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Q05513

- KPCZ_HUMAN

UniProt

Q05513 - KPCZ_HUMAN

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
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    • History
      Entry version 172 (01 Oct 2014)
      Sequence version 4 (21 Jun 2005)
      Previous versions | rss
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    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 binding Source: UniProtKB
    5. protein kinase activity Source: UniProtKB
    6. protein kinase C activity Source: UniProtKB-EC
    7. protein serine/threonine kinase activity Source: BHF-UCL
    8. 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. peptidyl-serine phosphorylation Source: BHF-UCL
    19. platelet activation Source: Reactome
    20. positive regulation of cell-matrix adhesion Source: Ensembl
    21. positive regulation of cell proliferation Source: Ensembl
    22. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    23. positive regulation of excitatory postsynaptic membrane potential Source: UniProtKB
    24. positive regulation of glucose import Source: Ensembl
    25. positive regulation of insulin receptor signaling pathway Source: UniProtKB
    26. positive regulation of interleukin-10 secretion Source: UniProtKB
    27. positive regulation of interleukin-13 secretion Source: UniProtKB
    28. positive regulation of interleukin-4 production Source: UniProtKB
    29. positive regulation of interleukin-5 secretion Source: UniProtKB
    30. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    31. positive regulation of T-helper 2 cell cytokine production Source: UniProtKB
    32. positive regulation of T-helper 2 cell differentiation Source: UniProtKB
    33. protein heterooligomerization Source: Ensembl
    34. protein kinase C signaling Source: Ensembl
    35. protein localization to plasma membrane Source: Ensembl
    36. protein phosphorylation Source: UniProtKB
    37. signal transduction Source: ProtInc
    38. transforming growth factor beta receptor signaling pathway Source: Reactome
    39. vesicle transport along microtubule Source: Ensembl

    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.
    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. cell-cell junction Source: UniProtKB
    4. cell junction Source: Reactome
    5. cell leading edge Source: Ensembl
    6. cytoplasm Source: ProtInc
    7. cytosol Source: Ensembl
    8. endosome Source: UniProtKB-SubCell
    9. extracellular vesicular exosome Source: UniProt
    10. membrane Source: ProtInc
    11. membrane raft Source: Ensembl
    12. myelin sheath abaxonal region Source: Ensembl
    13. nuclear envelope Source: Ensembl
    14. nuclear matrix Source: Ensembl
    15. perinuclear region of cytoplasm Source: Ensembl
    16. plasma membrane Source: ProtInc
    17. protein complex Source: Ensembl
    18. tight junction Source: Ensembl

    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 PI3K4 Publications
    Modified residuei560 – 5601Phosphothreonine2 Publications

    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

    ArrayExpressiQ05513.
    BgeeiQ05513.
    CleanExiHS_PRKCZ.
    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
    PARD6BQ9BYG53EBI-295351,EBI-295391
    PARD6GQ9BYG42EBI-295351,EBI-295417
    PRKCIP417432EBI-295351,EBI-286199
    PRKCQQ047593EBI-295351,EBI-374762
    VHLP403373EBI-295351,EBI-301246

    Protein-protein interaction databases

    BioGridi111576. 74 interactions.
    IntActiQ05513. 27 interactions.
    MINTiMINT-5004464.
    STRINGi9606.ENSP00000367830.

    Structurei

    3D structure databases

    ProteinModelPortaliQ05513.
    SMRiQ05513. Positions 13-182, 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.
    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.
    IPR012233. PKC_zeta.
    IPR017892. Pkinase_C.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    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

    MPSRTGPKME GSGGRVRLKA HYGGDIFITS VDAATTFEEL CEEVRDMCRL    50
    HQQHPLTLKW VDSEGDPCTV SSQMELEEAF RLARQCRDEG LIIHVFPSTP 100
    EQPGLPCPGE DKSIYRRGAR RWRKLYRANG HLFQAKRFNR RAYCGQCSER 150
    IWGLARQGYR CINCKLLVHK RCHGLVPLTC RKHMDSVMPS QEPPVDDKNE 200
    DADLPSEETD GIAYISSSRK HDSIKDDSED LKPVIDGMDG IKISQGLGLQ 250
    DFDLIRVIGR GSYAKVLLVR LKKNDQIYAM KVVKKELVHD DEDIDWVQTE 300
    KHVFEQASSN PFLVGLHSCF QTTSRLFLVI EYVNGGDLMF HMQRQRKLPE 350
    EHARFYAAEI CIALNFLHER GIIYRDLKLD NVLLDADGHI KLTDYGMCKE 400
    GLGPGDTTST FCGTPNYIAP EILRGEEYGF SVDWWALGVL MFEMMAGRSP 450
    FDIITDNPDM NTEDYLFQVI LEKPIRIPRF LSVKASHVLK GFLNKDPKER 500
    LGCRPQTGFS DIKSHAFFRS IDWDLLEKKQ ALPPFQPQIT DDYGLDNFDT 550
    QFTSEPVQLT PDDEDAIKRI DQSEFEGFEY INPLLLSTEE SV 592
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 13-182, 216-584.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111576. 74 interactions.
    IntActi Q05513. 27 interactions.
    MINTi MINT-5004464.
    STRINGi 9606.ENSP00000367830.

    Chemistry

    BindingDBi Q05513.
    ChEMBLi CHEMBL3438.
    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.
    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.
    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

    ArrayExpressi Q05513.
    Bgeei Q05513.
    CleanExi HS_PRKCZ.
    Genevestigatori Q05513.

    Family and domain databases

    InterProi IPR000961. AGC-kinase_C.
    IPR020454. DAG/PE-bd.
    IPR011009. Kinase-like_dom.
    IPR000270. OPR_PB1.
    IPR012233. PKC_zeta.
    IPR017892. Pkinase_C.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 172 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

    Dasty 3