CSK_MOUSE
ID CSK_MOUSE Reviewed; 450 AA.
AC P41241; Q03143; Q80WU4; Q8VCW1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Tyrosine-protein kinase CSK;
DE EC=2.7.10.2 {ECO:0000250|UniProtKB:P41240};
DE AltName: Full=C-Src kinase;
DE AltName: Full=Protein-tyrosine kinase MPK-2;
DE AltName: Full=p50CSK;
GN Name=Csk;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=7511815; DOI=10.1073/pnas.91.7.2597;
RA Klages S., Adam D., Class K., Fargnoli J., Bolen J.B., Penhallow R.C.;
RT "Ctk: a protein-tyrosine kinase related to Csk that defines an enzyme
RT family.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:2597-2601(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CAST/EiJ; TISSUE=Brain;
RA Farber C.R., Corva P.M., Medrano J.F.;
RT "Characterization of quantitative trait loci influencing growth and
RT adiposity using congenic mouse strains.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 316-367.
RC STRAIN=C57BL/6J; TISSUE=Embryonic brain;
RX PubMed=1281307;
RA Gilardi-Hebenstreit P., Nieto M.A., Frain M., Mattei M.-G., Chestier A.,
RA Wilkinson D.G., Charnay P.;
RT "An Eph-related receptor protein tyrosine kinase gene segmentally expressed
RT in the developing mouse hindbrain.";
RL Oncogene 7:2499-2506(1992).
RN [6]
RP PROTEIN SEQUENCE OF 338-347, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=7685657; DOI=10.1016/0092-8674(93)90641-3;
RA Imamoto A., Soriano P.;
RT "Disruption of the csk gene, encoding a negative regulator of Src family
RT tyrosine kinases, leads to neural tube defects and embryonic lethality in
RT mice.";
RL Cell 73:1117-1124(1993).
RN [8]
RP INTERACTION WITH PTPN22.
RX PubMed=8890164; DOI=10.1002/j.1460-2075.1996.tb00871.x;
RA Cloutier J.-F., Veillette A.;
RT "Association of inhibitory tyrosine protein kinase p50csk with protein
RT tyrosine phosphatase PEP in T cells and other hemopoietic cells.";
RL EMBO J. 15:4909-4918(1996).
RN [9]
RP INTERACTION WITH TGFB1I1.
RX PubMed=9858471; DOI=10.1242/jcs.112.2.181;
RA Thomas S.M., Hagel M., Turner C.E.;
RT "Characterization of a focal adhesion protein, Hic-5, that shares extensive
RT homology with paxillin.";
RL J. Cell Sci. 112:181-190(1999).
RN [10]
RP INTERACTION WITH PAG1.
RX PubMed=12218089; DOI=10.4049/jimmunol.169.6.2813;
RA Yasuda K., Nagafuku M., Shima T., Okada M., Yagi T., Yamada T., Minaki Y.,
RA Kato A., Tani-Ichi S., Hamaoka T., Kosugi A.;
RT "Fyn is essential for tyrosine phosphorylation of Csk-binding
RT protein/phosphoprotein associated with glycolipid-enriched microdomains in
RT lipid rafts in resting T cells.";
RL J. Immunol. 169:2813-2817(2002).
RN [11]
RP INTERACTION WITH PAG1.
RX PubMed=12612075; DOI=10.1128/mcb.23.6.2017-2028.2003;
RA Davidson D., Bakinowski M., Thomas M.L., Horejsi V., Veillette A.;
RT "Phosphorylation-dependent regulation of T-cell activation by PAG/Cbp, a
RT lipid raft-associated transmembrane adaptor.";
RL Mol. Cell. Biol. 23:2017-2028(2003).
RN [12]
RP INTERACTION WITH PAG1, AND SUBCELLULAR LOCATION.
RX PubMed=16166631; DOI=10.1128/mcb.25.19.8486-8495.2005;
RA Xu S., Huo J., Tan J.E.-L., Lam K.-P.;
RT "Cbp deficiency alters Csk localization in lipid rafts but does not affect
RT T-cell development.";
RL Mol. Cell. Biol. 25:8486-8495(2005).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP INTERACTION WITH SCIMP.
RX PubMed=28290451; DOI=10.1038/icb.2017.10;
RA Luo L., Tong S.J., Wall A.A., Khromykh T., Sweet M.J., Stow J.L.;
RT "Development of SH2 probes and pull-down assays to detect pathogen-induced,
RT site-specific tyrosine phosphorylation of the TLR adaptor SCIMP.";
RL Immunol. Cell Biol. 95:564-570(2017).
RN [15]
RP STRUCTURE BY NMR OF 1-83.
RX PubMed=11685249; DOI=10.1038/nsb1101-998;
RA Ghose R., Shekhtman A., Goger M.J., Ji H., Cowburn D.;
RT "A novel, specific interaction involving the Csk SH3 domain and its natural
RT ligand.";
RL Nat. Struct. Biol. 8:998-1004(2001).
CC -!- FUNCTION: Non-receptor tyrosine-protein kinase that plays an important
CC role in the regulation of cell growth, differentiation, migration and
CC immune response. Phosphorylates tyrosine residues located in the C-
CC terminal tails of Src-family kinases (SFKs) including LCK, SRC, HCK,
CC FYN, LYN, CSK or YES1. Upon tail phosphorylation, Src-family members
CC engage in intramolecular interactions between the phosphotyrosine tail
CC and the SH2 domain that result in an inactive conformation. To inhibit
CC SFKs, CSK is recruited to the plasma membrane via binding to
CC transmembrane proteins or adapter proteins located near the plasma
CC membrane. Suppresses signaling by various surface receptors, including
CC T-cell receptor (TCR) and B-cell receptor (BCR) by phosphorylating and
CC maintaining inactive several positive effectors such as FYN or LCK (By
CC similarity). {ECO:0000250}.
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:0000250|UniProtKB:P41240, ECO:0000255|PROSITE-
CC ProRule:PRU10028};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P41240};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P41240};
CC -!- SUBUNIT: Homodimer (via SH3-domain) (By similarity). Interacts with
CC PTPN22 (PubMed:8890164). Interacts with phosphorylated SIT1, PAG1,
CC LIME1 and TGFB1I1; these interactions serve to recruit CSK to the
CC membrane where it can phosphorylate and inhibit Src-family kinases
CC (PubMed:9858471, PubMed:12218089, PubMed:12612075, PubMed:16166631).
CC Interacts with SRCIN1 (By similarity). Interacts with RHOH (By
CC similarity). Interacts (via SH2 domain) with SCIMP; this interaction is
CC dependent on phosphorylation of SCIMP 'Tyr-96' (PubMed:28290451).
CC Interacts (via SH2 domain) with PRAG1 (when phosphorylated at 'Tyr-
CC 391'); this interaction prevents translocation of CSK from the
CC cytoplasm to the membrane leading to increased activity of CSK (By
CC similarity). {ECO:0000250|UniProtKB:P32577,
CC ECO:0000250|UniProtKB:P41240, ECO:0000269|PubMed:12218089,
CC ECO:0000269|PubMed:12612075, ECO:0000269|PubMed:16166631,
CC ECO:0000269|PubMed:28290451, ECO:0000269|PubMed:8890164,
CC ECO:0000269|PubMed:9858471}.
CC -!- INTERACTION:
CC P41241; Q3U1F9: Pag1; NbExp=9; IntAct=EBI-2553183, EBI-8468834;
CC P41241; P42337: Pik3ca; NbExp=2; IntAct=EBI-2553183, EBI-641748;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16166631}. Cell
CC membrane {ECO:0000269|PubMed:16166631}. Note=Mainly cytoplasmic, also
CC present in lipid rafts.
CC -!- TISSUE SPECIFICITY: Ubiquitous, but most abundant in thymus and spleen,
CC as well as in neonatal brain.
CC -!- DOMAIN: The architecture of this protein is similar to that of Src-
CC family kinases (SFKs) with one N-terminal SH3 domain, one SH2 domain,
CC and a C-terminal kinase domain. {ECO:0000250}.
CC -!- PTM: Phosphorylated at Ser-364 by PKA, leading to increased activity.
CC Autophosphorylated (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice die between day 9 and day 10 of gestation
CC with several defects including a non-functional neural tube. SRC and
CC FYN kinases show increased activity when CSK is missing.
CC {ECO:0000269|PubMed:7685657}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. CSK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; U05247; AAA18766.1; -; mRNA.
DR EMBL; AY902339; AAX90624.1; -; Genomic_DNA.
DR EMBL; AK156058; BAE33565.1; -; mRNA.
DR EMBL; AK170815; BAE42047.1; -; mRNA.
DR EMBL; BC018394; AAH18394.1; -; mRNA.
DR EMBL; BC052006; AAH52006.2; -; mRNA.
DR EMBL; X57242; CAA40518.1; -; mRNA.
DR CCDS; CCDS23228.1; -.
DR PIR; I48929; I48929.
DR RefSeq; NP_001291690.1; NM_001304761.1.
DR RefSeq; NP_031809.2; NM_007783.3.
DR RefSeq; XP_006510864.1; XM_006510801.3.
DR RefSeq; XP_006510865.1; XM_006510802.3.
DR PDB; 1JEG; NMR; -; A=1-83.
DR PDBsum; 1JEG; -.
DR AlphaFoldDB; P41241; -.
DR BMRB; P41241; -.
DR SMR; P41241; -.
DR BioGRID; 198936; 35.
DR CORUM; P41241; -.
DR IntAct; P41241; 35.
DR MINT; P41241; -.
DR STRING; 10090.ENSMUSP00000034863; -.
DR iPTMnet; P41241; -.
DR PhosphoSitePlus; P41241; -.
DR EPD; P41241; -.
DR MaxQB; P41241; -.
DR PaxDb; P41241; -.
DR PeptideAtlas; P41241; -.
DR PRIDE; P41241; -.
DR ProteomicsDB; 285348; -.
DR Antibodypedia; 4405; 794 antibodies from 42 providers.
DR DNASU; 12988; -.
DR Ensembl; ENSMUST00000034863; ENSMUSP00000034863; ENSMUSG00000032312.
DR Ensembl; ENSMUST00000215396; ENSMUSP00000150590; ENSMUSG00000032312.
DR Ensembl; ENSMUST00000217314; ENSMUSP00000150984; ENSMUSG00000032312.
DR GeneID; 12988; -.
DR KEGG; mmu:12988; -.
DR UCSC; uc009pvk.2; mouse.
DR CTD; 1445; -.
DR MGI; MGI:88537; Csk.
DR VEuPathDB; HostDB:ENSMUSG00000032312; -.
DR eggNOG; KOG0197; Eukaryota.
DR GeneTree; ENSGT00940000157431; -.
DR HOGENOM; CLU_000288_7_2_1; -.
DR InParanoid; P41241; -.
DR OMA; QTMPWFH; -.
DR OrthoDB; 491765at2759; -.
DR PhylomeDB; P41241; -.
DR TreeFam; TF351634; -.
DR BRENDA; 2.7.10.2; 3474.
DR Reactome; R-MMU-180292; GAB1 signalosome.
DR Reactome; R-MMU-202427; Phosphorylation of CD3 and TCR zeta chains.
DR Reactome; R-MMU-354192; Integrin signaling.
DR Reactome; R-MMU-389948; PD-1 signaling.
DR Reactome; R-MMU-5674135; MAP2K and MAPK activation.
DR Reactome; R-MMU-9013407; RHOH GTPase cycle.
DR Reactome; R-MMU-9706369; Negative regulation of FLT3.
DR BioGRID-ORCS; 12988; 9 hits in 62 CRISPR screens.
DR ChiTaRS; Csk; mouse.
DR EvolutionaryTrace; P41241; -.
DR PRO; PR:P41241; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P41241; protein.
DR Bgee; ENSMUSG00000032312; Expressed in granulocyte and 236 other tissues.
DR ExpressionAtlas; P41241; baseline and differential.
DR Genevisible; P41241; MM.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; TAS:HGNC-UCL.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0070064; F:proline-rich region binding; ISO:MGI.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI.
DR GO; GO:0016740; F:transferase activity; TAS:HGNC-UCL.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0034332; P:adherens junction organization; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; ISO:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:HGNC-UCL.
DR GO; GO:0045779; P:negative regulation of bone resorption; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0042997; P:negative regulation of Golgi to plasma membrane protein transport; ISO:MGI.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; ISO:MGI.
DR GO; GO:0033673; P:negative regulation of kinase activity; ISO:MGI.
DR GO; GO:0010989; P:negative regulation of low-density lipoprotein particle clearance; ISO:MGI.
DR GO; GO:0050765; P:negative regulation of phagocytosis; ISO:MGI.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0060368; P:regulation of Fc receptor mediated stimulatory signaling pathway; ISO:MGI.
DR GO; GO:0050863; P:regulation of T cell activation; TAS:HGNC-UCL.
DR CDD; cd09937; SH2_csk_like; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR035027; Csk-like_SH2.
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; 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; Acetylation; Adaptive immunity; ATP-binding; Cell membrane;
KW Cytoplasm; Direct protein sequencing; Immunity; Kinase; Magnesium;
KW Manganese; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; SH2 domain; SH3 domain; Transferase;
KW Tyrosine-protein kinase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P41240"
FT CHAIN 2..450
FT /note="Tyrosine-protein kinase CSK"
FT /id="PRO_0000088071"
FT DOMAIN 9..70
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 82..171
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 195..449
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 9..70
FT /note="Interaction with PTPN22"
FT /evidence="ECO:0000269|PubMed:8890164"
FT ACT_SITE 314
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 201..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P41240"
FT MOD_RES 184
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P41240"
FT MOD_RES 304
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P41240"
FT MOD_RES 364
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P41240"
FT MOD_RES 416
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P41240"
FT CONFLICT 299
FT /note="C -> L (in Ref. 1; AAA18766)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="E -> D (in Ref. 1; AAA18766)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="W -> S (in Ref. 1; AAA18766)"
FT /evidence="ECO:0000305"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:1JEG"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:1JEG"
FT STRAND 43..51
FT /evidence="ECO:0007829|PDB:1JEG"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:1JEG"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:1JEG"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1JEG"
SQ SEQUENCE 450 AA; 50716 MW; E8D3EC9357B86277 CRC64;
MSAIQAAWPS GTECIAKYNF HGTAEQDLPF CKGDVLTIVA VTKDPNWYKA KNKVGREGII
PANYVQKREG VKAGTKLSLM PWFHGKITRE QAERLLYPPE TGLFLVREST NYPGDYTLCV
SCEGKVEHYR IMYHASKLSI DEEVYFENLM QLVEHYTTDA DGLCTRLIKP KVMEGTVAAQ
DEFYRSGWAL NMKELKLLQT IGKGEFGDVM LGDYRGNKVA VKCIKNDATA QAFLAEASVM
TQLRHSNLVQ LLGVIVEEKG GLYIVTEYMA KGSLVDYLRS RGRSVLGGDC LLKFSLDVCE
AMEYLEGNNF VHRDLAARNV LVSEDNVAKV SDFGLTKEAS STQDTGKLPV KWTAPEALRE
KKFSTKSDVW SFGILLWEIY SFGRVPYPRI PLKDVVPRVE KGYKMDAPDG CPPAVYEVMK
NCWHLDAATR PTFLQLREQL EHIKTHELHL
