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A1A5H8 (YES_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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):
p61-Yes
Gene names
Name:yes1
Synonyms:yes
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length546 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, differentiation, G2/M progression and cytokinesis By similarity. Required for convergent extension cell movements during gastrulation, acting with fyna via rhoa. May be required for epiboly to occur, possibly through its effects in calcium signaling. During embryonic development, phosphorylates ptk2.1/fak. Ref.1 Ref.4

Catalytic activity

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

Subcellular location

Cell membrane. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cytoplasmcytosol By similarity Ref.4.

Tissue specificity

Widely expressed. Ref.1

Developmental stage

Expressed in unfertilized eggs (at protein level). Most highly enriched in the cortex of the newly fertilized egg. Becomes concentrated in the blastodisc by 30 minutes post-insemination and remains distributed among all regions of the embryo, excluding yolk. In the pharyngula stage (24 hours post-fertilization), observed all over the embryo, with highest levels in the eyes and central nervous system and somites (at protein level). Ref.4

Post-translational modification

Autophosphorylation at Tyr-429 maintains enzyme activity By similarity.

Palmitoylation at Cys-3 promotes membrane localization By similarity.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 546545Tyrosine-protein kinase yes
PRO_0000418881

Regions

Domain94 – 15562SH3
Domain161 – 25898SH2
Domain280 – 533254Protein kinase
Nucleotide binding286 – 2949ATP By similarity

Sites

Active site3991Proton acceptor By similarity
Binding site3081ATP By similarity

Amino acid modifications

Modified residue4291Phosphotyrosine; by autocatalysis By similarity
Modified residue5401Phosphotyrosine; by CSK By similarity
Lipidation21N-myristoyl glycine By similarity
Lipidation31S-palmitoyl cysteine; in membrane form By similarity

Experimental info

Sequence conflict211T → S in AAN73265. Ref.4
Sequence conflict561S → P in AAN73265. Ref.4
Sequence conflict1321W → C in AAN73265. Ref.4
Sequence conflict514 – 5152KE → NG in CAF06180. Ref.1

Sequences

Sequence LengthMass (Da)Tools
A1A5H8 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 7067657BA2B8F420

FASTA54661,269
        10         20         30         40         50         60 
MGCVKSKEDK GPTQKYRPDP TNPTPGSHMG LYGPDPTQMG QSPALKGPTN NYNSRSSGLT 

        70         80         90        100        110        120 
PFGGSSSVIT PFGGASSSFS TVAVNNPFPG VVTGGVTFFV ALYDYEARTS DDLSFSKGDR 

       130        140        150        160        170        180 
FQIINNTEGD WWEARSINTG QKGYIPSNYV APADSIQAEE WYFGKMGRKD AERLLLLPGN 

       190        200        210        220        230        240 
QRGTFLVRES ETTKGAYSLS IRDWDEMKGD NVKHYKIRKL DSGGYYITTR AQFDTLQKLV 

       250        260        270        280        290        300 
KHYTEHADGL CYRLTTVCPT VKPQTQGLAK DAWEIPRESL RLELKLGQGC FGEVWMGTWN 

       310        320        330        340        350        360 
GTTKVAIKTL KPGTMSPEAF LQEAQIMKKL RHDKLVPLYA VVSEEPIYIV TEYMGKGSLL 

       370        380        390        400        410        420 
DFLKEGEGKY LKLPQLVDMA AQIADGMAFI ERMNYIHRDL RAANILVGDN LVCKIADFGL 

       430        440        450        460        470        480 
ARLIEDNEYT ARQGAKFPIK WTAPEAALYG RFTIKSDVWS FGILLTELVT KGRVPYPGMV 

       490        500        510        520        530        540 
NREVLEQVER GYRMPCPQGC PESLHEMMRL CWKKEPDERP TFEYIQSFLE DYFTATEPQY 


QPGDNL 

« Hide

References

« Hide 'large scale' references
[1]"Fyn/Yes and non-canonical Wnt signalling converge on RhoA in vertebrate gastrulation cell movements."
Jopling C., den Hertog J.
EMBO Rep. 6:426-431(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
[2]"The zebrafish reference genome sequence and its relationship to the human genome."
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J. expand/collapse author list , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tuebingen.
[3]NIH - Zebrafish Gene Collection (ZGC) project
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Role of Yes kinase during early zebrafish development."
Tsai W.B., Zhang X., Sharma D., Wu W., Kinsey W.H.
Dev. Biol. 277:129-141(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-135, FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AUTOPHOSPHORYLATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ620749 mRNA. Translation: CAF06180.1.
BX927088 Genomic DNA. Translation: CAN88236.1.
BC128657 mRNA. Translation: AAI28658.1.
AY157872 mRNA. Translation: AAN73265.1.
RefSeqNP_001013288.2. NM_001013270.3.
UniGeneDr.75637.

3D structure databases

ProteinModelPortalA1A5H8.
SMRA1A5H8. Positions 96-546.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7955.ENSDARP00000009659.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000027090; ENSDARP00000009659; ENSDARG00000005941.
GeneID407620.
KEGGdre:407620.

Organism-specific databases

CTD7525.
ZFINZDB-GENE-050126-1. yes1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00620000087702.
HOGENOMHOG000233858.
HOVERGENHBG008761.
InParanoidA1A5H8.
KOK05705.
OMAIKYRTEN.
OrthoDBEOG7GTT2V.
TreeFamTF351634.

Gene expression databases

BgeeA1A5H8.

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

NextBio20818497.
PROA1A5H8.

Entry information

Entry nameYES_DANRE
AccessionPrimary (citable) accession number: A1A5H8
Secondary accession number(s): Q6EWH1, Q8AXW6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families