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P07947 (YES_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 171. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase Yes

EC=2.7.10.2
Alternative name(s):
Proto-oncogene c-Yes
p61-Yes
Gene names
Name:YES1
Synonyms:YES
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length543 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, and differentiation. Stimulation by receptor tyrosine kinases (RTKs) including EGRF, PDGFR, CSF1R and FGFR leads to recruitment of YES1 to the phosphorylated receptor, and activation and phosphorylation of downstream substrates. Upon EGFR activation, promotes the phosphorylation of PARD3 to favor epithelial tight junction assembly. Participates in the phosphorylation of specific junctional components such as CTNND1 by stimulating the FYN and FER tyrosine kinases at cell-cell contacts. Upon T-cell stimulation by CXCL12, phosphorylates collapsin response mediator protein 2/DPYSL2 and induces T-cell migration. Participates in CD95L/FASLG signaling pathway and mediates AKT-mediated cell migration. Plays a role in cell cycle progression by phosphorylating the cyclin-dependent kinase 4/CDK4 thus regulating the G1 phase. Also involved in G2/M progression and cytokinesis. Ref.10 Ref.12 Ref.16 Ref.19 Ref.20

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Subunit structure

Interacts with YAP1 and CSF1R By similarity. Interacts with CTNND1; this interaction allows YES1-mediated activation of FYN and FER and subsequent phosphorylation of CTNND1 By similarity. Interacts with FASLG. Ref.15

Subcellular location

Cell membrane. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytosol. Note: Newly synthesized protein initially accumulates in the Golgi region and traffics to the plasma membrane through the exocytic pathway. Ref.10 Ref.17 Ref.19

Tissue specificity

Expressed in the epithelial cells of renal proximal tubules and stomach as well as hematopoietic cells in the bone marrow and spleen in the fetal tissues. In adult, expressed in epithelial cells of the renal proximal tubules and present in keratinocytes in the basal epidermal layer of epidermis. Ref.5 Ref.6

Post-translational modification

Phosphorylation by CSK on the C-terminal tail maintains the enzyme in an inactive state. Autophosphorylation at Tyr-426 maintains enzyme activity by blocking CSK-mediated inhibition.

Palmitoylation at Cys-3 promotes membrane localization By similarity. Ref.7

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.

Contains 1 protein kinase domain.

Contains 1 SH2 domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityPolymorphism
   DiseaseProto-oncogene
   DomainSH2 domain
SH3 domain
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMLipoprotein
Myristate
Palmitate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

T cell costimulation

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

cellular protein modification process

Traceable author statement Ref.1. Source: ProtInc

glucose transport

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

leukocyte migration

Traceable author statement. Source: Reactome

peptidyl-tyrosine phosphorylation

Inferred from experiment. Source: GOC

protein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

regulation of vascular permeability

Traceable author statement PubMed 19267251. Source: BHF-UCL

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 20605918. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay PubMed 20605918. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

enzyme binding

Inferred from physical interaction PubMed 20605918. Source: UniProtKB

ion channel binding

Inferred from physical interaction PubMed 12538589. Source: BHF-UCL

non-membrane spanning protein tyrosine kinase activity

Traceable author statement PubMed 19267251. Source: BHF-UCL

protein tyrosine kinase activity

Inferred from experiment. Source: Reactome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MED28Q9H2042EBI-515331,EBI-514199

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 543542Tyrosine-protein kinase Yes
PRO_0000088181

Regions

Domain91 – 15262SH3
Domain158 – 25598SH2
Domain277 – 530254Protein kinase
Nucleotide binding283 – 2919ATP By similarity

Sites

Active site3961Proton acceptor By similarity
Binding site3051ATP By similarity

Amino acid modifications

Modified residue111Phosphoserine
Modified residue211Phosphothreonine Ref.14
Modified residue261Phosphoserine
Modified residue321Phosphotyrosine
Modified residue401Phosphoserine Ref.14
Modified residue1111Phosphoserine
Modified residue1941Phosphotyrosine
Modified residue1951Phosphoserine
Modified residue2221Phosphotyrosine
Modified residue2231Phosphotyrosine
Modified residue3361Phosphotyrosine Ref.18
Modified residue3451Phosphotyrosine Ref.18
Modified residue4261Phosphotyrosine; by autocatalysis
Modified residue4461Phosphotyrosine
Modified residue5371Phosphotyrosine; by CSK Ref.13 Ref.18
Lipidation21N-myristoyl glycine By similarity
Lipidation31S-palmitoyl cysteine; in membrane form By similarity

Natural variations

Natural variant1981I → V. Ref.22
Corresponds to variant rs34580680 [ dbSNP | Ensembl ].
VAR_041879
Natural variant2821K → R. Ref.22
Corresponds to variant rs35126906 [ dbSNP | Ensembl ].
VAR_041880

Experimental info

Mutagenesis4261Y → F: About 50% loss of CSK-mediated inhibition. Ref.9

Secondary structure

............ 543
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07947 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A2B376084686BBCD

FASTA54360,801
        10         20         30         40         50         60 
MGCIKSKENK SPAIKYRPEN TPEPVSTSVS HYGAEPTTVS PCPSSSAKGT AVNFSSLSMT 

        70         80         90        100        110        120 
PFGGSSGVTP FGGASSSFSV VPSSYPAGLT GGVTIFVALY DYEARTTEDL SFKKGERFQI 

       130        140        150        160        170        180 
INNTEGDWWE ARSIATGKNG YIPSNYVAPA DSIQAEEWYF GKMGRKDAER LLLNPGNQRG 

       190        200        210        220        230        240 
IFLVRESETT KGAYSLSIRD WDEIRGDNVK HYKIRKLDNG GYYITTRAQF DTLQKLVKHY 

       250        260        270        280        290        300 
TEHADGLCHK LTTVCPTVKP QTQGLAKDAW EIPRESLRLE VKLGQGCFGE VWMGTWNGTT 

       310        320        330        340        350        360 
KVAIKTLKPG TMMPEAFLQE AQIMKKLRHD KLVPLYAVVS EEPIYIVTEF MSKGSLLDFL 

       370        380        390        400        410        420 
KEGDGKYLKL PQLVDMAAQI ADGMAYIERM NYIHRDLRAA NILVGENLVC KIADFGLARL 

       430        440        450        460        470        480 
IEDNEYTARQ GAKFPIKWTA PEAALYGRFT IKSDVWSFGI LQTELVTKGR VPYPGMVNRE 

       490        500        510        520        530        540 
VLEQVERGYR MPCPQGCPES LHELMNLCWK KDPDERPTFE YIQSFLEDYF TATEPQYQPG 


ENL 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of cDNA clones for the human c-yes gene."
Sukegawa J., Semba K., Yamanashi Y., Nishizawa M., Miyajima N., Yamamoto T., Toyoshima K.
Mol. Cell. Biol. 7:41-47(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"DNA sequence and analysis of human chromosome 18."
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. expand/collapse author list , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.
Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]"Distribution of c-yes-1 gene product in various cells and tissues."
Sugawara K., Sugawara I., Sukegawa J., Akatsuka T., Yamamoto T., Morita M., Mori S., Toyoshima K.
Br. J. Cancer 63:508-513(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"Differential expression of p62c-yes in normal, hyperplastic and neoplastic human epidermis."
Krueger J., Zhao Y.H., Murphy D., Sudol M.
Oncogene 6:933-940(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"Palmitoylation of multiple Src-family kinases at a homologous N-terminal motif."
Koegl M., Zlatkine P., Ley S.C., Courtneidge S.A., Magee A.I.
Biochem. J. 303:749-753(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION.
[8]"Expression, purification, and initial characterization of human Yes protein tyrosine kinase from a bacterial expression system."
Sun G., Budde R.J.
Arch. Biochem. Biophys. 345:135-142(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY CSK.
[9]"Autophosphorylation of Src and Yes blocks their inactivation by Csk phosphorylation."
Sun G., Sharma A.K., Budde R.J.
Oncogene 17:1587-1595(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: AUTOPHOSPHORYLATION, MUTAGENESIS OF TYR-426.
[10]"CD46 is phosphorylated at tyrosine 354 upon infection of epithelial cells by Neisseria gonorrhoeae."
Lee S.W., Bonnah R.A., Higashi D.L., Atkinson J.P., Milgram S.L., So M.
J. Cell Biol. 156:951-957(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, FUNCTION.
[11]"c-Yes response to growth factor activation."
Clump D.A., Qazi I.H., Sudol M., Flynn D.C.
Growth Factors 23:263-272(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[12]"Phosphorylation of cyclin dependent kinase 4 on tyrosine 17 is mediated by Src family kinases."
Martin N.G., McAndrew P.C., Eve P.D., Garrett M.D.
FEBS J. 275:3099-3109(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF CDK4.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21 AND SER-40, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
Voss M., Lettau M., Janssen O.
BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FASLG.
[16]"Phosphorylation of collapsin response mediator protein 2 on Tyr-479 regulates CXCL12-induced T lymphocyte migration."
Varrin-Doyer M., Vincent P., Cavagna S., Auvergnon N., Noraz N., Rogemond V., Honnorat J., Moradi-Ameli M., Giraudon P.
J. Biol. Chem. 284:13265-13276(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF DPYSL2.
[17]"Differential trafficking of Src, Lyn, Yes and Fyn is specified by the state of palmitoylation in the SH4 domain."
Sato I., Obata Y., Kasahara K., Nakayama Y., Fukumoto Y., Yamasaki T., Yokoyama K.K., Saito T., Yamaguchi N.
J. Cell Sci. 122:965-975(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-336; TYR-345 AND TYR-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Clues for c-Yes involvement in the cell cycle and cytokinesis."
Jung J., Lee M.K., Jin Y., Fu S.B., Rosales J.L., Lee K.Y.
Cell Cycle 10:1502-1503(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[20]"The naturally processed CD95L elicits a c-yes/calcium/PI3K-driven cell migration pathway."
Tauzin S., Chaigne-Delalande B., Selva E., Khadra N., Daburon S., Contin-Bordes C., Blanco P., Le Seyec J., Ducret T., Counillon L., Moreau J.F., Hofman P., Vacher P., Legembre P.
PLoS Biol. 9:E1001090-E1001090(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[21]"Crystallographic structure of the SH3 domain of the human c-Yes tyrosine kinase: loop flexibility and amyloid aggregation."
Martin-Garcia J.M., Luque I., Mateo P.L., Ruiz-Sanz J., Camara-Artigas A.
FEBS Lett. 581:1701-1706(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 91-152.
[22]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-198 AND ARG-282.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M15990 mRNA. Translation: AAA35735.1.
AP001178 Genomic DNA. No translation available.
CH471113 Genomic DNA. Translation: EAX01709.1.
CH471113 Genomic DNA. Translation: EAX01710.1.
BC048960 mRNA. Translation: AAH48960.1.
PIRTVHUYS. A26714.
RefSeqNP_005424.1. NM_005433.3.
UniGeneHs.194148.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HDAX-ray1.90A89-152[»]
ProteinModelPortalP07947.
SMRP07947. Positions 92-543.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113357. 48 interactions.
DIPDIP-33849N.
IntActP07947. 24 interactions.
MINTMINT-93566.
STRING9606.ENSP00000324740.

Chemistry

BindingDBP07947.
ChEMBLCHEMBL2073.
DrugBankDB01254. Dasatinib.
GuidetoPHARMACOLOGY2284.

PTM databases

PhosphoSiteP07947.

Polymorphism databases

DMDM125870.

Proteomic databases

PaxDbP07947.
PRIDEP07947.

Protocols and materials databases

DNASU7525.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000314574; ENSP00000324740; ENSG00000176105.
ENST00000584307; ENSP00000462468; ENSG00000176105.
GeneID7525.
KEGGhsa:7525.
UCSCuc002kky.3. human.

Organism-specific databases

CTD7525.
GeneCardsGC18M000721.
HGNCHGNC:12841. YES1.
HPACAB004370.
HPA026480.
MIM164880. gene.
neXtProtNX_P07947.
PharmGKBPA37432.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233858.
HOVERGENHBG008761.
InParanoidP07947.
KOK05705.
PhylomeDBP07947.
TreeFamTF351634.

Enzyme and pathway databases

BRENDA2.7.10.2. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP07947.

Gene expression databases

ArrayExpressP07947.
BgeeP07947.
CleanExHS_YES1.
GenevestigatorP07947.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07947.
GeneWikiYES1.
GenomeRNAi7525.
NextBio29441.
PROP07947.
SOURCESearch...

Entry information

Entry nameYES_HUMAN
AccessionPrimary (citable) accession number: P07947
Secondary accession number(s): A6NLB3, D3DUH1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 171 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM