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SRC_CHICK
ID   SRC_CHICK               Reviewed;         533 AA.
AC   P00523; Q90992; Q90993; Q91343; Q91345; Q92013; Q98915;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 235.
DE   RecName: Full=Proto-oncogene tyrosine-protein kinase Src;
DE            EC=2.7.10.2;
DE   AltName: Full=Proto-oncogene c-Src;
DE   AltName: Full=pp60c-src;
DE            Short=p60-Src;
GN   Name=SRC;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=6299580; DOI=10.1016/0092-8674(83)90073-9;
RA   Takeya T., Hanafusa H.;
RT   "Structure and sequence of the cellular gene homologous to the RSV src gene
RT   and the mechanism for generating the transforming virus.";
RL   Cell 32:881-890(1983).
RN   [2]
RP   ERRATUM OF PUBMED:6299580, AND SEQUENCE REVISION TO 526.
RA   Takeya T., Hanafusa H.;
RL   Cell 34:319-319(1983).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Pectoralis muscle;
RX   PubMed=2115117; DOI=10.1128/mcb.10.8.4068-4079.1990;
RA   Dorai T., Wang L.-H.;
RT   "An alternative non-tyrosine protein kinase product of the c-src gene in
RT   chicken skeletal muscle.";
RL   Mol. Cell. Biol. 10:4068-4079(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PHOSPHORYLATION AT TYR-416 AND
RP   TYR-436.
RX   PubMed=8856081; DOI=10.1111/j.1432-1033.1996.0756h.x;
RA   Weijland A., Neubauer G., Courtneidge S.A., Mann M., Wierenga R.K.,
RA   Superti-Furga G.;
RT   "The purification and characterization of the catalytic domain of Src
RT   expressed in Schizosaccharomyces pombe. Comparison of unphosphorylated and
RT   tyrosine phosphorylated species.";
RL   Eur. J. Biochem. 240:756-764(1996).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
RX   PubMed=6292480; DOI=10.1128/jvi.44.1.12-18.1982;
RA   Takeya T., Hanafusa H.;
RT   "DNA sequence of the viral and cellular src gene of chickens. II.
RT   Comparison of the src genes of two strains of Avian sarcoma virus and of
RT   the cellular homolog.";
RL   J. Virol. 44:12-18(1982).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-19 AND 485-534 (ISOFORM 1).
RX   PubMed=1712905; DOI=10.1128/mcb.11.8.4165-4176.1991;
RA   Dorai T., Levy J.B., Kang L., Brugge J.S., Wang L.-H.;
RT   "Analysis of cDNAs of the proto-oncogene c-src: heterogeneity in 5' exons
RT   and possible mechanism for the genesis of the 3' end of v-src.";
RL   Mol. Cell. Biol. 11:4165-4176(1991).
RN   [7]
RP   ATP-BINDING SITE.
RX   PubMed=6431300; DOI=10.1038/310589a0;
RA   Kamps M.P., Taylor S.S., Sefton B.M.;
RT   "Direct evidence that oncogenic tyrosine kinases and cyclic AMP-dependent
RT   protein kinase have homologous ATP-binding sites.";
RL   Nature 310:589-592(1984).
RN   [8]
RP   PHOSPHORYLATION AT SER-12.
RX   PubMed=2996780; DOI=10.1016/0092-8674(85)90281-8;
RA   Gould K.L., Woodgett J.R., Cooper J.A., Buss J.E., Shalloway D., Hunter T.;
RT   "Protein kinase C phosphorylates pp60src at a novel site.";
RL   Cell 42:849-857(1985).
RN   [9]
RP   PHOSPHORYLATION AT TYR-416.
RX   PubMed=6273838; DOI=10.1073/pnas.78.10.6013;
RA   Smart J.E., Oppermann H., Czernilofsky A.P., Purchio A.F., Erikson R.L.,
RA   Bishop J.M.;
RT   "Characterization of sites for tyrosine phosphorylation in the transforming
RT   protein of Rous sarcoma virus (pp60v-src) and its normal cellular homologue
RT   (pp60c-src).";
RL   Proc. Natl. Acad. Sci. U.S.A. 78:6013-6017(1981).
RN   [10]
RP   PHOSPHORYLATION AT TYR-527.
RX   PubMed=2420005; DOI=10.1126/science.2420005;
RA   Cooper J.A., Gould K.L., Cartwright C.A., Hunter T.;
RT   "Tyr527 is phosphorylated in pp60c-src: implications for regulation.";
RL   Science 231:1431-1434(1986).
RN   [11]
RP   PHOSPHORYLATION AT THR-34; THR-46 AND SER-72.
RX   PubMed=2470512; DOI=10.1016/0092-8674(89)90791-5;
RA   Shenoy S., Choi J.K., Bagrodia S., Copeland T.D., Maller J.L.,
RA   Shalloway D.;
RT   "Purified maturation promoting factor phosphorylates pp60c-src at the sites
RT   phosphorylated during fibroblast mitosis.";
RL   Cell 57:763-774(1989).
RN   [12]
RP   FUNCTION IN THE NGF AND FGF SIGNALING PATHWAYS.
RX   PubMed=1717492; DOI=10.1083/jcb.115.3.809;
RA   Kremer N.E., D'Arcangelo G., Thomas S.M., DeMarco M., Brugge J.S.,
RA   Halegoua S.;
RT   "Signal transduction by nerve growth factor and fibroblast growth factor in
RT   PC12 cells requires a sequence of src and ras actions.";
RL   J. Cell Biol. 115:809-819(1991).
RN   [13]
RP   SUBCELLULAR LOCATION.
RX   PubMed=1378446; DOI=10.1083/jcb.118.2.321;
RA   Kaplan K.B., Swedlow J.R., Varmus H.E., Morgan D.O.;
RT   "Association of p60c-src with endosomal membranes in mammalian
RT   fibroblasts.";
RL   J. Cell Biol. 118:321-333(1992).
RN   [14]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH PXN.
RX   PubMed=8325872; DOI=10.1016/s0021-9258(18)82425-5;
RA   Weng Z., Taylor J.A., Turner C.E., Brugge J.S., Seidel-Dugan C.;
RT   "Detection of Src homology 3-binding proteins, including paxillin, in
RT   normal and v-Src-transformed Balb/c 3T3 cells.";
RL   J. Biol. Chem. 268:14956-14963(1993).
RN   [15]
RP   FUNCTION IN THE EDN1 SIGNALING PATHWAY, AND SUBCELLULAR LOCATION.
RX   PubMed=8550628; DOI=10.1074/jbc.271.1.77;
RA   Simonson M.S., Wang Y., Herman W.H.;
RT   "Nuclear signaling by endothelin-1 requires Src protein-tyrosine kinases.";
RL   J. Biol. Chem. 271:77-82(1996).
RN   [16]
RP   INTERACTION WITH AFAP-110.
RX   PubMed=9655255;
RX   DOI=10.1002/(sici)1098-2744(199806)22:2<110::aid-mc6>3.0.co;2-q;
RA   Guappone A.C., Weimer T., Flynn D.C.;
RT   "Formation of a stable src-AFAP-110 complex through either an amino-
RT   terminal or a carboxy-terminal SH2-binding motif.";
RL   Mol. Carcinog. 22:110-119(1998).
RN   [17]
RP   INTERACTION WITH GJA1.
RX   PubMed=15492000; DOI=10.1074/jbc.m409552200;
RA   Sorgen P.L., Duffy H.S., Sahoo P., Coombs W., Delmar M., Spray D.C.;
RT   "Structural changes in the carboxyl terminus of the gap junction protein
RT   connexin43 indicates signaling between binding domains for c-Src and zonula
RT   occludens-1.";
RL   J. Biol. Chem. 279:54695-54701(2004).
RN   [18]
RP   FUNCTION, AND MUTAGENESIS OF TYR-527.
RX   PubMed=19307596; DOI=10.1083/jcb.200810155;
RA   Zhang Y., Tu Y., Zhao J., Chen K., Wu C.;
RT   "Reversion-induced LIM interaction with Src reveals a novel Src
RT   inactivation cycle.";
RL   J. Cell Biol. 184:785-792(2009).
RN   [19]
RP   S-NITROSYLATION AT CYS-498, AND MUTAGENESIS OF CYS-498.
RX   PubMed=19948721; DOI=10.1074/jbc.m109.059782;
RA   Rahman M.A., Senga T., Ito S., Hyodo T., Hasegawa H., Hamaguchi M.;
RT   "S-nitrosylation at cysteine 498 of c-Src tyrosine kinase regulates nitric
RT   oxide-mediated cell invasion.";
RL   J. Biol. Chem. 285:3806-3814(2010).
RN   [20]
RP   REVIEW ON FUNCTION.
RX   PubMed=8672527; DOI=10.1016/0304-419x(96)00003-0;
RA   Brown M.T., Cooper J.A.;
RT   "Regulation, substrates and functions of src.";
RL   Biochim. Biophys. Acta 1287:121-149(1996).
RN   [21]
RP   REVIEW ON FUNCTION.
RX   PubMed=9442882; DOI=10.1146/annurev.cellbio.13.1.513;
RA   Thomas S.M., Brugge J.S.;
RT   "Cellular functions regulated by Src family kinases.";
RL   Annu. Rev. Cell Dev. Biol. 13:513-609(1997).
RN   [22]
RP   REVIEW ON FUNCTION.
RX   PubMed=11964124; DOI=10.1007/s00018-002-8438-2;
RA   Ma Y.C., Huang X.Y.;
RT   "Novel regulation and function of Src tyrosine kinase.";
RL   Cell. Mol. Life Sci. 59:456-462(2002).
RN   [23]
RP   X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 83-533.
RX   PubMed=9405157; DOI=10.1006/jmbi.1997.1426;
RA   Williams J.C., Weijland A., Gonfloni S., Thompson A., Courtneidge S.A.,
RA   Superti-Furga G., Wierenga R.K.;
RT   "The 2.35 A crystal structure of the inactivated form of chicken Src: a
RT   dynamic molecule with multiple regulatory interactions.";
RL   J. Mol. Biol. 274:757-775(1997).
RN   [24]
RP   STRUCTURE BY NMR OF 81-140.
RX   PubMed=8504863; DOI=10.1016/0014-5793(93)81538-b;
RA   Yu H., Rosen M.K., Schreiber S.L.;
RT   "1H and 15N assignments and secondary structure of the Src SH3 domain.";
RL   FEBS Lett. 324:87-92(1993).
CC   -!- FUNCTION: Non-receptor protein tyrosine kinase which is activated
CC       following engagement of many different classes of cellular receptors
CC       including immune response receptors, integrins and other adhesion
CC       receptors, receptor protein tyrosine kinases, G protein-coupled
CC       receptors as well as cytokine receptors. Participates in signaling
CC       pathways that control a diverse spectrum of biological activities
CC       including gene transcription, immune response, cell adhesion, cell
CC       cycle progression, apoptosis, migration, and transformation. Due to
CC       functional redundancy between members of the SRC kinase family,
CC       identification of the specific role of each SRC kinase is very
CC       difficult. SRC appears to be one of the primary kinases activated
CC       following engagement of receptors and plays a role in the activation of
CC       other protein tyrosine kinase (PTK) families. Receptor clustering or
CC       dimerization leads to recruitment of SRC to the receptor complexes
CC       where it phosphorylates the tyrosine residues within the receptor
CC       cytoplasmic domains. Plays an important role in the regulation of
CC       cytoskeletal organization through phosphorylation of specific
CC       substrates involved in this process (Probable). When cells adhere via
CC       focal adhesions to the extracellular matrix, signals are transmitted by
CC       integrins into the cell resulting in tyrosine phosphorylation of a
CC       number of focal adhesion proteins, including PTK2/FAK1 and paxillin
CC       (PXN) (By similarity). Also active at the sites of cell-cell contact
CC       adherens junctions and at gap junctions. Implicated in the regulation
CC       of pre-mRNA-processing (Probable). Might be involved not only in
CC       mediating the transduction of mitogenic signals at the level of the
CC       plasma membrane but also in controlling progression through the cell
CC       cycle via interaction with regulatory proteins in the nucleus
CC       (PubMed:1717492, PubMed:8550628). Involved in anchorage-independent
CC       cell growth (PubMed:19307596). {ECO:0000250|UniProtKB:P12931,
CC       ECO:0000269|PubMed:1717492, ECO:0000269|PubMed:19307596,
CC       ECO:0000269|PubMed:8550628, ECO:0000305|PubMed:11964124,
CC       ECO:0000305|PubMed:8672527, ECO:0000305|PubMed:9442882}.
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   -!- ACTIVITY REGULATION: Becomes activated when its major tyrosine
CC       phosphorylation site is not phosphorylated. It can also be activated by
CC       point mutations as well as by truncations at the C-terminal end or by
CC       other mutations. Heme regulates its activity by enhancing the
CC       phosphorylation on Tyr-527 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms a complex with polyoma virus middle T antigen. Interacts
CC       with AFAP-110. Interacts with GJA1 and PXN.
CC       {ECO:0000269|PubMed:15492000, ECO:0000269|PubMed:8325872,
CC       ECO:0000269|PubMed:9655255}.
CC   -!- INTERACTION:
CC       P00523; Q90738: AFAP1; NbExp=3; IntAct=EBI-848039, EBI-8562073;
CC       P00523; Q00944: PTK2; NbExp=3; IntAct=EBI-848039, EBI-2896409;
CC       P00523; Q9QWY8-1: Asap1; Xeno; NbExp=3; IntAct=EBI-848039, EBI-698517;
CC       P00523; Q9QWY8-2: Asap1; Xeno; NbExp=2; IntAct=EBI-848039, EBI-698524;
CC       P00523; Q9NZA1: CLIC5; Xeno; NbExp=2; IntAct=EBI-848039, EBI-5658997;
CC       P00523; P41240: CSK; Xeno; NbExp=7; IntAct=EBI-848039, EBI-1380630;
CC       P00523; Q9Y4D1: DAAM1; Xeno; NbExp=3; IntAct=EBI-848039, EBI-2817289;
CC       P00523; P03372: ESR1; Xeno; NbExp=2; IntAct=EBI-848039, EBI-78473;
CC       P00523; O88703: Hcn2; Xeno; NbExp=5; IntAct=EBI-848039, EBI-771231;
CC       P00523; P18052: Ptpra; Xeno; NbExp=2; IntAct=EBI-848039, EBI-6597520;
CC       P00523; P18433: PTPRA; Xeno; NbExp=4; IntAct=EBI-848039, EBI-2609645;
CC       P00523; Q9QWI6-2: Srcin1; Xeno; NbExp=2; IntAct=EBI-848039, EBI-775607;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1378446,
CC       ECO:0000269|PubMed:8325872}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P05480}. Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P05480}. Endosome membrane
CC       {ECO:0000269|PubMed:1378446}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:1378446}. Nucleus {ECO:0000269|PubMed:8550628}.
CC       Cytoplasm, cytoskeleton {ECO:0000269|PubMed:8325872}. Cell junction,
CC       focal adhesion {ECO:0000250|UniProtKB:P05480}. Cytoplasm, perinuclear
CC       region {ECO:0000250|UniProtKB:P12931}. Note=Localizes to focal adhesion
CC       sites following integrin engagement (By similarity). Localization to
CC       focal adhesion sites requires myristoylation and the SH3 domain.
CC       {ECO:0000250|UniProtKB:P05480, ECO:0000250|UniProtKB:P12931}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P00523-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P00523-2; Sequence=VSP_011844, VSP_011845;
CC   -!- TISSUE SPECIFICITY: Expressed to high levels, and with a high degree of
CC       kinase activity, in certain fully differentiated cells such as neurons,
CC       platelets and macrophages. Isoform 1 is widely expressed. Isoform 2 is
CC       expressed only in the muscle.
CC   -!- PTM: Myristoylated at Gly-2, and this is essential for targeting to
CC       membranes. {ECO:0000250}.
CC   -!- PTM: Dephosphorylated at Tyr-527 by PTPRJ. Phosphorylated on Tyr-527 by
CC       c-Src kinase (CSK). The phosphorylated form is termed pp60c-src.
CC       Dephosphorylated by PTPRJ at Tyr-416. Normally maintained in an
CC       inactive conformation with the SH2 domain engaged with Tyr-527, the SH3
CC       domain engaged with the SH2-kinase linker, and Tyr-416
CC       dephosphorylated. Dephosphorylation of Tyr-527 as a result of protein
CC       tyrosine phosphatase (PTP) action disrupts the intramolecular
CC       interaction between the SH2 domain and Tyr-527, Tyr-416 can then become
CC       autophosphorylated, resulting in SRC activation. Phosphorylation of
CC       Tyr-527 by CSK allows this interaction to reform, resulting in SRC
CC       inactivation (By similarity). {ECO:0000250}.
CC   -!- PTM: S-nitrosylation is important for activation of its kinase
CC       activity. {ECO:0000269|PubMed:19948721}.
CC   -!- MISCELLANEOUS: [Isoform 2]: Membrane-bound. {ECO:0000305}.
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; V00402; CAA23696.1; -; Genomic_DNA.
DR   EMBL; J00908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M57290; AAA49078.1; -; mRNA.
DR   EMBL; S43604; AAD13831.1; -; mRNA.
DR   EMBL; S43616; AAD13835.1; -; mRNA.
DR   EMBL; S43587; AAD13830.1; -; mRNA.
DR   EMBL; S43609; AAD13832.1; -; mRNA.
DR   EMBL; S43614; AAD13834.1; -; mRNA.
DR   EMBL; S43579; AAB19353.2; -; mRNA.
DR   PIR; A00630; TVCHS.
DR   RefSeq; NP_990788.2; NM_205457.2.
DR   RefSeq; XP_015151834.1; XM_015296348.1. [P00523-1]
DR   PDB; 1F1W; X-ray; 2.10 A; A=145-247.
DR   PDB; 1F2F; X-ray; 1.70 A; A=145-247.
DR   PDB; 1NLO; NMR; -; C=81-140.
DR   PDB; 1NLP; NMR; -; C=81-140.
DR   PDB; 1P13; X-ray; 1.63 A; A/B=145-246.
DR   PDB; 1PRL; NMR; -; C=77-140.
DR   PDB; 1PRM; NMR; -; C=77-140.
DR   PDB; 1RLP; NMR; -; C=77-140.
DR   PDB; 1RLQ; NMR; -; C=77-140.
DR   PDB; 1SRL; NMR; -; A=77-140.
DR   PDB; 1SRM; NMR; -; A=77-140.
DR   PDB; 2HWO; X-ray; 2.50 A; A/B=251-533.
DR   PDB; 2HWP; X-ray; 2.48 A; A/B=251-533.
DR   PDB; 2OIQ; X-ray; 2.07 A; A/B=251-533.
DR   PDB; 2PTK; X-ray; 2.35 A; A=81-533.
DR   PDB; 2QI8; X-ray; 2.32 A; A/B=251-533.
DR   PDB; 2QLQ; X-ray; 2.33 A; A/B=251-533.
DR   PDB; 2QQ7; X-ray; 2.38 A; A/B=251-533.
DR   PDB; 3D7T; X-ray; 2.90 A; B=251-533.
DR   PDB; 3D7U; X-ray; 4.11 A; B/D=260-523.
DR   PDB; 3DQW; X-ray; 2.02 A; A/B/C/D=251-533.
DR   PDB; 3DQX; X-ray; 2.30 A; A/B=251-533.
DR   PDB; 3EL7; X-ray; 2.80 A; A=251-533.
DR   PDB; 3EL8; X-ray; 2.30 A; A/B=251-533.
DR   PDB; 3EN4; X-ray; 2.55 A; A/B=251-533.
DR   PDB; 3EN5; X-ray; 2.66 A; A/B=251-533.
DR   PDB; 3EN6; X-ray; 2.39 A; A/B=251-533.
DR   PDB; 3EN7; X-ray; 2.81 A; A/B=251-533.
DR   PDB; 3F3T; X-ray; 2.50 A; A/B=251-533.
DR   PDB; 3F3U; X-ray; 2.50 A; A/B=251-533.
DR   PDB; 3F3V; X-ray; 2.60 A; A/B=251-533.
DR   PDB; 3F3W; X-ray; 2.60 A; A/B=251-533.
DR   PDB; 3F6X; X-ray; 2.35 A; A/B/C/D=251-533.
DR   PDB; 3FJ5; X-ray; 1.65 A; A/B=85-140.
DR   PDB; 3G5D; X-ray; 2.20 A; A/B=251-533.
DR   PDB; 3G6G; X-ray; 2.31 A; A/B=251-533.
DR   PDB; 3G6H; X-ray; 2.35 A; A/B=251-533.
DR   PDB; 3GEQ; X-ray; 2.20 A; A/B=251-533.
DR   PDB; 3LOK; X-ray; 2.48 A; A/B=251-533.
DR   PDB; 3OEZ; X-ray; 2.40 A; A/B=251-533.
DR   PDB; 3OF0; X-ray; 2.70 A; A/B=251-533.
DR   PDB; 3QLF; X-ray; 2.75 A; A/B=251-533.
DR   PDB; 3QLG; X-ray; 2.75 A; A/B=251-533.
DR   PDB; 3SVV; X-ray; 2.20 A; A/B=251-533.
DR   PDB; 3TZ7; X-ray; 3.30 A; A/B=251-533.
DR   PDB; 3TZ8; X-ray; 2.70 A; A/B=251-533.
DR   PDB; 3TZ9; X-ray; 3.10 A; A/B=251-533.
DR   PDB; 3U4W; X-ray; 1.90 A; A=259-533.
DR   PDB; 3U51; X-ray; 2.24 A; A/B=259-533.
DR   PDB; 3UQF; X-ray; 2.27 A; A/B=251-533.
DR   PDB; 3UQG; X-ray; 2.20 A; A/B=251-533.
DR   PDB; 4AGW; X-ray; 2.60 A; A/B=251-533.
DR   PDB; 4DGG; X-ray; 2.65 A; A/B=251-533.
DR   PDB; 4FIC; X-ray; 2.50 A; A/B=251-533.
DR   PDB; 4HVU; X-ray; 0.98 A; A=85-141.
DR   PDB; 4HVV; X-ray; 1.10 A; A=85-140.
DR   PDB; 4HVW; X-ray; 0.98 A; A=85-141.
DR   PDB; 4JZ3; X-ray; 1.85 A; A=85-141.
DR   PDB; 4JZ4; X-ray; 1.56 A; A/B=85-141.
DR   PDB; 4LE9; X-ray; 1.34 A; A=85-141.
DR   PDB; 4LGG; X-ray; 2.41 A; A/B=264-533.
DR   PDB; 4LGH; X-ray; 2.84 A; A/B=257-533.
DR   PDB; 4MCV; X-ray; 2.73 A; A/B=256-533.
DR   PDB; 4O2P; X-ray; 2.10 A; A/B=251-533.
DR   PDB; 4OML; X-ray; 1.60 A; A=85-141.
DR   PDB; 4OMM; X-ray; 1.90 A; A=85-140.
DR   PDB; 4OMN; X-ray; 1.50 A; A=85-140.
DR   PDB; 4OMO; X-ray; 1.04 A; A/B=85-141.
DR   PDB; 4OMP; X-ray; 2.00 A; A=85-139.
DR   PDB; 4OMQ; X-ray; 2.00 A; A=85-140.
DR   PDB; 4QT7; X-ray; 1.55 A; A=85-141.
DR   PDB; 4RTU; X-ray; 2.45 A; A=85-141.
DR   PDB; 4RTV; X-ray; 1.37 A; A=85-141.
DR   PDB; 4RTW; X-ray; 1.24 A; A/C=85-141.
DR   PDB; 4RTX; X-ray; 1.32 A; A/B/C/D=85-141.
DR   PDB; 4RTY; X-ray; 1.28 A; A=85-141.
DR   PDB; 4RTZ; X-ray; 0.98 A; A=85-141.
DR   PDB; 4U5J; X-ray; 2.26 A; A/B=251-533.
DR   PDB; 4YBJ; X-ray; 2.61 A; A/B=251-533.
DR   PDB; 4YBK; X-ray; 2.50 A; A=251-533.
DR   PDB; 5BMM; X-ray; 2.50 A; A/B=251-533.
DR   PDB; 5D10; X-ray; 2.70 A; A/B=251-533.
DR   PDB; 5D11; X-ray; 2.30 A; A/B=251-533.
DR   PDB; 5D12; X-ray; 3.00 A; A/B=251-533.
DR   PDB; 5EC7; X-ray; 1.65 A; A/B/C=85-140.
DR   PDB; 5ECA; X-ray; 1.16 A; A=85-141.
DR   PDB; 5I11; X-ray; 1.95 A; A=85-141.
DR   PDB; 5J5S; X-ray; 2.15 A; A/B=251-533.
DR   PDB; 5K9I; X-ray; 2.50 A; A/B=251-533.
DR   PDB; 5OAV; X-ray; 0.95 A; A/C=85-141.
DR   PDB; 5OB0; X-ray; 1.17 A; A=85-141.
DR   PDB; 5OB1; X-ray; 1.17 A; A=85-141.
DR   PDB; 5OB2; X-ray; 1.80 A; A/C=85-141.
DR   PDB; 5SWH; X-ray; 2.50 A; A/B=252-533.
DR   PDB; 5SYS; X-ray; 2.80 A; A/B=251-533.
DR   PDB; 5T0P; X-ray; 2.50 A; A/B=251-533.
DR   PDB; 5TEH; X-ray; 2.99 A; A/B=251-533.
DR   PDB; 5XP5; X-ray; 2.10 A; A/B=251-533.
DR   PDB; 5XP7; X-ray; 2.01 A; A/B=251-533.
DR   PDB; 6HVE; X-ray; 1.90 A; A/B=251-533.
DR   PDB; 6HVF; X-ray; 2.10 A; A/B=251-533.
DR   PDB; 6L8L; X-ray; 2.89 A; A/B/C/D=251-533.
DR   PDB; 6WIW; X-ray; 2.30 A; A/B=251-533.
DR   PDB; 6XVM; X-ray; 0.90 A; A/B/C/D=82-141.
DR   PDB; 6XVN; X-ray; 1.70 A; A/B=82-141.
DR   PDB; 6XVO; X-ray; 1.70 A; A=82-141.
DR   PDB; 6XX2; X-ray; 1.25 A; A=85-141.
DR   PDB; 6XX3; X-ray; 1.36 A; A=85-141.
DR   PDB; 6XX4; X-ray; 1.05 A; A=85-141.
DR   PDB; 6XX5; X-ray; 1.30 A; A=85-141.
DR   PDB; 7A30; X-ray; 1.67 A; A=82-141.
DR   PDB; 7A31; X-ray; 0.94 A; A/B=82-141.
DR   PDB; 7A32; X-ray; 1.15 A; A/B/C/D=82-141.
DR   PDB; 7A33; X-ray; 0.96 A; A/B=82-141.
DR   PDB; 7A34; X-ray; 1.85 A; A=82-141.
DR   PDB; 7A35; X-ray; 1.31 A; A/B=82-141.
DR   PDB; 7A36; X-ray; 1.50 A; A/B=82-141.
DR   PDB; 7A37; X-ray; 1.52 A; A/B=82-141.
DR   PDB; 7A38; X-ray; 1.62 A; A/B=82-141.
DR   PDB; 7A39; X-ray; 1.65 A; A/B=82-141.
DR   PDB; 7A3A; X-ray; 1.80 A; A=82-141.
DR   PDB; 7A3B; X-ray; 1.91 A; A=82-141.
DR   PDB; 7A3C; X-ray; 1.80 A; A/B/C/D=81-141.
DR   PDB; 7A3D; X-ray; 2.20 A; A/B=82-141.
DR   PDB; 7A3E; X-ray; 1.52 A; A=81-141.
DR   PDB; 7AH3; X-ray; 1.95 A; A/B=251-533.
DR   PDB; 7D57; X-ray; 2.10 A; A/B=251-533.
DR   PDB; 7D5O; X-ray; 2.69 A; A/B=251-533.
DR   PDB; 7NER; X-ray; 1.55 A; A=81-141.
DR   PDB; 7NES; X-ray; 1.35 A; A=81-141.
DR   PDB; 7NET; X-ray; 1.50 A; A/B=81-141.
DR   PDB; 7WF5; X-ray; 1.80 A; A/B=251-533.
DR   PDBsum; 1F1W; -.
DR   PDBsum; 1F2F; -.
DR   PDBsum; 1NLO; -.
DR   PDBsum; 1NLP; -.
DR   PDBsum; 1P13; -.
DR   PDBsum; 1PRL; -.
DR   PDBsum; 1PRM; -.
DR   PDBsum; 1RLP; -.
DR   PDBsum; 1RLQ; -.
DR   PDBsum; 1SRL; -.
DR   PDBsum; 1SRM; -.
DR   PDBsum; 2HWO; -.
DR   PDBsum; 2HWP; -.
DR   PDBsum; 2OIQ; -.
DR   PDBsum; 2PTK; -.
DR   PDBsum; 2QI8; -.
DR   PDBsum; 2QLQ; -.
DR   PDBsum; 2QQ7; -.
DR   PDBsum; 3D7T; -.
DR   PDBsum; 3D7U; -.
DR   PDBsum; 3DQW; -.
DR   PDBsum; 3DQX; -.
DR   PDBsum; 3EL7; -.
DR   PDBsum; 3EL8; -.
DR   PDBsum; 3EN4; -.
DR   PDBsum; 3EN5; -.
DR   PDBsum; 3EN6; -.
DR   PDBsum; 3EN7; -.
DR   PDBsum; 3F3T; -.
DR   PDBsum; 3F3U; -.
DR   PDBsum; 3F3V; -.
DR   PDBsum; 3F3W; -.
DR   PDBsum; 3F6X; -.
DR   PDBsum; 3FJ5; -.
DR   PDBsum; 3G5D; -.
DR   PDBsum; 3G6G; -.
DR   PDBsum; 3G6H; -.
DR   PDBsum; 3GEQ; -.
DR   PDBsum; 3LOK; -.
DR   PDBsum; 3OEZ; -.
DR   PDBsum; 3OF0; -.
DR   PDBsum; 3QLF; -.
DR   PDBsum; 3QLG; -.
DR   PDBsum; 3SVV; -.
DR   PDBsum; 3TZ7; -.
DR   PDBsum; 3TZ8; -.
DR   PDBsum; 3TZ9; -.
DR   PDBsum; 3U4W; -.
DR   PDBsum; 3U51; -.
DR   PDBsum; 3UQF; -.
DR   PDBsum; 3UQG; -.
DR   PDBsum; 4AGW; -.
DR   PDBsum; 4DGG; -.
DR   PDBsum; 4FIC; -.
DR   PDBsum; 4HVU; -.
DR   PDBsum; 4HVV; -.
DR   PDBsum; 4HVW; -.
DR   PDBsum; 4JZ3; -.
DR   PDBsum; 4JZ4; -.
DR   PDBsum; 4LE9; -.
DR   PDBsum; 4LGG; -.
DR   PDBsum; 4LGH; -.
DR   PDBsum; 4MCV; -.
DR   PDBsum; 4O2P; -.
DR   PDBsum; 4OML; -.
DR   PDBsum; 4OMM; -.
DR   PDBsum; 4OMN; -.
DR   PDBsum; 4OMO; -.
DR   PDBsum; 4OMP; -.
DR   PDBsum; 4OMQ; -.
DR   PDBsum; 4QT7; -.
DR   PDBsum; 4RTU; -.
DR   PDBsum; 4RTV; -.
DR   PDBsum; 4RTW; -.
DR   PDBsum; 4RTX; -.
DR   PDBsum; 4RTY; -.
DR   PDBsum; 4RTZ; -.
DR   PDBsum; 4U5J; -.
DR   PDBsum; 4YBJ; -.
DR   PDBsum; 4YBK; -.
DR   PDBsum; 5BMM; -.
DR   PDBsum; 5D10; -.
DR   PDBsum; 5D11; -.
DR   PDBsum; 5D12; -.
DR   PDBsum; 5EC7; -.
DR   PDBsum; 5ECA; -.
DR   PDBsum; 5I11; -.
DR   PDBsum; 5J5S; -.
DR   PDBsum; 5K9I; -.
DR   PDBsum; 5OAV; -.
DR   PDBsum; 5OB0; -.
DR   PDBsum; 5OB1; -.
DR   PDBsum; 5OB2; -.
DR   PDBsum; 5SWH; -.
DR   PDBsum; 5SYS; -.
DR   PDBsum; 5T0P; -.
DR   PDBsum; 5TEH; -.
DR   PDBsum; 5XP5; -.
DR   PDBsum; 5XP7; -.
DR   PDBsum; 6HVE; -.
DR   PDBsum; 6HVF; -.
DR   PDBsum; 6L8L; -.
DR   PDBsum; 6WIW; -.
DR   PDBsum; 6XVM; -.
DR   PDBsum; 6XVN; -.
DR   PDBsum; 6XVO; -.
DR   PDBsum; 6XX2; -.
DR   PDBsum; 6XX3; -.
DR   PDBsum; 6XX4; -.
DR   PDBsum; 6XX5; -.
DR   PDBsum; 7A30; -.
DR   PDBsum; 7A31; -.
DR   PDBsum; 7A32; -.
DR   PDBsum; 7A33; -.
DR   PDBsum; 7A34; -.
DR   PDBsum; 7A35; -.
DR   PDBsum; 7A36; -.
DR   PDBsum; 7A37; -.
DR   PDBsum; 7A38; -.
DR   PDBsum; 7A39; -.
DR   PDBsum; 7A3A; -.
DR   PDBsum; 7A3B; -.
DR   PDBsum; 7A3C; -.
DR   PDBsum; 7A3D; -.
DR   PDBsum; 7A3E; -.
DR   PDBsum; 7AH3; -.
DR   PDBsum; 7D57; -.
DR   PDBsum; 7D5O; -.
DR   PDBsum; 7NER; -.
DR   PDBsum; 7NES; -.
DR   PDBsum; 7NET; -.
DR   PDBsum; 7WF5; -.
DR   AlphaFoldDB; P00523; -.
DR   BMRB; P00523; -.
DR   SMR; P00523; -.
DR   BioGRID; 676691; 4.
DR   DIP; DIP-449N; -.
DR   ELM; P00523; -.
DR   IntAct; P00523; 19.
DR   MINT; P00523; -.
DR   STRING; 9031.ENSGALP00000006117; -.
DR   BindingDB; P00523; -.
DR   ChEMBL; CHEMBL3655; -.
DR   DrugCentral; P00523; -.
DR   iPTMnet; P00523; -.
DR   PaxDb; P00523; -.
DR   Ensembl; ENSGALT00000061823; ENSGALP00000049896; ENSGALG00000003855. [P00523-1]
DR   Ensembl; ENSGALT00000070498; ENSGALP00000054990; ENSGALG00000003855. [P00523-1]
DR   Ensembl; ENSGALT00000093274; ENSGALP00000068298; ENSGALG00000003855. [P00523-1]
DR   GeneID; 396442; -.
DR   KEGG; gga:396442; -.
DR   CTD; 6714; -.
DR   VEuPathDB; HostDB:geneid_396442; -.
DR   eggNOG; KOG0197; Eukaryota.
DR   GeneTree; ENSGT00940000158250; -.
DR   HOGENOM; CLU_000288_7_2_1; -.
DR   InParanoid; P00523; -.
DR   OrthoDB; 539311at2759; -.
DR   PhylomeDB; P00523; -.
DR   TreeFam; TF351634; -.
DR   BRENDA; 2.7.10.2; 1306.
DR   Reactome; R-GGA-1227986; Signaling by ERBB2.
DR   Reactome; R-GGA-1251985; Nuclear signaling by ERBB4.
DR   Reactome; R-GGA-1253288; Downregulation of ERBB4 signaling.
DR   Reactome; R-GGA-1257604; PIP3 activates AKT signaling.
DR   Reactome; R-GGA-1433557; Signaling by SCF-KIT.
DR   Reactome; R-GGA-180292; GAB1 signalosome.
DR   Reactome; R-GGA-186763; Downstream signal transduction.
DR   Reactome; R-GGA-191650; Regulation of gap junction activity.
DR   Reactome; R-GGA-2029481; FCGR activation.
DR   Reactome; R-GGA-210990; PECAM1 interactions.
DR   Reactome; R-GGA-354192; Integrin signaling.
DR   Reactome; R-GGA-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR   Reactome; R-GGA-372708; p130Cas linkage to MAPK signaling for integrins.
DR   Reactome; R-GGA-389356; CD28 co-stimulation.
DR   Reactome; R-GGA-389513; CTLA4 inhibitory signaling.
DR   Reactome; R-GGA-3928662; EPHB-mediated forward signaling.
DR   Reactome; R-GGA-3928663; EPHA-mediated growth cone collapse.
DR   Reactome; R-GGA-3928664; Ephrin signaling.
DR   Reactome; R-GGA-3928665; EPH-ephrin mediated repulsion of cells.
DR   Reactome; R-GGA-418592; ADP signalling through P2Y purinoceptor 1.
DR   Reactome; R-GGA-418594; G alpha (i) signalling events.
DR   Reactome; R-GGA-418885; DCC mediated attractive signaling.
DR   Reactome; R-GGA-430116; GP1b-IX-V activation signalling.
DR   Reactome; R-GGA-437239; Recycling pathway of L1.
DR   Reactome; R-GGA-4420097; VEGFA-VEGFR2 Pathway.
DR   Reactome; R-GGA-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR   Reactome; R-GGA-5218921; VEGFR2 mediated cell proliferation.
DR   Reactome; R-GGA-5674135; MAP2K and MAPK activation.
DR   Reactome; R-GGA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   Reactome; R-GGA-8853659; RET signaling.
DR   Reactome; R-GGA-8874081; MET activates PTK2 signaling.
DR   Reactome; R-GGA-8941858; Regulation of RUNX3 expression and activity.
DR   Reactome; R-GGA-9009391; Extra-nuclear estrogen signaling.
DR   EvolutionaryTrace; P00523; -.
DR   PRO; PR:P00523; -.
DR   Proteomes; UP000000539; Chromosome 20.
DR   Bgee; ENSGALG00000003855; Expressed in cerebellum and 12 other tissues.
DR   ExpressionAtlas; P00523; baseline and differential.
DR   GO; GO:0030054; C:cell junction; ISS:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR   GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0071253; F:connexin binding; IPI:CAFA.
DR   GO; GO:0070851; F:growth factor receptor binding; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR   GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; EXP:Reactome.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0045453; P:bone resorption; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR   GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IBA:GO_Central.
DR   GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IBA:GO_Central.
DR   GO; GO:0036035; P:osteoclast development; IBA:GO_Central.
DR   GO; GO:0050847; P:progesterone receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   Gene3D; 3.30.505.10; -; 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   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; SSF50044; SSF50044; 1.
DR   SUPFAM; SSF55550; SSF55550; 1.
DR   SUPFAM; SSF56112; SSF56112; 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   3D-structure; Alternative splicing; ATP-binding; Cell adhesion; Cell cycle;
KW   Cell junction; Cell membrane; Cytoplasm; Cytoskeleton; Endosome; Immunity;
KW   Kinase; Lipoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Myristate; Nucleotide-binding; Nucleus; Phosphoprotein; Proto-oncogene;
KW   Reference proteome; S-nitrosylation; SH2 domain; SH3 domain; Transferase;
KW   Tyrosine-protein kinase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..533
FT                   /note="Proto-oncogene tyrosine-protein kinase Src"
FT                   /id="PRO_0000088144"
FT   DOMAIN          81..142
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          148..245
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          267..520
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        8..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        386
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         273..281
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         295
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   MOD_RES         12
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000269|PubMed:2996780"
FT   MOD_RES         34
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:2470512"
FT   MOD_RES         46
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:2470512"
FT   MOD_RES         72
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:2470512"
FT   MOD_RES         416
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:6273838,
FT                   ECO:0000269|PubMed:8856081"
FT   MOD_RES         436
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:8856081"
FT   MOD_RES         498
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000269|PubMed:19948721"
FT   MOD_RES         527
FT                   /note="Phosphotyrosine; by CSK"
FT                   /evidence="ECO:0000269|PubMed:2420005"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         183..193
FT                   /note="AYCLSVSDFDN -> DPCIPLPSCLC (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:2115117"
FT                   /id="VSP_011844"
FT   VAR_SEQ         194..533
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:2115117"
FT                   /id="VSP_011845"
FT   MUTAGEN         498
FT                   /note="C->A: Significant reduction in S-nitrosylation."
FT                   /evidence="ECO:0000269|PubMed:19948721"
FT   MUTAGEN         527
FT                   /note="Y->F: Constitutively active."
FT                   /evidence="ECO:0000269|PubMed:19307596"
FT   CONFLICT        301
FT                   /note="T -> N (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        501
FT                   /note="K -> R (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   STRAND          85..90
FT                   /evidence="ECO:0007829|PDB:6XVM"
FT   STRAND          96..99
FT                   /evidence="ECO:0007829|PDB:6XVM"
FT   STRAND          107..110
FT                   /evidence="ECO:0007829|PDB:6XVM"
FT   HELIX           113..115
FT                   /evidence="ECO:0007829|PDB:4LE9"
FT   STRAND          116..123
FT                   /evidence="ECO:0007829|PDB:6XVM"
FT   TURN            124..126
FT                   /evidence="ECO:0007829|PDB:6XVM"
FT   STRAND          129..133
FT                   /evidence="ECO:0007829|PDB:6XVM"
FT   HELIX           134..136
FT                   /evidence="ECO:0007829|PDB:6XVM"
FT   STRAND          137..139
FT                   /evidence="ECO:0007829|PDB:6XVM"
FT   HELIX           143..145
FT                   /evidence="ECO:0007829|PDB:2PTK"
FT   STRAND          149..152
FT                   /evidence="ECO:0007829|PDB:1F1W"
FT   HELIX           155..162
FT                   /evidence="ECO:0007829|PDB:1P13"
FT   STRAND          165..167
FT                   /evidence="ECO:0007829|PDB:2PTK"
FT   STRAND          172..176
FT                   /evidence="ECO:0007829|PDB:1P13"
FT   STRAND          178..180
FT                   /evidence="ECO:0007829|PDB:1P13"
FT   STRAND          184..192
FT                   /evidence="ECO:0007829|PDB:1P13"
FT   TURN            193..195
FT                   /evidence="ECO:0007829|PDB:1P13"
FT   STRAND          196..206
FT                   /evidence="ECO:0007829|PDB:1P13"
FT   STRAND          212..215
FT                   /evidence="ECO:0007829|PDB:1P13"
FT   STRAND          218..222
FT                   /evidence="ECO:0007829|PDB:1P13"
FT   HELIX           223..232
FT                   /evidence="ECO:0007829|PDB:1P13"
FT   STRAND          237..239
FT                   /evidence="ECO:0007829|PDB:1P13"
FT   STRAND          253..258
FT                   /evidence="ECO:0007829|PDB:2PTK"
FT   STRAND          259..261
FT                   /evidence="ECO:0007829|PDB:3GEQ"
FT   HELIX           264..266
FT                   /evidence="ECO:0007829|PDB:3U4W"
FT   STRAND          267..275
FT                   /evidence="ECO:0007829|PDB:3U4W"
FT   STRAND          277..286
FT                   /evidence="ECO:0007829|PDB:3U4W"
FT   TURN            287..289
FT                   /evidence="ECO:0007829|PDB:3U4W"
FT   STRAND          290..297
FT                   /evidence="ECO:0007829|PDB:3U4W"
FT   TURN            299..301
FT                   /evidence="ECO:0007829|PDB:5XP7"
FT   HELIX           304..314
FT                   /evidence="ECO:0007829|PDB:3U4W"
FT   STRAND          325..329
FT                   /evidence="ECO:0007829|PDB:3U4W"
FT   STRAND          331..333
FT                   /evidence="ECO:0007829|PDB:3U4W"
FT   STRAND          335..338
FT                   /evidence="ECO:0007829|PDB:3U4W"
FT   HELIX           346..351
FT                   /evidence="ECO:0007829|PDB:3U4W"
FT   HELIX           353..357
FT                   /evidence="ECO:0007829|PDB:3U4W"
FT   HELIX           360..379
FT                   /evidence="ECO:0007829|PDB:3U4W"
FT   HELIX           389..391
FT                   /evidence="ECO:0007829|PDB:3U4W"
FT   STRAND          392..394
FT                   /evidence="ECO:0007829|PDB:3U4W"
FT   HELIX           396..398
FT                   /evidence="ECO:0007829|PDB:3U4W"
FT   STRAND          400..402
FT                   /evidence="ECO:0007829|PDB:3U4W"
FT   HELIX           405..407
FT                   /evidence="ECO:0007829|PDB:2QI8"
FT   HELIX           408..410
FT                   /evidence="ECO:0007829|PDB:3U4W"
FT   HELIX           414..417
FT                   /evidence="ECO:0007829|PDB:3U4W"
FT   STRAND          421..424
FT                   /evidence="ECO:0007829|PDB:5BMM"
FT   HELIX           426..428
FT                   /evidence="ECO:0007829|PDB:3U4W"
FT   HELIX           431..436
FT                   /evidence="ECO:0007829|PDB:3U4W"
FT   HELIX           441..456
FT                   /evidence="ECO:0007829|PDB:3U4W"
FT   TURN            457..459
FT                   /evidence="ECO:0007829|PDB:3U4W"
FT   HELIX           468..476
FT                   /evidence="ECO:0007829|PDB:3U4W"
FT   HELIX           489..498
FT                   /evidence="ECO:0007829|PDB:3U4W"
FT   HELIX           503..505
FT                   /evidence="ECO:0007829|PDB:3U4W"
FT   HELIX           509..517
FT                   /evidence="ECO:0007829|PDB:3U4W"
FT   HELIX           519..522
FT                   /evidence="ECO:0007829|PDB:3U4W"
SQ   SEQUENCE   533 AA;  60010 MW;  ABDB036F7D63C30A CRC64;
     MGSSKSKPKD PSQRRRSLEP PDSTHHGGFP ASQTPNKTAA PDTHRTPSRS FGTVATEPKL
     FGGFNTSDTV TSPQRAGALA GGVTTFVALY DYESRTETDL SFKKGERLQI VNNTEGDWWL
     AHSLTTGQTG YIPSNYVAPS DSIQAEEWYF GKITRRESER LLLNPENPRG TFLVRESETT
     KGAYCLSVSD FDNAKGLNVK HYKIRKLDSG GFYITSRTQF SSLQQLVAYY SKHADGLCHR
     LTNVCPTSKP QTQGLAKDAW EIPRESLRLE VKLGQGCFGE VWMGTWNGTT RVAIKTLKPG
     TMSPEAFLQE AQVMKKLRHE KLVQLYAVVS EEPIYIVTEY MSKGSLLDFL KGEMGKYLRL
     PQLVDMAAQI ASGMAYVERM NYVHRDLRAA NILVGENLVC KVADFGLARL IEDNEYTARQ
     GAKFPIKWTA PEAALYGRFT IKSDVWSFGI LLTELTTKGR VPYPGMVNRE VLDQVERGYR
     MPCPPECPES LHDLMCQCWR KDPEERPTFE YLQAFLEDYF TSTEPQYQPG ENL
 
 
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