOFORMS 1; 2 AND 3).
    Tissue: Brain and Teratocarcinoma.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Colon and Ovary.
  6. "Activation and substrate specificity of the human protein kinase C alpha and zeta isoenzymes."
    Kochs G., Hummel R., Meyer D., Hug H., Marme D., Sarre T.F.
    Eur. J. Biochem. 216:597-606(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-592.
    Tissue: Hippocampus.
  7. "Activation of the mitogen-activated protein kinase/extracellular signal-regulated kinase pathway by conventional, novel, and atypical protein kinase C isotypes."
    Schoenwasser D.C., Marais R.M., Marshall C.J., Parker P.J.
    Mol. Cell. Biol. 18:790-798(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACTIVATION OF MAP2K1/MEK1 AND MAPK1/ERK2.
  8. "Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62."
    Sanchez P., De Carcer G., Sandoval I.V., Moscat J., Diaz-Meco M.T.
    Mol. Cell. Biol. 18:3069-3080(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SQSTM1, SUBCELLULAR LOCATION.
  9. Cited for: PHOSPHORYLATION AT THR-410 BY PDPK1.
  10. "The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation."
    Sanz L., Sanchez P., Lallena M.-J., Diaz-Meco M.T., Moscat J.
    EMBO J. 18:3044-3053(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SQSTM1 AND IKBKB.
  11. "Protein kinase C zeta plays a central role in activation of the p42/44 mitogen-activated protein kinase by endotoxin in alveolar macrophages."
    Monick M.M., Carter A.B., Flaherty D.M., Peterson M.W., Hunninghake G.W.
    J. Immunol. 165:4632-4639(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACTIVATION OF MAPK1/ERK2.
  12. "Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C."
    Noda Y., Takeya R., Ohno S., Naito S., Ito T., Sumimoto H.
    Genes Cells 6:107-119(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PARD6A; PARD6B AND PARD6G.
    Tissue: Neuroblastoma.
  13. "Regulation of both PDK1 and the phosphorylation of PKC-zeta and -delta by a C-terminal PRK2 fragment."
    Hodgkinson C.P., Sale G.J.
    Biochemistry 41:561-569(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDPK1, PHOSPHORYLATION.
  14. "Characterization of PDK2 activity against protein kinase B gamma."
    Hodgkinson C.P., Sale E.M., Sale G.J.
    Biochemistry 41:10351-10359(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACTIVATION OF AKT3.
  15. "p62 forms a ternary complex with PKCzeta and PAR-4 and antagonizes PAR-4-induced PKCzeta inhibition."
    Chang S., Kim J.H., Shin J.
    FEBS Lett. 510:57-61(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SQSTM1 AND PAWR.
  16. "Multiple splice variants of Par3 and of a novel related gene, Par3L, produce proteins with different binding properties."
    Gao L., Macara I.G., Joberty G.
    Gene 294:99-107(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PARD3.
  17. "Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C."
    Zemlickova E., Dubois T., Kerai P., Clokie S., Cronshaw A.D., Wakefield R.I.D., Johannes F.-J., Aitken A.
    Biochem. Biophys. Res. Commun. 307:459-465(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ADAP1.
  18. "PB1 domain-mediated heterodimerization in NADPH oxidase and signaling complexes of atypical protein kinase C with Par6 and p62."
    Wilson M.I., Gill D.J., Perisic O., Quinn M.T., Williams R.L.
    Mol. Cell 12:39-50(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SQSTM1 AND PARD6B, DOMAIN, MUTAGENESIS OF LYS-19; ASP-62 AND ASP-66.
  19. "Atypical PKC phosphorylates PAR-1 kinases to regulate localization and activity."
    Hurov J.B., Watkins J.L., Piwnica-Worms H.
    Curr. Biol. 14:736-741(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF MARK2 AND MARK3.
  20. "aPKC acts upstream of PAR-1b in both the establishment and maintenance of mammalian epithelial polarity."
    Suzuki A., Hirata M., Kamimura K., Maniwa R., Yamanaka T., Mizuno K., Kishikawa M., Hirose H., Amano Y., Izumi N., Miwa Y., Ohno S.
    Curr. Biol. 14:1425-1435(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF MARK2.
  21. "Role of atypical protein kinase C in estradiol-triggered G1/S progression of MCF-7 cells."
    Castoria G., Migliaccio A., Di Domenico M., Lombardi M., de Falco A., Varricchio L., Bilancio A., Barone M.V., Auricchio F.
    Mol. Cell. Biol. 24:7643-7653(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-410 BY PI3K.
  22. "KIBRA interacts with discoidin domain receptor 1 to modulate collagen-induced signalling."
    Hilton H.N., Stanford P.M., Harris J., Oakes S.R., Kaplan W., Daly R.J., Ormandy C.J.
    Biochim. Biophys. Acta 1783:383-393(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WWC1 AND DDR1.
  23. "Protein kinase Czeta-dependent LKB1 serine 428 phosphorylation increases LKB1 nucleus export and apoptosis in endothelial cells."
    Song P., Xie Z., Wu Y., Xu J., Dong Y., Zou M.H.
    J. Biol. Chem. 283:12446-12455(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF STK11.
  24. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  25. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-560, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  26. "CCM1 regulates vascular-lumen organization by inducing endothelial polarity."
    Lampugnani M.G., Orsenigo F., Rudini N., Maddaluno L., Boulday G., Chapon F., Dejana E.
    J. Cell Sci. 123:1073-1080(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, SUBUNIT, PHOSPHORYLATION AT THR-410.
  27. "Protein kinase Czeta (PKCzeta): activation mechanisms and cellular functions."
    Hirai T., Chida K.
    J. Biochem. 133:1-7(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  28. Cited for: REVIEW ON FUNCTION.
  29. "PKCzeta at the crossroad of NF-kappaB and Jak1/Stat6 signaling pathways."
    Moscat J., Rennert P., Diaz-Meco M.T.
    Cell Death Differ. 13:702-711(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  30. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. Cited for: VARIANT [LARGE SCALE ANALYSIS] PHE-514.
  32. "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] HIS-84 AND CYS-519.

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 26, 2014
This is version 174 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

External Data

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