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Tensin-3 (Tensin-like SH2 domain-containing protein 1) (Tumor endothelial marker 6)

 TENS3_HUMAN             Reviewed;        1445 AA.
Q68CZ2; B2RNV1; Q6IPQ2; Q8IZW7; Q8NAD0; Q96PE0; Q96S48;
24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
24-JUL-2007, sequence version 2.
22-NOV-2017, entry version 125.
RecName: Full=Tensin-3;
AltName: Full=Tensin-like SH2 domain-containing protein 1;
AltName: Full=Tumor endothelial marker 6;
Name=TNS3; Synonyms=TEM6, TENS1, TPP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
PubMed=11559528;
Carson-Walter E.B., Watkins D.N., Nanda A., Vogelstein B.,
Kinzler K.W., St Croix B.;
"Cell surface tumor endothelial markers are conserved in mice and
humans.";
Cancer Res. 61:6649-6655(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, INDUCTION, AND INTERACTION WITH EGFR; PTK2/FAK1 AND
BCAR1.
PubMed=15140944;
Cui Y., Liao Y.-C., Lo S.H.;
"Epidermal growth factor modulates tyrosine phosphorylation of a novel
tensin family member, tensin3.";
Mol. Cancer Res. 2:225-232(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Spleen;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Amygdala;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
TISSUE=Brain, and Kidney;
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 749-1445, AND TISSUE SPECIFICITY.
PubMed=16461921; DOI=10.1677/jme.1.01913;
Maeda I., Takano T., Yoshida H., Matsuzuka F., Amino N., Miyauchi A.;
"Tensin3 is a novel thyroid-specific gene.";
J. Mol. Endocrinol. 36:R1-R8(2006).
[9]
FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND KNOCKDOWN IN MCF10A
CELLS.
PubMed=17643115; DOI=10.1038/ncb1622;
Katz M., Amit I., Citri A., Shay T., Carvalho S., Lavi S.,
Milanezi F., Lyass L., Amariglio N., Jacob-Hirsch J., Ben-Chetrit N.,
Tarcic G., Lindzen M., Avraham R., Liao Y.C., Trusk P., Lyass A.,
Rechavi G., Spector N.L., Lo S.H., Schmitt F., Bacus S.S., Yarden Y.;
"A reciprocal tensin-3-cten switch mediates EGF-driven mammary cell
migration.";
Nat. Cell Biol. 9:961-969(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; THR-632; SER-660;
SER-776; SER-866; SER-901; SER-1149; SER-1154 AND SER-1293, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649; SER-660; SER-735;
SER-776; TYR-780; SER-811; SER-1149 AND SER-1154, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-660; SER-776; SER-1149
AND SER-1441, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361; SER-440; SER-516;
SER-776; SER-811; SER-901; SER-1149 AND SER-1154, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: May play a role in actin remodeling. Involved in the
dissociation of the integrin-tensin-actin complex. EGF activates
TNS4 and down-regulates TNS3 which results in capping the tail of
ITGB1. Seems to be involved in mammary cell migration. May be
involved in cell migration and bone development (By similarity).
{ECO:0000250, ECO:0000269|PubMed:17643115}.
-!- SUBUNIT: EGF promotes the interaction with EGFR. Interacts with
PTK2/FAK1 and BCAR1. Tyrosine phosphorylation is critical for
these interactions. {ECO:0000269|PubMed:15140944}.
-!- INTERACTION:
P56945:BCAR1; NbExp=8; IntAct=EBI-1220488, EBI-702093;
P12830:CDH1; NbExp=2; IntAct=EBI-1220488, EBI-727477;
P00533:EGFR; NbExp=4; IntAct=EBI-1220488, EBI-297353;
P04626:ERBB2; NbExp=2; IntAct=EBI-1220488, EBI-641062;
P21860:ERBB3; NbExp=2; IntAct=EBI-1220488, EBI-720706;
P10721:KIT; NbExp=5; IntAct=EBI-1220488, EBI-1379503;
P08581:MET; NbExp=3; IntAct=EBI-1220488, EBI-1039152;
Q05397:PTK2; NbExp=3; IntAct=EBI-1220488, EBI-702142;
P12931:SRC; NbExp=13; IntAct=EBI-1220488, EBI-621482;
-!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
{ECO:0000269|PubMed:15140944, ECO:0000269|PubMed:17643115}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q68CZ2-1; Sequence=Displayed;
Name=2;
IsoId=Q68CZ2-2; Sequence=VSP_027123;
Name=3;
IsoId=Q68CZ2-3; Sequence=VSP_027126, VSP_027127;
Name=4;
IsoId=Q68CZ2-4; Sequence=VSP_027124, VSP_027125;
-!- TISSUE SPECIFICITY: Expressed in umbilical vein endothelial cells,
epithelial cells, and fibroblasts cells (at protein level). Highly
expressed in thyroid, kidney and placenta. Low expression in
heart, skeletal muscle, spleen, liver, and lung. Expressed in
tumor endothelial cells. Expression seems to be down-regulated in
thyroid tumor tissues and in anaplastic carcinomas.
{ECO:0000269|PubMed:11559528, ECO:0000269|PubMed:15140944,
ECO:0000269|PubMed:16461921}.
-!- INDUCTION: Down-regulated by EGF. {ECO:0000269|PubMed:15140944,
ECO:0000269|PubMed:17643115}.
-!- PTM: EGF/epidermal growth factor induces tyrosine phosphorylation
in a time- and dose-dependent manner.
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EMBL; AF378756; AAL11993.1; -; mRNA.
EMBL; AF417489; AAN32667.1; -; mRNA.
EMBL; AK092864; BAC03993.1; -; mRNA.
EMBL; CR749644; CAH18438.1; -; mRNA.
EMBL; AC073341; AAQ96841.1; -; Genomic_DNA.
EMBL; CH471128; EAW61011.1; -; Genomic_DNA.
EMBL; BC071791; AAH71791.1; -; mRNA.
EMBL; BC137133; AAI37134.1; -; mRNA.
EMBL; BC137134; AAI37135.1; -; mRNA.
EMBL; AB062750; BAB60681.1; -; mRNA.
CCDS; CCDS5506.2; -. [Q68CZ2-1]
RefSeq; NP_073585.8; NM_022748.11. [Q68CZ2-1]
RefSeq; XP_011513782.1; XM_011515480.2. [Q68CZ2-1]
RefSeq; XP_011513783.1; XM_011515481.2. [Q68CZ2-1]
RefSeq; XP_011513784.1; XM_011515482.2. [Q68CZ2-1]
RefSeq; XP_011513785.1; XM_011515483.2. [Q68CZ2-1]
RefSeq; XP_016868028.1; XM_017012539.1. [Q68CZ2-1]
UniGene; Hs.520814; -.
ProteinModelPortal; Q68CZ2; -.
BioGrid; 122272; 22.
IntAct; Q68CZ2; 21.
MINT; MINT-1494711; -.
STRING; 9606.ENSP00000312143; -.
iPTMnet; Q68CZ2; -.
PhosphoSitePlus; Q68CZ2; -.
BioMuta; TNS3; -.
DMDM; 156637424; -.
EPD; Q68CZ2; -.
MaxQB; Q68CZ2; -.
PaxDb; Q68CZ2; -.
PeptideAtlas; Q68CZ2; -.
PRIDE; Q68CZ2; -.
Ensembl; ENST00000311160; ENSP00000312143; ENSG00000136205. [Q68CZ2-1]
Ensembl; ENST00000442536; ENSP00000389285; ENSG00000136205. [Q68CZ2-4]
Ensembl; ENST00000458317; ENSP00000388318; ENSG00000136205. [Q68CZ2-4]
GeneID; 64759; -.
KEGG; hsa:64759; -.
UCSC; uc003tnw.3; human. [Q68CZ2-1]
CTD; 64759; -.
DisGeNET; 64759; -.
EuPathDB; HostDB:ENSG00000136205.16; -.
GeneCards; TNS3; -.
HGNC; HGNC:21616; TNS3.
HPA; HPA055338; -.
HPA; HPA056015; -.
MIM; 606825; gene.
neXtProt; NX_Q68CZ2; -.
OpenTargets; ENSG00000136205; -.
PharmGKB; PA134888115; -.
eggNOG; KOG1930; Eukaryota.
eggNOG; KOG2283; Eukaryota.
eggNOG; COG2453; LUCA.
GeneTree; ENSGT00760000119113; -.
HOVERGEN; HBG060186; -.
InParanoid; Q68CZ2; -.
KO; K18080; -.
OMA; EPRGCPE; -.
OrthoDB; EOG091G0G8Y; -.
PhylomeDB; Q68CZ2; -.
TreeFam; TF315996; -.
Reactome; R-HSA-8875513; MET interacts with TNS proteins.
SignaLink; Q68CZ2; -.
SIGNOR; Q68CZ2; -.
ChiTaRS; TNS3; human.
GenomeRNAi; 64759; -.
PRO; PR:Q68CZ2; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000136205; -.
CleanEx; HS_TNS3; -.
ExpressionAtlas; Q68CZ2; baseline and differential.
Genevisible; Q68CZ2; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0016477; P:cell migration; IEA:Ensembl.
GO; GO:0048286; P:lung alveolus development; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
CDD; cd01213; PTB_tensin; 1.
CDD; cd09927; SH2_Tensin_like; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.30.505.10; -; 1.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR013625; PTB.
InterPro; IPR006020; PTB/PI_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR014020; Tensin_C2-dom.
InterPro; IPR035012; Tensin_like_SH2.
InterPro; IPR029023; Tensin_phosphatase.
InterPro; IPR033929; Tensin_PTB.
InterPro; IPR003595; Tyr_Pase_cat.
Pfam; PF08416; PTB; 1.
Pfam; PF10409; PTEN_C2; 1.
Pfam; PF00017; SH2; 1.
SMART; SM00462; PTB; 1.
SMART; SM01326; PTEN_C2; 1.
SMART; SM00404; PTPc_motif; 1.
SMART; SM00252; SH2; 1.
SUPFAM; SSF49562; SSF49562; 1.
SUPFAM; SSF50729; SSF50729; 1.
SUPFAM; SSF52799; SSF52799; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS51182; C2_TENSIN; 1.
PROSITE; PS51181; PPASE_TENSIN; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
Alternative splicing; Cell junction; Complete proteome;
Phosphoprotein; Polymorphism; Reference proteome; SH2 domain.
CHAIN 1 1445 Tensin-3.
/FTId=PRO_0000295915.
DOMAIN 1 170 Phosphatase tensin-type.
{ECO:0000255|PROSITE-ProRule:PRU00590}.
DOMAIN 175 301 C2 tensin-type. {ECO:0000255|PROSITE-
ProRule:PRU00589}.
DOMAIN 1172 1282 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
COMPBIAS 941 944 Poly-Ser.
MOD_RES 332 332 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 361 361 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 440 440 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 516 516 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 571 571 Phosphoserine.
{ECO:0000250|UniProtKB:Q5SSZ5}.
MOD_RES 632 632 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 649 649 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 660 660 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 687 687 Phosphoserine.
{ECO:0000250|UniProtKB:Q5SSZ5}.
MOD_RES 690 690 Phosphoserine.
{ECO:0000250|UniProtKB:Q5SSZ5}.
MOD_RES 735 735 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 776 776 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 780 780 Phosphotyrosine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 811 811 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 866 866 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 901 901 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 1149 1149 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1154 1154 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 1293 1293 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1441 1441 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 241 480 Missing (in isoform 2).
{ECO:0000303|PubMed:11559528}.
/FTId=VSP_027123.
VAR_SEQ 243 250 KCYHKKYR -> MNYNIANI (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_027124.
VAR_SEQ 251 1445 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_027125.
VAR_SEQ 381 391 DHSDHTLSVSS -> ANVLFELIGQV (in isoform
3). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_027126.
VAR_SEQ 392 1445 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_027127.
VARIANT 600 600 Q -> H (in dbSNP:rs2293362).
/FTId=VAR_034593.
VARIANT 679 679 G -> S (in dbSNP:rs7808646).
/FTId=VAR_034594.
VARIANT 1034 1034 E -> K (in dbSNP:rs3807590).
/FTId=VAR_052548.
CONFLICT 31 31 L -> P (in Ref. 2; AAN32667).
{ECO:0000305}.
CONFLICT 458 458 V -> A (in Ref. 4; CAH18438).
{ECO:0000305}.
CONFLICT 505 505 A -> V (in Ref. 2; AAN32667).
{ECO:0000305}.
CONFLICT 917 917 T -> A (in Ref. 4; CAH18438).
{ECO:0000305}.
CONFLICT 1047 1047 A -> T (in Ref. 4; CAH18438).
{ECO:0000305}.
SEQUENCE 1445 AA; 155266 MW; 40B02C6269899320 CRC64;
MEEGHGLDLT YITERIIAVS FPAGCSEESY LHNLQEVTRM LKSKHGDNYL VLNLSEKRYD
LTKLNPKIMD VGWPELHAPP LDKMCTICKA QESWLNSNLQ HVVVIHCRGG KGRIGVVISS
YMHFTNVSAS ADQALDRFAM KKFYDDKVSA LMQPSQKRYV QFLSGLLSGS VKMNASPLFL
HFVILHGTPN FDTGGVCRPF LKLYQAMQPV YTSGIYNVGP ENPSRICIVI EPAQLLKGDV
MVKCYHKKYR SATRDVIFRL QFHTGAVQGY GLVFGKEDLD NASKDDRFPD YGKVELVFSA
TPEKIQGSEH LYNDHGVIVD YNTTDPLIRW DSYENLSADG EVLHTQGPVD GSLYAKVRKK
SSSDPGIPGG PQAIPATNSP DHSDHTLSVS SDSGHSTASA RTDKTEERLA PGTRRGLSAQ
EKAELDQLLS GFGLEDPGSS LKEMTDARSK YSGTRHVVPA QVHVNGDAAL KDRETDILDD
EMPHHDLHSV DSLGTLSSSE GPQSAHLGPF TCHKSSQNSL LSDGFGSNVG EDPQGTLVPD
LGLGMDGPYE RERTFGSREP KQPQPLLRKP SVSAQMQAYG QSSYSTQTWV RQQQMVVAHQ
YSFAPDGEAR LVSRCPADNP GLVQAQPRVP LTPTRGTSSR VAVQRGVGSG PHPPDTQQPS
PSKAFKPRFP GDQVVNGAGP ELSTGPSPGS PTLDIDQSIE QLNRLILELD PTFEPIPTHM
NALGSQANGS VSPDSVGGGL RASSRLPDTG EGPSRATGRQ GSSAEQPLGG RLRKLSLGQY
DNDAGGQLPF SKCAWGKAGV DYAPNLPPFP SPADVKETMT PGYPQDLDII DGRILSSKES
MCSTPAFPVS PETPYVKTAL RHPPFSPPEP PLSSPASQHK GGREPRSCPE TLTHAVGMSE
SPIGPKSTML RADASSTPSF QQAFASSCTI SSNGPGQRRE SSSSAERQWV ESSPKPMVSL
LGSGRPTGSP LSAEFSGTRK DSPVLSCFPP SELQAPFHSH ELSLAEPPDS LAPPSSQAFL
GFGTAPVGSG LPPEEDLGAL LANSHGASPT PSIPLTATGA ADNGFLSHNF LTVAPGHSSH
HSPGLQGQGV TLPGQPPLPE KKRASEGDRS LGSVSPSSSG FSSPHSGSTI SIPFPNVLPD
FSKASEAASP LPDSPGDKLV IVKFVQDTSK FWYKADISRE QAIAMLKDKE PGSFIVRDSH
SFRGAYGLAM KVATPPPSVL QLNKKAGDLA NELVRHFLIE CTPKGVRLKG CSNEPYFGSL
TALVCQHSIT PLALPCKLLI PERDPLEEIA ESSPQTAANS AAELLKQGAA CNVWYLNSVE
MESLTGHQAI QKALSITLVQ EPPPVSTVVH FKVSAQGITL TDNQRKLFFR RHYPVNSVIF
CALDPQDRKW IKDGPSSKVF GFVARKQGSA TDNVCHLFAE HDPEQPASAI VNFVSKVMIG
SPKKV


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