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P00523 (SRC_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 166. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SRC
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length533 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 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. Ref.12 Ref.15

Catalytic activity

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

Enzyme regulation

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-527 By similarity.

Subunit structure

Forms a complex with polyoma virus middle T antigen. Interacts with AFAP-110. Interacts with GJA1 and PXN. Ref.14 Ref.16 Ref.17

Subcellular location

Cell membrane By similarity. Mitochondrion inner membrane By similarity. Endosome membrane; Peripheral membrane protein. Nucleus By similarity. Cytoplasmcytoskeleton By similarity. Note: Localizes to focal adhesion sites after integrin engagement By similarity. Localization to focal adhesion sites requires myristoylation and the SH3 domain By similarity. Ref.13 Ref.14

Tissue specificity

Expressed to high levels, and with a high degree of kinase activity, in certain fully differentiated cells such as neurons, platelets and macrophages. Isoform 1 is widely expressed. Isoform 2 is expressed only in the muscle.

Post-translational modification

Myristoylated at Gly-2, and this is essential for targeting to membranes By similarity.

Dephosphorylated at Tyr-527 by PTPRJ. Phosphorylated on Tyr-527 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src. Dephosphorylated by PTPRJ at Tyr-416. Normally maintained in an inactive conformation with the SH2 domain engaged with Tyr-527, the SH3 domain engaged with the SH2-kinase linker, and Tyr-416 dephosphorylated. Dephosphorylation of Tyr-527 as a result of protein tyrosine phosphatase (PTP) action disrupts the intramolecular interaction between the SH2 domain and Tyr-527, Tyr-416 can then become autophosphorylated, resulting in SRC activation. Phosphorylation of Tyr-527 by CSK allows this interaction to reform, resulting in SRC inactivation By similarity. Ref.4 Ref.8 Ref.9 Ref.10 Ref.11

S-nitrosylation is important for activation of its kinase activity.

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
   Biological processCell adhesion
Cell cycle
Immunity
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Endosome
Membrane
Mitochondrion
Mitochondrion inner membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseProto-oncogene
   DomainSH2 domain
SH3 domain
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMLipoprotein
Myristate
Phosphoprotein
S-nitrosylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbone resorption

Inferred from electronic annotation. Source: Ensembl

branching involved in mammary gland duct morphogenesis

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell migration

Inferred from electronic annotation. Source: Ensembl

forebrain development

Inferred from electronic annotation. Source: Ensembl

immune system process

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of anoikis

Inferred from electronic annotation. Source: Ensembl

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of extrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of intrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein homooligomerization

Inferred from electronic annotation. Source: Ensembl

oogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of ERK1 and ERK2 cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of canonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of podosome assembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

regulation of intracellular estrogen receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of protein binding

Inferred from electronic annotation. Source: Ensembl

response to interleukin-1

Inferred from electronic annotation. Source: Ensembl

uterus development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcaveola

Inferred from electronic annotation. Source: Ensembl

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

late endosome

Inferred from electronic annotation. Source: Ensembl

lysosome

Inferred from electronic annotation. Source: Ensembl

mitochondrial inner membrane

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

heme binding

Inferred from sequence or structural similarity. Source: UniProtKB

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein phosphatase binding

Inferred from physical interaction PubMed 15696169. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AFAP1Q907383EBI-848039,EBI-8562073
Asap1Q9QWY8-12EBI-848039,EBI-698517From a different organism.
Asap1Q9QWY8-23EBI-848039,EBI-698524From a different organism.
CLIC5Q9NZA12EBI-848039,EBI-5658997From a different organism.
CSKP412406EBI-848039,EBI-1380630From a different organism.
DAAM1Q9Y4D13EBI-848039,EBI-2817289From a different organism.
Hcn2O887035EBI-848039,EBI-771231From a different organism.
PTK2Q009443EBI-848039,EBI-2896409
PTPRAP184334EBI-848039,EBI-2609645From a different organism.
PtpraP180522EBI-848039,EBI-6597520From a different organism.
Srcin1Q9QWI6-22EBI-848039,EBI-775607From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P00523-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P00523-2)

The sequence of this isoform differs from the canonical sequence as follows:
     183-193: AYCLSVSDFDN → DPCIPLPSCLC
     194-533: Missing.
Note: Membrane-bound.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 533532Proto-oncogene tyrosine-protein kinase Src
PRO_0000088144

Regions

Domain81 – 14262SH3
Domain148 – 24598SH2
Domain267 – 520254Protein kinase
Nucleotide binding273 – 2819ATP By similarity

Sites

Active site3861Proton acceptor By similarity
Binding site2951ATP

Amino acid modifications

Modified residue121Phosphoserine; by PKC
Modified residue341Phosphothreonine Ref.11
Modified residue461Phosphothreonine Ref.11
Modified residue721Phosphoserine Ref.11
Modified residue4161Phosphotyrosine; by autocatalysis Ref.4 Ref.9
Modified residue4361Phosphotyrosine; by autocatalysis Ref.4
Modified residue4981S-nitrosocysteine Ref.18
Modified residue5271Phosphotyrosine; by CSK Ref.10
Lipidation21N-myristoyl glycine By similarity

Natural variations

Alternative sequence183 – 19311AYCLSVSDFDN → DPCIPLPSCLC in isoform 2.
VSP_011844
Alternative sequence194 – 533340Missing in isoform 2.
VSP_011845

Experimental info

Mutagenesis4981C → A: Significant reduction in S-nitrosylation. Ref.18
Sequence conflict3011T → N Ref.1
Sequence conflict5011K → R Ref.1

Secondary structure

............................................................................................ 533
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: ABDB036F7D63C30A

FASTA53360,010
        10         20         30         40         50         60 
MGSSKSKPKD PSQRRRSLEP PDSTHHGGFP ASQTPNKTAA PDTHRTPSRS FGTVATEPKL 

        70         80         90        100        110        120 
FGGFNTSDTV TSPQRAGALA GGVTTFVALY DYESRTETDL SFKKGERLQI VNNTEGDWWL 

       130        140        150        160        170        180 
AHSLTTGQTG YIPSNYVAPS DSIQAEEWYF GKITRRESER LLLNPENPRG TFLVRESETT 

       190        200        210        220        230        240 
KGAYCLSVSD FDNAKGLNVK HYKIRKLDSG GFYITSRTQF SSLQQLVAYY SKHADGLCHR 

       250        260        270        280        290        300 
LTNVCPTSKP QTQGLAKDAW EIPRESLRLE VKLGQGCFGE VWMGTWNGTT RVAIKTLKPG 

       310        320        330        340        350        360 
TMSPEAFLQE AQVMKKLRHE KLVQLYAVVS EEPIYIVTEY MSKGSLLDFL KGEMGKYLRL 

       370        380        390        400        410        420 
PQLVDMAAQI ASGMAYVERM NYVHRDLRAA NILVGENLVC KVADFGLARL IEDNEYTARQ 

       430        440        450        460        470        480 
GAKFPIKWTA PEAALYGRFT IKSDVWSFGI LLTELTTKGR VPYPGMVNRE VLDQVERGYR 

       490        500        510        520        530 
MPCPPECPES LHDLMCQCWR KDPEERPTFE YLQAFLEDYF TSTEPQYQPG ENL 

« Hide

Isoform 2 [UniParc].

Checksum: 9D1BE54C33B02D98
Show »

FASTA19321,180

References

[1]"Structure and sequence of the cellular gene homologous to the RSV src gene and the mechanism for generating the transforming virus."
Takeya T., Hanafusa H.
Cell 32:881-890(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]Erratum
Takeya T., Hanafusa H.
Cell 34:319-319(1983)
Cited for: SEQUENCE REVISION TO 526.
[3]"An alternative non-tyrosine protein kinase product of the c-src gene in chicken skeletal muscle."
Dorai T., Wang L.-H.
Mol. Cell. Biol. 10:4068-4079(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Pectoralis muscle.
[4]"The purification and characterization of the catalytic domain of Src expressed in Schizosaccharomyces pombe. Comparison of unphosphorylated and tyrosine phosphorylated species."
Weijland A., Neubauer G., Courtneidge S.A., Mann M., Wierenga R.K., Superti-Furga G.
Eur. J. Biochem. 240:756-764(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PHOSPHORYLATION AT TYR-416 AND TYR-436.
[5]"DNA sequence of the viral and cellular src gene of chickens. II. Comparison of the src genes of two strains of Avian sarcoma virus and of the cellular homolog."
Takeya T., Hanafusa H.
J. Virol. 44:12-18(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
[6]"Analysis of cDNAs of the proto-oncogene c-src: heterogeneity in 5' exons and possible mechanism for the genesis of the 3' end of v-src."
Dorai T., Levy J.B., Kang L., Brugge J.S., Wang L.-H.
Mol. Cell. Biol. 11:4165-4176(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-19 AND 485-534 (ISOFORM 1).
[7]"Direct evidence that oncogenic tyrosine kinases and cyclic AMP-dependent protein kinase have homologous ATP-binding sites."
Kamps M.P., Taylor S.S., Sefton B.M.
Nature 310:589-592(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: ATP-BINDING SITE.
[8]"Protein kinase C phosphorylates pp60src at a novel site."
Gould K.L., Woodgett J.R., Cooper J.A., Buss J.E., Shalloway D., Hunter T.
Cell 42:849-857(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[9]"Characterization of sites for tyrosine phosphorylation in the transforming protein of Rous sarcoma virus (pp60v-src) and its normal cellular homologue (pp60c-src)."
Smart J.E., Oppermann H., Czernilofsky A.P., Purchio A.F., Erikson R.L., Bishop J.M.
Proc. Natl. Acad. Sci. U.S.A. 78:6013-6017(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-416.
[10]"Tyr527 is phosphorylated in pp60c-src: implications for regulation."
Cooper J.A., Gould K.L., Cartwright C.A., Hunter T.
Science 231:1431-1434(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-527.
[11]"Purified maturation promoting factor phosphorylates pp60c-src at the sites phosphorylated during fibroblast mitosis."
Shenoy S., Choi J.K., Bagrodia S., Copeland T.D., Maller J.L., Shalloway D.
Cell 57:763-774(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-34; THR-46 AND SER-72.
[12]"Signal transduction by nerve growth factor and fibroblast growth factor in PC12 cells requires a sequence of src and ras actions."
Kremer N.E., D'Arcangelo G., Thomas S.M., DeMarco M., Brugge J.S., Halegoua S.
J. Cell Biol. 115:809-819(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN THE NGF AND FGF SIGNALING PATHWAYS.
[13]"Association of p60c-src with endosomal membranes in mammalian fibroblasts."
Kaplan K.B., Swedlow J.R., Varmus H.E., Morgan D.O.
J. Cell Biol. 118:321-333(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[14]"Detection of Src homology 3-binding proteins, including paxillin, in normal and v-Src-transformed Balb/c 3T3 cells."
Weng Z., Taylor J.A., Turner C.E., Brugge J.S., Seidel-Dugan C.
J. Biol. Chem. 268:14956-14963(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PXN.
[15]"Nuclear signaling by endothelin-1 requires Src protein-tyrosine kinases."
Simonson M.S., Wang Y., Herman W.H.
J. Biol. Chem. 271:77-82(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN THE EDN1 SIGNALING PATHWAY.
[16]"Formation of a stable src-AFAP-110 complex through either an amino-terminal or a carboxy-terminal SH2-binding motif."
Guappone A.C., Weimer T., Flynn D.C.
Mol. Carcinog. 22:110-119(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AFAP-110.
[17]"Structural changes in the carboxyl terminus of the gap junction protein connexin43 indicates signaling between binding domains for c-Src and zonula occludens-1."
Sorgen P.L., Duffy H.S., Sahoo P., Coombs W., Delmar M., Spray D.C.
J. Biol. Chem. 279:54695-54701(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GJA1.
[18]"S-nitrosylation at cysteine 498 of c-Src tyrosine kinase regulates nitric oxide-mediated cell invasion."
Rahman M.A., Senga T., Ito S., Hyodo T., Hasegawa H., Hamaguchi M.
J. Biol. Chem. 285:3806-3814(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: S-NITROSYLATION AT CYS-498, MUTAGENESIS OF CYS-498.
[19]"Regulation, substrates and functions of src."
Brown M.T., Cooper J.A.
Biochim. Biophys. Acta 1287:121-149(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[20]"Cellular functions regulated by Src family kinases."
Thomas S.M., Brugge J.S.
Annu. Rev. Cell Dev. Biol. 13:513-609(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[21]"Novel regulation and function of Src tyrosine kinase."
Ma Y.C., Huang X.Y.
Cell. Mol. Life Sci. 59:456-462(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[22]"The 2.35 A crystal structure of the inactivated form of chicken Src: a dynamic molecule with multiple regulatory interactions."
Williams J.C., Weijland A., Gonfloni S., Thompson A., Courtneidge S.A., Superti-Furga G., Wierenga R.K.
J. Mol. Biol. 274:757-775(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 83-533.
[23]"1H and 15N assignments and secondary structure of the Src SH3 domain."
Yu H., Rosen M.K., Schreiber S.L.
FEBS Lett. 324:87-92(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 81-140.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00402 Genomic DNA. Translation: CAA23696.1.
J00908 Genomic DNA. No translation available.
M57290 mRNA. Translation: AAA49078.1.
S43604 mRNA. Translation: AAD13831.1.
S43616 mRNA. Translation: AAD13835.1.
S43587 mRNA. Translation: AAD13830.1.
S43609 mRNA. Translation: AAD13832.1.
S43614 mRNA. Translation: AAD13834.1.
S43579 mRNA. Translation: AAB19353.2.
PIRTVCHS. A00630.
RefSeqNP_990788.2. NM_205457.2.
UniGeneGga.46254.
Gga.51508.
Gga.9406.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F1WX-ray2.10A145-246[»]
1F2FX-ray1.70A145-246[»]
1NLONMR-C81-140[»]
1NLPNMR-C81-140[»]
1P13X-ray1.63A/B145-245[»]
1PRLNMR-C77-139[»]
1PRMNMR-C77-139[»]
1RLPNMR-C77-139[»]
1RLQNMR-C77-139[»]
1SRLNMR-A77-140[»]
1SRMNMR-A77-140[»]
2HWOX-ray2.50A/B251-532[»]
2HWPX-ray2.48A/B251-532[»]
2OIQX-ray2.07A/B251-532[»]
2PTKX-ray2.35A81-533[»]
2QI8X-ray2.32A/B251-533[»]
2QLQX-ray2.33A/B251-533[»]
2QQ7X-ray2.38A/B251-533[»]
3D7TX-ray2.90B258-533[»]
3D7UX-ray4.11B/D260-523[»]
3DQWX-ray2.02A/B/C/D251-533[»]
3DQXX-ray2.30A/B251-533[»]
3EL7X-ray2.80A251-533[»]
3EL8X-ray2.30A/B251-533[»]
3EN4X-ray2.55A/B251-533[»]
3EN5X-ray2.66A/B251-533[»]
3EN6X-ray2.39A/B251-533[»]
3EN7X-ray2.81A/B251-533[»]
3F3TX-ray2.50A/B251-533[»]
3F3UX-ray2.50A/B251-533[»]
3F3VX-ray2.60A/B251-533[»]
3F3WX-ray2.60A/B251-533[»]
3F6XX-ray2.35A/B/C/D251-533[»]
3FJ5X-ray1.65A/B85-140[»]
3G5DX-ray2.20A/B251-533[»]
3G6GX-ray2.31A/B251-533[»]
3G6HX-ray2.35A/B251-533[»]
3GEQX-ray2.20A/B251-533[»]
3LOKX-ray2.48A/B251-533[»]
3OEZX-ray2.40A/B251-533[»]
3OF0X-ray2.70A/B251-533[»]
3QLFX-ray2.75A/B251-533[»]
3QLGX-ray2.75A/B251-533[»]
3SVVX-ray2.20A/B251-533[»]
3TZ7X-ray3.30A/B251-533[»]
3TZ8X-ray2.70A/B251-533[»]
3TZ9X-ray3.10A/B251-533[»]
3U4WX-ray1.90A259-533[»]
3U51X-ray2.24A/B259-533[»]
3UQFX-ray2.27A/B251-533[»]
3UQGX-ray2.20A/B251-533[»]
4AGWX-ray2.60A/B251-533[»]
4DGGX-ray2.65A/B251-533[»]
4FICX-ray2.50A/B251-533[»]
4HVUX-ray0.98A85-141[»]
4HVVX-ray1.10A85-140[»]
4HVWX-ray0.98A85-141[»]
4LGGX-ray2.41A/B264-533[»]
4LGHX-ray2.84A/B257-533[»]
4MCVX-ray2.73A/B256-533[»]
ProteinModelPortalP00523.
SMRP00523. Positions 83-533.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid676691. 1 interaction.
DIPDIP-449N.
IntActP00523. 18 interactions.
MINTMINT-139173.

Chemistry

BindingDBP00523.
ChEMBLCHEMBL3655.

Proteomic databases

PaxDbP00523.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSGALT00000006127; ENSGALP00000006117; ENSGALG00000003855. [P00523-1]
GeneID396442.
KEGGgga:396442.

Organism-specific databases

CTD6714.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00620000087702.
HOVERGENHBG008761.
InParanoidP00523.
KOK05704.
OMACQCWRKD.
OrthoDBEOG7GTT2V.
PhylomeDBP00523.
TreeFamTF351634.

Enzyme and pathway databases

BRENDA2.7.10.2. 1306.

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

EvolutionaryTraceP00523.
NextBio20816483.
PROP00523.

Entry information

Entry nameSRC_CHICK
AccessionPrimary (citable) accession number: P00523
Secondary accession number(s): Q90992 expand/collapse secondary AC list , Q90993, Q91343, Q91345, Q92013, Q98915
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 166 of the entry and version 4 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references