SRBS2_MOUSE
ID SRBS2_MOUSE Reviewed; 1180 AA.
AC Q3UTJ2; Q3USC6; Q80TS1; Q8BJL6; Q8BJU3; Q8BLW9; Q8BX47; Q8CHU0;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Sorbin and SH3 domain-containing protein 2;
DE AltName: Full=Arg-binding protein 2;
DE Short=ArgBP2;
DE AltName: Full=Arg/Abl-interacting protein 2;
GN Name=Sorbs2; Synonyms=Argbp2, Kiaa0777;
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 [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 6), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-532 (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 229-313 (ISOFORM 7), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 1097-1180 (ISOFORM 5).
RC STRAIN=C57BL/6J;
RC TISSUE=Aorta, Brain cortex, Cerebellum, Embryoid bodies, and Vein;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 162-1180 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-829, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-339; SER-378;
RP SER-379; SER-382 AND SER-1097, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP SER-345; SER-353 AND SER-355 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-322; SER-330 AND SER-332 (ISOFORM 5), AND IDENTIFICATION
RP 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 SER-27, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-28; SER-130; SER-143;
RP SER-239; SER-319; SER-325; SER-328; SER-339; SER-377; SER-378; SER-379;
RP SER-381; SER-382; SER-463; SER-577; SER-630; SER-633; SER-829; SER-923 AND
RP SER-1097, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-345; SER-347;
RP SER-353; SER-355; SER-368 AND SER-373 (ISOFORM 2), PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-322; SER-324; SER-330 AND SER-332 (ISOFORM 5), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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).
CC -!- FUNCTION: Adapter protein that plays a role in the assembling of
CC signaling complexes, being a link between ABL kinases and actin
CC cytoskeleton. Can form complex with ABL1 and CBL, thus promoting
CC ubiquitination and degradation of ABL1 (By similarity). May play a role
CC in the regulation of pancreatic cell adhesion, possibly by acting on
CC WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well as
CC dephosphorylation by PTPN12 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:O94875}.
CC -!- SUBUNIT: Interacts with ABL, CBL, DNM1, DNM2, FLOT1, AFDN, PTK2B/PYK2,
CC SAPAP, SPTAN1, SYNJ1, SYNJ2, VCL/vinculin, WASF, ABL1/c-Abl, ABL2/v-
CC Abl/Arg, ACTN, CBL and PALLD. Interacts with PTPN12 and WASF1 via its
CC SH3 domains; this interaction may mediate the partial PTPN12 and WASF1
CC translocation to focal adhesion sites. {ECO:0000250,
CC ECO:0000250|UniProtKB:O94875}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
CC Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250}. Apical cell
CC membrane {ECO:0000250|UniProtKB:O94875}. Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:O94875}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:O94875}. Cytoplasm, cytoskeleton {ECO:0000250}.
CC Note=Found at the Z line sarcomeres, stress fibers, dense bodies and
CC focal adhesion. In pancreatic acinar cells, localized preferentially to
CC the apical membrane. Colocalized with vinculin and filamentous actin at
CC focal adhesions and lamellipodia of pancreatic cells. {ECO:0000250,
CC ECO:0000250|UniProtKB:O94875}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q3UTJ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UTJ2-2; Sequence=VSP_034802, VSP_034803;
CC Name=3;
CC IsoId=Q3UTJ2-3; Sequence=VSP_034800, VSP_034802, VSP_034809,
CC VSP_034810;
CC Name=4;
CC IsoId=Q3UTJ2-4; Sequence=VSP_034800, VSP_034809;
CC Name=5;
CC IsoId=Q3UTJ2-5; Sequence=VSP_034801, VSP_034802, VSP_034804,
CC VSP_034809, VSP_034811;
CC Name=6;
CC IsoId=Q3UTJ2-6; Sequence=VSP_034801, VSP_034802, VSP_034805,
CC VSP_034808;
CC Name=7;
CC IsoId=Q3UTJ2-7; Sequence=VSP_034806, VSP_034807;
CC -!- DOMAIN: The first 2 SH3 domains are required for WASF1-binding. All 3
CC SH3 domains can bind independently to PTPN12.
CC {ECO:0000250|UniProtKB:O94875}.
CC -!- PTM: Ubiquitinated by CBL. {ECO:0000250}.
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DR EMBL; AK041051; BAC30799.1; -; mRNA.
DR EMBL; AK049030; BAC33518.1; -; mRNA.
DR EMBL; AK079130; BAC37554.1; -; mRNA.
DR EMBL; AK083429; BAC38913.1; -; mRNA.
DR EMBL; AK139388; BAE23988.1; -; mRNA.
DR EMBL; AK140498; BAE24407.1; -; mRNA.
DR EMBL; BC039163; AAH39163.1; -; mRNA.
DR EMBL; AK122369; BAC65651.1; -; mRNA.
DR CCDS; CCDS80872.1; -. [Q3UTJ2-5]
DR RefSeq; NP_001297636.1; NM_001310707.1.
DR RefSeq; XP_006509449.1; XM_006509386.1.
DR AlphaFoldDB; Q3UTJ2; -.
DR SMR; Q3UTJ2; -.
DR BioGRID; 231503; 37.
DR IntAct; Q3UTJ2; 10.
DR MINT; Q3UTJ2; -.
DR iPTMnet; Q3UTJ2; -.
DR PhosphoSitePlus; Q3UTJ2; -.
DR jPOST; Q3UTJ2; -.
DR MaxQB; Q3UTJ2; -.
DR PaxDb; Q3UTJ2; -.
DR PeptideAtlas; Q3UTJ2; -.
DR PRIDE; Q3UTJ2; -.
DR ProteomicsDB; 262688; -. [Q3UTJ2-1]
DR ProteomicsDB; 262689; -. [Q3UTJ2-2]
DR ProteomicsDB; 262690; -. [Q3UTJ2-3]
DR ProteomicsDB; 262691; -. [Q3UTJ2-4]
DR ProteomicsDB; 262692; -. [Q3UTJ2-5]
DR ProteomicsDB; 262693; -. [Q3UTJ2-6]
DR ProteomicsDB; 262694; -. [Q3UTJ2-7]
DR Antibodypedia; 28990; 114 antibodies from 24 providers.
DR DNASU; 234214; -.
DR Ensembl; ENSMUST00000134675; ENSMUSP00000118160; ENSMUSG00000031626. [Q3UTJ2-6]
DR Ensembl; ENSMUST00000141039; ENSMUSP00000117544; ENSMUSG00000031626. [Q3UTJ2-6]
DR Ensembl; ENSMUST00000153798; ENSMUSP00000118353; ENSMUSG00000031626. [Q3UTJ2-3]
DR GeneID; 234214; -.
DR KEGG; mmu:234214; -.
DR UCSC; uc009lpb.2; mouse. [Q3UTJ2-6]
DR UCSC; uc009lpc.2; mouse. [Q3UTJ2-1]
DR UCSC; uc009lpf.1; mouse. [Q3UTJ2-3]
DR UCSC; uc009lpi.2; mouse. [Q3UTJ2-4]
DR UCSC; uc029wsw.1; mouse. [Q3UTJ2-2]
DR CTD; 8470; -.
DR MGI; MGI:1924574; Sorbs2.
DR VEuPathDB; HostDB:ENSMUSG00000031626; -.
DR eggNOG; KOG4225; Eukaryota.
DR GeneTree; ENSGT00940000157056; -.
DR InParanoid; Q3UTJ2; -.
DR BioGRID-ORCS; 234214; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Sorbs2; mouse.
DR PRO; PR:Q3UTJ2; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q3UTJ2; protein.
DR Bgee; ENSMUSG00000031626; Expressed in otolith organ and 247 other tissues.
DR ExpressionAtlas; Q3UTJ2; baseline and differential.
DR Genevisible; Q3UTJ2; MM.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; IGI:MGI.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; ISO:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
DR GO; GO:1904393; P:regulation of skeletal muscle acetylcholine-gated channel clustering; IGI:MGI.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR003127; SoHo_dom.
DR InterPro; IPR028506; Sorbin_SH3.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR14167:SF56; PTHR14167:SF56; 1.
DR Pfam; PF00018; SH3_1; 2.
DR Pfam; PF14604; SH3_9; 1.
DR Pfam; PF02208; Sorb; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 3.
DR SMART; SM00459; Sorb; 1.
DR SUPFAM; SSF50044; SSF50044; 3.
DR PROSITE; PS50002; SH3; 3.
DR PROSITE; PS50831; SOHO; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Cell projection;
KW Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; SH3 domain; Ubl conjugation.
FT CHAIN 1..1180
FT /note="Sorbin and SH3 domain-containing protein 2"
FT /id="PRO_0000344478"
FT DOMAIN 166..230
FT /note="SoHo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00195"
FT DOMAIN 943..1002
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1018..1079
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1121..1180
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 25..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..930
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..945
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35413"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 357
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O94875"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94875"
FT MOD_RES 372
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O94875"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94875"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 574
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35413"
FT MOD_RES 577
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 829
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 923
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1097
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 4..34
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034800"
FT VAR_SEQ 45..67
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_034801"
FT VAR_SEQ 211
FT /note="P -> PDEDTDMYNTPYTYNA (in isoform 2, isoform 3,
FT isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_034802"
FT VAR_SEQ 308
FT /note="P -> PPPLPPTPTPVPREPSRKPLSVSPSTDGLRSPSPPPRSCVPAPRPSA
FT PDLSPTRTGRINPADIDLENEPWYKFFSELEFGHPPPKKALDYVQDHSSGVSNE (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_034803"
FT VAR_SEQ 308
FT /note="P -> PPPLPPTPTPVPREPSRKPLSVSPSTDGLRSPSPPPRSCVPAPCPSA
FT PDLSPTRPPKKALDYVQDHSSGVSNE (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_034804"
FT VAR_SEQ 309..316
FT /note="VSIYQSSI -> RSVSSRPL (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034805"
FT VAR_SEQ 311..313
FT /note="IYQ -> PCH (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034806"
FT VAR_SEQ 314..1180
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034807"
FT VAR_SEQ 317..1180
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034808"
FT VAR_SEQ 388..914
FT /note="Missing (in isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_034809"
FT VAR_SEQ 1126..1180
FT /note="FQALYNYTPRNEDELELRESDVVDVMEKCDDGWFVGTSRRTKFFGTFPGNYV
FT KRL -> LQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034810"
FT VAR_SEQ 1126..1135
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_034811"
FT CONFLICT 249
FT /note="V -> A (in Ref. 2; AAH39163)"
FT /evidence="ECO:0000305"
FT CONFLICT 944
FT /note="E -> EV (in Ref. 1; BAE24407)"
FT /evidence="ECO:0000305"
FT MOD_RES Q3UTJ2-2:345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES Q3UTJ2-2:347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q3UTJ2-2:353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES Q3UTJ2-2:355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES Q3UTJ2-2:368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q3UTJ2-2:373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q3UTJ2-5:322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES Q3UTJ2-5:324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q3UTJ2-5:330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES Q3UTJ2-5:332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1180 AA; 132349 MW; 99ECA798E95A092E CRC64;
MNTDSGGCAR KRAAMSVTLT SVKRVQSSPN LLAAGRESQS PDSAWRSYND RNPETLNGDA
TYSSLAAKGF RSVRPNLQDK RSPTQSQITI NGNSGGAVSP VSYYQRPFSP SAYSLPASLN
SSIIMQHGRS LDSAETYSQH AQSLDGTMGS SIPLYRSSEE EKRVTVIKAP HYPGIGPVDE
SGIPTAIRTT VDRPKDWYKT MFKQIHMVHK PGLYNSPYSA QSHPAAKTQT YRPLSKSHSD
NGTDAFKEVP SPVPPPHVPP RPRDQSSTLK HDWDPPDRKV DTRKFRSEPR SIFEYEPGKS
SILQHERPVS IYQSSIDRSL ERPSSSASMA GDFRKRRKSE PAVGPLRGLG DQSSSRTSPG
RADLPGSSST FTKSFISSSP SSPSRAQGGD DSKMCPPLCS YSGLNGTPSG ELECCNAYRQ
HLDVPGDSQR AITFKNGWQM ARQNAEIWSS TEETVSPKIK SRSCDDLLND DCDSFPDPKT
KSESMGSLLC EEDSKESCPM TWASPYIQEV CGNSRSRLKH RSAHNAPGFL KMYKKMHRIN
RKDLMNSEVI CSVKSRILQY EKEQQHRGLL HGWSQSSTEE VPRDVVPTRI SEFEKLIQKS
KSMPNLGDEM LSPITLEPPQ NGLCPKRRFS IESLLEEETQ VRHPSQGQRS CKSNTLVPIH
IEVTSDEQPR THMEFSDSDQ DGVVSDHSDY VHVEGSSFCS ESDFDHFSFT SSESFYGSSH
HHHHHHHHHR HLISSCKGRC PASYTRFTTM LKHERAKHEN MDRPRRQEMD PGLSKLAFLV
SPVPFRRKKI LTPQKQTEKA KCKASVVEAL DSALKDICDQ IKAEKRRGSL PDNSILHRLI
SELLPQIPER NSSLHALKRS PMHQPFHPLP PDGASHCPLY QNDCGRMPHS ASFPDVDTTS
NYHAQDYGSA LSLQDHESPR SYSSTLTDLG RSASRERRGT PEKEKLPAKA VYDFKAQTSK
ELSFKKGDTV YILRKIDQNW YEGEHHGRVG IFPISYVEKL TPPEKAQPAR PPPPVQPGEI
GEAIAKYNFN ADTNVELSLR KGDRIILLKR VDQNWYEGKI PGTNRQGIFP VSYVEVVKRN
AKGAEDYPDP PLPHSYSSDR IYTLSSNKPQ RPGFSHENIQ GGGEPFQALY NYTPRNEDEL
ELRESDVVDV MEKCDDGWFV GTSRRTKFFG TFPGNYVKRL
