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Tyrosine-protein kinase Tec (EC 2.7.10.2)

 TEC_MOUSE               Reviewed;         630 AA.
P24604; Q9R1M9; Q9WVN0; Q9WVN1; Q9WVN2; Q9WVN3;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 2.
28-MAR-2018, entry version 188.
RecName: Full=Tyrosine-protein kinase Tec;
EC=2.7.10.2;
Name=Tec;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=7678927;
Mano H., Mano K., Tang B., Koehler M., Yi T., Gilbert D.J.,
Jenkins N.A., Copeland N.G., Ihle J.N.;
"Expression of a novel form of Tec kinase in hematopoietic cells and
mapping of the gene to chromosome 5 near Kit.";
Oncogene 8:417-424(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 3; 4; 5 AND 6).
STRAIN=129;
PubMed=10343129;
Merkel A.L., Atmosukarto I.I.C., Stevens K., Rathjen P.D.,
Booker G.W.;
"Splice variants of the mouse Tec gene are differentially expressed in
vivo.";
Cytogenet. Cell Genet. 84:132-139(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 82-630 (ISOFORM 2).
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=2284097;
Mano H., Ishikawa F., Nishida J., Hirai H., Takaku F.;
"A novel protein-tyrosine kinase, tec, is preferentially expressed in
liver.";
Oncogene 5:1781-1786(1990).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 485-553.
PubMed=2482828; DOI=10.1016/0378-1119(89)90465-4;
Wilks A.F., Kurban R.R., Hovens C.M., Ralph S.J.;
"The application of the polymerase chain reaction to cloning members
of the protein tyrosine kinase family.";
Gene 85:67-74(1989).
[5]
PHOSPHORYLATION, ENZYME REGULATION, AND INTERACTION WITH VAV1.
PubMed=8877094;
Miyazato A., Yamashita Y., Hatake K., Miura Y., Ozawa K., Mano H.;
"Tec protein tyrosine kinase is involved in the signaling mechanism of
granulocyte colony-stimulating factor receptor.";
Cell Growth Differ. 7:1135-1139(1996).
[6]
PHOSPHORYLATION BY LYN, ENZYME REGULATION, AND MUTAGENESIS OF LYS-397.
PubMed=8621063;
Mano H., Yamashita Y., Miyazato A., Miura Y., Ozawa K.;
"Tec protein-tyrosine kinase is an effector molecule of Lyn protein-
tyrosine kinase.";
FASEB J. 10:637-642(1996).
[7]
FUNCTION, PHOSPHORYLATION OF JAK2, AND PHOSPHORYLATION AT TYR-518.
PubMed=9473212;
Yamashita Y., Watanabe S., Miyazato A., Ohya K., Ikeda U., Shimada K.,
Komatsu N., Hatake K., Miura Y., Ozawa K., Mano H.;
"Tec and Jak2 kinases cooperate to mediate cytokine-driven activation
of c-fos transcription.";
Blood 91:1496-1507(1998).
[8]
ENZYME REGULATION, AND FUNCTION IN THE CD28 SIGNALING PATHWAY.
PubMed=10382746;
DOI=10.1002/(SICI)1521-4141(199906)29:06<1842::AID-IMMU1842>3.0.CO;2-D;
Yang W.C., Olive D.;
"Tec kinase is involved in transcriptional regulation of IL-2 and IL-4
in the CD28 pathway.";
Eur. J. Immunol. 29:1842-1849(1999).
[9]
INTERACTION WITH CD28, ENZYME REGULATION, AND FUNCTION IN
PHOSPHORYLATION OF DOK1.
PubMed=9872994; DOI=10.1074/jbc.274.2.607;
Yang W.C., Ghiotto M., Barbarat B., Olive D.;
"The role of Tec protein-tyrosine kinase in T cell signaling.";
J. Biol. Chem. 274:607-617(1999).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=15214045; DOI=10.1002/eji.200324777;
Garcon F., Ghiotto M., Gerard A., Yang W.C., Olive D., Nunes J.A.;
"The SH3 domain of Tec kinase is essential for its targeting to
activated CD28 costimulatory molecule.";
Eur. J. Immunol. 34:1972-1980(2004).
[11]
SUBCELLULAR LOCATION.
PubMed=15817477; DOI=10.1074/jbc.M412913200;
Kane L.P., Watkins S.C.;
"Dynamic regulation of Tec kinase localization in membrane-proximal
vesicles of a T cell clone revealed by total internal reflection
fluorescence and confocal microscopy.";
J. Biol. Chem. 280:21949-21954(2005).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-518, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[13]
FUNCTION.
PubMed=19688741; DOI=10.1002/eji.200838839;
Schmidt U., Abramova A., Boucheron N., Eckelhart E., Schebesta A.,
Bilic I., Kneidinger M., Unger B., Hammer M., Sibilia M., Valent P.,
Ellmeier W.;
"The protein tyrosine kinase Tec regulates mast cell function.";
Eur. J. Immunol. 39:3228-3238(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-518, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[15]
SUBCELLULAR LOCATION.
PubMed=20543088; DOI=10.1152/ajpheart.00273.2010;
Zhang M.J., Franklin S., Li Y., Wang S., Ru X., Mitchell-Jordan S.A.,
Mano H., Stefani E., Ping P., Vondriska T.M.;
"Stress signaling by Tec tyrosine kinase in the ischemic myocardium.";
Am. J. Physiol. 299:H713-H722(2010).
[16]
FUNCTION IN THE HGF-INDUCED ERK SIGNALING PATHWAY.
PubMed=21094130; DOI=10.1016/j.bbrc.2010.11.068;
Li F., Jiang Y., Zheng Q., Yang X., Wang S.;
"TEC protein tyrosine kinase is involved in the Erk signaling pathway
induced by HGF.";
Biochem. Biophys. Res. Commun. 404:79-85(2011).
[17]
STRUCTURE BY NMR OF 179-245.
PubMed=11684687; DOI=10.1074/jbc.M108318200;
Pursglove S.E., Mulhern T.D., Mackay J.P., Hinds M.G., Booker G.W.;
"The solution structure and intramolecular associations of the Tec
kinase SRC homology 3 domain.";
J. Biol. Chem. 277:755-762(2002).
-!- FUNCTION: Non-receptor tyrosine kinase that contributes to
signaling from many receptors and participates as a signal
transducer in multiple downstream pathways, including regulation
of the actin cytoskeleton. Plays a redundant role to ITK in
regulation of the adaptive immune response. Regulates the
development, function and differentiation of conventional T-cells
and nonconventional NKT-cells. Required for TCR-dependent IL2 gene
induction. Phosphorylates DOK1, one CD28-specific substrate, and
contributes to CD28-signaling. Mediates signals that negatively
regulate IL2RA expression induced by TCR cross-linking. Plays a
redundant role to BTK in BCR-signaling for B-cell development and
activation, especially by phosphorylating STAP1, a BCR-signaling
protein. Required in mast cells for efficient cytokine production.
Involved in both growth and differentiation mechanisms of myeloid
cells through activation by the granulocyte colony-stimulating
factor CSF3, a critical cytokine to promoting the growth,
differentiation, and functional activation of myeloid cells.
Participates in platelet signaling downstream of integrin
activation. Cooperates with JAK2 through reciprocal
phosphorylation to mediate cytokine-driven activation of FOS
transcription. GRB10, a negative modifier of the FOS activation
pathway, is another substrate of TEC. TEC is involved in G
protein-coupled receptor- and integrin-mediated signalings in
blood platelets. Plays a role in hepatocyte proliferation and
liver regeneration and is involved in HGF-induced ERK signaling
pathway. TEC regulates also FGF2 unconventional secretion
(endoplasmic reticulum (ER)/Golgi-independent mechanism) under
various physiological conditions through phosphorylation of FGF2
'Tyr-82'. May also be involved in the regulation of osteoclast
differentiation. {ECO:0000269|PubMed:10382746,
ECO:0000269|PubMed:15214045, ECO:0000269|PubMed:19688741,
ECO:0000269|PubMed:21094130, ECO:0000269|PubMed:9473212,
ECO:0000269|PubMed:9872994}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- ENZYME REGULATION: Activated by tyrosine phosphorylation by a wide
range of cytokine stimulations. When T-cells or B-cells receptors
are activated, a series of phosphorylation leads to the
recruitment of TEC to the cell membrane, where it is
phosphorylated at Tyr-518. Also activated in response to SCF.
Integrin engagement induces tyrosine phosphorylation of TEC in
platelets. STAP1 participates in a positive feedback loop by
increasing the activity of TEC. SOCS1 is an inhibitor of TEC
kinase activity. {ECO:0000269|PubMed:10382746,
ECO:0000269|PubMed:8621063, ECO:0000269|PubMed:8877094,
ECO:0000269|PubMed:9872994}.
-!- SUBUNIT: Interacts with INPP5D/SHIP1 and INPPL1/SHIP2. Interacts
with CD28, FASLG, FGF2, GRB10 and KIT (By similarity). Interacts
with VAV1 and JAK2. Interacts with LYN. {ECO:0000250,
ECO:0000269|PubMed:8877094, ECO:0000269|PubMed:9872994}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral
membrane protein. Cytoplasm, cytoskeleton. Note=Following B-cell
or T-cell receptors activation by antigen, translocates to the
plasma membrane through its PH domain. Thrombin and integrin
engagement induces translocation of TEC to the cytoskeleton during
platelet activation. In cardiac myocytes, assumes a diffuse
intracellular localization under basal conditions but is recruited
to striated structures upon various stimuli, including ATP (By
similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1; Synonyms=TecIV;
IsoId=P24604-1; Sequence=Displayed;
Name=2;
IsoId=P24604-2; Sequence=VSP_005012, VSP_005015;
Name=3; Synonyms=TecIIb;
IsoId=P24604-3; Sequence=VSP_005016;
Name=4; Synonyms=TecIIa;
IsoId=P24604-4; Sequence=VSP_005015, VSP_005016;
Name=5; Synonyms=TecIII;
IsoId=P24604-5; Sequence=VSP_005015;
Name=6; Synonyms=TecI;
IsoId=P24604-6; Sequence=VSP_005013, VSP_005014;
-!- TISSUE SPECIFICITY: Preferentially expressed in liver. Expression
is also seen in the hematopoietic cells such as bone marrow,
thymus and spleen. Lower expression is seen in the heart, kidney
and ovary.
-!- DOMAIN: The PH domain mediates the binding to inositol
polyphosphate and phosphoinositides, leading to its targeting to
the plasma membrane. It is extended in the BTK kinase family by a
region designated the TH (Tec homology) domain, which consists of
about 80 residues preceding the SH3 domain.
{ECO:0000269|PubMed:15214045}.
-!- DOMAIN: The SH3 domain is essential for its targeting to activated
CD28 costimulatory molecule. {ECO:0000250}.
-!- PTM: Following B-cell or T-cell receptors engagement, translocates
to the plasma membrane where it gets phosphorylated at Tyr-518.
Undergoes also tyrosine phosphorylation during platelet
activation. {ECO:0000269|PubMed:8621063,
ECO:0000269|PubMed:8877094, ECO:0000269|PubMed:9473212}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. TEC subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; S53716; AAA13515.2; -; mRNA.
EMBL; AF071938; AAD43404.1; -; Genomic_DNA.
EMBL; AF071936; AAD43404.1; JOINED; Genomic_DNA.
EMBL; AF071937; AAD43404.1; JOINED; Genomic_DNA.
EMBL; AF071946; AAD43402.1; -; Genomic_DNA.
EMBL; AF071936; AAD43402.1; JOINED; Genomic_DNA.
EMBL; AF071937; AAD43402.1; JOINED; Genomic_DNA.
EMBL; AF071938; AAD43402.1; JOINED; Genomic_DNA.
EMBL; AF071939; AAD43402.1; JOINED; Genomic_DNA.
EMBL; AF071940; AAD43402.1; JOINED; Genomic_DNA.
EMBL; AF071941; AAD43402.1; JOINED; Genomic_DNA.
EMBL; AF071942; AAD43402.1; JOINED; Genomic_DNA.
EMBL; AF071943; AAD43402.1; JOINED; Genomic_DNA.
EMBL; AF071944; AAD43402.1; JOINED; Genomic_DNA.
EMBL; AF071945; AAD43402.1; JOINED; Genomic_DNA.
EMBL; AF071946; AAD43405.1; -; Genomic_DNA.
EMBL; AF071936; AAD43405.1; JOINED; Genomic_DNA.
EMBL; AF071937; AAD43405.1; JOINED; Genomic_DNA.
EMBL; AF071938; AAD43405.1; JOINED; Genomic_DNA.
EMBL; AF071939; AAD43405.1; JOINED; Genomic_DNA.
EMBL; AF071940; AAD43405.1; JOINED; Genomic_DNA.
EMBL; AF071941; AAD43405.1; JOINED; Genomic_DNA.
EMBL; AF071942; AAD43405.1; JOINED; Genomic_DNA.
EMBL; AF071943; AAD43405.1; JOINED; Genomic_DNA.
EMBL; AF071944; AAD43405.1; JOINED; Genomic_DNA.
EMBL; AF071945; AAD43405.1; JOINED; Genomic_DNA.
EMBL; AF071946; AAD43406.1; -; Genomic_DNA.
EMBL; AF071936; AAD43406.1; JOINED; Genomic_DNA.
EMBL; AF071937; AAD43406.1; JOINED; Genomic_DNA.
EMBL; AF071938; AAD43406.1; JOINED; Genomic_DNA.
EMBL; AF071940; AAD43406.1; JOINED; Genomic_DNA.
EMBL; AF071941; AAD43406.1; JOINED; Genomic_DNA.
EMBL; AF071942; AAD43406.1; JOINED; Genomic_DNA.
EMBL; AF071943; AAD43406.1; JOINED; Genomic_DNA.
EMBL; AF071944; AAD43406.1; JOINED; Genomic_DNA.
EMBL; AF071945; AAD43406.1; JOINED; Genomic_DNA.
EMBL; AF071946; AAD43407.1; -; Genomic_DNA.
EMBL; AF071936; AAD43407.1; JOINED; Genomic_DNA.
EMBL; AF071937; AAD43407.1; JOINED; Genomic_DNA.
EMBL; AF071938; AAD43407.1; JOINED; Genomic_DNA.
EMBL; AF071940; AAD43407.1; JOINED; Genomic_DNA.
EMBL; AF071941; AAD43407.1; JOINED; Genomic_DNA.
EMBL; AF071942; AAD43407.1; JOINED; Genomic_DNA.
EMBL; AF071943; AAD43407.1; JOINED; Genomic_DNA.
EMBL; AF071944; AAD43407.1; JOINED; Genomic_DNA.
EMBL; AF071945; AAD43407.1; JOINED; Genomic_DNA.
EMBL; X55663; CAA39196.1; -; mRNA.
EMBL; M33427; AAA40018.1; -; mRNA.
CCDS; CCDS51515.1; -. [P24604-5]
CCDS; CCDS51516.1; -. [P24604-1]
PIR; JU0215; JU0215.
PIR; S13763; S13763.
PIR; T01380; T01380.
RefSeq; NP_001106931.1; NM_001113460.2.
RefSeq; NP_001106932.1; NM_001113461.2.
RefSeq; NP_001106935.1; NM_001113464.2.
RefSeq; XP_006503908.1; XM_006503845.3.
RefSeq; XP_006503909.1; XM_006503846.3.
RefSeq; XP_011239020.1; XM_011240718.2.
RefSeq; XP_011239021.1; XM_011240719.2.
UniGene; Mm.319581; -.
PDB; 1GL5; NMR; -; A=181-244.
PDBsum; 1GL5; -.
ProteinModelPortal; P24604; -.
SMR; P24604; -.
BioGrid; 204103; 2.
IntAct; P24604; 1.
STRING; 10090.ENSMUSP00000071836; -.
iPTMnet; P24604; -.
PhosphoSitePlus; P24604; -.
MaxQB; P24604; -.
PaxDb; P24604; -.
PeptideAtlas; P24604; -.
PRIDE; P24604; -.
GeneID; 21682; -.
KEGG; mmu:21682; -.
CTD; 7006; -.
MGI; MGI:98662; Tec.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
HOGENOM; HOG000233859; -.
HOVERGEN; HBG008761; -.
InParanoid; P24604; -.
KO; K07364; -.
PhylomeDB; P24604; -.
BRENDA; 2.7.10.2; 3474.
EvolutionaryTrace; P24604; -.
PRO; PR:P24604; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0005856; C:cytoskeleton; ISO:MGI.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; ISO:MGI.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0050853; P:B cell receptor signaling pathway; ISO:MGI.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:MGI.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; ISO:MGI.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISO:MGI.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0010543; P:regulation of platelet activation; ISO:MGI.
GO; GO:0042246; P:tissue regeneration; IBA:GO_Central.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
CDD; cd11905; SH3_Tec; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR035572; Tec_SH3.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR001562; Znf_Btk_motif.
Pfam; PF00779; BTK; 1.
Pfam; PF00169; PH; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00452; SH3DOMAIN.
PRINTS; PR00402; TECBTKDOMAIN.
PRINTS; PR00109; TYRKINASE.
SMART; SM00107; BTK; 1.
SMART; SM00233; PH; 1.
SMART; SM00252; SH2; 1.
SMART; SM00326; SH3; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF55550; SSF55550; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 1.
PROSITE; PS51113; ZF_BTK; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Alternative splicing; ATP-binding;
Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Immunity;
Kinase; Lipid-binding; Membrane; Metal-binding; Nucleotide-binding;
Phosphoprotein; Reference proteome; SH2 domain; SH3 domain;
Transferase; Tyrosine-protein kinase; Zinc; Zinc-finger.
CHAIN 1 630 Tyrosine-protein kinase Tec.
/FTId=PRO_0000088171.
DOMAIN 4 111 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 178 238 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 246 344 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 369 622 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ZN_FING 113 149 Btk-type. {ECO:0000255|PROSITE-
ProRule:PRU00432}.
NP_BIND 375 383 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 488 488 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
METAL 121 121 Zinc. {ECO:0000250}.
METAL 132 132 Zinc. {ECO:0000250}.
METAL 133 133 Zinc. {ECO:0000250}.
METAL 143 143 Zinc. {ECO:0000250}.
BINDING 397 397 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 205 205 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P42680}.
MOD_RES 227 227 Phosphotyrosine.
{ECO:0000250|UniProtKB:P42680}.
MOD_RES 518 518 Phosphotyrosine; by autocatalysis, LYN
and JAK2. {ECO:0000244|PubMed:17947660,
ECO:0000244|PubMed:19144319,
ECO:0000269|PubMed:9473212}.
VAR_SEQ 1 94 MNFNTILEEILIKRSQQKKKTSLLNYKERLCVLPKSVLSYY
EGRAEKKYRKGVIDISKIKCVEIVKNDDGVIPCQNKFPFQV
VHDANTLYIFAP -> MMVSFPVKINFHS (in isoform
2). {ECO:0000303|PubMed:2284097}.
/FTId=VSP_005012.
VAR_SEQ 82 100 VVHDANTLYIFAPSPQSRD -> STKQGPMGEEVKRRNKEQ
Q (in isoform 6). {ECO:0000305}.
/FTId=VSP_005013.
VAR_SEQ 101 630 Missing (in isoform 6). {ECO:0000305}.
/FTId=VSP_005014.
VAR_SEQ 224 245 Missing (in isoform 2, isoform 4 and
isoform 5). {ECO:0000303|PubMed:2284097}.
/FTId=VSP_005015.
VAR_SEQ 604 630 RPEGRPSLEDLLRTIDELVECEETFGR -> ESCLCRVAQD
LSSKNLIGSRF (in isoform 3 and isoform 4).
{ECO:0000305}.
/FTId=VSP_005016.
MUTAGEN 397 397 K->M: Impairs kinase activity.
{ECO:0000269|PubMed:8621063}.
CONFLICT 23 23 L -> P (in Ref. 2; AAD43404/AAD43402/
AAD43405/AAD43406/AAD43407).
{ECO:0000305}.
CONFLICT 31 31 C -> F (in Ref. 2; AAD43404/AAD43402/
AAD43405/AAD43406/AAD43407).
{ECO:0000305}.
CONFLICT 34 34 P -> T (in Ref. 2; AAD43404/AAD43402/
AAD43405/AAD43406/AAD43407).
{ECO:0000305}.
CONFLICT 535 535 V -> E (in Ref. 4; AAA40018).
{ECO:0000305}.
CONFLICT 550 553 FGVL -> YGIP (in Ref. 4; AAA40018).
{ECO:0000305}.
CONFLICT 590 590 T -> S (in Ref. 2; AAD43402/AAD43405/
AAD43406/AAD43407). {ECO:0000305}.
CONFLICT 611 611 L -> F (in Ref. 2; AAD43404/AAD43402/
AAD43405/AAD43406/AAD43407 and 3;
CAA39196). {ECO:0000305}.
STRAND 183 185 {ECO:0000244|PDB:1GL5}.
STRAND 192 196 {ECO:0000244|PDB:1GL5}.
STRAND 204 209 {ECO:0000244|PDB:1GL5}.
STRAND 211 219 {ECO:0000244|PDB:1GL5}.
STRAND 221 223 {ECO:0000244|PDB:1GL5}.
STRAND 225 229 {ECO:0000244|PDB:1GL5}.
STRAND 232 236 {ECO:0000244|PDB:1GL5}.
TURN 237 241 {ECO:0000244|PDB:1GL5}.
SEQUENCE 630 AA; 73426 MW; 262640EE90D4A6D2 CRC64;
MNFNTILEEI LIKRSQQKKK TSLLNYKERL CVLPKSVLSY YEGRAEKKYR KGVIDISKIK
CVEIVKNDDG VIPCQNKFPF QVVHDANTLY IFAPSPQSRD RWVKKLKEEI KNNNNIMIKY
HPKFWADGSY QCCRQTEKLA PGCEKYNLFE SSIRKTLPPA PEIKKRRPPP PIPPEEENTE
EIVVAMYDFQ ATEAHDLRLE RGQEYIILEK NDLHWWRARD KYGSEGYIPS NYVTGKKSNN
LDQYEWYCRN TNRSKAEQLL RTEDKEGGFM VRDSSQPGLY TVSLYTKFGG EGSSGFRHYH
IKETATSPKK YYLAEKHAFG SIPEIIEYHK HNAAGLVTRL RYPVSTKGKN APTTAGFSYD
KWEINPSELT FMRELGSGLF GVVRLGKWRA QYKVAIKAIR EGAMCEEDFI EEAKVMMKLT
HPKLVQLYGV CTQQKPIYIV TEFMERGCLL NFLRQRQGHF SRDMLLSMCQ DVCEGMEYLE
RNSFIHRDLA ARNCLVNEAG VVKVSDFGMA RYVLDDQYTS SSGAKFPVKW CPPEVFNYSR
FSSKSDVWSF GVLMWEIFTE GRMPFEKNTN YEVVTMVTRG HRLHRPKLAT KYLYEVMLRC
WQERPEGRPS LEDLLRTIDE LVECEETFGR


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