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Reviewed, UniProtKB/Swiss-Prot Q05513 (KPCZ_HUMAN)

Last modified February 9, 2010. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Protein kinase C zeta type
    EC=2.7.11.13
Alternative name(s):
    nPKC-zeta
Gene names
Name: PRKCZ
Synonyms: PKC2
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length592 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

This is a calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme.

PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters. Subunit of a quaternary complex that plays a central role in epithelial cell polarization.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Phosphatidylinositol 3,4,5-trisphosphate might be a physiological activator. Two specific sites, Thr-410 (activation loop of the kinase domain) and Thr-560 (turn motif), need to be phosphorylated for its full activation.

Subunit structure

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. Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14

Subcellular location

Cytoplasm. Endosome. Note: In the retina, localizes in the terminals of the rod bipolar cells By similarity. Associates with endosomes. Ref.7

Tissue specificity

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

Domain

The OPR domain mediates mutually exclusive interactions with SQSTM1 and PARD6B. Ref.14

The C1 domain does not bind the diacylglycerol (DAG). Ref.14

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 OPR domain.

Contains 1 phorbol-ester/DAG-type zinc finger.

Contains 1 protein kinase domain.

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

PARD6BQ9BYG51EBI-295351,EBI-295391
PRKCQQ047592EBI-295351,EBI-374762

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 592592Protein kinase C zeta type
PRO_0000055701

Regions

Domain15 – 9884OPR
Domain252 – 518267Protein kinase
Domain519 – 59072AGC-kinase C-terminal
Zinc finger130 – 18051Phorbol-ester/DAG-type
Nucleotide binding258 – 2669ATP By similarity
Region79 – 14567Interaction with SQSTM1 By similarity

Sites

Active site3761Proton acceptor By similarity
Binding site2811ATP By similarity

Amino acid modifications

Modified residue2231Phosphoserine Ref.15
Modified residue4101Phosphothreonine; by PDPK1 Ref.8 Ref.16
Modified residue5601Phosphothreonine Ref.17

Natural variations

Natural variant491R → H: dbSNP rs35271800.
VAR_050560
Natural variant841R → H: dbSNP rs56017162. Ref.20
VAR_042310
Natural variant5141S → F in a colorectal cancer sample; somatic mutation. Ref.19
VAR_035467
Natural variant5191R → C in a colorectal adenocarcinoma sample; somatic mutation. Ref.20
VAR_042311

Experimental info

Mutagenesis191K → A: No effect on interaction with SQSTM1 and PARD6B. Ref.14
Mutagenesis621D → A: Loss of interaction with SQSTM1 and PARD6B. Ref.14
Mutagenesis661D → A: Loss of interaction with SQSTM1 and PARD6B. Ref.14
Sequence conflict61G → D in AAA36488. Ref.1
Sequence conflict1981K → R in BAF83684. Ref.3
Sequence conflict2621S → T in AAA36488. Ref.1
Sequence conflict3661F → L in BAF83684. Ref.3
Sequence conflict5001R → G in BAF83684. Ref.3
Sequence conflict5221D → G in BAF83684. Ref.3

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Sequences

Sequence LengthMass (Da)Tools
Q05513-1 [UniParc].

Last modified June 21, 2005. Version 4.
Checksum: 88CCD0577E6A596C

FASTA59267,660
        10         20         30         40         50         60 
MPSRTGPKME GSGGRVRLKA HYGGDIFITS VDAATTFEEL CEEVRDMCRL HQQHPLTLKW 

        70         80         90        100        110        120 
VDSEGDPCTV SSQMELEEAF RLARQCRDEG LIIHVFPSTP EQPGLPCPGE DKSIYRRGAR 

       130        140        150        160        170        180 
RWRKLYRANG HLFQAKRFNR RAYCGQCSER IWGLARQGYR CINCKLLVHK RCHGLVPLTC 

       190        200        210        220        230        240 
RKHMDSVMPS QEPPVDDKNE DADLPSEETD GIAYISSSRK HDSIKDDSED LKPVIDGMDG 

       250        260        270        280        290        300 
IKISQGLGLQ DFDLIRVIGR GSYAKVLLVR LKKNDQIYAM KVVKKELVHD DEDIDWVQTE 

       310        320        330        340        350        360 
KHVFEQASSN PFLVGLHSCF QTTSRLFLVI EYVNGGDLMF HMQRQRKLPE EHARFYAAEI 

       370        380        390        400        410        420 
CIALNFLHER GIIYRDLKLD NVLLDADGHI KLTDYGMCKE GLGPGDTTST FCGTPNYIAP 

       430        440        450        460        470        480 
EILRGEEYGF SVDWWALGVL MFEMMAGRSP FDIITDNPDM NTEDYLFQVI LEKPIRIPRF 

       490        500        510        520        530        540 
LSVKASHVLK GFLNKDPKER LGCRPQTGFS DIKSHAFFRS IDWDLLEKKQ ALPPFQPQIT 

       550        560        570        580        590 
DDYGLDNFDT QFTSEPVQLT PDDEDAIKRI DQSEFEGFEY INPLLLSTEE SV

« Hide

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References

« Hide 'large scale' references
[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: 8224878] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
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].
[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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: 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. expand/collapse author list , 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: 16710414] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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: 8375396] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-592.
Tissue: Hippocampus.
[7]"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: 9566925] [Abstract]
Cited for: INTERACTION WITH SQSTM1, SUBCELLULAR LOCATION.
[8]"Regulation of protein kinase C zeta by PI 3-kinase and PDK-1."
Chou M.M., Hou W., Johnson J., Graham L.K., Lee M.H., Chen C.S., Newton A.C., Schaffhausen B.S., Toker A.
Curr. Biol. 8:1069-1077(1998) [PubMed: 9768361] [Abstract]
Cited for: PHOSPHORYLATION AT THR-410 BY PDPK1.
[9]"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: 10356400] [Abstract]
Cited for: INTERACTION WITH SQSTM1 AND IKBKB.
[10]"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: 11260256] [Abstract]
Cited for: INTERACTION WITH PARD6A; PARD6B AND PARD6G.
Tissue: Neuroblastoma.
[11]"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: 11755531] [Abstract]
Cited for: INTERACTION WITH SQSTM1 AND PAWR.
[12]"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: 12234671] [Abstract]
Cited for: INTERACTION WITH PARD3.
[13]"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: 12893243] [Abstract]
Cited for: INTERACTION WITH ADAP1.
[14]"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: 12887891] [Abstract]
Cited for: INTERACTION WITH SQSTM1 AND PARD6B, DOMAIN, MUTAGENESIS OF LYS-19; ASP-62 AND ASP-66.
[15]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, MASS SPECTROMETRY.
Tissue: Epithelium.
[16]"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: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-410, MASS SPECTROMETRY.
[17]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-560, MASS SPECTROMETRY.
[18]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[19]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] PHE-514.
[20]"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. expand/collapse author list , 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: 17344846] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] HIS-84 AND CYS-519.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L14283 mRNA. Translation: AAA36488.1.
BT007082 mRNA. Translation: AAP35745.1.
AK290995 mRNA. Translation: BAF83684.1.
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.
IPIIPI00013749.
PIRJN0877.
RefSeqNP_001028753.1.
NP_001028754.1.
NP_002735.3.
UniGeneHs.496255

3D structure databases

SMRQ05513. Positions 12-98, 109-181, 247-584.
ModBaseSearch...

Protein-protein interaction databases

IntActQ05513. 6 interactions.
STRINGQ05513.

PTM databases

PhosphoSiteQ05513.

Proteomic databases

PRIDEQ05513.

Genome annotation databases

EnsemblENST00000378567; ENSP00000367830; ENSG00000067606; Homo sapiens. [Genome view]
GeneID5590.
KEGGhsa:5590.
UCSCuc001aiq.1. human.

Organism-specific databases

CTD5590.
GeneCardsGC01P001939.
H-InvDBHIX0000046.
HGNCHGNC:9412. PRKCZ.
HPACAB004533.
HPA021851.
MIM176982. gene.
PharmGKBPA33775.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG08632.
HOGENOMHBG755340.
HOVERGENQ05513.
InParanoidQ05513.
OMAAYISSTR.
OrthoDBEOG93N9ZG.
PhylomeDBQ05513.

Enzyme and pathway databases

BRENDA2.7.11.13. 247.
Pathway_Interaction_DBamb2_neutrophils_pathway. amb2 Integrin signaling.
ceramidepathway. Ceramide signaling pathway.
igf1_pathway. IGF1 pathway.
il1pathway. IL1-mediated signaling events.
il2_pi3kpathway. IL2 signaling events mediated by PI3K.
insulin_pathway. Insulin Pathway.
insulin_glucose_pathway. Insulin-mediated glucose transport.
trkrpathway. Neurotrophic factor-mediated Trk receptor signaling.
p75ntrpathway. p75(NTR)-mediated signaling.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.
txa2pathway. Thromboxane A2 receptor signaling.
tnfpathway. TNF receptor signaling pathway.
ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressQ05513.
BgeeQ05513.
CleanExHS_PRKCZ.
GenevestigatorQ05513.
GermOnlineENSG00000067606. Homo sapiens.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR020454. DAG/PE_bd.
IPR011009. Kinase-like_dom.
IPR000270. OPR_PB1.
IPR015745. PKC.
IPR012233. PKC_zeta.
IPR017892. Pkinase_C.
IPR002219. Prot_Kinase_C-like_PE/DAG_bd.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR002290. Ser/Thr_prot_kinase_dom.
[Graphical view]
PANTHERPTHR22985:SF86. PKC. 1 hit.
PfamPF00130. C1_1. 1 hit.
PF00564. PB1. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFPIRSF000554. PKC_zeta. 1 hit.
PRINTSPR00008. DAGPEDOMAIN.
SMARTSM00109. C1. 1 hit.
SM00666. PB1. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS51285. 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]
ProtoNetSearch...

Other Resources

BindingDBQ05513.
NextBio21684.
PMAP-CutDBQ05513.
SOURCESearch...

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Entry information

Entry nameKPCZ_HUMAN
AccessionPrimary (citable) accession number: Q05513
Secondary accession number(s): A8K4N0 expand/collapse secondary AC list , Q15207, Q5SYT5, Q969S4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: June 21, 2005
Last modified: February 9, 2010
This is version 121 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents