ID YES_DANRE Reviewed; 546 AA.
AC A1A5H8; Q6EWH1; Q8AXW6;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 128.
DE RecName: Full=Tyrosine-protein kinase yes;
DE EC=2.7.10.2;
DE AltName: Full=p61-Yes;
GN Name=yes1; Synonyms=yes;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15815683; DOI=10.1038/sj.embor.7400386;
RA Jopling C., den Hertog J.;
RT "Fyn/Yes and non-canonical Wnt signalling converge on RhoA in vertebrate
RT gastrulation cell movements.";
RL EMBO Rep. 6:426-431(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-135, FUNCTION, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND AUTOPHOSPHORYLATION.
RX PubMed=15572145; DOI=10.1016/j.ydbio.2004.08.052;
RA Tsai W.B., Zhang X., Sharma D., Wu W., Kinsey W.H.;
RT "Role of Yes kinase during early zebrafish development.";
RL Dev. Biol. 277:129-141(2005).
CC -!- FUNCTION: Non-receptor protein tyrosine kinase that is involved in the
CC regulation of cell growth and survival, apoptosis, cell-cell adhesion,
CC cytoskeleton remodeling, differentiation, G2/M progression and
CC cytokinesis (By similarity). Required for convergent extension cell
CC movements during gastrulation, acting with fyna via rhoa. May be
CC required for epiboly to occur, possibly through its effects in calcium
CC signaling. During embryonic development, phosphorylates ptk2.1/fak.
CC {ECO:0000250, ECO:0000269|PubMed:15572145,
CC ECO:0000269|PubMed:15815683}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15572145}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15815683}.
CC -!- DEVELOPMENTAL STAGE: Expressed in unfertilized eggs (at protein level).
CC Most highly enriched in the cortex of the newly fertilized egg. Becomes
CC concentrated in the blastodisc by 30 minutes post-insemination and
CC remains distributed among all regions of the embryo, excluding yolk. In
CC the pharyngula stage (24 hours post-fertilization), observed all over
CC the embryo, with highest levels in the eyes and central nervous system
CC and somites (at protein level). {ECO:0000269|PubMed:15572145}.
CC -!- PTM: Autophosphorylation at Tyr-429 maintains enzyme activity.
CC {ECO:0000250}.
CC -!- PTM: Palmitoylation at Cys-3 promotes membrane localization.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AJ620749; CAF06180.1; -; mRNA.
DR EMBL; BX927088; CAN88236.1; -; Genomic_DNA.
DR EMBL; BC128657; AAI28658.1; -; mRNA.
DR EMBL; AY157872; AAN73265.1; -; mRNA.
DR RefSeq; NP_001013288.2; NM_001013270.3.
DR AlphaFoldDB; A1A5H8; -.
DR SMR; A1A5H8; -.
DR STRING; 7955.ENSDARP00000009659; -.
DR PaxDb; 7955-ENSDARP00000009659; -.
DR PeptideAtlas; A1A5H8; -.
DR GeneID; 407620; -.
DR KEGG; dre:407620; -.
DR AGR; ZFIN:ZDB-GENE-050126-1; -.
DR CTD; 7525; -.
DR ZFIN; ZDB-GENE-050126-1; yes1.
DR eggNOG; KOG0197; Eukaryota.
DR HOGENOM; CLU_000288_7_2_1; -.
DR InParanoid; A1A5H8; -.
DR OMA; PSHMGHY; -.
DR OrthoDB; 1614410at2759; -.
DR PhylomeDB; A1A5H8; -.
DR TreeFam; TF351634; -.
DR BRENDA; 2.7.10.2; 928.
DR Reactome; R-DRE-1227986; Signaling by ERBB2.
DR Reactome; R-DRE-1433557; Signaling by SCF-KIT.
DR Reactome; R-DRE-1433559; Regulation of KIT signaling.
DR Reactome; R-DRE-210990; PECAM1 interactions.
DR Reactome; R-DRE-389356; CD28 co-stimulation.
DR Reactome; R-DRE-389513; CTLA4 inhibitory signaling.
DR Reactome; R-DRE-3928662; EPHB-mediated forward signaling.
DR Reactome; R-DRE-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-DRE-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-DRE-912631; Regulation of signaling by CBL.
DR PRO; PR:A1A5H8; -.
DR Proteomes; UP000000437; Chromosome 2.
DR Bgee; ENSDARG00000005941; Expressed in presomitic mesoderm and 24 other cell types or tissues.
DR ExpressionAtlas; A1A5H8; baseline and differential.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:ZFIN.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0034334; P:adherens junction maintenance; IGI:ZFIN.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0060027; P:convergent extension involved in gastrulation; IGI:ZFIN.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd05069; PTKc_Yes; 1.
DR CDD; cd09933; SH2_Src_family; 1.
DR CDD; cd12007; SH3_Yes; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR035751; Yes_SH3.
DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24418:SF90; TYROSINE-PROTEIN KINASE YES; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Cytoplasm; Cytoskeleton; Developmental protein;
KW Kinase; Lipoprotein; Membrane; Myristate; Nucleotide-binding; Palmitate;
KW Phosphoprotein; Reference proteome; SH2 domain; SH3 domain; Transferase;
KW Tyrosine-protein kinase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..546
FT /note="Tyrosine-protein kinase yes"
FT /id="PRO_0000418881"
FT DOMAIN 94..155
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 161..258
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 280..533
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 399
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 286..294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 308
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 429
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 540
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT LIPID 3
FT /note="S-palmitoyl cysteine; in membrane form"
FT /evidence="ECO:0000250"
FT CONFLICT 21
FT /note="T -> S (in Ref. 4; AAN73265)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="S -> P (in Ref. 4; AAN73265)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="W -> C (in Ref. 4; AAN73265)"
FT /evidence="ECO:0000305"
FT CONFLICT 514..515
FT /note="KE -> NG (in Ref. 1; CAF06180)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 546 AA; 61269 MW; 7067657BA2B8F420 CRC64;
MGCVKSKEDK GPTQKYRPDP TNPTPGSHMG LYGPDPTQMG QSPALKGPTN NYNSRSSGLT
PFGGSSSVIT PFGGASSSFS TVAVNNPFPG VVTGGVTFFV ALYDYEARTS DDLSFSKGDR
FQIINNTEGD WWEARSINTG QKGYIPSNYV APADSIQAEE WYFGKMGRKD AERLLLLPGN
QRGTFLVRES ETTKGAYSLS IRDWDEMKGD NVKHYKIRKL DSGGYYITTR AQFDTLQKLV
KHYTEHADGL CYRLTTVCPT VKPQTQGLAK DAWEIPRESL RLELKLGQGC FGEVWMGTWN
GTTKVAIKTL KPGTMSPEAF LQEAQIMKKL RHDKLVPLYA VVSEEPIYIV TEYMGKGSLL
DFLKEGEGKY LKLPQLVDMA AQIADGMAFI ERMNYIHRDL RAANILVGDN LVCKIADFGL
ARLIEDNEYT ARQGAKFPIK WTAPEAALYG RFTIKSDVWS FGILLTELVT KGRVPYPGMV
NREVLEQVER GYRMPCPQGC PESLHEMMRL CWKKEPDERP TFEYIQSFLE DYFTATEPQY
QPGDNL
//
