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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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. DR Genevisible; O94875; HS. 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 //