TNS2_MOUSE
ID TNS2_MOUSE Reviewed; 1400 AA.
AC Q8CGB6; Q3TZ93; Q3UGR8; Q8CJ95; Q8R122;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Tensin-2;
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:Q63HR2};
DE AltName: Full=C1 domain-containing phosphatase and tensin homolog;
DE Short=C1-TEN;
DE AltName: Full=Tensin-like C1 domain-containing phosphatase;
GN Name=Tns2; Synonyms=Tenc1;
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] (ISOFORM 2).
RA Lo S.H.;
RT "Molecular cloning and characterization of mouse tensin 2.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 753-1400 (ISOFORM 3).
RC STRAIN=FVB/N; TISSUE=Liver, and Salivary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-935 (ISOFORM 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-875 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Inner ear, and Melanocyte;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-483 AND SER-1087, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118; SER-120; SER-455;
RP SER-466; SER-481; TYR-483; SER-830; SER-832; SER-835; THR-909; SER-941;
RP SER-1087 AND SER-1238, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-555, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [9]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=23401856; DOI=10.1128/mcb.01447-12;
RA Koh A., Lee M.N., Yang Y.R., Jeong H., Ghim J., Noh J., Kim J., Ryu D.,
RA Park S., Song P., Koo S.H., Leslie N.R., Berggren P.O., Choi J.H.,
RA Suh P.G., Ryu S.H.;
RT "C1-Ten is a protein tyrosine phosphatase of insulin receptor substrate 1
RT (IRS-1), regulating IRS-1 stability and muscle atrophy.";
RL Mol. Cell. Biol. 33:1608-1620(2013).
CC -!- FUNCTION: Tyrosine-protein phosphatase which regulates cell motility
CC proliferation and muscle-response to insulin. In muscles and under
CC catabolic conditions, dephosphorylates IRS1 leading to its degradation
CC and muscle atrophy. Negatively regulates PI3K-AKT pathway activation.
CC {ECO:0000250|UniProtKB:Q63HR2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000250|UniProtKB:Q63HR2};
CC -!- SUBUNIT: Interacts with AXL. Interacts with SYK; leading to its
CC phosphorylation (By similarity). {ECO:0000250|UniProtKB:Q63HR2}.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:Q63HR2}. Cell membrane
CC {ECO:0000250|UniProtKB:Q63HR2}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q63HR2}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q63HR2}. Note=Detected at the end of actin
CC stress fibers. Detected in cytoplasmic punctate bodies.
CC {ECO:0000250|UniProtKB:Q63HR2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8CGB6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CGB6-2; Sequence=VSP_026462;
CC Name=3;
CC IsoId=Q8CGB6-3; Sequence=VSP_026464;
CC Name=4;
CC IsoId=Q8CGB6-4; Sequence=VSP_026463;
CC -!- TISSUE SPECIFICITY: Low expression levels in anabolic skeletal muscles.
CC {ECO:0000269|PubMed:23401856}.
CC -!- DEVELOPMENTAL STAGE: Expressed in skeletal muscle at 17.5 dpc until
CC post natal day P0 and then decreases at P21.
CC {ECO:0000269|PubMed:23401856}.
CC -!- INDUCTION: Induced under catabolic conditions in skeletal muscles.
CC {ECO:0000269|PubMed:23401856}.
CC -!- SIMILARITY: Belongs to the PTEN phosphatase protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE34316.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF424789; AAN32753.1; -; mRNA.
DR EMBL; BC025818; AAH25818.1; -; mRNA.
DR EMBL; BC042190; AAH42190.1; -; mRNA.
DR EMBL; AK147789; BAE28139.1; -; mRNA.
DR EMBL; AK158009; BAE34316.1; ALT_FRAME; mRNA.
DR CCDS; CCDS37224.1; -. [Q8CGB6-1]
DR CCDS; CCDS88852.1; -. [Q8CGB6-3]
DR RefSeq; NP_705761.2; NM_153533.2. [Q8CGB6-1]
DR RefSeq; XP_006520755.1; XM_006520692.2. [Q8CGB6-4]
DR RefSeq; XP_006520757.1; XM_006520694.2. [Q8CGB6-2]
DR RefSeq; XP_011243839.1; XM_011245537.2.
DR AlphaFoldDB; Q8CGB6; -.
DR BMRB; Q8CGB6; -.
DR SMR; Q8CGB6; -.
DR BioGRID; 229043; 2.
DR CORUM; Q8CGB6; -.
DR STRING; 10090.ENSMUSP00000041087; -.
DR iPTMnet; Q8CGB6; -.
DR PhosphoSitePlus; Q8CGB6; -.
DR SwissPalm; Q8CGB6; -.
DR jPOST; Q8CGB6; -.
DR MaxQB; Q8CGB6; -.
DR PaxDb; Q8CGB6; -.
DR PeptideAtlas; Q8CGB6; -.
DR PRIDE; Q8CGB6; -.
DR ProteomicsDB; 259148; -. [Q8CGB6-1]
DR ProteomicsDB; 259149; -. [Q8CGB6-2]
DR ProteomicsDB; 259150; -. [Q8CGB6-3]
DR ProteomicsDB; 259151; -. [Q8CGB6-4]
DR Antibodypedia; 26823; 87 antibodies from 23 providers.
DR DNASU; 209039; -.
DR Ensembl; ENSMUST00000046144; ENSMUSP00000041087; ENSMUSG00000037003. [Q8CGB6-3]
DR Ensembl; ENSMUST00000169627; ENSMUSP00000129146; ENSMUSG00000037003. [Q8CGB6-1]
DR Ensembl; ENSMUST00000228958; ENSMUSP00000155830; ENSMUSG00000037003. [Q8CGB6-4]
DR GeneID; 209039; -.
DR KEGG; mmu:209039; -.
DR UCSC; uc007xum.1; mouse. [Q8CGB6-4]
DR UCSC; uc007xun.1; mouse. [Q8CGB6-2]
DR UCSC; uc007xuo.1; mouse. [Q8CGB6-1]
DR UCSC; uc011zzx.1; mouse. [Q8CGB6-3]
DR CTD; 23371; -.
DR MGI; MGI:2387586; Tns2.
DR VEuPathDB; HostDB:ENSMUSG00000037003; -.
DR eggNOG; KOG1930; Eukaryota.
DR eggNOG; KOG2283; Eukaryota.
DR GeneTree; ENSGT00940000161535; -.
DR HOGENOM; CLU_002189_0_0_1; -.
DR InParanoid; Q8CGB6; -.
DR OMA; RCKTATH; -.
DR OrthoDB; 172407at2759; -.
DR PhylomeDB; Q8CGB6; -.
DR TreeFam; TF315996; -.
DR BioGRID-ORCS; 209039; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Tns2; mouse.
DR PRO; PR:Q8CGB6; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8CGB6; protein.
DR Bgee; ENSMUSG00000037003; Expressed in ankle joint and 219 other tissues.
DR ExpressionAtlas; Q8CGB6; baseline and differential.
DR Genevisible; Q8CGB6; MM.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0019725; P:cellular homeostasis; IMP:MGI.
DR GO; GO:0032963; P:collagen metabolic process; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0048871; P:multicellular organismal homeostasis; IMP:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISS:UniProtKB.
DR GO; GO:0014850; P:response to muscle activity; IMP:MGI.
DR CDD; cd00029; C1; 1.
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; IPR046349; C1-like_sf.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR002219; PE/DAG-bd.
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 Pfam; PF08416; PTB; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR Pfam; PF00017; SH2; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Hydrolase; Membrane;
KW Metal-binding; Methylation; Phosphoprotein; Protein phosphatase;
KW Reference proteome; SH2 domain; Zinc; Zinc-finger.
FT CHAIN 1..1400
FT /note="Tensin-2"
FT /id="PRO_0000292988"
FT DOMAIN 122..294
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT DOMAIN 299..425
FT /note="C2 tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00589"
FT DOMAIN 1131..1238
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT ZN_FING 31..79
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 425..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..506
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..938
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..1005
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1055
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 231
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT MOD_RES 91
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q63HR2"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 456
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q63HR2"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 474
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q63HR2"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 483
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 555
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63HR2"
FT MOD_RES 825
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63HR2"
FT MOD_RES 830
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 832
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 835
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 909
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 931
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63HR2"
FT MOD_RES 941
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 972
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63HR2"
FT MOD_RES 977
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q63HR2"
FT MOD_RES 991
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63HR2"
FT MOD_RES 1003
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63HR2"
FT MOD_RES 1087
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1173
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q63HR2"
FT MOD_RES 1238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..25
FT /note="MKSSGPVERLLRALGRRDSSRATSR -> MK (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_026462"
FT VAR_SEQ 1..25
FT /note="MKSSGPVERLLRALGRRDSSRATSR -> MGWSGGAPCCCPSSPRPRPSGRP
FT PQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026463"
FT VAR_SEQ 872
FT /note="T -> TELFPPVS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026464"
FT CONFLICT 54
FT /note="D -> N (in Ref. 3; BAE28139)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="F -> L (in Ref. 3; BAE28139)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="P -> H (in Ref. 3; BAE28139)"
FT /evidence="ECO:0000305"
FT CONFLICT 1112..1114
FT /note="HPL -> NPFVVQE (in Ref. 1; AAN32753)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1400 AA; 152013 MW; 72CB109A17BB021C CRC64;
MKSSGPVERL LRALGRRDSS RATSRPRKAE PHSFREKVFR KKTPVCAVCK VTIDGTGVSC
RVCKVATHRK CEAKVTSSCQ ALPPAELRRS TAPVRRIEHL GSTKSLNHSK QRSTLPRSFS
LDPLMERRWD LDLTYVTERI LAAAFPARPD EQRHRGHLRE LAHVLQSKHR DKYLLFNLSE
KRHDLTRLNP KVQDFGWPEL HAPPLDKLCS ICKAMETWLS ADPQHVVVLY CKGSKGKLGV
IVSAYMHYSK ISAGADQALA TLTMRKFCED KVATELQPSQ RRYVSYFSGL LSGSIRMNSS
PLFLHYVFVP VLPAFEPNTG FQPFLKIYQS MQLVYTSGVY RIAGPGPQQL CISLEPALLL
KGDVMVTCYH KGGQGTDRTL VFRVQFHTCT IHGSRLTFPK DQLDEAWADE RFPFQASVEF
VFSSSPEKVK GNTPRNDPSV SVDYNTTEPA VRWDSYENFN QHHEDSVDGA LAHTRGPLDG
SPYAQVQRVP RQTPPAPSPE LPPPPMLSVS SDSGHSSTLT TEHTAESPGR PPPTAAERQE
LDRLLGGCGV ASAGRGAGRE TAILDDEEQP SVGGGLHLGM YSGHRPGLSR RCSCRQGFRE
PCGVPNGSYY RPEGTLERRR PPYGGYEGHP QGYAEASVEK RRLCRSLSEG PYPYAPELGK
PANGDFGYRP AGYREVVILE DPGVPALCSC PACEEKLALP TAALYGLRLE REAAEGWSSE
VGKPLLHPVR PGHPLPLLVP ACGHHHAPMP DYGCLKPPKV GEEGHEGCSY AVCSEGRYGH
SGYPALVTYG YGGAVPSYCP AYGRAPHSCG SPSEGRGYPS PGAHSPRAGS VSPGSPPYLQ
PRKLGYEISA EDGRDKYPLS GHLASTGPLA STESPEPSWR DGSSGHSTLP RSPRDPQCSA
SSELSGPSTP LHTSSPVQGK ESNRRQDTTR SPSLAPTQRL SPGEALPSVV QGVAEKTPEL
LTSSRPEQLD PSPFSQTSAP GSPNGWPQER SPGGHTNSAS PRSPVPTTLP GLRHAPWQGP
RGTSDSPDGS PLTPVPTQMP WLVGSPEPPQ SSPTPAFPLA TSYDANGPIQ PPLPEKRHLP
GSGQQPSPPA RSTNQHVTFA SPLPDVTQPP EHPLQENQSN VKFVQDTSKF WYKPHLSRDQ
AIALLKDKDP GAFLIRDSHS FQGAYGLALK VATPPPSAQP WKGDPSEQLV RHFLIETGPK
GVKIKGCPTE PYFGSLSALV SQHSISPISL PCCLRIPSKD PLEETPEAPV PTNMSTAADL
LRQGAACSVL YLTSVETESL TGPQAVAKAS SAALSCSPVP VPAIVHFKVS AQGITLTDNQ
RKLFFRRHYP VNSITFSSTD PQDRRWTNPD GATSKIFGFV AKKPGSPWEN VCHLFAELDP
DQPASAIVTF ITKVLLGQRK
