P07947 (YES_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	543 AA.
Sequence status	Complete.
Protein existence	Evidence 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.13 Ref.17 Ref.20 Ref.21
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.16
Subcellular location	Cell membrane. Cytoplasm › cytoskeleton › centrosome. Cytoplasm › cytosol. Note: Newly synthesized protein initially accumulates in the Golgi region and traffics to the plasma membrane through the exocytic pathway. Ref.10 Ref.18 Ref.20
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 component	Cell membrane Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Polymorphism
Disease	Proto-oncogene
Domain	SH2 domain SH3 domain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Lipoprotein Myristate Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Fc-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 glucose transport Inferred from electronic annotation. Source: Compara innate immune response Traceable author statement. Source: Reactome leukocyte migration Traceable author statement. Source: Reactome protein autophosphorylation Inferred from electronic annotation. Source: Compara regulation of vascular permeability Traceable author statement PubMed 19267251. Source: BHF-UCL
Cellular_component	Golgi apparatus Inferred from direct assay PubMed 20605918. Source: UniProtKB cytosol Traceable author statement. Source: Reactome microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay PubMed 20605918. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Traceable author statement PubMed 19267251. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 543

543

Tyrosine-protein kinase Yes

PRO_0000088181

Regions

Domain

91 – 152

62

SH3

Domain

158 – 255

98

SH2

Domain

277 – 530

254

Protein kinase

Nucleotide binding

283 – 291

9

ATP By similarity

Sites

Active site

396

1

Proton acceptor By similarity

Binding site

305

1

ATP By similarity

Amino acid modifications

Modified residue

11

1

Phosphoserine

Modified residue

21

1

Phosphothreonine Ref.15

Modified residue

26

1

Phosphoserine

Modified residue

32

1

Phosphotyrosine

Modified residue

40

1

Phosphoserine Ref.15

Modified residue

111

1

Phosphoserine

Modified residue

194

1

Phosphotyrosine

Modified residue

195

1

Phosphoserine

Modified residue

222

1

Phosphotyrosine

Modified residue

223

1

Phosphotyrosine

Modified residue

336

1

Phosphotyrosine Ref.19

Modified residue

345

1

Phosphotyrosine Ref.19

Modified residue

426

1

Phosphotyrosine; by autocatalysis

Modified residue

446

1

Phosphotyrosine

Modified residue

537

1

Phosphotyrosine; by CSK Ref.14 Ref.19

Lipidation

2

1

N-myristoyl glycine By similarity

Lipidation

3

1

S-palmitoyl cysteine; in membrane form By similarity

Natural variations

Natural variant

198

1

I → V. Ref.23
Corresponds to variant rs34580680 [ dbSNP | Ensembl ].

VAR_041879

Natural variant

282

1

K → R. Ref.23
Corresponds to variant rs35126906 [ dbSNP | Ensembl ].

VAR_041880

Experimental info

Mutagenesis

426

1

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

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

543

Helix Strand Turn

Details...

Beta strand

93 – 100

8

Beta strand

117 – 121

5

Beta strand

126 – 133

8

Turn

134 – 136

3

Beta strand

139 – 143

5

Helix

144 – 146

3

Beta strand

147 – 149

3

Sequences

	Sequence		Length	Mass (Da)
	P07947 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: A2B376084686BBCD	FASTA	543	60,801
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling." Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A., Lottspeich F., Chen Z. EMBO J. 25:5058-5070(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF PARD3.
[13]	"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.
[14]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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, MASS SPECTROMETRY.
[20]	"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.
[21]	"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.
[22]	"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.
[23]	"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] 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.

IPI

IPI00013981.

PIR

TVHUYS. A26714.

RefSeq

NP_005424.1. NM_005433.3.

UniGene

Hs.194148.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HDA	X-ray	1.90	A	91-152	[»]

ProteinModelPortal

P07947.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33849N.

IntAct

P07947. 10 interactions.

MINT

MINT-93566.

STRING

9606.ENSP00000324740.

PTM databases

PhosphoSite

P07947.

Polymorphism databases

DMDM

125870.

Proteomic databases

PaxDb

P07947.

PRIDE

P07947.

Protocols and materials databases

DNASU

7525.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000314574; ENSP00000324740; ENSG00000176105.
ENST00000584307; ENSP00000462468; ENSG00000176105.

GeneID

7525.

KEGG

hsa:7525.

UCSC

uc002kky.3. human.

Organism-specific databases

CTD

7525.

GeneCards

GC18M000721.

HGNC

HGNC:12841. YES1.

HPA

CAB004370.
HPA026480.

MIM

164880. gene.

neXtProt

NX_P07947.

PharmGKB

PA37432.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233858.

HOVERGEN

HBG008761.

InParanoid

P07947.

KO

K05705.

OMA

IKYRTEN.

OrthoDB

EOG4KKZ2S.

Enzyme and pathway databases

BRENDA

2.7.10.2. 2681.

Pathway_Interaction_DB

alphasynuclein_pathway. Alpha-synuclein signaling.
amb2_neutrophils_pathway. amb2 Integrin signaling.
pi3kcipathway. Class I PI3K signaling events.
epha_fwdpathway. EPHA forward signaling.
ephrinbrevpathway. Ephrin B reverse signaling.
glypican_1pathway. Glypican 1 network.
wnt_calcium_pathway. Noncanonical Wnt signaling pathway.
pdgfrbpathway. PDGFR-beta signaling pathway.
p38alphabetapathway. Regulation of p38-alpha and p38-beta.
ptp1bpathway. Signaling events mediated by PTP1B.
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.
txa2pathway. Thromboxane A2 receptor signaling.

Reactome

REACT_111102. Signal Transduction.
REACT_604. Hemostasis.
REACT_6900. Immune System.

SignaLink

P07947.

Gene expression databases

Bgee

P07947.

CleanEx

HS_YES1.

Genevestigator

P07947.

GermOnline

ENSG00000176105. Homo sapiens.

Family and domain databases

Gene3D

3.30.505.10. 1 hit.

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_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]

Pfam

PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.

SMART

SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.
SSF50044. SH3. 1 hit.

PROSITE

PS00107. 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]

ProtoNet

Search...

Other

BindingDB

P07947.

ChEMBL

CHEMBL2073.

DrugBank

DB01254. Dasatinib.

EvolutionaryTrace

P07947.

GenomeRNAi

7525.

NextBio

29441.

SOURCE

Search...

Entry information

Entry name

YES_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 161 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.