TENS1_HUMAN
ID TENS1_HUMAN Reviewed; 1735 AA.
AC Q9HBL0; Q4ZG71; Q6IPI5;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Tensin-1;
GN Name=TNS1; Synonyms=TNS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANTS
RP ARG-1197 AND ILE-1604.
RC TISSUE=Heart;
RX PubMed=11023826; DOI=10.1042/bj3510403;
RA Chen H., Ishii A., Wong W.K., Chen L.B., Lo S.H.;
RT "Molecular characterization of human tensin.";
RL Biochem. J. 351:403-411(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Skin;
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 [4]
RP PROTEIN SEQUENCE OF 764-781; 1105-1129; 1164-1181; 1440-1450; 1621-1653 AND
RP 1689-1695, PHOSPHORYLATION AT SER-1177, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lempens A., Norman J.C.;
RL Submitted (OCT-2009) to UniProtKB.
RN [5]
RP INTERACTION WITH STARD8.
RX PubMed=17517630; DOI=10.1073/pnas.0703033104;
RA Qian X., Li G., Asmussen H.K., Asnaghi L., Vass W.C., Braverman R.,
RA Yamada K.M., Popescu N.C., Papageorge A.G., Lowy D.R.;
RT "Oncogenic inhibition by a deleted in liver cancer gene requires
RT cooperation between tensin binding and Rho-specific GTPase-activating
RT protein activities.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:9012-9017(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1192 AND SER-1314, VARIANT
RP [LARGE SCALE ANALYSIS] ARG-1197, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1192 AND SER-1314, VARIANT
RP [LARGE SCALE ANALYSIS] ARG-1197, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1177; SER-1192; THR-1266;
RP SER-1269; SER-1381 AND SER-1446, VARIANT [LARGE SCALE ANALYSIS] ARG-1197,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-701; SER-1177; THR-1189;
RP SER-1192; SER-1269; SER-1294 AND SER-1314, VARIANT [LARGE SCALE ANALYSIS]
RP ARG-1197, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21768292; DOI=10.1083/jcb.201007108;
RA Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A., Mosher D.,
RA Block M.R., Albiges-Rizo C., Bouvard D.;
RT "Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent
RT fibronectin deposition.";
RL J. Cell Biol. 194:307-322(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621; SER-899; SER-963;
RP SER-1177; SER-1269; SER-1314; SER-1381 AND SER-1400, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-364; TYR-366;
RP SER-378; THR-379; SER-433; SER-764; SER-769; SER-794; THR-860; SER-899;
RP TYR-903; SER-907; SER-963; SER-967; SER-1124; SER-1177; SER-1192; SER-1309;
RP SER-1314; SER-1381; SER-1393 AND SER-1588, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-1093.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Involved in fibrillar adhesion formation. May be involved in
CC cell migration, cartilage development and in linking signal
CC transduction pathways to the cytoskeleton.
CC {ECO:0000269|PubMed:21768292}.
CC -!- SUBUNIT: Binds to actin filaments and interacts with phosphotyrosine-
CC containing proteins. Interacts with STARD8.
CC {ECO:0000269|PubMed:17517630}.
CC -!- INTERACTION:
CC Q9HBL0; P10275: AR; NbExp=3; IntAct=EBI-3389814, EBI-608057;
CC Q9HBL0; P10721: KIT; NbExp=2; IntAct=EBI-3389814, EBI-1379503;
CC Q9HBL0; P08581: MET; NbExp=2; IntAct=EBI-3389814, EBI-1039152;
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:21768292}. Cell
CC junction, focal adhesion {ECO:0000269|PubMed:21768292}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:21768292}. Note=Localized at cell
CC periphery preferentially to fibrillar adhesions than focal adhesions.
CC Translocates from the cell edge to cell center in an ITGB1BP1-dependent
CC manner.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9HBL0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HBL0-2; Sequence=VSP_056335, VSP_056336, VSP_056337;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11023826}.
CC -!- PTM: Rapidly cleaved by calpain II.
CC -!- SIMILARITY: Belongs to the PTEN phosphatase protein family.
CC {ECO:0000305}.
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DR EMBL; AF225896; AAG33700.1; -; mRNA.
DR EMBL; AC009469; AAX88952.1; -; Genomic_DNA.
DR EMBL; AC010136; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC071905; AAH71905.1; -; mRNA.
DR CCDS; CCDS2407.1; -. [Q9HBL0-1]
DR RefSeq; NP_001294951.1; NM_001308022.1.
DR RefSeq; NP_072174.3; NM_022648.5. [Q9HBL0-1]
DR AlphaFoldDB; Q9HBL0; -.
DR SMR; Q9HBL0; -.
DR BioGRID; 112999; 32.
DR DIP; DIP-60948N; -.
DR IntAct; Q9HBL0; 25.
DR MINT; Q9HBL0; -.
DR STRING; 9606.ENSP00000171887; -.
DR CarbonylDB; Q9HBL0; -.
DR DEPOD; TNS1; -.
DR GlyGen; Q9HBL0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9HBL0; -.
DR PhosphoSitePlus; Q9HBL0; -.
DR BioMuta; TNS1; -.
DR DMDM; 212276466; -.
DR EPD; Q9HBL0; -.
DR jPOST; Q9HBL0; -.
DR MassIVE; Q9HBL0; -.
DR MaxQB; Q9HBL0; -.
DR PaxDb; Q9HBL0; -.
DR PeptideAtlas; Q9HBL0; -.
DR PRIDE; Q9HBL0; -.
DR ProteomicsDB; 66449; -.
DR ProteomicsDB; 81568; -. [Q9HBL0-1]
DR ABCD; Q9HBL0; 6 sequenced antibodies.
DR Antibodypedia; 4366; 222 antibodies from 35 providers.
DR DNASU; 7145; -.
DR Ensembl; ENST00000171887.8; ENSP00000171887.4; ENSG00000079308.20. [Q9HBL0-1]
DR Ensembl; ENST00000310858.10; ENSP00000308321.6; ENSG00000079308.20. [Q9HBL0-2]
DR GeneID; 7145; -.
DR KEGG; hsa:7145; -.
DR UCSC; uc002vgt.3; human. [Q9HBL0-1]
DR CTD; 7145; -.
DR DisGeNET; 7145; -.
DR GeneCards; TNS1; -.
DR HGNC; HGNC:11973; TNS1.
DR HPA; ENSG00000079308; Low tissue specificity.
DR MIM; 600076; gene.
DR neXtProt; NX_Q9HBL0; -.
DR OpenTargets; ENSG00000079308; -.
DR PharmGKB; PA36660; -.
DR VEuPathDB; HostDB:ENSG00000079308; -.
DR eggNOG; KOG1930; Eukaryota.
DR eggNOG; KOG2283; Eukaryota.
DR GeneTree; ENSGT00940000155400; -.
DR InParanoid; Q9HBL0; -.
DR OrthoDB; 172407at2759; -.
DR PhylomeDB; Q9HBL0; -.
DR TreeFam; TF315996; -.
DR PathwayCommons; Q9HBL0; -.
DR SignaLink; Q9HBL0; -.
DR BioGRID-ORCS; 7145; 11 hits in 1081 CRISPR screens.
DR ChiTaRS; TNS1; human.
DR GeneWiki; TNS1; -.
DR GenomeRNAi; 7145; -.
DR Pharos; Q9HBL0; Tbio.
DR PRO; PR:Q9HBL0; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9HBL0; protein.
DR Bgee; ENSG00000079308; Expressed in blood vessel layer and 199 other tissues.
DR ExpressionAtlas; Q9HBL0; baseline and differential.
DR Genevisible; Q9HBL0; HS.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0010761; P:fibroblast migration; IBA:GO_Central.
DR CDD; cd01213; PTB_tensin; 1.
DR CDD; cd09927; SH2_Tensin_like; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR013625; PTB.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR035012; Tensin-like_SH2.
DR InterPro; IPR014020; Tensin_C2-dom.
DR InterPro; IPR029023; Tensin_phosphatase.
DR InterPro; IPR033929; Tensin_PTB.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR Pfam; PF08416; PTB; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR Pfam; PF00017; SH2; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell junction; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Phosphoprotein;
KW Reference proteome; SH2 domain.
FT CHAIN 1..1735
FT /note="Tensin-1"
FT /id="PRO_0000215900"
FT DOMAIN 4..176
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT DOMAIN 181..307
FT /note="C2 tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00589"
FT DOMAIN 1463..1572
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 377..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1032..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1173..1192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..839
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1016
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1225..1243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1332..1353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1362..1378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 366
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 379
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 764
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 769
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 794
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 860
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 899
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 903
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 907
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 963
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 967
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1177
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1189
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 1266
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1294
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1446
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1588
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1
FT /note="M -> MVPFQQRKDCVLEGSTRVTPSVQPHLQPIRNM (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056335"
FT VAR_SEQ 352..385
FT /note="EVVGHTQGPLDGSLYAKVKKKDSLHGSTGAVNAT -> DGNKQNTNSQSIGS
FT ISGGLEDQYTWPDTHWPSQS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056336"
FT VAR_SEQ 386..1735
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056337"
FT VARIANT 311
FT /note="I -> M (in dbSNP:rs11680854)"
FT /id="VAR_047066"
FT VARIANT 466
FT /note="R -> C (in dbSNP:rs3815849)"
FT /id="VAR_047067"
FT VARIANT 528
FT /note="T -> I (in dbSNP:rs3796033)"
FT /id="VAR_047068"
FT VARIANT 1004
FT /note="R -> W (in dbSNP:rs3796028)"
FT /id="VAR_047069"
FT VARIANT 1093
FT /note="F -> L (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_048004"
FT VARIANT 1197
FT /note="W -> R (in dbSNP:rs2571445)"
FT /evidence="ECO:0000269|PubMed:11023826,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231"
FT /id="VAR_047070"
FT VARIANT 1604
FT /note="V -> I (in dbSNP:rs918949)"
FT /evidence="ECO:0000269|PubMed:11023826"
FT /id="VAR_047071"
FT CONFLICT 179
FT /note="M -> I (in Ref. 1; AAG33700)"
FT /evidence="ECO:0000305"
FT CONFLICT 1412
FT /note="S -> A (in Ref. 1; AAG33700)"
FT /evidence="ECO:0000305"
FT CONFLICT 1416
FT /note="A -> P (in Ref. 1; AAG33700)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1735 AA; 185701 MW; 90C173D5E371EF3E CRC64;
MSVSRTMEDS CELDLVYVTE RIIAVSFPST ANEENFRSNL REVAQMLKSK HGGNYLLFNL
SERRPDITKL HAKVLEFGWP DLHTPALEKI CSICKAMDTW LNADPHNVVV LHNKGNRGRI
GVVIAAYMHY SNISASADQA LDRFAMKRFY EDKIVPIGQP SQRRYVHYFS GLLSGSIKMN
NKPLFLHHVI MHGIPNFESK GGCRPFLRIY QAMQPVYTSG IYNIPGDSQT SVCITIEPGL
LLKGDILLKC YHKKFRSPAR DVIFRVQFHT CAIHDLGVVF GKEDLDDAFK DDRFPEYGKV
EFVFSYGPEK IQGMEHLENG PSVSVDYNTS DPLIRWDSYD NFSGHRDDGM EEVVGHTQGP
LDGSLYAKVK KKDSLHGSTG AVNATRPTLS ATPNHVEHTL SVSSDSGNST ASTKTDKTDE
PVPGASSATA ALSPQEKREL DRLLSGFGLE REKQGAMYHT QHLRSRPAGG SAVPSSGRHV
VPAQVHVNGG ALASERETDI LDDELPNQDG HSAGSMGTLS SLDGVTNTSE GGYPEALSPL
TNGLDKSYPM EPMVNGGGYP YESASRAGPA HAGHTAPMRP SYSAQEGLAG YQREGPHPAW
PQPVTTSHYA HDPSGMFRSQ SFSEAEPQLP PAPVRGGSSR EAVQRGLNSW QQQQQQQQQP
RPPPRQQERA HLESLVASRP SPQPLAETPI PSLPEFPRAA SQQEIEQSIE TLNMLMLDLE
PASAAAPLHK SQSVPGAWPG ASPLSSQPLS GSSRQSHPLT QSRSGYIPSG HSLGTPEPAP
RASLESVPPG RSYSPYDYQP CLAGPNQDFH SKSPASSSLP AFLPTTHSPP GPQQPPASLP
GLTAQPLLSP KEATSDPSRT PEEEPLNLEG LVAHRVAGVQ AREKQPAEPP APLRRRAASD
GQYENQSPEA TSPRSPGVRS PVQCVSPELA LTIALNPGGR PKEPHLHSYK EAFEEMEGTS
PSSPPPSGVR SPPGLAKTPL SALGLKPHNP ADILLHPTGV TRRRIQPEED EGKVVVRLSE
EPRSYVESVA RTAVAGPRAQ DSEPKSFSAP ATQAYGHEIP LRNGTLGGSF VSPSPLSTSS
PILSADSTSV GSFPSGESSD QGPRTPTQPL LESGFRSGSL GQPSPSAQRN YQSSSPLPTV
GSSYSSPDYS LQHFSSSPES QARAQFSVAG VHTVPGSPQA RHRTVGTNTP PSPGFGWRAI
NPSMAAPSSP SLSHHQMMGP PGTGFHGSTV SSPQSSAATT PGSPSLCRHP AGVYQVSGLH
NKVATTPGSP SLGRHPGAHQ GNLASGLHSN AIASPGSPSL GRHLGGSGSV VPGSPCLDRH
VAYGGYSTPE DRRPTLSRQS SASGYQAPST PSFPVSPAYY PGLSSPATSP SPDSAAFRQG
SPTPALPEKR RMSVGDRAGS LPNYATINGK VSSPVASGMS SPSGGSTVSF SHTLPDFSKY
SMPDNSPETR AKVKFVQDTS KYWYKPEISR EQAIALLKDQ EPGAFIIRDS HSFRGAYGLA
MKVSSPPPTI MQQNKKGDMT HELVRHFLIE TGPRGVKLKG CPNEPNFGSL SALVYQHSII
PLALPCKLVI PNRDPTDESK DSSGPANSTA DLLKQGAACN VLFVNSVDME SLTGPQAISK
ATSETLAADP TPAATIVHFK VSAQGITLTD NQRKLFFRRH YPLNTVTFCD LDPQERKWMK
TEGGAPAKLF GFVARKQGST TDNACHLFAE LDPNQPASAI VNFVSKVMLN AGQKR
