ID BIN1_HUMAN Reviewed; 593 AA. AC O00499; O00297; O00545; O43867; O60552; O60553; O60554; O60555; O75514; AC O75515; O75516; O75517; O75518; Q659B7; Q92944; Q99688; DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 24-JAN-2024, entry version 229. DE RecName: Full=Myc box-dependent-interacting protein 1; DE AltName: Full=Amphiphysin II; DE AltName: Full=Amphiphysin-like protein; DE AltName: Full=Box-dependent myc-interacting protein 1; DE AltName: Full=Bridging integrator 1; GN Name=BIN1; Synonyms=AMPHL; 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] (ISOFORM IIA). RC TISSUE=Brain; RX PubMed=9195986; DOI=10.1074/jbc.272.26.16700; RA Ramjaun A.R., Micheva K.D., Bouchelet I., McPherson P.S.; RT "Identification and characterization of a nerve terminal-enriched RT amphiphysin isoform."; RL J. Biol. Chem. 272:16700-16706(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS IIA AND BIN1), TISSUE SPECIFICITY, AND RP SUBCELLULAR LOCATION. RC TISSUE=Brain, and Skeletal muscle; RX PubMed=9182667; DOI=10.1083/jcb.137.6.1355; RA Butler M.H., David C., Ochoa G.-C., Freyberg Z., Daniell L., Grabs D., RA Cremona O., De Camilli P.; RT "Amphiphysin II (SH3P9; BIN1), a member of the amphiphysin/Rvs family, is RT concentrated in the cortical cytomatrix of axon initial segments and nodes RT of Ranvier in brain and around T tubules in skeletal muscle."; RL J. Cell Biol. 137:1355-1367(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BIN1), FUNCTION, AND SUBCELLULAR RP LOCATION. RC TISSUE=Skeletal muscle; RX PubMed=8782822; DOI=10.1038/ng0996-69; RA Sakamuro D., Elliott K.J., Wechsler-Reya R., Prendergast G.C.; RT "BIN1 is a novel Myc-interacting protein with features of a tumour RT suppressor."; RL Nat. Genet. 14:69-76(1996). RN [4] RP SEQUENCE REVISION TO N-TERMINUS. RA Sakamuro D., Elliott K.J., Wechsler-Reya R., Prendergast G.C.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS IIB; IIC1; IIC2 AND IID), AND RP INTERACTION WITH CLTC. RC TISSUE=Brain; RX PubMed=9603201; DOI=10.1046/j.1471-4159.1998.70062369.x; RA Ramjaun A.R., McPherson P.S.; RT "Multiple amphiphysin II splice variants display differential clathrin RT binding: identification of two distinct clathrin-binding sites."; RL J. Neurochem. 70:2369-2376(1998). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS II2 AND II3). RC TISSUE=Brain; RX PubMed=9223448; DOI=10.1006/bbrc.1997.6927; RA Tsutsui K., Maeda Y., Tsutsui K., Seki S., Tokunaga A.; RT "cDNA cloning of a novel amphiphysin isoform and tissue-specific expression RT of its multiple splice variants."; RL Biochem. Biophys. Res. Commun. 236:178-183(1997). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS II3; II3; BIN1-10-13; RP BIN1-13 AND BIN1+12A). RC TISSUE=Fibroblast; RX PubMed=9395479; DOI=10.1074/jbc.272.50.31453; RA Wechsler-Reya R.J., Sakamuro D., Zhang J., Duhadaway J., Prendergast G.C.; RT "Structural analysis of the human BIN1 gene. Evidence for tissue-specific RT transcriptional regulation and alternate RNA splicing."; RL J. Biol. Chem. 272:31453-31458(1997). RN [8] RP NUCLEOTIDE SEQUENCE (ISOFORM II2). RA Zhang J., Du W., Wechsler-Reya R.J., Duhadaway J., Sakamuro D., RA Prendergast G.C.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IIA). RC TISSUE=Brain; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [10] 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 [11] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 133-593. RC TISSUE=Brain; RA Yu W., Gibbs R.A.; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. RN [13] RP CHARACTERIZATION. RC TISSUE=Skeletal muscle; RX PubMed=9418903; DOI=10.1128/mcb.18.1.566; RA Wechsler-Reya R.J., Elliott K.J., Prendergast G.C.; RT "A role for the putative tumor suppressor Bin1 in muscle cell RT differentiation."; RL Mol. Cell. Biol. 18:566-575(1998). RN [14] RP INTERACTION WITH BIN2, AND TISSUE SPECIFICITY. RX PubMed=10903846; DOI=10.1006/geno.2000.6216; RA Ge K., Prendergast G.C.; RT "Bin2, a functionally nonredundant member of the BAR adaptor gene family."; RL Genomics 67:210-220(2000). RN [15] RP INTERACTION WITH SNX4. RX PubMed=12668730; DOI=10.1242/jcs.00403; RA Leprince C., Le Scolan E., Meunier B., Fraisier V., Brandon N., RA De Gunzburg J., Camonis J.; RT "Sorting nexin 4 and amphiphysin 2, a new partnership between endocytosis RT and intracellular trafficking."; RL J. Cell Sci. 116:1937-1948(2003). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [17] RP INTERACTION WITH HCV NS5A (MICROBIAL INFECTION). RX PubMed=16530520; DOI=10.1053/j.gastro.2005.12.030; RA Nanda S.K., Herion D., Liang T.J.; RT "The SH3 binding motif of HCV NS5A protein interacts with Bin1 and is RT important for apoptosis and infectivity."; RL Gastroenterology 130:794-809(2006). RN [18] RP INTERACTION WITH DNM2, INVOLVEMENT IN CNM2, VARIANTS CNM2 ASN-35; ASN-151 RP AND 575-LYS--PRO-593 DEL, AND CHARACTERIZATION OF VARIANTS CNM2 ASN-151 AND RP 575-LYS--PRO-593 DEL. RX PubMed=17676042; DOI=10.1038/ng2086; RA Nicot A.-S., Toussaint A., Tosch V., Kretz C., Wallgren-Pettersson C., RA Iwarsson E., Kingston H., Garnier J.-M., Biancalana V., Oldfors A., RA Mandel J.-L., Laporte J.; RT "Mutations in amphiphysin 2 (BIN1) disrupt interaction with dynamin 2 and RT cause autosomal recessive centronuclear myopathy."; RL Nat. Genet. 39:1134-1139(2007). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-307, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=T-cell; RX PubMed=19367720; DOI=10.1021/pr800500r; RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; RT "Phosphorylation analysis of primary human T lymphocytes using sequential RT IMAC and titanium oxide enrichment."; RL J. Proteome Res. 7:5167-5176(2008). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-298; SER-303; RP THR-307; THR-323 AND SER-331, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE 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 [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; THR-323 AND SER-331, AND RP 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 [24] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-298 AND SER-303, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296 AND SER-298, AND RP IDENTIFICATION BY MASS 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). RN [27] RP FUNCTION, AND CHARACTERIZATION OF VARIANTS CNM2 ASN-151 AND GLN-154. RX PubMed=24755653; DOI=10.1371/journal.pone.0093060; RA Wu T., Shi Z., Baumgart T.; RT "Mutations in BIN1 associated with centronuclear myopathy disrupt membrane RT remodeling by affecting protein density and oligomerization."; RL PLoS ONE 9:E93060-E93060(2014). RN [28] RP FUNCTION, AND INTERACTION WITH BACE1. RX PubMed=27179792; DOI=10.1093/hmg/ddw146; RA Miyagawa T., Ebinuma I., Morohashi Y., Hori Y., Young Chang M., Hattori H., RA Maehara T., Yokoshima S., Fukuyama T., Tsuji S., Iwatsubo T., RA Prendergast G.C., Tomita T.; RT "BIN1 regulates BACE1 intracellular trafficking and amyloid-beta RT production."; RL Hum. Mol. Genet. 25:2948-2958(2016). RN [29] RP TISSUE SPECIFICITY. RX PubMed=27488240; DOI=10.1186/s13024-016-0124-1; RA De Rossi P., Buggia-Prevot V., Clayton B.L., Vasquez J.B., van Sanford C., RA Andrew R.J., Lesnick R., Botte A., Deyts C., Salem S., Rao E., Rice R.C., RA Parent A., Kar S., Popko B., Pytel P., Estus S., Thinakaran G.; RT "Predominant expression of Alzheimer's disease-associated BIN1 in mature RT oligodendrocytes and localization to white matter tracts."; RL Mol. Neurodegener. 11:59-59(2016). RN [30] RP FUNCTION, AND INTERACTION WITH F-ACTIN. RX PubMed=28893863; DOI=10.15252/embr.201744137; RA Draeger N.M., Nachman E., Winterhoff M., Bruehmann S., Shah P., RA Katsinelos T., Boulant S., Teleman A.A., Faix J., Jahn T.R.; RT "Bin1 directly remodels actin dynamics through its BAR domain."; RL EMBO Rep. 18:2051-2066(2017). RN [31] RP VARIANT CNM2 GLN-154. RX PubMed=20142620; DOI=10.1212/wnl.0b013e3181cef7f9; RA Claeys K.G., Maisonobe T., Boehm J., Laporte J., Hezode M., Romero N.B., RA Brochier G., Bitoun M., Carlier R.Y., Stojkovic T.; RT "Phenotype of a patient with recessive centronuclear myopathy and a novel RT BIN1 mutation."; RL Neurology 74:519-521(2010). RN [32] RP INVOLVEMENT IN AUTOSOMAL DOMINANT CENTRONUCLEAR MYOPATHY, AND VARIANTS RP LYS-21 DEL AND CYS-24. RX PubMed=25260562; DOI=10.1093/brain/awu272; RA Boehm J., Biancalana V., Malfatti E., Dondaine N., Koch C., Vasli N., RA Kress W., Strittmatter M., Taratuto A.L., Gonorazky H., Laforet P., RA Maisonobe T., Olive M., Gonzalez-Mera L., Fardeau M., Carriere N., RA Clavelou P., Eymard B., Bitoun M., Rendu J., Faure J., Weis J., RA Mandel J.L., Romero N.B., Laporte J.; RT "Adult-onset autosomal dominant centronuclear myopathy due to BIN1 RT mutations."; RL Brain 137:3160-3170(2014). RN [33] RP VARIANTS CNM2 CYS-145 AND CYS-234. RX PubMed=29950440; DOI=10.1212/wnl.0000000000005862; RA Cabrera-Serrano M., Mavillard F., Biancalana V., Rivas E., Morar B., RA Hernandez-Lain A., Olive M., Muelas N., Khan E., Carvajal A., Quiroga P., RA Diaz-Manera J., Davis M., Avila R., Dominguez C., Romero N.B., RA Vilchez J.J., Comas D., Laing N.G., Laporte J., Kalaydjieva L., Paradas C.; RT "A Roma founder BIN1 mutation causes a novel phenotype of centronuclear RT myopathy with rigid spine."; RL Neurology 91:E339-E348(2018). CC -!- FUNCTION: Is a key player in the control of plasma membrane curvature, CC membrane shaping and membrane remodeling. Required in muscle cells for CC the formation of T-tubules, tubular invaginations of the plasma CC membrane that function in depolarization-contraction coupling CC (PubMed:24755653). Is a negative regulator of endocytosis (By CC similarity). Is also involved in the regulation of intracellular CC vesicles sorting, modulation of BACE1 trafficking and the control of CC amyloid-beta production (PubMed:27179792). In neuronal circuits, CC endocytosis regulation may influence the internalization of PHF-tau CC aggregates (By similarity). May be involved in the regulation of MYC CC activity and the control cell proliferation (PubMed:8782822). Has actin CC bundling activity and stabilizes actin filaments against CC depolymerization in vitro (PubMed:28893863). CC {ECO:0000250|UniProtKB:O08839, ECO:0000269|PubMed:24755653, CC ECO:0000269|PubMed:27179792, ECO:0000269|PubMed:28893863, CC ECO:0000269|PubMed:8782822}. CC -!- SUBUNIT: Heterodimer with AMPH (By similarity). Binds SH3GLB1 (By CC similarity). Interacts (via SH3 domain) with DNM1. Interacts with SYNJ1 CC (By similarity). Interacts (via SH3 domain) with DNM2 CC (PubMed:17676042). Isoform IIA interacts with CLTC. Isoform IIB does CC not interact with CLTC. Isoform IIC1 does not interact with CLTC. CC Isoform IIC2 does not interact with CLTC (PubMed:9603201). Interacts CC with AP2A2. Interacts with AP2B1 (By similarity). Interacts with MYC CC (via N-terminal transactivation domain); the interaction requires the CC integrity of the conserved MYC box regions 1 and 2 (By similarity). CC Interacts with BIN2 (PubMed:10903846). Interacts with SNX4 CC (PubMed:12668730). Interacts (via BAR domain) with BACE1 CC (PubMed:27179792). Binds (via BAR domain) F-actin (PubMed:28893863). CC {ECO:0000250|UniProtKB:O08539, ECO:0000250|UniProtKB:O08839, CC ECO:0000269|PubMed:10903846, ECO:0000269|PubMed:12668730, CC ECO:0000269|PubMed:17676042, ECO:0000269|PubMed:27179792, CC ECO:0000269|PubMed:28893863, ECO:0000269|PubMed:9603201}. CC -!- SUBUNIT: (Microbial infection) Interacts (SH3 domain) with HCV NS5A. CC {ECO:0000269|PubMed:16530520}. CC -!- INTERACTION: CC O00499; O00499: BIN1; NbExp=3; IntAct=EBI-719094, EBI-719094; CC O00499; Q9UBW5: BIN2; NbExp=2; IntAct=EBI-719094, EBI-2042570; CC O00499; Q9Y2H0: DLGAP4; NbExp=4; IntAct=EBI-719094, EBI-722139; CC O00499; P09467: FBP1; NbExp=4; IntAct=EBI-719094, EBI-712740; CC O00499; Q13496: MTM1; NbExp=6; IntAct=EBI-719094, EBI-2864109; CC O00499; Q8NFH8: REPS2; NbExp=6; IntAct=EBI-719094, EBI-7067016; CC O00499; Q8TB24: RIN3; NbExp=2; IntAct=EBI-719094, EBI-1570523; CC O00499; O95219: SNX4; NbExp=4; IntAct=EBI-719094, EBI-724909; CC O00499; Q13426: XRCC4; NbExp=4; IntAct=EBI-719094, EBI-717592; CC O00499; PRO_0000037576 [P27958]; Xeno; NbExp=11; IntAct=EBI-719094, EBI-8753518; CC O00499; PRO_0000037551 [Q9WMX2]; Xeno; NbExp=5; IntAct=EBI-719094, EBI-6863748; CC O00499-1; P10636-7: MAPT; NbExp=5; IntAct=EBI-6926280, EBI-6926270; CC O00499-1; P10636-8: MAPT; NbExp=6; IntAct=EBI-6926280, EBI-366233; CC O00499-7; PRO_0000037576 [P27958]; Xeno; NbExp=2; IntAct=EBI-8870146, EBI-8753518; CC O00499-10; P01106: MYC; NbExp=3; IntAct=EBI-7689134, EBI-447544; CC O00499-11; P01106: MYC; NbExp=2; IntAct=EBI-7689211, EBI-447544; CC -!- SUBCELLULAR LOCATION: [Isoform BIN1]: Nucleus CC {ECO:0000269|PubMed:8782822}. Cytoplasm {ECO:0000269|PubMed:9182667}. CC Endosome {ECO:0000250|UniProtKB:O08539}. Cell membrane, sarcolemma, T- CC tubule {ECO:0000250|UniProtKB:O08839}. CC -!- SUBCELLULAR LOCATION: [Isoform IIA]: Cytoplasm CC {ECO:0000269|PubMed:9182667}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=11; CC Comment=Additional isoforms seem to exist.; CC Name=IIA; CC IsoId=O00499-1; Sequence=Displayed; CC Name=IIB; CC IsoId=O00499-2; Sequence=VSP_000246, VSP_000252; CC Name=IIC1; CC IsoId=O00499-3; Sequence=VSP_000249; CC Name=IIC2; CC IsoId=O00499-4; Sequence=VSP_000246, VSP_000249; CC Name=IID; CC IsoId=O00499-5; Sequence=VSP_000248; CC Name=II2; CC IsoId=O00499-6; Sequence=VSP_000246, VSP_000253; CC Name=II3; CC IsoId=O00499-7; Sequence=VSP_000246, VSP_000250; CC Name=BIN1; CC IsoId=O00499-8; Sequence=VSP_000246, VSP_000247, VSP_000250; CC Name=BIN1-10-13; CC IsoId=O00499-9; Sequence=VSP_000246, VSP_000251; CC Name=BIN1-13; CC IsoId=O00499-10; Sequence=VSP_000246, VSP_000247, VSP_000251; CC Name=BIN1+12A; CC IsoId=O00499-11; Sequence=VSP_000246, VSP_000247, VSP_000253; CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in the brain and CC muscle (PubMed:9182667). Expressed in oligodendrocytes CC (PubMed:27488240). Isoform IIA is expressed only in the brain, where it CC is detected in the gray matter, but not in the white matter CC (PubMed:27488240). Isoform BIN1 is widely expressed with highest CC expression in skeletal muscle. {ECO:0000269|PubMed:10903846, CC ECO:0000269|PubMed:27488240, ECO:0000269|PubMed:9182667}. CC -!- PTM: Phosphorylated by protein kinase C. {ECO:0000250}. CC -!- DISEASE: Myopathy, centronuclear, 2 (CNM2) [MIM:255200]: A congenital CC muscle disorder characterized by progressive muscular weakness and CC wasting involving mainly limb girdle, trunk, and neck muscles. It may CC also affect distal muscles. Weakness may be present during childhood or CC adolescence or may not become evident until the third decade of life. CC Ptosis is a frequent clinical feature. The most prominent CC histopathologic features include high frequency of centrally located CC nuclei in muscle fibers not secondary to regeneration, radial CC arrangement of sarcoplasmic strands around the central nuclei, and CC predominance and hypotrophy of type 1 fibers. CC {ECO:0000269|PubMed:17676042, ECO:0000269|PubMed:20142620, CC ECO:0000269|PubMed:24755653, ECO:0000269|PubMed:29950440}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Note=BIN1 mutations have been found in families segregating CC autosomal dominant centronuclear myopathy. Patients show adult-onset, CC mildly progressive muscle weakness affecting selected proximal muscles CC and all distal muscles of the lower limbs. CC {ECO:0000269|PubMed:25260562}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC23441.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/794/bin1-(bridging-integrator-1)"; 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; AF004015; AAC51345.1; -; mRNA. DR EMBL; AF070576; AAC28646.1; -; mRNA. DR EMBL; AF001383; AAB61363.1; -; mRNA. DR EMBL; U68485; AAC17461.1; -; mRNA. DR EMBL; AF043898; AAC39710.1; -; mRNA. DR EMBL; AF043899; AAC39711.1; -; mRNA. DR EMBL; AF043900; AAC39712.1; -; mRNA. DR EMBL; AF043901; AAC39713.1; -; mRNA. DR EMBL; U87558; AAB63263.1; -; mRNA. DR EMBL; AF068914; AAC24126.1; -; mRNA. DR EMBL; AF068915; AAC24127.1; -; mRNA. DR EMBL; AF068916; AAC24128.1; -; mRNA. DR EMBL; AF068917; AAC23750.1; -; mRNA. DR EMBL; AF068918; AAC23751.1; -; mRNA. DR EMBL; U84004; AAC23440.1; -; Genomic_DNA. DR EMBL; U83999; AAC23440.1; JOINED; Genomic_DNA. DR EMBL; U84001; AAC23440.1; JOINED; Genomic_DNA. DR EMBL; U84002; AAC23440.1; JOINED; Genomic_DNA. DR EMBL; U84003; AAC23440.1; JOINED; Genomic_DNA. DR EMBL; U84004; AAC23441.1; ALT_INIT; Genomic_DNA. DR EMBL; U83999; AAC23441.1; JOINED; Genomic_DNA. DR EMBL; U84001; AAC23441.1; JOINED; Genomic_DNA. DR EMBL; U84002; AAC23441.1; JOINED; Genomic_DNA. DR EMBL; U84003; AAC23441.1; JOINED; Genomic_DNA. DR EMBL; AL713697; CAD28496.1; -; mRNA. DR EMBL; AC012508; AAY24328.1; -; Genomic_DNA. DR EMBL; CH471103; EAW95302.1; -; Genomic_DNA. DR CCDS; CCDS2137.1; -. [O00499-8] DR CCDS; CCDS2138.1; -. [O00499-1] DR CCDS; CCDS2139.1; -. [O00499-5] DR CCDS; CCDS2140.1; -. [O00499-3] DR CCDS; CCDS2141.1; -. [O00499-11] DR CCDS; CCDS2142.1; -. [O00499-2] DR CCDS; CCDS2143.1; -. [O00499-9] DR CCDS; CCDS42743.1; -. [O00499-4] DR CCDS; CCDS42744.1; -. [O00499-6] DR CCDS; CCDS46403.1; -. [O00499-7] DR CCDS; CCDS82508.1; -. [O00499-10] DR PIR; JC5593; JC5593. DR RefSeq; NP_001307561.1; NM_001320632.1. [O00499-10] DR RefSeq; NP_001307562.1; NM_001320633.1. DR RefSeq; NP_001307569.1; NM_001320640.1. DR RefSeq; NP_001307570.1; NM_001320641.1. DR RefSeq; NP_001307571.1; NM_001320642.1. DR RefSeq; NP_004296.1; NM_004305.3. [O00499-8] DR RefSeq; NP_647593.1; NM_139343.2. [O00499-1] DR RefSeq; NP_647594.1; NM_139344.2. [O00499-5] DR RefSeq; NP_647595.1; NM_139345.2. [O00499-3] DR RefSeq; NP_647596.1; NM_139346.2. [O00499-11] DR RefSeq; NP_647597.1; NM_139347.2. [O00499-2] DR RefSeq; NP_647598.1; NM_139348.2. [O00499-6] DR RefSeq; NP_647599.1; NM_139349.2. [O00499-4] DR RefSeq; NP_647600.1; NM_139350.2. [O00499-7] DR RefSeq; NP_647601.1; NM_139351.2. [O00499-9] DR PDB; 1MUZ; NMR; -; A=513-593. DR PDB; 1MV0; NMR; -; B=513-593. DR PDB; 1MV3; NMR; -; A=301-593. DR PDB; 2FIC; X-ray; 1.99 A; A/B=1-272. DR PDB; 2RMY; NMR; -; A=1-33. DR PDB; 2RND; NMR; -; A=1-33. DR PDB; 5I22; NMR; -; A=513-593. DR PDBsum; 1MUZ; -. DR PDBsum; 1MV0; -. DR PDBsum; 1MV3; -. DR PDBsum; 2FIC; -. DR PDBsum; 2RMY; -. DR PDBsum; 2RND; -. DR PDBsum; 5I22; -. DR AlphaFoldDB; O00499; -. DR BMRB; O00499; -. DR SMR; O00499; -. DR BioGRID; 106771; 105. DR ComplexPortal; CPX-514; c-MYC-BIN1 complex. DR CORUM; O00499; -. DR DIP; DIP-41480N; -. DR ELM; O00499; -. DR IntAct; O00499; 77. DR MINT; O00499; -. DR STRING; 9606.ENSP00000316779; -. DR MoonDB; O00499; Predicted. DR GlyCosmos; O00499; 2 sites, 1 glycan. DR GlyGen; O00499; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; O00499; -. DR MetOSite; O00499; -. DR PhosphoSitePlus; O00499; -. DR BioMuta; BIN1; -. DR EPD; O00499; -. DR jPOST; O00499; -. DR MassIVE; O00499; -. DR MaxQB; O00499; -. DR PaxDb; 9606-ENSP00000316779; -. DR PeptideAtlas; O00499; -. DR ProteomicsDB; 47934; -. [O00499-1] DR ProteomicsDB; 47935; -. [O00499-10] DR ProteomicsDB; 47936; -. [O00499-11] DR ProteomicsDB; 47937; -. [O00499-2] DR ProteomicsDB; 47938; -. [O00499-3] DR ProteomicsDB; 47939; -. [O00499-4] DR ProteomicsDB; 47940; -. [O00499-5] DR ProteomicsDB; 47941; -. [O00499-6] DR ProteomicsDB; 47942; -. [O00499-7] DR ProteomicsDB; 47943; -. [O00499-8] DR ProteomicsDB; 47944; -. [O00499-9] DR Pumba; O00499; -. DR Antibodypedia; 1297; 493 antibodies from 42 providers. DR DNASU; 274; -. DR Ensembl; ENST00000259238.8; ENSP00000259238.4; ENSG00000136717.15. [O00499-11] DR Ensembl; ENST00000316724.10; ENSP00000316779.5; ENSG00000136717.15. [O00499-1] DR Ensembl; ENST00000346226.7; ENSP00000315411.3; ENSG00000136717.15. [O00499-2] DR Ensembl; ENST00000348750.8; ENSP00000259237.5; ENSG00000136717.15. [O00499-9] DR Ensembl; ENST00000351659.7; ENSP00000315388.3; ENSG00000136717.15. [O00499-3] DR Ensembl; ENST00000352848.8; ENSP00000315284.4; ENSG00000136717.15. [O00499-8] DR Ensembl; ENST00000357970.7; ENSP00000350654.3; ENSG00000136717.15. [O00499-5] DR Ensembl; ENST00000376113.6; ENSP00000365281.2; ENSG00000136717.15. [O00499-10] DR Ensembl; ENST00000393040.7; ENSP00000376760.3; ENSG00000136717.15. [O00499-6] DR Ensembl; ENST00000393041.7; ENSP00000376761.3; ENSG00000136717.15. [O00499-4] DR Ensembl; ENST00000409400.1; ENSP00000386797.1; ENSG00000136717.15. [O00499-7] DR GeneID; 274; -. DR KEGG; hsa:274; -. DR MANE-Select; ENST00000316724.10; ENSP00000316779.5; NM_139343.3; NP_647593.1. DR UCSC; uc002tns.3; human. [O00499-1] DR AGR; HGNC:1052; -. DR CTD; 274; -. DR DisGeNET; 274; -. DR GeneCards; BIN1; -. DR HGNC; HGNC:1052; BIN1. DR HPA; ENSG00000136717; Group enriched (skeletal muscle, tongue). DR MalaCards; BIN1; -. DR MIM; 255200; phenotype. DR MIM; 601248; gene. DR neXtProt; NX_O00499; -. DR NIAGADS; ENSG00000136717; -. DR OpenTargets; ENSG00000136717; -. DR Orphanet; 169189; Autosomal dominant centronuclear myopathy. DR Orphanet; 169186; Autosomal recessive centronuclear myopathy. DR PharmGKB; PA25355; -. DR VEuPathDB; HostDB:ENSG00000136717; -. DR eggNOG; KOG3771; Eukaryota. DR GeneTree; ENSGT00950000182882; -. DR HOGENOM; CLU_017859_3_0_1; -. DR InParanoid; O00499; -. DR OMA; QEYDYYN; -. DR OrthoDB; 4243832at2759; -. DR PhylomeDB; O00499; -. DR TreeFam; TF313542; -. DR PathwayCommons; O00499; -. DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis. DR SignaLink; O00499; -. DR SIGNOR; O00499; -. DR BioGRID-ORCS; 274; 13 hits in 1161 CRISPR screens. DR ChiTaRS; BIN1; human. DR EvolutionaryTrace; O00499; -. DR GeneWiki; BIN1; -. DR GenomeRNAi; 274; -. DR Pharos; O00499; Tbio. DR PRO; PR:O00499; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; O00499; Protein. DR Bgee; ENSG00000136717; Expressed in gastrocnemius and 203 other cell types or tissues. DR ExpressionAtlas; O00499; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc. DR GO; GO:0030424; C:axon; IDA:Alzheimers_University_of_Toronto. DR GO; GO:0043194; C:axon initial segment; ISS:Alzheimers_University_of_Toronto. DR GO; GO:0043679; C:axon terminus; IEA:Ensembl. DR GO; GO:0044300; C:cerebellar mossy fiber; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0030425; C:dendrite; ISS:ARUK-UCL. DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell. DR GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; IEA:Ensembl. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0031674; C:I band; ISS:Alzheimers_University_of_Toronto. DR GO; GO:0060987; C:lipid tube; IMP:Alzheimers_University_of_Toronto. DR GO; GO:0016020; C:membrane; IDA:AgBase. DR GO; GO:0033268; C:node of Ranvier; ISS:Alzheimers_University_of_Toronto. DR GO; GO:0005635; C:nuclear envelope; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IDA:ARUK-UCL. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IPI:ComplexPortal. DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central. DR GO; GO:0030315; C:T-tubule; ISS:Alzheimers_University_of_Toronto. DR GO; GO:0043196; C:varicosity; IEA:Ensembl. DR GO; GO:0031982; C:vesicle; ISS:ARUK-UCL. DR GO; GO:0030018; C:Z disc; ISS:Alzheimers_University_of_Toronto. DR GO; GO:0051015; F:actin filament binding; IDA:WormBase. DR GO; GO:0019828; F:aspartic-type endopeptidase inhibitor activity; IMP:ARUK-UCL. DR GO; GO:0030276; F:clathrin binding; TAS:ARUK-UCL. DR GO; GO:0051020; F:GTPase binding; IEA:Ensembl. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central. DR GO; GO:0002020; F:protease binding; IPI:ARUK-UCL. DR GO; GO:0051087; F:protein-folding chaperone binding; IPI:ARUK-UCL. DR GO; GO:0070063; F:RNA polymerase binding; IPI:AgBase. DR GO; GO:0048156; F:tau protein binding; IPI:ARUK-UCL. DR GO; GO:0007010; P:cytoskeleton organization; TAS:ARUK-UCL. DR GO; GO:0006897; P:endocytosis; TAS:ARUK-UCL. DR GO; GO:0008333; P:endosome to lysosome transport; IMP:ARUK-UCL. DR GO; GO:0060988; P:lipid tube assembly; IMP:Alzheimers_University_of_Toronto. DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; IMP:ARUK-UCL. DR GO; GO:1902960; P:negative regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process; IMP:ARUK-UCL. DR GO; GO:1904878; P:negative regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; ISS:ARUK-UCL. DR GO; GO:1901380; P:negative regulation of potassium ion transmembrane transport; ISS:ARUK-UCL. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:1903946; P:negative regulation of ventricular cardiac muscle cell action potential; ISS:ARUK-UCL. DR GO; GO:0051647; P:nucleus localization; IEA:Ensembl. DR GO; GO:0006997; P:nucleus organization; IMP:WormBase. DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISS:ARUK-UCL. DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:AgBase. DR GO; GO:0048711; P:positive regulation of astrocyte differentiation; IMP:Alzheimers_University_of_Toronto. DR GO; GO:0045807; P:positive regulation of endocytosis; IEA:Ensembl. DR GO; GO:0010564; P:regulation of cell cycle process; IDA:ComplexPortal. DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISS:ARUK-UCL. DR GO; GO:0045664; P:regulation of neuron differentiation; IMP:Alzheimers_University_of_Toronto. DR GO; GO:0048488; P:synaptic vesicle endocytosis; IEA:Ensembl. DR GO; GO:0033292; P:T-tubule organization; IDA:UniProtKB. DR CDD; cd07611; BAR_Amphiphysin_I_II; 1. DR CDD; cd12139; SH3_Bin1; 1. DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR027267; AH/BAR_dom_sf. DR InterPro; IPR003005; Amphiphysin. DR InterPro; IPR035471; Amphiphysin-2_SH3. DR InterPro; IPR003023; Amphiphysin_2. DR InterPro; IPR004148; BAR_dom. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR46514; AMPHIPHYSIN; 1. DR PANTHER; PTHR46514:SF4; MYC BOX-DEPENDENT-INTERACTING PROTEIN 1; 1. DR Pfam; PF03114; BAR; 1. DR Pfam; PF14604; SH3_9; 1. DR PRINTS; PR01251; AMPHIPHYSIN. DR PRINTS; PR01253; AMPHIPHYSIN2. DR PRINTS; PR00452; SH3DOMAIN. DR SMART; SM00721; BAR; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF103657; BAR/IMD domain-like; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS51021; BAR; 1. DR PROSITE; PS50002; SH3; 1. DR UCD-2DPAGE; O00499; -. DR Genevisible; O00499; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cell membrane; KW Coiled coil; Cytoplasm; Developmental protein; Differentiation; KW Disease variant; Endocytosis; Endosome; Host-virus interaction; Membrane; KW Nucleus; Phosphoprotein; Reference proteome; SH3 domain. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..593 FT /note="Myc box-dependent-interacting protein 1" FT /id="PRO_0000192951" FT DOMAIN 29..276 FT /note="BAR" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361" FT DOMAIN 520..593 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT REGION 2..122 FT /note="Interaction with BIN2" FT /evidence="ECO:0000269|PubMed:10903846" FT REGION 280..354 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 378..421 FT /note="Clathrin-binding" FT REGION 400..488 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 15..42 FT /evidence="ECO:0000255" FT COILED 193..267 FT /evidence="ECO:0000255" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 296 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 298 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 303 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163" FT MOD_RES 307 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19367720" FT MOD_RES 323 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 331 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT VAR_SEQ 174..204 FT /note="Missing (in isoform IIB, isoform IIC2, isoform II2, FT isoform II3, isoform BIN1, isoform BIN1+12A, isoform FT BIN1-10-13 and isoform BIN1-13)" FT /evidence="ECO:0000303|PubMed:8782822, FT ECO:0000303|PubMed:9182667, ECO:0000303|PubMed:9223448, FT ECO:0000303|PubMed:9395479, ECO:0000303|PubMed:9603201" FT /id="VSP_000246" FT VAR_SEQ 285 FT /note="P -> PRKKSKLFSRLRRKKN (in isoform BIN1, isoform FT BIN1+12A and isoform BIN1-13)" FT /evidence="ECO:0000303|PubMed:8782822, FT ECO:0000303|PubMed:9182667, ECO:0000303|PubMed:9395479" FT /id="VSP_000247" FT VAR_SEQ 335..487 FT /note="Missing (in isoform BIN1-10-13 and isoform BIN1-13)" FT /evidence="ECO:0000303|PubMed:9395479" FT /id="VSP_000251" FT VAR_SEQ 335..457 FT /note="Missing (in isoform II3 and isoform BIN1)" FT /evidence="ECO:0000303|PubMed:8782822, FT ECO:0000303|PubMed:9182667, ECO:0000303|PubMed:9223448, FT ECO:0000303|PubMed:9395479" FT /id="VSP_000250" FT VAR_SEQ 335..421 FT /note="Missing (in isoform IIC1 and isoform IIC2)" FT /evidence="ECO:0000303|PubMed:9603201" FT /id="VSP_000249" FT VAR_SEQ 335..377 FT /note="Missing (in isoform IID)" FT /evidence="ECO:0000303|PubMed:9603201" FT /id="VSP_000248" FT VAR_SEQ 378..457 FT /note="Missing (in isoform II2 and isoform BIN1+12A)" FT /evidence="ECO:0000303|PubMed:9223448, FT ECO:0000303|PubMed:9395479" FT /id="VSP_000253" FT VAR_SEQ 378..421 FT /note="Missing (in isoform IIB)" FT /evidence="ECO:0000303|PubMed:9603201" FT /id="VSP_000252" FT VARIANT 21 FT /note="Missing (found in a sporadic case of centronulear FT myopathy; uncertain significance; does not induce membrane FT tubulation in cultured cells)" FT /evidence="ECO:0000269|PubMed:25260562" FT /id="VAR_081080" FT VARIANT 24 FT /note="R -> C (found in a sporadic case of centronulear FT myopathy; uncertain significance; does not induce membrane FT tubulation in cultured cells)" FT /evidence="ECO:0000269|PubMed:25260562" FT /id="VAR_081081" FT VARIANT 35 FT /note="K -> N (in CNM2; dbSNP:rs121909273)" FT /evidence="ECO:0000269|PubMed:17676042, FT ECO:0000269|PubMed:24755653" FT /id="VAR_037425" FT VARIANT 145 FT /note="R -> C (in CNM2; dbSNP:rs1249621033)" FT /evidence="ECO:0000269|PubMed:29950440" FT /id="VAR_081082" FT VARIANT 151 FT /note="D -> N (in CNM2; results in severely decreased FT membrane tubulation; dbSNP:rs121909274)" FT /evidence="ECO:0000269|PubMed:17676042, FT ECO:0000269|PubMed:24755653" FT /id="VAR_037426" FT VARIANT 154 FT /note="R -> Q (in CNM2; results in severely decreased FT membrane tubulation; dbSNP:rs267606681)" FT /evidence="ECO:0000269|PubMed:20142620, FT ECO:0000269|PubMed:24755653" FT /id="VAR_081083" FT VARIANT 234 FT /note="R -> C (in CNM2; dbSNP:rs777176261)" FT /evidence="ECO:0000269|PubMed:29950440" FT /id="VAR_081084" FT VARIANT 575..593 FT /note="Missing (in CNM2; decreased interaction with DNM2)" FT /evidence="ECO:0000269|PubMed:17676042" FT /id="VAR_081085" FT CONFLICT 474 FT /note="A -> P (in Ref. 2; AAB63263)" FT /evidence="ECO:0000305" FT CONFLICT 481 FT /note="A -> S (in Ref. 10; AAC24126/AAC23750/AAC23751)" FT /evidence="ECO:0000305" FT CONFLICT 510 FT /note="S -> C (in Ref. 7; AAC23440/AAC23441)" FT /evidence="ECO:0000305" FT CONFLICT 528 FT /note="Q -> H (in Ref. 7; AAC23440/AAC23441)" FT /evidence="ECO:0000305" FT CONFLICT 576 FT /note="E -> K (in Ref. 7; AAC23440/AAC23441)" FT /evidence="ECO:0000305" FT HELIX 8..33 FT /evidence="ECO:0007829|PDB:2RMY" FT HELIX 43..89 FT /evidence="ECO:0007829|PDB:2FIC" FT HELIX 97..121 FT /evidence="ECO:0007829|PDB:2FIC" FT HELIX 123..131 FT /evidence="ECO:0007829|PDB:2FIC" FT HELIX 133..161 FT /evidence="ECO:0007829|PDB:2FIC" FT STRAND 163..165 FT /evidence="ECO:0007829|PDB:2FIC" FT HELIX 205..268 FT /evidence="ECO:0007829|PDB:2FIC" FT STRAND 523..527 FT /evidence="ECO:0007829|PDB:1MUZ" FT STRAND 535..537 FT /evidence="ECO:0007829|PDB:1MUZ" FT STRAND 546..549 FT /evidence="ECO:0007829|PDB:1MUZ" FT HELIX 555..557 FT /evidence="ECO:0007829|PDB:1MUZ" FT STRAND 562..567 FT /evidence="ECO:0007829|PDB:1MUZ" FT HELIX 568..572 FT /evidence="ECO:0007829|PDB:1MUZ" FT HELIX 573..579 FT /evidence="ECO:0007829|PDB:1MUZ" FT STRAND 582..585 FT /evidence="ECO:0007829|PDB:1MUZ" FT HELIX 586..588 FT /evidence="ECO:0007829|PDB:1MUZ" FT STRAND 589..591 FT /evidence="ECO:0007829|PDB:1MUZ" SQ SEQUENCE 593 AA; 64699 MW; 0FF1956F0C7E3B50 CRC64; MAEMGSKGVT AGKIASNVQK KLTRAQEKVL QKLGKADETK DEQFEQCVQN FNKQLTEGTR LQKDLRTYLA SVKAMHEASK KLNECLQEVY EPDWPGRDEA NKIAENNDLL WMDYHQKLVD QALLTMDTYL GQFPDIKSRI AKRGRKLVDY DSARHHYESL QTAKKKDEAK IAKPVSLLEK AAPQWCQGKL QAHLVAQTNL LRNQAEEELI KAQKVFEEMN VDLQEELPSL WNSRVGFYVN TFQSIAGLEE NFHKEMSKLN QNLNDVLVGL EKQHGSNTFT VKAQPSDNAP AKGNKSPSPP DGSPAATPEI RVNHEPEPAG GATPGATLPK SPSQLRKGPP VPPPPKHTPS KEVKQEQILS LFEDTFVPEI SVTTPSQFEA PGPFSEQASL LDLDFDPLPP VTSPVKAPTP SGQSIPWDLW EPTESPAGSL PSGEPSAAEG TFAVSWPSQT AEPGPAQPAE ASEVAGGTQP AAGAQEPGET AASEAASSSL PAVVVETFPA TVNGTVEGGS GAGRLDLPPG FMFKVQAQHD YTATDTDELQ LKAGDVVLVI PFQNPEEQDE GWLMGVKESD WNQHKELEKC RGVFPENFTE RVP //