Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q1JPZ3

- SRC_DANRE

UniProt

Q1JPZ3 - SRC_DANRE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Proto-oncogene tyrosine-protein kinase Src

Gene

src

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each src kinase is very difficult. Src appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of src to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates involved in this process. When cells adhere via focal adhesions to the extra-cellular matrix, signals are transmitted by integrins into the cell and result in tyrosine phosphorylation of a number of focal adhesion proteins, including ptk2/fak1 and paxillin (pxn). Also active at the sites of cell-cell contact adherens junctions and at gap junctions. Implicated in the regulation of pre-mRNA-processing. Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus (By similarity).By similarity

Catalytic activityi

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

Enzyme regulationi

Becomes activated when its major tyrosine phosphorylation site is not phosphorylated. It can also be activated by point mutations as well as by truncations at the C-terminal end or by other mutations. Heme regulates its activity by enhancing the phosphorylation on Tyr-528 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei296 – 2961ATPPROSITE-ProRule annotation
Active sitei387 – 3871Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi274 – 2829ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
  2. cell cycle Source: UniProtKB-KW
  3. response to yeast Source: ZFIN
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Cell adhesion, Cell cycle

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_174907. Regulation of KIT signaling.
REACT_181648. Signaling by SCF-KIT.
REACT_182698. Signaling by ERBB2.
REACT_206122. ADP signalling through P2Y purinoceptor 1.
REACT_214033. Netrin mediated repulsion signals.
REACT_221534. FCGR activation.

Names & Taxonomyi

Protein namesi
Recommended name:
Proto-oncogene tyrosine-protein kinase Src (EC:2.7.10.2)
Alternative name(s):
Proto-oncogene c-Src
pp60c-src
Short name:
p60-Src
Gene namesi
Name:src
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
ProteomesiUP000000437: Chromosome 23

Organism-specific databases

ZFINiZDB-GENE-030131-3809. src.

Subcellular locationi

Cell membrane By similarity. Mitochondrion inner membrane By similarity. Nucleus By similarity. Cytoplasmcytoskeleton By similarity
Note: Localizes to focal adhesion sites following integrin engagement. Localization to focal adhesion sites requires myristoylation and the SH3 domain (By similarity).By similarity

GO - Cellular componenti

  1. cytoskeleton Source: UniProtKB-KW
  2. mitochondrial inner membrane Source: UniProtKB-KW
  3. nucleus Source: UniProtKB-KW
  4. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Mitochondrion, Mitochondrion inner membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi528 – 5281Y → F: Lower affinity for AMOTL2-binding compared with wild-type. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 534533Proto-oncogene tyrosine-protein kinase SrcPRO_0000418880Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Modified residuei17 – 171PhosphoserineBy similarity
Modified residuei34 – 341PhosphoserineBy similarity
Modified residuei67 – 671PhosphoserineBy similarity
Modified residuei73 – 731PhosphothreonineBy similarity
Modified residuei74 – 741Phosphoserine; by CDK5By similarity
Modified residuei185 – 1851PhosphotyrosineBy similarity
Modified residuei417 – 4171Phosphotyrosine; by autocatalysisBy similarity
Modified residuei417 – 4171Phosphotyrosine; by FAK2By similarity
Modified residuei437 – 4371PhosphotyrosineBy similarity
Modified residuei499 – 4991S-nitrosocysteineBy similarity
Modified residuei509 – 5091PhosphothreonineBy similarity
Modified residuei520 – 5201PhosphotyrosineBy similarity
Modified residuei528 – 5281Phosphotyrosine; by CSKBy similarity

Post-translational modificationi

Myristoylated at Gly-2, and this is essential for targeting to membranes.By similarity
Dephosphorylated at Tyr-528 by PTPRJ. Phosphorylated on Tyr-528 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src. Dephosphorylated by PTPRJ at Tyr-417. Normally maintained in an inactive conformation with the SH2 domain engaged with Tyr-528, the SH3 domain engaged with the SH2-kinase linker, and Tyr-417 dephosphorylated. Dephosphorylation of Tyr-528 as a result of protein tyrosine phosphatase (PTP) action disrupts the intramolecular interaction between the SH2 domain and Tyr-528, Tyr-417 can then become autophosphorylated, resulting in SRC activation. Phosphorylation of Tyr-528 by CSK allows this interaction to reform, resulting in SRC inactivation (By similarity).By similarity
S-nitrosylation is important for activation of kinase activity.By similarity

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein, S-nitrosylation

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Interactioni

Subunit structurei

Interacts with amotl2; this interaction promotes the translocation of phosphorylated src to peripheral cell-matrix adhesion sites.1 Publication

Protein-protein interaction databases

STRINGi7955.ENSDARP00000093618.

Structurei

3D structure databases

ProteinModelPortaliQ1JPZ3.
SMRiQ1JPZ3. Positions 84-534.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini82 – 14362SH3PROSITE-ProRule annotationAdd
BLAST
Domaini149 – 253105SH2PROSITE-ProRule annotationAdd
BLAST
Domaini268 – 521254Protein kinasePROSITE-ProRule annotationAdd
BLAST

Domaini

The SH2 and SH3 domains are important for the intramolecular and intermolecular interactions that regulate catalytic activity, localization, and substrate recruitment.By similarity

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118938.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiQ1JPZ3.
KOiK05704.
OMAiCQCWRKD.
OrthoDBiEOG7GTT2V.
PhylomeDBiQ1JPZ3.
TreeFamiTF351634.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR011009. 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]
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q1JPZ3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGGVKSKPKE LGQRSRSLDD GTGGHHHHTP NPTSFTPNRS PPVEGSRRGT
60 70 80 90 100
QPNIINAEQA LFGGVNSTTN SITSPNRIGI LGGVTTFVAL YDYESRTASD
110 120 130 140 150
LSFRKGERLQ IVNNTEGDWW LARSLTTGES GYIPSNYVAP SDSIQAEEWY
160 170 180 190 200
FGKITRRDSE RLLLNLENRR GTFLVRESET TKGAYCLSVL DYDNVKGLNV
210 220 230 240 250
KHYKIRKLDS GGFYITSRTQ FSTLQQLVNH YRQHADGLCH SLTDVCPVLK
260 270 280 290 300
PPTQGLARDA WEIPRDSLRL DVKLGQGCFG EVWMGTWNGT TRVAIKTLKP
310 320 330 340 350
GTMSPEAFLQ EAQVMKKLRH EKLVQLYAVV SEEPIYIVTE YMGQGSLLDF
360 370 380 390 400
LKGDMGKMLR LPQLVDMASQ IASGMAYVER MNYVHRDLRA ANILVGDNLV
410 420 430 440 450
CKVADFGLAR LIEDNEYTAR QGAKFPIKWT APEAALYGRF TIKSDVWSFG
460 470 480 490 500
ILLTELTTKG RVPYPGMVNR EVLDQVERGY RMPCPAECPD SLHELMLTCW
510 520 530
RKEPEERPTF EYLQGFLEDY FTSTEPQYQP GENL
Length:534
Mass (Da):60,147
Last modified:September 5, 2012 - v2
Checksum:iEC09B5A1BC01A38A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41V → A in AAI16545. 1 PublicationCurated
Sequence conflicti166 – 1661L → M in AAI16545. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ620750 mRNA. Translation: CAF06181.1.
BX548066 Genomic DNA. No translation available.
CU302205 Genomic DNA. No translation available.
BC116544 mRNA. Translation: AAI16545.1.
RefSeqiNP_001003837.2. NM_001003837.2.
UniGeneiDr.2731.

Genome annotation databases

EnsembliENSDART00000102843; ENSDARP00000093618; ENSDARG00000008107.
ENSDART00000112198; ENSDARP00000097596; ENSDARG00000008107.
GeneIDi325084.
KEGGidre:325084.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ620750 mRNA. Translation: CAF06181.1 .
BX548066 Genomic DNA. No translation available.
CU302205 Genomic DNA. No translation available.
BC116544 mRNA. Translation: AAI16545.1 .
RefSeqi NP_001003837.2. NM_001003837.2.
UniGenei Dr.2731.

3D structure databases

ProteinModelPortali Q1JPZ3.
SMRi Q1JPZ3. Positions 84-534.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 7955.ENSDARP00000093618.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSDART00000102843 ; ENSDARP00000093618 ; ENSDARG00000008107 .
ENSDART00000112198 ; ENSDARP00000097596 ; ENSDARG00000008107 .
GeneIDi 325084.
KEGGi dre:325084.

Organism-specific databases

CTDi 6714.
ZFINi ZDB-GENE-030131-3809. src.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118938.
HOGENOMi HOG000233858.
HOVERGENi HBG008761.
InParanoidi Q1JPZ3.
KOi K05704.
OMAi CQCWRKD.
OrthoDBi EOG7GTT2V.
PhylomeDBi Q1JPZ3.
TreeFami TF351634.

Enzyme and pathway databases

Reactomei REACT_174907. Regulation of KIT signaling.
REACT_181648. Signaling by SCF-KIT.
REACT_182698. Signaling by ERBB2.
REACT_206122. ADP signalling through P2Y purinoceptor 1.
REACT_214033. Netrin mediated repulsion signals.
REACT_221534. FCGR activation.

Miscellaneous databases

NextBioi 20809110.
PROi Q1JPZ3.

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
InterProi IPR011009. 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 ]
Pfami PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTi SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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], 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.
    , 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 (MAY-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovary.
  4. "Amotl2 is essential for cell movements in zebrafish embryo and regulates c-Src translocation."
    Huang H., Lu F.I., Jia S., Meng S., Cao Y., Wang Y., Ma W., Yin K., Wen Z., Peng J., Thisse C., Thisse B., Meng A.
    Development 134:979-988(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AMOTL2, MUTAGENESIS OF TYR-528.

Entry informationi

Entry nameiSRC_DANRE
AccessioniPrimary (citable) accession number: Q1JPZ3
Secondary accession number(s): Q6EWH0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: September 5, 2012
Last modified: October 29, 2014
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3