Protein kinase C delta type - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot Q05655 (KPCD_HUMAN)

Last modified February 9, 2010. Version 116. History...

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

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Names and origin

Protein names

Recommended name:
    Protein kinase C delta type
    EC=2.7.11.13
Alternative name(s):
    nPKC-delta

Gene names

Name:

PRKCD

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	676 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	This is 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. May play a role in antigen-dependent control of B-cell function. Phosphorylates MUC1 in the C-terminal and regulates the interaction between MUC1 and beta-catenin. Ref.8
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Three specific sites; Thr-507 (activation loop of the kinase domain), Ser-645 (turn motif) and Ser-664 (hydrophobic region), need to be phosphorylated for its full activation.
Subunit structure	Interacts with PDK1, RAD9A, CDCP1 and MUC1. Ref.8 Ref.9 Ref.20
Subcellular location	Cytoplasm By similarity. Membrane; Peripheral membrane protein By similarity.
Domain	The C1 domain, containing the phorbol ester/DAG-type region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor. The C2 domain is a non-calcium binding domain. It binds proteins containing phosphotyrosine in a sequence-specific manner.
Post-translational modification	Phosphorylated on Thr-507, within the activation loop. Autophosphorylated and/or phosphorylated. Although the Thr-507 phosphorylation occurs it is not a prerequisite for enzymatic activity By similarity. Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.19
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 C2 domain. Contains 2 phorbol-ester/DAG-type zinc fingers. Contains 1 protein kinase domain.

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Ontologies

Keywords
Cellular component	Cytoplasm Membrane
Coding sequence diversity	Polymorphism
Domain	Repeat Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	intracellular signaling cascade Inferred from electronic annotation. Source: InterPro negative regulation of insulin receptor signaling pathway Traceable author statement. Source: UniProtKB negative regulation of peptidyl-tyrosine phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of protein binding Traceable author statement. Source: UniProtKB protein amino acid phosphorylation Inferred from direct assay. Source: UniProtKB protein stabilization Non-traceable author statement. Source: UniProtKB regulation of receptor activity Traceable author statement. Source: UniProtKB senescence Inferred from mutant phenotype. Source: UniProtKB
Cellular component	cytosol Inferred from Experiment. Source: Reactome extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: UniProtKB plasma membrane Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium-independent protein kinase C activity Traceable author statement. Source: UniProtKB enzyme activator activity Inferred from direct assay. Source: UniProtKB enzyme binding Inferred from physical interaction. Source: UniProtKB insulin receptor substrate binding Inferred from sequence or structural similarity. Source: UniProtKB protein C-terminus binding Inferred from physical interaction. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
FYN	P06241	3	EBI-704279,EBI-515315
GAP43	P17677	3	EBI-704279,EBI-1267511

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 676

676

Protein kinase C delta type

PRO_0000055694

Regions

Domain

1 – 90

Domain

349 – 603

255

Protein kinase

Domain

604 – 675

AGC-kinase C-terminal

Zinc finger

158 – 208

Phorbol-ester/DAG-type 1

Zinc finger

230 – 280

Phorbol-ester/DAG-type 2

Nucleotide binding

355 – 363

ATP By similarity

Sites

Active site

473

Proton acceptor By similarity

Binding site

378

ATP By similarity

Site

Interaction with phosphotyrosine-containing peptide

Site

Interaction with phosphotyrosine-containing peptide

Site

Interaction with phosphotyrosine-containing peptide

Site

123

Interaction with phosphotyrosine-containing peptide

Amino acid modifications

Modified residue

Phosphothreonine Ref.13

Modified residue

Phosphothreonine Ref.13

Modified residue

130

Phosphoserine Ref.14

Modified residue

218

Phosphothreonine

Modified residue

295

Phosphothreonine

Modified residue

299

Phosphoserine Ref.13

Modified residue

302

Phosphoserine Ref.13 Ref.14

Modified residue

304

Phosphoserine Ref.12 Ref.14

Modified residue

307

Phosphoserine Ref.13 Ref.14

Modified residue

313

Phosphotyrosine Ref.11 Ref.13 Ref.17 Ref.19

Modified residue

331

Phosphoserine Ref.16

Modified residue

334

Phosphotyrosine Ref.11 Ref.13

Modified residue

374

Phosphotyrosine Ref.11 Ref.17

Modified residue

503

Phosphoserine Ref.13

Modified residue

506

Phosphoserine

Modified residue

507

Phosphothreonine; by PDPK1 By similarity

Modified residue

645

Phosphoserine

Modified residue

647

Phosphoserine Ref.13

Modified residue

654

Phosphoserine Ref.13

Modified residue

658

Phosphoserine Ref.13

Modified residue

664

Phosphoserine Ref.10 Ref.13 Ref.14 Ref.19

Natural variations

Natural variant

348

N → S: dbSNP rs33911937.

VAR_035347

Natural variant

375

F → S: dbSNP rs1056998. Ref.1

VAR_006175

Natural variant

410

L → F: dbSNP rs34502209.

VAR_035348

Natural variant

483

R → W: dbSNP rs35891605.

VAR_046009

Natural variant

494

M → V

VAR_020610

Natural variant

593

V → M

VAR_006176

Experimental info

Sequence conflict

524

K → R in BAG36031. Ref.2

Sequence conflict

533

S → A Ref.7

Secondary structure

676

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q05655-1 [UniParc].

Last modified September 2, 2008. Version 2.
Checksum: 013F4314A2EE331A
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FASTA

676

77,505

        10         20         30         40         50         60 
MAPFLRIAFN SYELGSLQAE DEANQPFCAV KMKEALSTER GKTLVQKKPT MYPEWKSTFD 

        70         80         90        100        110        120 
AHIYEGRVIQ IVLMRAAEEP VSEVTVGVSV LAERCKKNNG KAEFWLDLQP QAKVLMSVQY 

       130        140        150        160        170        180 
FLEDVDCKQS MRSEDEAKFP TMNRRGAIKQ AKIHYIKNHE FIATFFGQPT FCSVCKDFVW 

       190        200        210        220        230        240 
GLNKQGYKCR QCNAAIHKKC IDKIIGRCTG TAANSRDTIF QKERFNIDMP HRFKVHNYMS 

       250        260        270        280        290        300 
PTFCDHCGSL LWGLVKQGLK CEDCGMNVHH KCREKVANLC GINQKLLAEA LNQVTQRASR 

       310        320        330        340        350        360 
RSDSASSEPV GIYQGFEKKT GVAGEDMQDN SGTYGKIWEG SSKCNINNFI FHKVLGKGSF 

       370        380        390        400        410        420 
GKVLLGELKG RGEYFAIKAL KKDVVLIDDD VECTMVEKRV LTLAAENPFL THLICTFQTK 

       430        440        450        460        470        480 
DHLFFVMEFL NGGDLMYHIQ DKGRFELYRA TFYAAEIMCG LQFLHSKGII YRDLKLDNVL 

       490        500        510        520        530        540 
LDRDGHIKIA DFGMCKENIF GESRASTFCG TPDYIAPEIL QGLKYTFSVD WWSFGVLLYE 

       550        560        570        580        590        600 
MLIGQSPFHG DDEDELFESI RVDTPHYPRW ITKESKDILE KLFEREPTKR LGVTGNIKIH 

       610        620        630        640        650        660 
PFFKTINWTL LEKRRLEPPF RPKVKSPRDY SNFDQEFLNE KARLSYSDKN LIDSMDQSAF 

       670 
AGFSFVNPKF EHLLED

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular and biochemical characterization of a recombinant human PKC-delta family member." Aris J.P., Basta P.V., Holmes W.D., Ballas L.M., Moomaw C., Rankl N.B., Blobel G., Loomis C.R., Burns D.J. Biochim. Biophys. Acta 1174:171-181(1993) [PubMed: 8357834] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS SER-375 AND MET-593. Tissue: Liver.
[2]	"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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: Skin.
[5]	"Partial cDNA Sequence of human protein kinase C delta." Hug H. Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-365. Tissue: Hippocampus.
[6]	"Functional analyses of mammalian protein kinase C isozymes in budding yeast and mammalian fibroblasts." Nomoto S., Watanabe Y., Ninomiya-Tsuji J., Yang L.-X., Kikuchi K., Hagiwara M., Hidaka H., Matsumoto K., Irie K. Genes Cells 2:601-614(1997) [PubMed: 9427282] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 51-676.
[7]	"Identification of multiple, novel, protein kinase C-related gene products." Palmer R.H., Ridden J., Parker P.J. FEBS Lett. 356:5-8(1994) [PubMed: 7988719] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 432-533, VARIANT VAL-494.
[8]	"Protein kinase C delta regulates function of the DF3/MUC1 carcinoma antigen in beta-catenin signaling." Ren J., Li Y., Kufe D. J. Biol. Chem. 277:17616-17622(2002) [PubMed: 11877440] [Abstract] Cited for: INTERACTION WITH MUC1, FUNCTION.
[9]	"Protein kinase Cdelta is responsible for constitutive and DNA damage-induced phosphorylation of Rad9." Yoshida K., Wang H.-G., Miki Y., Kufe D. EMBO J. 22:1431-1441(2003) [PubMed: 12628935] [Abstract] Cited for: INTERACTION WITH RAD9A.
[10]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664, MASS SPECTROMETRY. Tissue: Epithelium.
[11]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-313; TYR-334 AND TYR-374, MASS SPECTROMETRY.
[12]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, MASS SPECTROMETRY. Tissue: Platelet.
[13]	"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-43; THR-50; SER-299; SER-302; SER-307; TYR-313; TYR-334; SER-503; SER-647; SER-654; SER-658 AND SER-664, MASS SPECTROMETRY.
[14]	"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 SER-130; SER-302; SER-304; SER-307 AND SER-664, MASS SPECTROMETRY.
[15]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[16]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331, MASS SPECTROMETRY.
[17]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-313 AND TYR-374, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[18]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-43; THR-218; THR-295; SER-299; SER-302; SER-304; TYR-313; TYR-334; SER-506; SER-645; SER-647 AND SER-664, MASS SPECTROMETRY.
[19]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-313 AND SER-664, MASS SPECTROMETRY. Tissue: T-cell.
[20]	"The C2 domain of PKCdelta is a phosphotyrosine binding domain." Benes C.H., Wu N., Elia A.E.H., Dharia T., Cantley L.C., Soltoff S.P. Cell 121:271-280(2005) [PubMed: 15851033] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-123 IN COMPLEX WITH PHOSPHOTYROSINE-CONTAINING PEPTIDE, INTERACTION WITH CDCP1.
[21]	"Solution structure of the first phorbol esters/diacylglycerol binding domain of human protein kinase C, delta." RIKEN structural genomics initiative (RSGI) Submitted (APR-2008) to the PDB data bank Cited for: STRUCTURE BY NMR OF 149-218.
+	Additional computationally mapped references.

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Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L07860 mRNA. Translation: AAA03176.1.
L07861 mRNA. Translation: AAA03175.1.
AK313216 mRNA. Translation: BAG36031.1.
CH471055 Genomic DNA. Translation: EAW65279.1.
BC043350 mRNA. Translation: AAH43350.1.
Z22521 mRNA. Translation: CAA80249.1.
D10495 mRNA. Translation: BAA01381.1.

IPI

IPI00329236.

PIR

S35704.

RefSeq

NP_006245.2.
NP_997704.1.

UniGene

Hs.155342

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YRK	X-ray	1.70	A	1-123	[»]
2YUU	NMR	-	A	149-218	[»]

SMR

Q05655. Positions 155-262, 227-283, 346-668.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29954N.

IntAct

Q05655. 5 interactions.

STRING

Q05655.

PTM databases

PhosphoSite

Q05655.

Proteomic databases

PRIDE

Q05655.

Genome annotation databases

Ensembl

ENST00000330452; ENSP00000331602; ENSG00000163932; Homo sapiens. [Genome view]
ENST00000394729; ENSP00000378217; ENSG00000163932; Homo sapiens. [Genome view]

GeneID

5580.

KEGG

hsa:5580.

Organism-specific databases

CTD

5580.

GeneCards

GC03P053170.

HGNC

HGNC:9399. PRKCD.

HPA

CAB010469.
CAB013225.
HPA001863.
HPA001890.

MIM

176977. gene.

PharmGKB

PA33763.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG17515.

HOGENOM

HBG755340.

HOVERGEN

Q05655.

InParanoid

Q05655.

OMA

GEDEAKF.

OrthoDB

EOG95F081.

PhylomeDB

Q05655.

Enzyme and pathway databases

BRENDA

2.7.11.13. 247.

Pathway_Interaction_DB

alphasynuclein_pathway. Alpha-synuclein signaling.
ceramidepathway. Ceramide signaling pathway.
endothelinpathway. Endothelins.
hedgehog_glipathway. Hedgehog signaling events mediated by Gli proteins.
ifngpathway. IFN-gamma pathway.
igf1_pathway. IGF1 pathway.
il6_7pathway. IL6-mediated signaling events.
lysophospholipid_pathway. LPA receptor mediated events.
pdgfrbpathway. PDGFR-beta signaling pathway.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.
syndecan_2_pathway. Syndecan-2-mediated signaling events.
syndecan_4_pathway. Syndecan-4-mediated signaling events.
txa2pathway. Thromboxane A2 receptor signaling.
pi3kplctrkpathway. Trk receptor signaling mediated by PI3K and PLC-gamma.
mapktrkpathway. Trk receptor signaling mediated by the MAPK pathway.

Reactome

REACT_11061. Signalling by NGF.
REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

Q05655.

Bgee

Q05655.

CleanEx

HS_PRKCD.

Genevestigator

Q05655.

GermOnline

ENSG00000163932. Homo sapiens.

Family and domain databases

InterPro

IPR000961. AGC-kinase_C.
IPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR020454. DAG/PE_bd.
IPR011009. Kinase-like_dom.
IPR015745. PKC.
IPR017892. Pkinase_C.
IPR014376. Prot_kin_PKC_delta.
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]

PANTHER

PTHR22985:SF86. PKC. 1 hit.

Pfam

PF00130. C1_1. 2 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]

PIRSF

PIRSF000551. PKC_delta. 1 hit.

PRINTS

PR00008. DAGPEDOMAIN.

SMART

SM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

PROSITE

PS51285. AGC_KINASE_CTER. 1 hit.
PS50004. C2. False negative.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00479. ZF_DAG_PE_1. 2 hits.
PS50081. ZF_DAG_PE_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

PMAP-CutDB

Q05655.

SOURCE

Search...

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Entry information

Entry name

KPCD_HUMAN

Accession

Primary (citable) accession number: Q05655
Secondary accession number(s): B2R834, Q15144, Q86XJ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	September 2, 2008
Last modified:	February 9, 2010
This is version 116 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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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Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents