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Tyrosine-protein kinase Tec (EC 2.7.10.2)

 TEC_HUMAN               Reviewed;         631 AA.
P42680; B7ZKZ6; Q3MIS5;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
11-SEP-2007, sequence version 2.
25-OCT-2017, entry version 178.
RecName: Full=Tyrosine-protein kinase Tec;
EC=2.7.10.2;
Name=TEC; Synonyms=PSCTK4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Blood;
PubMed=7934162;
Sato K., Mano H., Ariyama T., Inazawa J., Yazaki Y., Hirai H.;
"Molecular cloning and analysis of the human Tec protein-tyrosine
kinase.";
Leukemia 8:1663-1672(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 203-206, AND PHOSPHORYLATION AT TYR-206.
PubMed=12573241; DOI=10.1016/S1570-9639(02)00524-1;
Nore B.F., Mattsson P.T., Antonsson P., Backesjo C.-M., Westlund A.,
Lennartsson J., Hansson H., Low P., Ronnstrand L., Smith C.I.E.;
"Identification of phosphorylation sites within the SH3 domains of Tec
family tyrosine kinases.";
Biochim. Biophys. Acta 1645:123-132(2003).
[5]
PHOSPHORYLATION, INTERACTION WITH KIT, AND ENZYME REGULATION.
PubMed=7526158; DOI=10.1128/MCB.14.12.8432;
Tang B., Mano H., Yi T., Ihle J.N.;
"Tec kinase associates with c-kit and is tyrosine phosphorylated and
activated following stem cell factor binding.";
Mol. Cell. Biol. 14:8432-8437(1994).
[6]
PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
PubMed=9299487; DOI=10.1006/bbrc.1997.7269;
Laffargue M., Monnereau L., Tuech J., Ragab A., Ragab-Thomas J.,
Payrastre B., Raynal P., Chap H.;
"Integrin-dependent tyrosine phosphorylation and cytoskeletal
translocation of Tec in thrombin-activated platelets.";
Biochem. Biophys. Res. Commun. 238:247-251(1997).
[7]
ENZYME REGULATION.
PubMed=9341160; DOI=10.1074/jbc.272.43.27178;
Ohya K., Kajigaya S., Yamashita Y., Miyazato A., Hatake K., Miura Y.,
Ikeda U., Shimada K., Ozawa K., Mano H.;
"SOCS-1/JAB/SSI-1 can bind to and suppress Tec protein-tyrosine
kinase.";
J. Biol. Chem. 272:27178-27182(1997).
[8]
INTERACTION WITH GRB10, AND FUNCTION IN PHOSPHORYLATION OF GRB10.
PubMed=9753425; DOI=10.1046/j.1365-2443.1998.00201.x;
Mano H., Ohya K., Miyazato A., Yamashita Y., Ogawa W., Inazawa J.,
Ikeda U., Shimada K., Hatake K., Kasuga M., Ozawa K., Kajigaya S.;
"Grb10/GrbIR as an in vivo substrate of Tec tyrosine kinase.";
Genes Cells 3:431-441(1998).
[9]
PHOSPHORYLATION, ENZYME REGULATION, AND SUBCELLULAR LOCATION.
PubMed=9652744; DOI=10.1038/sj.onc.1201799;
Hamazaki Y., Kojima H., Mano H., Nagata Y., Todokoro K., Abe T.,
Nagasawa T.;
"Tec is involved in G protein-coupled receptor- and integrin-mediated
signalings in human blood platelets.";
Oncogene 16:2773-2779(1998).
[10]
FUNCTION IN PHOSPHORYLATION OF STAP1, AND ENZYME REGULATION.
PubMed=10518561; DOI=10.1073/pnas.96.21.11976;
Ohya K., Kajigaya S., Kitanaka A., Yoshida K., Miyazato A.,
Yamashita Y., Yamanaka T., Ikeda U., Shimada K., Ozawa K., Mano H.;
"Molecular cloning of a docking protein, BRDG1, that acts downstream
of the Tec tyrosine kinase.";
Proc. Natl. Acad. Sci. U.S.A. 96:11976-11981(1999).
[11]
INTERACTION WITH INPP5D AND INPPL1.
PubMed=15492005; DOI=10.1074/jbc.M408141200;
Tomlinson M.G., Heath V.L., Turck C.W., Watson S.P., Weiss A.;
"SHIP family inositol phosphatases interact with and negatively
regulate the Tec tyrosine kinase.";
J. Biol. Chem. 279:55089-55096(2004).
[12]
INTERACTION WITH FASLG.
PubMed=19807924; DOI=10.1186/1471-2172-10-53;
Voss M., Lettau M., Janssen O.;
"Identification of SH3 domain interaction partners of human FasL
(CD178) by phage display screening.";
BMC Immunol. 10:53-53(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-206 AND TYR-228, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-519, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
FUNCTION.
PubMed=19883687; DOI=10.1016/j.imlet.2009.10.009;
Susaki K., Kitanaka A., Dobashi H., Kubota Y., Kittaka K., Kameda T.,
Yamaoka G., Mano H., Mihara K., Ishida T.;
"Tec protein tyrosine kinase inhibits CD25 expression in human T-
lymphocyte.";
Immunol. Lett. 127:135-142(2010).
[16]
FUNCTION IN PHOSPHORYLATION OF FGF2, AND INTERACTION WITH FGF2.
PubMed=20230531; DOI=10.1111/j.1600-0854.2010.01059.x;
Ebert A.D., Laussmann M., Wegehingel S., Kaderali L., Erfle H.,
Reichert J., Lechner J., Beer H.D., Pepperkok R., Nickel W.;
"Tec-kinase-mediated phosphorylation of fibroblast growth factor 2 is
essential for unconventional secretion.";
Traffic 11:813-826(2010).
[17]
VARIANTS [LARGE SCALE ANALYSIS] GLN-44 AND LYS-563.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- 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-215'. May also be involved in the regulation of osteoclast
differentiation. {ECO:0000269|PubMed:10518561,
ECO:0000269|PubMed:19883687, ECO:0000269|PubMed:20230531,
ECO:0000269|PubMed:9753425}.
-!- 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-519. 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:10518561,
ECO:0000269|PubMed:7526158, ECO:0000269|PubMed:9341160,
ECO:0000269|PubMed:9652744}.
-!- SUBUNIT: Interacts with INPP5D/SHIP1 and INPPL1/SHIP2. Interacts
with CD28, FASLG, FGF2, GRB10, LYN and KIT. Interacts with VAV1
and JAK2 (By similarity). {ECO:0000250}.
-!- INTERACTION:
Q13480:GAB1; NbExp=2; IntAct=EBI-1383480, EBI-517684;
P08581:MET; NbExp=2; IntAct=EBI-1383480, EBI-1039152;
-!- 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}.
-!- TISSUE SPECIFICITY: Expressed in a wide range of cells, including
hematopoietic cell lines like myeloid, B-, and T-cell lineages.
-!- 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.
-!- 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-519.
Undergoes also tyrosine phosphorylation during platelet
activation. {ECO:0000269|PubMed:12573241,
ECO:0000269|PubMed:7526158, ECO:0000269|PubMed:9299487,
ECO:0000269|PubMed:9652744}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. TEC subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- CAUTION: It is uncertain whether Met-1 is the initiator.
{ECO:0000305}.
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EMBL; D29767; BAA06171.1; -; mRNA.
EMBL; CH471069; EAW93055.1; -; Genomic_DNA.
EMBL; BC101711; AAI01712.1; -; mRNA.
EMBL; BC101713; AAI01714.1; -; mRNA.
EMBL; BC143487; AAI43488.1; -; mRNA.
CCDS; CCDS3481.1; -.
PIR; I38268; I38268.
PIR; I56997; I56997.
RefSeq; NP_003206.2; NM_003215.2.
UniGene; Hs.479670; -.
PDB; 2LUL; NMR; -; A=1-154.
PDBsum; 2LUL; -.
ProteinModelPortal; P42680; -.
SMR; P42680; -.
BioGrid; 112865; 23.
IntAct; P42680; 18.
MINT; MINT-1498364; -.
STRING; 9606.ENSP00000370912; -.
BindingDB; P42680; -.
ChEMBL; CHEMBL4246; -.
GuidetoPHARMACOLOGY; 2238; -.
iPTMnet; P42680; -.
PhosphoSitePlus; P42680; -.
BioMuta; TEC; -.
DMDM; 158518392; -.
EPD; P42680; -.
MaxQB; P42680; -.
PaxDb; P42680; -.
PeptideAtlas; P42680; -.
PRIDE; P42680; -.
DNASU; 7006; -.
Ensembl; ENST00000381501; ENSP00000370912; ENSG00000135605.
GeneID; 7006; -.
KEGG; hsa:7006; -.
UCSC; uc003gxz.4; human.
CTD; 7006; -.
DisGeNET; 7006; -.
EuPathDB; HostDB:ENSG00000135605.12; -.
GeneCards; TEC; -.
HGNC; HGNC:11719; TEC.
HPA; HPA005733; -.
HPA; HPA024657; -.
MalaCards; TEC; -.
MIM; 600583; gene.
neXtProt; NX_P42680; -.
OpenTargets; ENSG00000135605; -.
PharmGKB; PA36436; -.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000119011; -.
HOGENOM; HOG000233859; -.
HOVERGEN; HBG008761; -.
InParanoid; P42680; -.
KO; K07364; -.
OMA; MKLTHPK; -.
OrthoDB; EOG091G0D46; -.
PhylomeDB; P42680; -.
TreeFam; TF351634; -.
BRENDA; 2.7.10.2; 2681.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-HSA-512988; Interleukin-3, 5 and GM-CSF signaling.
SignaLink; P42680; -.
SIGNOR; P42680; -.
ChiTaRS; TEC; human.
GeneWiki; TEC_(gene); -.
GenomeRNAi; 7006; -.
PRO; PR:P42680; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000135605; -.
CleanEx; HS_TEC; -.
ExpressionAtlas; P42680; baseline and differential.
Genevisible; P42680; HS.
GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
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; IDA:HPA.
GO; GO:0005524; F:ATP 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; IDA:UniProtKB.
GO; GO:0005543; F:phospholipid binding; NAS:BHF-UCL.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0050853; P:B cell receptor signaling pathway; IDA:UniProtKB.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IMP:BHF-UCL.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0010543; P:regulation of platelet activation; IDA:UniProtKB.
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.
InterPro; IPR011993; PH_dom-like.
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.
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; SSF50729; SSF50729; 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; ATP-binding; Cell membrane;
Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
Immunity; Kinase; Lipid-binding; Membrane; Metal-binding;
Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
SH2 domain; SH3 domain; Transferase; Tyrosine-protein kinase; Zinc;
Zinc-finger.
CHAIN 1 631 Tyrosine-protein kinase Tec.
/FTId=PRO_0000088170.
DOMAIN 4 111 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 179 239 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 247 345 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 370 623 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ZN_FING 113 149 Btk-type. {ECO:0000255|PROSITE-
ProRule:PRU00432}.
NP_BIND 376 384 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 489 489 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 398 398 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 206 206 Phosphotyrosine; by autocatalysis.
{ECO:0000244|PubMed:19369195,
ECO:0000269|PubMed:12573241}.
MOD_RES 228 228 Phosphotyrosine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 519 519 Phosphotyrosine; by autocatalysis, LYN
and JAK2. {ECO:0000244|PubMed:19690332}.
VARIANT 44 44 R -> Q (in dbSNP:rs35374286).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041850.
VARIANT 563 563 R -> K (in a lung adenocarcinoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041851.
CONFLICT 514 514 V -> F (in Ref. 1; BAA06171).
{ECO:0000305}.
STRAND 3 14 {ECO:0000244|PDB:2LUL}.
STRAND 19 21 {ECO:0000244|PDB:2LUL}.
STRAND 26 41 {ECO:0000244|PDB:2LUL}.
STRAND 45 47 {ECO:0000244|PDB:2LUL}.
STRAND 53 55 {ECO:0000244|PDB:2LUL}.
HELIX 56 58 {ECO:0000244|PDB:2LUL}.
STRAND 61 64 {ECO:0000244|PDB:2LUL}.
STRAND 69 71 {ECO:0000244|PDB:2LUL}.
STRAND 74 76 {ECO:0000244|PDB:2LUL}.
STRAND 78 83 {ECO:0000244|PDB:2LUL}.
STRAND 88 92 {ECO:0000244|PDB:2LUL}.
HELIX 96 110 {ECO:0000244|PDB:2LUL}.
STRAND 118 120 {ECO:0000244|PDB:2LUL}.
STRAND 132 134 {ECO:0000244|PDB:2LUL}.
STRAND 143 145 {ECO:0000244|PDB:2LUL}.
SEQUENCE 631 AA; 73581 MW; F55DECBF9916E1F9 CRC64;
MNFNTILEEI LIKRSQQKKK TSPLNYKERL FVLTKSMLTY YEGRAEKKYR KGFIDVSKIK
CVEIVKNDDG VIPCQNKYPF QVVHDANTLY IFAPSPQSRD LWVKKLKEEI KNNNNIMIKY
HPKFWTDGSY QCCRQTEKLA PGCEKYNLFE SSIRKALPPA PETKKRRPPP PIPLEEEDNS
EEIVVAMYDF QAAEGHDLRL ERGQEYLILE KNDVHWWRAR DKYGNEGYIP SNYVTGKKSN
NLDQYEWYCR NMNRSKAEQL LRSEDKEGGF MVRDSSQPGL YTVSLYTKFG GEGSSGFRHY
HIKETTTSPK KYYLAEKHAF GSIPEIIEYH KHNAAGLVTR LRYPVSVKGK NAPTTAGFSY
EKWEINPSEL TFMRELGSGL FGVVRLGKWR AQYKVAIKAI REGAMCEEDF IEEAKVMMKL
THPKLVQLYG VCTQQKPIYI VTEFMERGCL LNFLRQRQGH FSRDVLLSMC QDVCEGMEYL
ERNSFIHRDL AARNCLVSEA GVVKVSDFGM ARYVLDDQYT SSSGAKFPVK WCPPEVFNYS
RFSSKSDVWS FGVLMWEVFT EGRMPFEKYT NYEVVTMVTR GHRLYQPKLA SNYVYEVMLR
CWQEKPEGRP SFEDLLRTID ELVECEETFG R


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