BIN1_HUMAN
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 03-AUG-2022, entry version 221.
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)";
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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; 92.
DR ComplexPortal; CPX-514; c-MYC-BIN1 complex.
DR CORUM; O00499; -.
DR DIP; DIP-41480N; -.
DR ELM; O00499; -.
DR IntAct; O00499; 78.
DR MINT; O00499; -.
DR STRING; 9606.ENSP00000316779; -.
DR MoonDB; O00499; Predicted.
DR GlyGen; O00499; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; O00499; -.
DR MetOSite; O00499; -.
DR PhosphoSitePlus; O00499; -.
DR BioMuta; BIN1; -.
DR UCD-2DPAGE; O00499; -.
DR EPD; O00499; -.
DR jPOST; O00499; -.
DR MassIVE; O00499; -.
DR MaxQB; O00499; -.
DR PaxDb; O00499; -.
DR PeptideAtlas; O00499; -.
DR PRIDE; 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 Antibodypedia; 1297; 441 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; ENST00000352848.7; 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 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; AEIYKPI; -.
DR OrthoDB; 1366218at2759; -.
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 1083 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 202 other tissues.
DR ExpressionAtlas; O00499; baseline and differential.
DR Genevisible; O00499; HS.
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:0051087; F:chaperone binding; IPI: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: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:0043547; P:positive regulation of GTPase activity; 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; cd12139; SH3_Bin1; 1.
DR Gene3D; 1.20.1270.60; -; 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:SF4; PTHR46514:SF4; 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; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50002; SH3; 1.
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 BIN1-
FT 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 (probable disease-associated variant found
FT in a sporadic case of centronulear myopathy; does not
FT induce membrane tubulation in cultured cells)"
FT /evidence="ECO:0000269|PubMed:25260562"
FT /id="VAR_081080"
FT VARIANT 24
FT /note="R -> C (probable disease-associated variant found in
FT a sporadic case of centronulear myopathy; does not induce
FT membrane 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
