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SRBS2_HUMAN
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   03-AUG-2022, entry version 186.
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; 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; P63104: YWHAZ; NbExp=2; 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="http://atlasgeneticsoncology.org/Genes/SORBS2ID693ch4q35.html";
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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. [O94875-4]
DR   RefSeq; XP_006714453.1; XM_006714390.1. [O94875-8]
DR   RefSeq; XP_016864260.1; XM_017008771.1. [O94875-3]
DR   PDB; 5VEI; X-ray; 1.33 A; A=866-921.
DR   PDBsum; 5VEI; -.
DR   AlphaFoldDB; O94875; -.
DR   SMR; O94875; -.
DR   BioGRID; 114047; 79.
DR   CORUM; O94875; -.
DR   DIP; DIP-31634N; -.
DR   IntAct; O94875; 64.
DR   MINT; O94875; -.
DR   STRING; 9606.ENSP00000347852; -.
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; O94875; -.
DR   PeptideAtlas; O94875; -.
DR   PRIDE; 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   ABCD; O94875; 10 sequenced antibodies.
DR   Antibodypedia; 28990; 114 antibodies from 24 providers.
DR   DNASU; 8470; -.
DR   Ensembl; ENST00000284776.11; ENSP00000284776.7; ENSG00000154556.18. [O94875-1]
DR   Ensembl; ENST00000319471.13; ENSP00000322182.9; ENSG00000154556.18. [O94875-12]
DR   Ensembl; ENST00000355634.9; ENSP00000347852.5; ENSG00000154556.18. [O94875-11]
DR   Ensembl; ENST00000393528.7; ENSP00000377162.3; ENSG00000154556.18. [O94875-2]
DR   Ensembl; ENST00000418609.5; ENSP00000397482.1; ENSG00000154556.18. [O94875-7]
DR   Ensembl; ENST00000437304.6; ENSP00000396008.2; ENSG00000154556.18. [O94875-10]
DR   Ensembl; ENST00000448662.6; ENSP00000409158.2; ENSG00000154556.18. [O94875-8]
DR   Ensembl; ENST00000449407.6; ENSP00000397262.2; ENSG00000154556.18. [O94875-9]
DR   GeneID; 8470; -.
DR   KEGG; hsa:8470; -.
DR   UCSC; uc003iyh.4; human. [O94875-1]
DR   CTD; 8470; -.
DR   DisGeNET; 8470; -.
DR   GeneCards; SORBS2; -.
DR   HGNC; HGNC:24098; SORBS2.
DR   HPA; ENSG00000154556; Tissue enhanced (heart muscle, thyroid gland).
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; HPVPETH; -.
DR   OrthoDB; 228183at2759; -.
DR   PhylomeDB; O94875; -.
DR   TreeFam; TF320680; -.
DR   PathwayCommons; O94875; -.
DR   SignaLink; O94875; -.
DR   SIGNOR; O94875; -.
DR   BioGRID-ORCS; 8470; 13 hits in 1076 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 205 other 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:0007015; P:actin filament organization; IEA:InterPro.
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   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   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
 
 
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