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UniProtKB/Swiss-Prot entry Q05513


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name KPCZ_HUMAN
Primary accession number Q05513
Secondary accession numbers Q15207 Q5SYT5 Q969S4
Integrated into Swiss-Prot on February 1, 1994
Sequence was last modified on June 21, 2005 (Sequence version 4)
Annotations were last modified on    June 16, 2009 (Entry version 111)
Name and origin of the protein
Protein name Protein kinase C zeta type
Synonyms EC 2.7.11.13
nPKC-zeta
Gene name
Name: PRKCZ
Synonyms: PKC2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] OF 7-592.
TISSUE=Hippocampus;
DOI=10.1111/j.1432-1033.1993.tb18179.x; PubMed=8375396 [NCBI, ExPASy, EBI, Israel, Japan]
Kochs G., Hummel R., Meyer D., Hug H., Marme D., Sarre T.F.;
"Activation and substrate specificity of the human protein kinase C alpha and zeta isoenzymes.";
Eur. J. Biochem. 216:597-606(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Frontal cortex;
DOI=10.1016/0378-1119(93)90213-M; PubMed=8224878 [NCBI, ExPASy, EBI, Israel, Japan]
Barbee J.L., Loomis C.R., Deutscher S.L., Burns D.J.;
"The cDNA sequence encoding human protein kinase C-zeta.";
Gene 132:305-306(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon, and Ovary;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INTERACTION WITH SQSTM1, AND SUBCELLULAR LOCATION.
PubMed=9566925 [NCBI, ExPASy, EBI, Israel, Japan]
Sanchez P., De Carcer G., Sandoval I.V., Moscat J., Diaz-Meco M.T.;
"Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62.";
Mol. Cell. Biol. 18:3069-3080(1998).
[7]
PHOSPHORYLATION AT THR-410 BY PDPK1.
DOI=10.1016/S0960-9822(98)70444-0; PubMed=9768361 [NCBI, ExPASy, EBI, Israel, Japan]
Chou M.M., Hou W., Johnson J., Graham L.K., Lee M.H., Chen C.S., Newton A.C., Schaffhausen B.S., Toker A.;
"Regulation of protein kinase C zeta by PI 3-kinase and PDK-1.";
Curr. Biol. 8:1069-1077(1998).
[8]
INTERACTION WITH SQSTM1 AND IKBKB.
DOI=10.1093/emboj/18.11.3044; PubMed=10356400 [NCBI, ExPASy, EBI, Israel, Japan]
Sanz L., Sanchez P., Lallena M.-J., Diaz-Meco M.T., Moscat J.;
"The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation.";
EMBO J. 18:3044-3053(1999).
[9]
INTERACTION WITH PARD6A; PARD6B AND PARD6G.
TISSUE=Neuroblastoma;
DOI=10.1046/j.1365-2443.2001.00404.x; PubMed=11260256 [NCBI, ExPASy, EBI, Israel, Japan]
Noda Y., Takeya R., Ohno S., Naito S., Ito T., Sumimoto H.;
"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.";
Genes Cells 6:107-119(2001).
[10]
INTERACTION WITH SQSTM1 AND PAWR.
DOI=10.1016/S0014-5793(01)03224-0; PubMed=11755531 [NCBI, ExPASy, EBI, Israel, Japan]
Chang S., Kim J.H., Shin J.;
"p62 forms a ternary complex with PKCzeta and PAR-4 and antagonizes PAR-4-induced PKCzeta inhibition.";
FEBS Lett. 510:57-61(2002).
[11]
INTERACTION WITH PARD3.
DOI=10.1016/S0378-1119(02)00681-9; PubMed=12234671 [NCBI, ExPASy, EBI, Israel, Japan]
Gao L., Macara I.G., Joberty G.;
"Multiple splice variants of Par3 and of a novel related gene, Par3L, produce proteins with different binding properties.";
Gene 294:99-107(2002).
[12]
INTERACTION WITH ADAP1.
DOI=10.1016/S0006-291X(03)01187-2; PubMed=12893243 [NCBI, ExPASy, EBI, Israel, Japan]
Zemlickova E., Dubois T., Kerai P., Clokie S., Cronshaw A.D., Wakefield R.I.D., Johannes F.-J., Aitken A.;
"Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C.";
Biochem. Biophys. Res. Commun. 307:459-465(2003).
[13]
INTERACTION WITH SQSTM1 AND PARD6B, DOMAIN, AND MUTAGENESIS OF LYS-19; ASP-62 AND ASP-66.
DOI=10.1016/S1097-2765(03)00246-6; PubMed=12887891 [NCBI, ExPASy, EBI, Israel, Japan]
Wilson M.I., Gill D.J., Perisic O., Quinn M.T., Williams R.L.;
"PB1 domain-mediated heterodimerization in NADPH oxidase and signaling complexes of atypical protein kinase C with Par6 and p62.";
Mol. Cell 12:39-50(2003).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-410, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-560, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[18]
VARIANT [LARGE SCALE ANALYSIS] PHE-514.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
[19]
VARIANTS [LARGE SCALE ANALYSIS] HIS-84 AND CYS-519.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z15108; CAA78813.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L14283; AAA36488.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT007082; AAP35745.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL590822; CAI12484.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL391845; CAI12484.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL645703; CAI12484.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL391845; CAI15438.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL590822; CAI15438.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL645703; CAI15438.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL645703; CAI21535.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL391845; CAI21535.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL590822; CAI21535.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008058; AAH08058.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC014270; AAH14270.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00013749; -.
PIR JN0877; JN0877.
RefSeq NP_001028753.1; -.
NP_001028754.1; -.
NP_002735.3; -.
UniGene Hs.496255
3D structure databases
HSSP P31751; 1GZK. [HSSP ENTRY / PDB]
ModBase Q05513.
Protein-protein interaction databases
IntAct Q05513; 4.
PTM databases
PhosphoSite Q05513; -.
Enzyme and pathway databases
BRENDA 2.7.11.13; 247.
Pathway_Interaction_DB amb2_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.
Organism-specific databases
GeneCards GC01P001939; -.
H-InvDB HIX0000046; -.
HGNC HGNC:9412; PRKCZ.
GenAtlas PRKCZ.
HPA CAB004533; -.
MIM 176982; gene. [NCBI / EBI]
PharmGKB PA33775; -.
Gene expression databases
ArrayExpress Q05513; -.
Bgee Q05513; -.
CleanEx HS_PRKCZ; -.
GermOnline ENSG00000067606; Homo sapiens.
Ontologies
GO
GO:0005768; Cellular component: endosome (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005624; Cellular component: membrane fraction (traceable author statement from ProtInc).
GO:0005886; Cellular component: plasma membrane (traceable author statement from ProtInc).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0019992; Molecular function: diacylglycerol binding (inferred from electronic annotation from UniProtKB-KW).
GO:0043560; Molecular function: insulin receptor substrate binding (inferred by curator from UniProtKB).
GO:0004697; Molecular function: protein kinase C activity (inferred from electronic annotation from EC).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006916; Biological process: anti-apoptosis (traceable author statement from ProtInc).
GO:0007242; Biological process: intracellular signaling cascade (inferred from electronic annotation from InterPro).
GO:0046627; Biological process: negative regulation of insulin receptor signaling pathway (inferred from mutant phenotype from UniProtKB).
GO:0050732; Biological process: negative regulation of peptidyl-tyrosine phosphorylation (inferred from mutant phenotype from UniProtKB).
GO:0031333; Biological process: negative regulation of protein complex assembly (inferred from mutant phenotype from UniProtKB).
GO:0018105; Biological process: peptidyl-serine phosphorylation (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000961; AGC-kinase_C.
IPR002219; DAG_PE_bd.
IPR000270; OPR_PB1.
IPR015745; PKC.
IPR012233; PKC_zeta.
IPR017892; Pkinase_C.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_BS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.
PANTHER PTHR22985:SF86; PKC; 1.
Pfam PF00130; C1_1; 1.
PF00564; PB1; 1.
PF00069; Pkinase; 1.
PF00433; Pkinase_C; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000554; PKC_zeta; 1.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00109; C1; 1.
SM00666; PB1; 1.
SM00133; S_TK_X; 1.
SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS51285; AGC_KINASE_CTER; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PS00479; ZF_DAG_PE_1; 1.
PS50081; ZF_DAG_PE_2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q05513; -.
Genome annotation databases
Ensembl ENSG00000067606; Homo sapiens. [Contig view]
GeneID 5590; -.
KEGG hsa:5590; -.
Phylogenomic databases
HOGENOM Q05513; -.
HOVERGEN Q05513; -.
OMA Q05513; RHMDSVM.
Other
BindingDB Q05513; -.
NextBio 21684; -.
PMAP-CutDB Q05513; -.
SOURCE PRKCZ; Homo sapiens.
ProtoNet Q05513.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Cytoplasm; Endosome; Kinase; Metal-binding; Nucleotide-binding; Phorbol-ester binding; Phosphoprotein; Polymorphism; Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   592  592     Protein kinase C zeta type. PRO_0000055701
DOMAIN   15    98  84     OPR. 
DOMAIN   252   518  267     Protein kinase. 
DOMAIN   519   590  72     AGC-kinase C-terminal. 
ZN_FING   130   180  51     Phorbol-ester/DAG-type. 
NP_BIND   258   266  9     ATP (By similarity). 
REGION   79   145  67     Interaction with SQSTM1 (By similarity). 
ACT_SITE   376   376        Proton acceptor (By similarity). 
BINDING   281   281        ATP (By similarity). 
MOD_RES   223   223        Phosphoserine. 
MOD_RES   410   410        Phosphothreonine; by PDPK1. 
MOD_RES   560   560        Phosphothreonine. 
VARIANT   49    49  1     R -> H (in dbSNP:rs35271800 [NCBI]). VAR_050560 
VARIANT   84    84  1     R -> H. VAR_042310 
VARIANT   514   514  1     S -> F (in a colorectal cancer sample; somatic mutation). VAR_035467 
VARIANT   519   519  1     R -> C (in a colorectal adenocarcinoma sample; somatic mutation). VAR_042311 
MUTAGEN   19    19        K->A: No effect on interaction with SQSTM1 and PARD6B. 
MUTAGEN   62    62        D->A: Loss of interaction with SQSTM1 and PARD6B. 
MUTAGEN   66    66        D->A: Loss of interaction with SQSTM1 and PARD6B. 
CONFLICT   6     6        G -> D (in Ref. 2; AAA36488). 
CONFLICT   262   262        S -> T (in Ref. 2; AAA36488). 
Sequence information
Length: 592 AA [This is the length of the unprocessed precursor] Molecular weight: 67660 Da [This is the MW of the unprocessed precursor] CRC64: 88CCD0577E6A596C [This is a checksum on the sequence]
        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 

Q05513 in FASTA format

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