ID SRBS2_HUMAN Reviewed; 1100 AA.
AC O94875; A6NEK9; B3KPQ7; B7Z1G5; B7Z3X6; C9JKV9; D3DP62; D3DP63; E9PAS5;
AC E9PAW4; G3XAI0; H7BXR4; J3KNZ5; O60592; O60593; Q96EX0;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 3.
DT 27-MAR-2024, entry version 195.
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;
DE AltName: Full=Sorbin;
GN Name=SORBS2; Synonyms=ARGBP2, KIAA0777;
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] (ISOFORMS 2 AND 5), NUCLEOTIDE SEQUENCE [MRNA]
RP OF 1-1049 (ISOFORM 4), PHOSPHORYLATION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, INTERACTION WITH ABL1 AND ABL2, AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=9211900; DOI=10.1074/jbc.272.28.17542;
RA Wang B., Golemis E.A., Kruh G.D.;
RT "ArgBP2, a multiple Src homology 3 domain-containing, Arg/Abl-interacting
RT protein, is phosphorylated in v-Abl-transformed cells and localized in
RT stress fibers and cardiocyte Z-disks.";
RL J. Biol. Chem. 272:17542-17550(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), AMIDATION AT ALA-153 (ISOFORM 6),
RP AND TISSUE SPECIFICITY.
RX PubMed=11786189; DOI=10.1016/s0196-9781(01)00558-7;
RA Wahbi K., Magaud J.-P., Pansu D., Descroix-Vagne M.;
RT "Coding region of the sorbin gene in different species.";
RL Peptides 22:2045-2053(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7; 8 AND 11).
RC TISSUE=Embryonic brain, Thalamus, and Urinary bladder;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 9 AND 10).
RC TISSUE=Heart, and Hepatoma;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Lymph;
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 [9]
RP INTERACTION WITH CBL, UBIQUITINATION BY CBL, AND FUNCTION.
RX PubMed=12475393; DOI=10.1042/bj20021539;
RA Soubeyran P., Barac A., Szymkiewicz I., Dikic I.;
RT "Cbl-ArgBP2 complex mediates ubiquitination and degradation of c-Abl.";
RL Biochem. J. 370:29-34(2003).
RN [10]
RP INTERACTION WITH PALLD AND ACTN, AND SUBCELLULAR LOCATION.
RX PubMed=16125169; DOI=10.1016/j.yexcr.2005.06.026;
RA Roenty M., Taivainen A., Moza M., Kruh G.D., Ehler E., Carpen O.;
RT "Involvement of palladin and alpha-actinin in targeting of the Abl/Arg
RT kinase adaptor ArgBP2 to the actin cytoskeleton.";
RL Exp. Cell Res. 310:88-98(2005).
RN [11]
RP RETRACTED PAPER.
RX PubMed=15784622; DOI=10.1074/jbc.m500097200;
RA Yuan Z.-Q., Kim D., Kaneko S., Sussman M., Bokoch G.M., Kruh G.D.,
RA Nicosia S.V., Testa J.R., Cheng J.Q.;
RT "ArgBP2gamma interacts with Akt and p21-activated kinase-1 and promotes
RT cell survival.";
RL J. Biol. Chem. 280:21483-21490(2005).
RN [12]
RP RETRACTION NOTICE OF PUBMED:15784622.
RX PubMed=27825083; DOI=10.1074/jbc.a116.500097;
RA Yuan Z.Q., Kim D., Kaneko S., Sussman M., Bokoch G.M., Kruh G.D.,
RA Nicosia S.V., Testa J.R., Cheng J.Q.;
RT "ArgBP2gamma interacts with Akt and p21-activated kinase-1 and promotes
RT cell survival.";
RL J. Biol. Chem. 291:22845-22845(2016).
RN [13]
RP FUNCTION, INTERACTION WITH PTPN12 AND WASF1, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEPHOSPHORYLATION BY PTPN12, AND DOMAIN.
RX PubMed=18559503; DOI=10.1158/0008-5472.can-08-0958;
RA Taieb D., Roignot J., Andre F., Garcia S., Masson B., Pierres A.,
RA Iovanna J.L., Soubeyran P.;
RT "ArgBP2-dependent signaling regulates pancreatic cell migration, adhesion,
RT and tumorigenicity.";
RL Cancer Res. 68:4588-4596(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; THR-277; SER-301 AND
RP SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439
RP (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346
RP (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260
RP (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306
RP (ISOFORMS 4 AND 5), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-298; SER-299 AND
RP SER-302, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-439
RP (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 (ISOFORM
RP 11), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346 (ISOFORM
RP 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORMS 12 AND 9),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260 (ISOFORM 3),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-306 (ISOFORMS 4
RP AND 5), 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; SER-157; SER-239;
RP SER-259; SER-287; THR-292; SER-302; SER-304; SER-843 AND SER-1023,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-413; THR-415; SER-439;
RP THR-459 AND SER-474 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP SER-27 AND SER-28 (ISOFORM 11), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP THR-320; THR-322; SER-346; THR-366 AND SER-381 (ISOFORM 12),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-14 (ISOFORMS 12
RP AND 9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316 (ISOFORM 2),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-234; THR-236; SER-260 AND
RP SER-295 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-280
RP (ISOFORMS 3; 4 AND 5), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-282;
RP SER-306; THR-326 AND SER-341 (ISOFORMS 4 AND 5), PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-311 (ISOFORM 8), 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).
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. May play a role in the
CC regulation of pancreatic cell adhesion, possibly by acting on WASF1
CC phosphorylation, enhancing phosphorylation by ABL1, as well as
CC dephosphorylation by PTPN12 (PubMed:18559503). Isoform 6 increases
CC water and sodium absorption in the intestine and gall-bladder.
CC {ECO:0000269|PubMed:12475393, ECO:0000269|PubMed:18559503,
CC ECO:0000269|PubMed:9211900}.
CC -!- SUBUNIT: Interacts with ABL, CBL, DNM1, DNM2, FLOT1, AFDN, PTK2B/PYK2,
CC SAPAP, SPTAN1, SYNJ1, SYNJ2, VCL/vinculin and WASF (By similarity).
CC Interacts with ABL1/c-Abl, ABL2/v-Abl/Arg, ACTN, CBL and PALLD.
CC Interacts with PTPN12 and WASF1 via its SH3 domains; this interaction
CC may mediate the partial PTPN12 and WASF1 translocation to focal
CC adhesion sites. {ECO:0000250, ECO:0000269|PubMed:12475393,
CC ECO:0000269|PubMed:16125169, ECO:0000269|PubMed:18559503,
CC ECO:0000269|PubMed:9211900}.
CC -!- INTERACTION:
CC O94875; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-311323, EBI-1166928;
CC O94875; O43281: EFS; NbExp=3; IntAct=EBI-311323, EBI-718488;
CC O94875; V9HW98: HEL2; NbExp=3; IntAct=EBI-311323, EBI-10190883;
CC O94875; O43639: NCK2; NbExp=3; IntAct=EBI-311323, EBI-713635;
CC O94875; Q13177: PAK2; NbExp=2; IntAct=EBI-311323, EBI-1045887;
CC O94875; Q8WX93: PALLD; NbExp=2; IntAct=EBI-311323, EBI-2803991;
CC O94875; P31947: SFN; NbExp=4; IntAct=EBI-311323, EBI-476295;
CC O94875; Q9H788-2: SH2D4A; NbExp=3; IntAct=EBI-311323, EBI-10308083;
CC O94875; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-311323, EBI-2559305;
CC O94875; P42768: WAS; NbExp=3; IntAct=EBI-311323, EBI-346375;
CC O94875; P62258: YWHAE; NbExp=4; IntAct=EBI-311323, EBI-356498;
CC O94875; P63104: YWHAZ; NbExp=4; IntAct=EBI-311323, EBI-347088;
CC O94875; PRO_0000037551 [Q9WMX2]; Xeno; NbExp=2; IntAct=EBI-311323, EBI-6863748;
CC O94875-10; Q8IZP0-5: ABI1; NbExp=3; IntAct=EBI-12037893, EBI-11743294;
CC O94875-10; O43707: ACTN4; NbExp=4; IntAct=EBI-12037893, EBI-351526;
CC O94875-10; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-12037893, EBI-1166928;
CC O94875-10; Q13191: CBLB; NbExp=3; IntAct=EBI-12037893, EBI-744027;
CC O94875-10; Q9Y2H0-1: DLGAP4; NbExp=3; IntAct=EBI-12037893, EBI-12000556;
CC O94875-10; O43281-2: EFS; NbExp=3; IntAct=EBI-12037893, EBI-11525448;
CC O94875-10; O15372: EIF3H; NbExp=3; IntAct=EBI-12037893, EBI-709735;
CC O94875-10; Q08379: GOLGA2; NbExp=3; IntAct=EBI-12037893, EBI-618309;
CC O94875-10; O14512: SOCS7; NbExp=3; IntAct=EBI-12037893, EBI-1539606;
CC O94875-10; O94875-10: SORBS2; NbExp=3; IntAct=EBI-12037893, EBI-12037893;
CC O94875-10; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-12037893, EBI-11139477;
CC O94875-10; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-12037893, EBI-2559305;
CC O94875-10; O00401: WASL; NbExp=3; IntAct=EBI-12037893, EBI-957615;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:16125169, ECO:0000269|PubMed:9211900}. Apical cell
CC membrane {ECO:0000269|PubMed:18559503}. Cell junction, focal adhesion
CC {ECO:0000269|PubMed:18559503}. Cell projection, lamellipodium
CC {ECO:0000269|PubMed:18559503}. Note=Found at the Z-disk sarcomeres,
CC stress fibers, dense bodies and focal adhesion. In pancreatic acinar
CC cells, localized preferentially to the apical membrane. Colocalized
CC with vinculin and filamentous actin at focal adhesions and lamellipodia
CC of pancreatic cells. {ECO:0000269|PubMed:18559503}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=12;
CC Name=1;
CC IsoId=O94875-1; Sequence=Displayed;
CC Name=2; Synonyms=ArgBP2a;
CC IsoId=O94875-2; Sequence=VSP_034792, VSP_034794, VSP_034798;
CC Name=3;
CC IsoId=O94875-3; Sequence=VSP_034795, VSP_034798;
CC Name=4;
CC IsoId=O94875-4; Sequence=VSP_034792, VSP_034795, VSP_034798;
CC Name=5; Synonyms=ArgBP2b;
CC IsoId=O94875-5; Sequence=VSP_034792, VSP_034795, VSP_034798,
CC VSP_034799;
CC Name=6; Synonyms=Sorbin;
CC IsoId=O94875-6; Sequence=VSP_034791, VSP_034793, VSP_034796,
CC VSP_034797;
CC Name=7;
CC IsoId=O94875-7; Sequence=VSP_043665, VSP_043666;
CC Name=8;
CC IsoId=O94875-8; Sequence=VSP_045640, VSP_045641, VSP_034798;
CC Name=9;
CC IsoId=O94875-9; Sequence=VSP_046219, VSP_043666, VSP_034798;
CC Name=10;
CC IsoId=O94875-10; Sequence=VSP_046220, VSP_034795, VSP_034798;
CC Name=11;
CC IsoId=O94875-11; Sequence=VSP_047056;
CC Name=12;
CC IsoId=O94875-12; Sequence=VSP_046219, VSP_034795, VSP_034798;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in heart. In cardiac muscle
CC cells, located in the Z-disks of sarcomere. Also found, but to a lower
CC extent, in small and large intestine, pancreas, thymus, colon, spleen,
CC prostate, testis, brain, ovary and epithelial cells. In the pancreas,
CC mainly expressed in acinar cells, duct cells and all cell types in
CC islets (at protein level). Tends to be down-regulated in pancreatic
CC adenocarcinomas ans metastases. {ECO:0000269|PubMed:11786189,
CC ECO:0000269|PubMed:18559503, ECO:0000269|PubMed:9211900}.
CC -!- DOMAIN: The first 2 SH3 domains are required for WASF1-binding. All 3
CC SH3 domains can bind independently to PTPN12.
CC {ECO:0000269|PubMed:18559503}.
CC -!- PTM: Ubiquitinated by CBL. {ECO:0000269|PubMed:12475393}.
CC -!- PTM: Dephosphorylated by PTPN12. {ECO:0000269|PubMed:18559503}.
CC -!- CAUTION: Was shown to interact with AKT1 and PAK1 (PubMed:15784622).
CC This work has later been retracted due to concerns of image
CC manipulation. {ECO:0000269|PubMed:15784622,
CC ECO:0000305|PubMed:27825083}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34497.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="https://atlasgeneticsoncology.org/gene/693/SORBS2";
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DR EMBL; AF049884; AAC05508.1; -; mRNA.
DR EMBL; AF049885; AAC05509.1; -; mRNA.
DR EMBL; AB018320; BAA34497.2; ALT_INIT; mRNA.
DR EMBL; AK056628; BAG51769.1; -; mRNA.
DR EMBL; AK293400; BAH11501.1; -; mRNA.
DR EMBL; AK296461; BAH12362.1; -; mRNA.
DR EMBL; AK225327; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK225812; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC093797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC096659; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471056; EAX04630.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04631.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04632.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04635.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04636.1; -; Genomic_DNA.
DR EMBL; BC011883; AAH11883.1; -; mRNA.
DR CCDS; CCDS3845.1; -. [O94875-1]
DR CCDS; CCDS43289.2; -. [O94875-2]
DR CCDS; CCDS47173.1; -. [O94875-9]
DR CCDS; CCDS47174.1; -. [O94875-12]
DR CCDS; CCDS47175.1; -. [O94875-10]
DR CCDS; CCDS47176.1; -. [O94875-7]
DR CCDS; CCDS54825.1; -. [O94875-8]
DR CCDS; CCDS59482.1; -. [O94875-11]
DR RefSeq; NP_001139142.1; NM_001145670.1. [O94875-9]
DR RefSeq; NP_001139143.1; NM_001145671.2. [O94875-12]
DR RefSeq; NP_001139144.1; NM_001145672.1. [O94875-8]
DR RefSeq; NP_001139145.1; NM_001145673.1. [O94875-10]
DR RefSeq; NP_001139146.1; NM_001145674.1. [O94875-7]
DR RefSeq; NP_001257700.1; NM_001270771.1. [O94875-11]
DR RefSeq; NP_003594.3; NM_003603.6. [O94875-2]
DR RefSeq; NP_066547.1; NM_021069.4. [O94875-1]
DR RefSeq; XP_005263369.1; XM_005263312.1.
DR RefSeq; XP_006714453.1; XM_006714390.1.
DR RefSeq; XP_016864260.1; XM_017008771.1.
DR PDB; 5VEI; X-ray; 1.33 A; A=866-921.
DR PDBsum; 5VEI; -.
DR AlphaFoldDB; O94875; -.
DR SMR; O94875; -.
DR BioGRID; 114047; 86.
DR CORUM; O94875; -.
DR DIP; DIP-31634N; -.
DR IntAct; O94875; 67.
DR MINT; O94875; -.
DR STRING; 9606.ENSP00000347852; -.
DR GlyCosmos; O94875; 2 sites, 1 glycan.
DR GlyGen; O94875; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; O94875; -.
DR PhosphoSitePlus; O94875; -.
DR BioMuta; SORBS2; -.
DR EPD; O94875; -.
DR jPOST; O94875; -.
DR MassIVE; O94875; -.
DR MaxQB; O94875; -.
DR PaxDb; 9606-ENSP00000347852; -.
DR PeptideAtlas; O94875; -.
DR ProteomicsDB; 10626; -.
DR ProteomicsDB; 19072; -.
DR ProteomicsDB; 19092; -.
DR ProteomicsDB; 33754; -.
DR ProteomicsDB; 43369; -.
DR ProteomicsDB; 50512; -. [O94875-1]
DR ProteomicsDB; 50513; -. [O94875-2]
DR ProteomicsDB; 50514; -. [O94875-3]
DR ProteomicsDB; 50515; -. [O94875-4]
DR ProteomicsDB; 50516; -. [O94875-5]
DR ProteomicsDB; 50517; -. [O94875-6]
DR ProteomicsDB; 50518; -. [O94875-7]
DR Pumba; O94875; -.
DR ABCD; O94875; 10 sequenced antibodies.
DR Antibodypedia; 28990; 143 antibodies from 25 providers.
DR DNASU; 8470; -.
DR Ensembl; ENST00000284776.11; ENSP00000284776.7; ENSG00000154556.20. [O94875-1]
DR Ensembl; ENST00000319471.13; ENSP00000322182.9; ENSG00000154556.20. [O94875-12]
DR Ensembl; ENST00000355634.9; ENSP00000347852.5; ENSG00000154556.20. [O94875-11]
DR Ensembl; ENST00000393528.7; ENSP00000377162.3; ENSG00000154556.20. [O94875-2]
DR Ensembl; ENST00000437304.6; ENSP00000396008.2; ENSG00000154556.20. [O94875-10]
DR Ensembl; ENST00000449407.6; ENSP00000397262.2; ENSG00000154556.20. [O94875-9]
DR Ensembl; ENST00000451974.6; ENSP00000401818.2; ENSG00000154556.20. [O94875-8]
DR Ensembl; ENST00000487836.6; ENSP00000511887.1; ENSG00000154556.20. [O94875-7]
DR GeneID; 8470; -.
DR KEGG; hsa:8470; -.
DR UCSC; uc003iyh.4; human. [O94875-1]
DR AGR; HGNC:24098; -.
DR CTD; 8470; -.
DR DisGeNET; 8470; -.
DR GeneCards; SORBS2; -.
DR HGNC; HGNC:24098; SORBS2.
DR HPA; ENSG00000154556; Tissue enhanced (heart).
DR MIM; 616349; gene.
DR neXtProt; NX_O94875; -.
DR OpenTargets; ENSG00000154556; -.
DR PharmGKB; PA142670890; -.
DR VEuPathDB; HostDB:ENSG00000154556; -.
DR eggNOG; KOG4225; Eukaryota.
DR GeneTree; ENSGT00940000157056; -.
DR HOGENOM; CLU_003951_2_0_1; -.
DR InParanoid; O94875; -.
DR OMA; XEDELEL; -.
DR OrthoDB; 5407056at2759; -.
DR PhylomeDB; O94875; -.
DR TreeFam; TF320680; -.
DR PathwayCommons; O94875; -.
DR SignaLink; O94875; -.
DR SIGNOR; O94875; -.
DR BioGRID-ORCS; 8470; 13 hits in 1152 CRISPR screens.
DR ChiTaRS; SORBS2; human.
DR GeneWiki; SORBS2; -.
DR GenomeRNAi; 8470; -.
DR Pharos; O94875; Tbio.
DR PRO; PR:O94875; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; O94875; Protein.
DR Bgee; ENSG00000154556; Expressed in heart right ventricle and 207 other cell types or tissues.
DR ExpressionAtlas; O94875; baseline and differential.
DR Genevisible; O94875; HS.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; NAS:UniProtKB.
DR GO; GO:0008093; F:cytoskeletal anchor activity; TAS:ProtInc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR GO; GO:0008307; F:structural constituent of muscle; TAS:ProtInc.
DR GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; ISS:BHF-UCL.
DR GO; GO:0007219; P:Notch signaling pathway; IBA:GO_Central.
DR CDD; cd11920; SH3_Sorbs2_1; 1.
DR CDD; cd11923; SH3_Sorbs2_2; 1.
DR CDD; cd11917; SH3_Sorbs2_3; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR003127; SoHo_dom.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR14167:SF56; DREBRIN-LIKE PROTEIN-RELATED; 1.
DR PANTHER; PTHR14167; SH3 DOMAIN-CONTAINING; 1.
DR Pfam; PF00018; SH3_1; 2.
DR Pfam; PF14604; SH3_9; 1.
DR Pfam; PF02208; Sorb; 1.
DR PRINTS; PR00499; P67PHOX.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 3.
DR SMART; SM00459; Sorb; 1.
DR SUPFAM; SSF50044; SH3-domain; 3.
DR PROSITE; PS50002; SH3; 3.
DR PROSITE; PS50831; SOHO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Amidation; Cell junction;
KW Cell membrane; Cell projection; Cytoplasm; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain; Ubl conjugation.
FT CHAIN 1..1100
FT /note="Sorbin and SH3 domain-containing protein 2"
FT /id="PRO_0000344477"
FT DOMAIN 66..127
FT /note="SoHo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00195"
FT DOMAIN 863..922
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 938..999
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1041..1100
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 30..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..182
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..866
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UTJ2"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UTJ2"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UTJ2"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UTJ2"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 277
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 292
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UTJ2"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UTJ2"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35413"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UTJ2"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UTJ2"
FT MOD_RES 750
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UTJ2"
FT MOD_RES 843
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1017
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UTJ2"
FT MOD_RES 1023
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..89
FT /note="MSYYQRPFSPSAYSLPASLNSSIVMQHGTSLDSTDTYPQHAQSLDGTTSSSI
FT PLYRSSEEEKRVTVIKAPHYPGIGPVDESGIPTAIRT -> MKATTPLQ (in
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043665"
FT VAR_SEQ 1..81
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:11786189"
FT /id="VSP_034791"
FT VAR_SEQ 1
FT /note="M -> MYSNEDSRQTIVYSEESNTTMSYTQKITNPLPAASSTDPAPFANINT
FT PVLQEDYRQDSQTRRISTLKLTHNQDLGSSSPISTPQFSKSVEVPSFLKRPRSLTPNPV
FT PETHTASLSIQIAPLSGQDLESHKQLPELSPETAKIPLQQERQKSAVAAASQSSDCRVS
FT QITVNGNSGGAVSPM (in isoform 10)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_046220"
FT VAR_SEQ 1
FT /note="M -> MNTDSGGCARKRAAMSVTLTSVKRVQSSPNLLAAGRDSQSPDSAWRS
FT YNDGNQETLNGDATYSSLAAKGFRSVRPNLQDKRSPTQSQITVNGNSGGAVSPM (in
FT isoform 11)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047056"
FT VAR_SEQ 1
FT /note="M -> MNTGRDSQSPDSAKGFRSVRPNLQDKRSPTQSQITVNGNSGGAVSPM
FT (in isoform 2, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:9211900"
FT /id="VSP_034792"
FT VAR_SEQ 1
FT /note="M -> MNTGRDSQSPDSAWRSYNDGNQETLNGDATYSSLAAKGFRSVRPNLQ
FT DKRSPTQSQITVNGNSGGAVSPM (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045640"
FT VAR_SEQ 1
FT /note="M -> MSVTLTSVKRVQSSPNLLAAGRDSQSPDSAWRSYNDGNQETLNGDAT
FT YSSLAAKGFRSVRPNLQDKRSPTQSQITVNGNSGGAVSPM (in isoform 9 and
FT isoform 12)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_046219"
FT VAR_SEQ 82..89
FT /note="GIPTAIRT -> MKATTPLQ (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:11786189"
FT /id="VSP_034793"
FT VAR_SEQ 112..126
FT /note="Missing (in isoform 7 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.5"
FT /id="VSP_043666"
FT VAR_SEQ 228
FT /note="P -> PTDRINPDDIDLENEPWYKFFSELEFGRPPPKKPLDYVQDHSSGVFN
FT E (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9211900"
FT /id="VSP_034794"
FT VAR_SEQ 228
FT /note="P -> PPPLPTTPTPVPREPGRKPLSSSRLGEVTGSPSPPPRSGAPTPSSRA
FT PALSPTRPPKKPLDYVQDHSSGVFNE (in isoform 3, isoform 4,
FT isoform 5, isoform 10 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9211900, ECO:0000303|Ref.5"
FT /id="VSP_034795"
FT VAR_SEQ 228
FT /note="P -> PPPKKPLDYVQDHSSGVFNE (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045641"
FT VAR_SEQ 229..237
FT /note="ASLYQSSID -> VSKPQAGRR (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:11786189"
FT /id="VSP_034796"
FT VAR_SEQ 238..1100
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:11786189"
FT /id="VSP_034797"
FT VAR_SEQ 308..834
FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT 5, isoform 8, isoform 9, isoform 10 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9211900,
FT ECO:0000303|Ref.5"
FT /id="VSP_034798"
FT VAR_SEQ 1050..1100
FT /note="YNYTPRNEDELELRESDVIDVMEKCDDGWFVGTSRRTKFFGTFPGNYVKRL
FT -> GYTLT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:9211900"
FT /id="VSP_034799"
FT VARIANT 1048
FT /note="A -> V (in dbSNP:rs725185)"
FT /id="VAR_045624"
FT CONFLICT 73
FT /note="P -> L (in Ref. 5; AK225327)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="R -> Q (in Ref. 5; AK225327)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="L -> S (in Ref. 4; BAG51769)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="L -> P (in Ref. 4; BAG51769)"
FT /evidence="ECO:0000305"
FT CONFLICT 891
FT /note="Y -> N (in Ref. 4; BAG51769)"
FT /evidence="ECO:0000305"
FT CONFLICT 1034
FT /note="F -> L (in Ref. 4; BAH11501)"
FT /evidence="ECO:0000305"
FT STRAND 866..872
FT /evidence="ECO:0007829|PDB:5VEI"
FT STRAND 889..905
FT /evidence="ECO:0007829|PDB:5VEI"
FT STRAND 908..913
FT /evidence="ECO:0007829|PDB:5VEI"
FT HELIX 914..916
FT /evidence="ECO:0007829|PDB:5VEI"
FT STRAND 917..919
FT /evidence="ECO:0007829|PDB:5VEI"
FT MOD_RES O94875-2:316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CONFLICT O94875-2:13
FT /note="A -> P (in Ref. 1; AAC05509)"
FT /evidence="ECO:0000305"
FT MOD_RES O94875-3:234
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-3:236
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-3:258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES O94875-3:260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-3:280
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-3:295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-4:280
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-4:282
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-4:304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES O94875-4:306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-4:326
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-4:341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-5:280
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-5:282
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-5:304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES O94875-5:306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-5:326
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-5:341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CONFLICT O94875-5:13
FT /note="A -> P (in Ref. 1; AAC05508)"
FT /evidence="ECO:0000305"
FT MOD_RES O94875-6:153
FT /note="Alanine amide"
FT /evidence="ECO:0000269|PubMed:11786189"
FT MOD_RES O94875-8:311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-9:13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-9:14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-10:413
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-10:415
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-10:437
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES O94875-10:439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-10:459
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-10:474
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CONFLICT O94875-10:424
FT /note="K -> E (in Ref. 5; AK225812)"
FT /evidence="ECO:0000305"
FT MOD_RES O94875-11:27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-11:28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-12:13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-12:14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-12:320
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-12:322
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-12:344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES O94875-12:346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-12:366
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES O94875-12:381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
SQ SEQUENCE 1100 AA; 124108 MW; 7E98B196D4DB38E6 CRC64;
MSYYQRPFSP SAYSLPASLN SSIVMQHGTS LDSTDTYPQH AQSLDGTTSS SIPLYRSSEE
EKRVTVIKAP HYPGIGPVDE SGIPTAIRTT VDRPKDWYKT MFKQIHMVHK PDDDTDMYNT
PYTYNAGLYN PPYSAQSHPA AKTQTYRPLS KSHSDNSPNA FKDASSPVPP PHVPPPVPPL
RPRDRSSTEK HDWDPPDRKV DTRKFRSEPR SIFEYEPGKS SILQHERPAS LYQSSIDRSL
ERPMSSASMA SDFRKRRKSE PAVGPPRGLG DQSASRTSPG RVDLPGSSTT LTKSFTSSSP
SSPSRAKGGD DSKICPSLCS YSGLNGNPSS ELDYCSTYRQ HLDVPRDSPR AISFKNGWQM
ARQNAEIWSS TEETVSPKIK SRSCDDLLND DCDSFPDPKV KSESMGSLLC EEDSKESCPM
AWGSPYVPEV RSNGRSRIRH RSARNAPGFL KMYKKMHRIN RKDLMNSEVI CSVKSRILQY
ESEQQHKDLL RAWSQCSTEE VPRDMVPTRI SEFEKLIQKS KSMPNLGDDM LSPVTLEPPQ
NGLCPKRRFS IEYLLEEENQ SGPPARGRRG CQSNALVPIH IEVTSDEQPR AHVEFSDSDQ
DGVVSDHSDY IHLEGSSFCS ESDFDHFSFT SSESFYGSSH HHHHHHHHHH RHLISSCKGR
CPASYTRFTT MLKHERARHE NTEEPRRQEM DPGLSKLAFL VSPVPFRRKK NSAPKKQTEK
AKCKASVFEA LDSALKDICD QIKAEKKRGS LPDNSILHRL ISELLPDVPE RNSSLRALRR
SPLHQPLHPL PPDGAIHCPP YQNDCGRMPR SASFQDVDTA NSSCHHQDRG GALQDRESPR
SYSSTLTDMG RSAPRERRGT PEKEKLPAKA VYDFKAQTSK ELSFKKGDTV YILRKIDQNW
YEGEHHGRVG IFPISYVEKL TPPEKAQPAR PPPPAQPGEI GEAIAKYNFN ADTNVELSLR
KGDRVILLKR VDQNWYEGKI PGTNRQGIFP VSYVEVVKKN TKGAEDYPDP PIPHSYSSDR
IHSLSSNKPQ RPVFTHENIQ GGGEPFQALY NYTPRNEDEL ELRESDVIDV MEKCDDGWFV
GTSRRTKFFG TFPGNYVKRL
//
