Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

P00523

- SRC_CHICK

UniProt

P00523 - SRC_CHICK

Protein

Proto-oncogene tyrosine-protein kinase Src

Gene

SRC

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 171 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.2 Publications

    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-527 By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei295 – 2951ATP
    Active sitei386 – 3861Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi273 – 2819ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. heme binding Source: UniProtKB
    3. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
    4. protein binding Source: UniProtKB
    5. protein phosphatase binding Source: UniProtKB

    GO - Biological processi

    1. bone resorption Source: Ensembl
    2. branching involved in mammary gland duct morphogenesis Source: Ensembl
    3. cell adhesion Source: UniProtKB-KW
    4. cell cycle Source: UniProtKB-KW
    5. cell migration Source: Ensembl
    6. forebrain development Source: Ensembl
    7. immune system process Source: UniProtKB-KW
    8. intracellular signal transduction Source: Ensembl
    9. negative regulation of anoikis Source: Ensembl
    10. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
    11. negative regulation of extrinsic apoptotic signaling pathway Source: Ensembl
    12. negative regulation of intrinsic apoptotic signaling pathway Source: Ensembl
    13. negative regulation of mitochondrial depolarization Source: Ensembl
    14. negative regulation of protein homooligomerization Source: Ensembl
    15. oogenesis Source: Ensembl
    16. positive regulation of canonical Wnt signaling pathway Source: Ensembl
    17. positive regulation of ERK1 and ERK2 cascade Source: Ensembl
    18. positive regulation of podosome assembly Source: Ensembl
    19. positive regulation of protein kinase B signaling Source: Ensembl
    20. protein autophosphorylation Source: Ensembl
    21. regulation of intracellular estrogen receptor signaling pathway Source: Ensembl
    22. regulation of protein binding Source: Ensembl
    23. response to interleukin-1 Source: Ensembl
    24. uterus development Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Cell adhesion, Cell cycle, Immunity

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 1306.
    ReactomeiREACT_189763. Signaling by ERBB2.
    REACT_194391. Signaling by SCF-KIT.
    REACT_196766. Regulation of KIT signaling.
    REACT_204997. Netrin mediated repulsion signals.
    REACT_207020. DCC mediated attractive signaling.
    REACT_217737. GAB1 signalosome.
    REACT_220416. c-src mediated regulation of Cx43 function and closure of gap junctions.
    REACT_226416. p38MAPK events.

    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
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Chromosome 20

    Subcellular locationi

    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. Localization to focal adhesion sites requires myristoylation and the SH3 domain.By similarity

    GO - Cellular componenti

    1. caveola Source: Ensembl
    2. cytoskeleton Source: UniProtKB-SubCell
    3. cytosol Source: Ensembl
    4. endosome membrane Source: UniProtKB-SubCell
    5. late endosome Source: Ensembl
    6. lysosome Source: Ensembl
    7. mitochondrial inner membrane Source: UniProtKB
    8. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi498 – 4981C → A: Significant reduction in S-nitrosylation. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 533532Proto-oncogene tyrosine-protein kinase SrcPRO_0000088144Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineBy similarity
    Modified residuei12 – 121Phosphoserine; by PKC1 Publication
    Modified residuei34 – 341Phosphothreonine2 Publications
    Modified residuei46 – 461Phosphothreonine2 Publications
    Modified residuei72 – 721Phosphoserine2 Publications
    Modified residuei416 – 4161Phosphotyrosine; by autocatalysis3 Publications
    Modified residuei436 – 4361Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei498 – 4981S-nitrosocysteine1 Publication
    Modified residuei527 – 5271Phosphotyrosine; by CSK2 Publications

    Post-translational modificationi

    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.By similarity
    S-nitrosylation is important for activation of its kinase activity.1 Publication

    Keywords - PTMi

    Lipoprotein, Myristate, Phosphoprotein, S-nitrosylation

    Proteomic databases

    PaxDbiP00523.

    Expressioni

    Tissue specificityi

    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.

    Interactioni

    Subunit structurei

    Forms a complex with polyoma virus middle T antigen. Interacts with AFAP-110. Interacts with GJA1 and PXN.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    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.

    Protein-protein interaction databases

    BioGridi676691. 1 interaction.
    DIPiDIP-449N.
    IntActiP00523. 19 interactions.
    MINTiMINT-139173.

    Structurei

    Secondary structure

    1
    533
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi86 – 905
    Beta strandi96 – 994
    Beta strandi107 – 1126
    Beta strandi115 – 1239
    Turni124 – 1263
    Beta strandi129 – 1335
    Helixi134 – 1363
    Beta strandi137 – 1393
    Helixi143 – 1453
    Beta strandi149 – 1524
    Helixi155 – 1628
    Beta strandi165 – 1673
    Beta strandi172 – 1765
    Beta strandi178 – 1803
    Beta strandi184 – 1929
    Turni193 – 1953
    Beta strandi196 – 20611
    Beta strandi212 – 2154
    Beta strandi218 – 2225
    Helixi223 – 23210
    Beta strandi237 – 2393
    Beta strandi253 – 2586
    Beta strandi259 – 2613
    Helixi264 – 2663
    Beta strandi267 – 2759
    Beta strandi277 – 28610
    Turni287 – 2893
    Beta strandi290 – 2978
    Turni299 – 3013
    Helixi304 – 31411
    Beta strandi325 – 3295
    Beta strandi331 – 3333
    Beta strandi335 – 3384
    Helixi346 – 3516
    Helixi353 – 3575
    Helixi360 – 37920
    Helixi389 – 3913
    Beta strandi392 – 3943
    Helixi396 – 3983
    Beta strandi400 – 4023
    Helixi405 – 4073
    Helixi408 – 4103
    Helixi414 – 4174
    Helixi426 – 4283
    Helixi431 – 4366
    Helixi441 – 45616
    Turni457 – 4593
    Helixi468 – 4769
    Helixi489 – 49810
    Helixi503 – 5053
    Helixi509 – 5179
    Helixi519 – 5224

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F1WX-ray2.10A145-247[»]
    1F2FX-ray1.70A145-247[»]
    1NLONMR-C81-140[»]
    1NLPNMR-C81-140[»]
    1P13X-ray1.63A/B145-246[»]
    1PRLNMR-C77-140[»]
    1PRMNMR-C77-140[»]
    1RLPNMR-C77-140[»]
    1RLQNMR-C77-140[»]
    1SRLNMR-A77-140[»]
    1SRMNMR-A77-140[»]
    2HWOX-ray2.50A/B251-533[»]
    2HWPX-ray2.48A/B251-533[»]
    2OIQX-ray2.07A/B251-533[»]
    2PTKX-ray2.35A81-533[»]
    2QI8X-ray2.32A/B251-533[»]
    2QLQX-ray2.33A/B251-533[»]
    2QQ7X-ray2.38A/B251-533[»]
    3D7TX-ray2.90B251-533[»]
    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[»]
    4JZ3X-ray1.85A85-141[»]
    4JZ4X-ray1.56A/B85-141[»]
    4LE9X-ray1.34A85-141[»]
    4LGGX-ray2.41A/B264-533[»]
    4LGHX-ray2.84A/B257-533[»]
    4MCVX-ray2.73A/B256-533[»]
    ProteinModelPortaliP00523.
    SMRiP00523. Positions 83-533.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00523.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini81 – 14262SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini148 – 24598SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini267 – 520254Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    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.
    GeneTreeiENSGT00620000087702.
    HOVERGENiHBG008761.
    InParanoidiP00523.
    KOiK05704.
    OMAiCQCWRKD.
    OrthoDBiEOG7GTT2V.
    PhylomeDBiP00523.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P00523-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MGSSKSKPKD PSQRRRSLEP PDSTHHGGFP ASQTPNKTAA PDTHRTPSRS    50
    FGTVATEPKL FGGFNTSDTV TSPQRAGALA GGVTTFVALY DYESRTETDL 100
    SFKKGERLQI VNNTEGDWWL AHSLTTGQTG YIPSNYVAPS DSIQAEEWYF 150
    GKITRRESER LLLNPENPRG TFLVRESETT KGAYCLSVSD FDNAKGLNVK 200
    HYKIRKLDSG GFYITSRTQF SSLQQLVAYY SKHADGLCHR LTNVCPTSKP 250
    QTQGLAKDAW EIPRESLRLE VKLGQGCFGE VWMGTWNGTT RVAIKTLKPG 300
    TMSPEAFLQE AQVMKKLRHE KLVQLYAVVS EEPIYIVTEY MSKGSLLDFL 350
    KGEMGKYLRL PQLVDMAAQI ASGMAYVERM NYVHRDLRAA NILVGENLVC 400
    KVADFGLARL IEDNEYTARQ GAKFPIKWTA PEAALYGRFT IKSDVWSFGI 450
    LLTELTTKGR VPYPGMVNRE VLDQVERGYR MPCPPECPES LHDLMCQCWR 500
    KDPEERPTFE YLQAFLEDYF TSTEPQYQPG ENL 533
    Length:533
    Mass (Da):60,010
    Last modified:January 23, 2007 - v4
    Checksum:iABDB036F7D63C30A
    GO
    Isoform 2 (identifier: P00523-2) [UniParc]FASTAAdd to Basket

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

    Note: Membrane-bound.

    Show »
    Length:193
    Mass (Da):21,180
    Checksum:i9D1BE54C33B02D98
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti301 – 3011T → N(PubMed:6299580)Curated
    Sequence conflicti501 – 5011K → R(PubMed:6299580)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei183 – 19311AYCLSVSDFDN → DPCIPLPSCLC in isoform 2. 1 PublicationVSP_011844Add
    BLAST
    Alternative sequencei194 – 533340Missing in isoform 2. 1 PublicationVSP_011845Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiA00630. TVCHS.
    RefSeqiNP_990788.2. NM_205457.2. [P00523-1]
    UniGeneiGga.46254.
    Gga.51508.
    Gga.9406.

    Genome annotation databases

    EnsembliENSGALT00000006127; ENSGALP00000006117; ENSGALG00000003855. [P00523-1]
    GeneIDi396442.
    KEGGigga:396442.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi A00630. TVCHS.
    RefSeqi NP_990788.2. NM_205457.2. [P00523-1 ]
    UniGenei Gga.46254.
    Gga.51508.
    Gga.9406.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F1W X-ray 2.10 A 145-247 [» ]
    1F2F X-ray 1.70 A 145-247 [» ]
    1NLO NMR - C 81-140 [» ]
    1NLP NMR - C 81-140 [» ]
    1P13 X-ray 1.63 A/B 145-246 [» ]
    1PRL NMR - C 77-140 [» ]
    1PRM NMR - C 77-140 [» ]
    1RLP NMR - C 77-140 [» ]
    1RLQ NMR - C 77-140 [» ]
    1SRL NMR - A 77-140 [» ]
    1SRM NMR - A 77-140 [» ]
    2HWO X-ray 2.50 A/B 251-533 [» ]
    2HWP X-ray 2.48 A/B 251-533 [» ]
    2OIQ X-ray 2.07 A/B 251-533 [» ]
    2PTK X-ray 2.35 A 81-533 [» ]
    2QI8 X-ray 2.32 A/B 251-533 [» ]
    2QLQ X-ray 2.33 A/B 251-533 [» ]
    2QQ7 X-ray 2.38 A/B 251-533 [» ]
    3D7T X-ray 2.90 B 251-533 [» ]
    3D7U X-ray 4.11 B/D 260-523 [» ]
    3DQW X-ray 2.02 A/B/C/D 251-533 [» ]
    3DQX X-ray 2.30 A/B 251-533 [» ]
    3EL7 X-ray 2.80 A 251-533 [» ]
    3EL8 X-ray 2.30 A/B 251-533 [» ]
    3EN4 X-ray 2.55 A/B 251-533 [» ]
    3EN5 X-ray 2.66 A/B 251-533 [» ]
    3EN6 X-ray 2.39 A/B 251-533 [» ]
    3EN7 X-ray 2.81 A/B 251-533 [» ]
    3F3T X-ray 2.50 A/B 251-533 [» ]
    3F3U X-ray 2.50 A/B 251-533 [» ]
    3F3V X-ray 2.60 A/B 251-533 [» ]
    3F3W X-ray 2.60 A/B 251-533 [» ]
    3F6X X-ray 2.35 A/B/C/D 251-533 [» ]
    3FJ5 X-ray 1.65 A/B 85-140 [» ]
    3G5D X-ray 2.20 A/B 251-533 [» ]
    3G6G X-ray 2.31 A/B 251-533 [» ]
    3G6H X-ray 2.35 A/B 251-533 [» ]
    3GEQ X-ray 2.20 A/B 251-533 [» ]
    3LOK X-ray 2.48 A/B 251-533 [» ]
    3OEZ X-ray 2.40 A/B 251-533 [» ]
    3OF0 X-ray 2.70 A/B 251-533 [» ]
    3QLF X-ray 2.75 A/B 251-533 [» ]
    3QLG X-ray 2.75 A/B 251-533 [» ]
    3SVV X-ray 2.20 A/B 251-533 [» ]
    3TZ7 X-ray 3.30 A/B 251-533 [» ]
    3TZ8 X-ray 2.70 A/B 251-533 [» ]
    3TZ9 X-ray 3.10 A/B 251-533 [» ]
    3U4W X-ray 1.90 A 259-533 [» ]
    3U51 X-ray 2.24 A/B 259-533 [» ]
    3UQF X-ray 2.27 A/B 251-533 [» ]
    3UQG X-ray 2.20 A/B 251-533 [» ]
    4AGW X-ray 2.60 A/B 251-533 [» ]
    4DGG X-ray 2.65 A/B 251-533 [» ]
    4FIC X-ray 2.50 A/B 251-533 [» ]
    4HVU X-ray 0.98 A 85-141 [» ]
    4HVV X-ray 1.10 A 85-140 [» ]
    4HVW X-ray 0.98 A 85-141 [» ]
    4JZ3 X-ray 1.85 A 85-141 [» ]
    4JZ4 X-ray 1.56 A/B 85-141 [» ]
    4LE9 X-ray 1.34 A 85-141 [» ]
    4LGG X-ray 2.41 A/B 264-533 [» ]
    4LGH X-ray 2.84 A/B 257-533 [» ]
    4MCV X-ray 2.73 A/B 256-533 [» ]
    ProteinModelPortali P00523.
    SMRi P00523. Positions 83-533.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 676691. 1 interaction.
    DIPi DIP-449N.
    IntActi P00523. 19 interactions.
    MINTi MINT-139173.

    Chemistry

    BindingDBi P00523.
    ChEMBLi CHEMBL3655.

    Proteomic databases

    PaxDbi P00523.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSGALT00000006127 ; ENSGALP00000006117 ; ENSGALG00000003855 . [P00523-1 ]
    GeneIDi 396442.
    KEGGi gga:396442.

    Organism-specific databases

    CTDi 6714.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00620000087702.
    HOVERGENi HBG008761.
    InParanoidi P00523.
    KOi K05704.
    OMAi CQCWRKD.
    OrthoDBi EOG7GTT2V.
    PhylomeDBi P00523.
    TreeFami TF351634.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 1306.
    Reactomei REACT_189763. Signaling by ERBB2.
    REACT_194391. Signaling by SCF-KIT.
    REACT_196766. Regulation of KIT signaling.
    REACT_204997. Netrin mediated repulsion signals.
    REACT_207020. DCC mediated attractive signaling.
    REACT_217737. GAB1 signalosome.
    REACT_220416. c-src mediated regulation of Cx43 function and closure of gap junctions.
    REACT_226416. p38MAPK events.

    Miscellaneous databases

    EvolutionaryTracei P00523.
    NextBioi 20816483.
    PROi P00523.

    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

    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. 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.

    Entry informationi

    Entry nameiSRC_CHICK
    AccessioniPrimary (citable) accession number: P00523
    Secondary accession number(s): Q90992
    , Q90993, Q91343, Q91345, Q92013, Q98915
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 171 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3