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Myc box-dependent-interacting protein 1 (Amphiphysin II) (Amphiphysin-like protein) (Box-dependent myc-interacting protein 1) (Bridging integrator 1)

 BIN1_HUMAN              Reviewed;         593 AA.
O00499; O00297; O00545; O43867; O60552; O60553; O60554; O60555;
O75514; O75515; O75516; O75517; O75518; Q659B7; Q92944; Q99688;
11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
25-OCT-2017, entry version 187.
RecName: Full=Myc box-dependent-interacting protein 1;
AltName: Full=Amphiphysin II;
AltName: Full=Amphiphysin-like protein;
AltName: Full=Box-dependent myc-interacting protein 1;
AltName: Full=Bridging integrator 1;
Name=BIN1; Synonyms=AMPHL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IIA).
TISSUE=Brain;
PubMed=9195986; DOI=10.1074/jbc.272.26.16700;
Ramjaun A.R., Micheva K.D., Bouchelet I., McPherson P.S.;
"Identification and characterization of a nerve terminal-enriched
amphiphysin isoform.";
J. Biol. Chem. 272:16700-16706(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS IIA AND BIN1).
TISSUE=Brain, and Skeletal muscle;
PubMed=9182667; DOI=10.1083/jcb.137.6.1355;
Butler M.H., David C., Ochoa G.-C., Freyberg Z., Daniell L., Grabs D.,
Cremona O., De Camilli P.;
"Amphiphysin II (SH3P9; BIN1), a member of the amphiphysin/Rvs family,
is concentrated in the cortical cytomatrix of axon initial segments
and nodes of Ranvier in brain and around T tubules in skeletal
muscle.";
J. Cell Biol. 137:1355-1367(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BIN1).
TISSUE=Skeletal muscle;
PubMed=8782822; DOI=10.1038/ng0996-69;
Sakamuro D., Elliott K.J., Wechsler-Reya R., Prendergast G.C.;
"BIN1 is a novel Myc-interacting protein with features of a tumour
suppressor.";
Nat. Genet. 14:69-76(1996).
[4]
SEQUENCE REVISION TO N-TERMINUS.
Sakamuro D., Elliott K.J., Wechsler-Reya R., Prendergast G.C.;
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS IIB; IIC1; IIC2 AND IID), AND
INTERACTION WITH CLTC.
TISSUE=Brain;
PubMed=9603201;
Ramjaun A.R., McPherson P.S.;
"Multiple amphiphysin II splice variants display differential clathrin
binding: identification of two distinct clathrin-binding sites.";
J. Neurochem. 70:2369-2376(1998).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS II2 AND II3).
TISSUE=Brain;
PubMed=9223448; DOI=10.1006/bbrc.1997.6927;
Tsutsui K., Maeda Y., Tsutsui K., Seki S., Tokunaga A.;
"cDNA cloning of a novel amphiphysin isoform and tissue-specific
expression of its multiple splice variants.";
Biochem. Biophys. Res. Commun. 236:178-183(1997).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS II3; II3;
BIN1-10-13; BIN1-13 AND BIN1+12A).
TISSUE=Fibroblast;
PubMed=9395479; DOI=10.1074/jbc.272.50.31453;
Wechsler-Reya R.J., Sakamuro D., Zhang J., Duhadaway J.,
Prendergast G.C.;
"Structural analysis of the human BIN1 gene. Evidence for tissue-
specific transcriptional regulation and alternate RNA splicing.";
J. Biol. Chem. 272:31453-31458(1997).
[8]
NUCLEOTIDE SEQUENCE (ISOFORM II2).
Zhang J., Du W., Wechsler-Reya R.J., Duhadaway J., Sakamuro D.,
Prendergast G.C.;
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IIA).
TISSUE=Brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 133-593.
TISSUE=Brain;
Yu W., Gibbs R.A.;
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[13]
CHARACTERIZATION.
TISSUE=Skeletal muscle;
PubMed=9418903; DOI=10.1128/MCB.18.1.566;
Wechsler-Reya R.J., Elliott K.J., Prendergast G.C.;
"A role for the putative tumor suppressor Bin1 in muscle cell
differentiation.";
Mol. Cell. Biol. 18:566-575(1998).
[14]
INTERACTION WITH BIN2, AND TISSUE SPECIFICITY.
PubMed=10903846; DOI=10.1006/geno.2000.6216;
Ge K., Prendergast G.C.;
"Bin2, a functionally nonredundant member of the BAR adaptor gene
family.";
Genomics 67:210-220(2000).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[16]
INTERACTION WITH HCV NS5A.
PubMed=16530520; DOI=10.1053/j.gastro.2005.12.030;
Nanda S.K., Herion D., Liang T.J.;
"The SH3 binding motif of HCV NS5A protein interacts with Bin1 and is
important for apoptosis and infectivity.";
Gastroenterology 130:794-809(2006).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-307, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-298; SER-303;
THR-307; THR-323 AND SER-331, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; THR-323 AND
SER-331, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-298 AND
SER-303, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296 AND SER-298, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[25]
VARIANTS CNM2 ASN-35 AND ASN-151, AND CHARACTERIZATION OF VARIANTS
CNM2 ASN-35 AND ASN-151.
PubMed=17676042; DOI=10.1038/ng2086;
Nicot A.-S., Toussaint A., Tosch V., Kretz C., Wallgren-Pettersson C.,
Iwarsson E., Kingston H., Garnier J.-M., Biancalana V., Oldfors A.,
Mandel J.-L., Laporte J.;
"Mutations in amphiphysin 2 (BIN1) disrupt interaction with dynamin 2
and cause autosomal recessive centronuclear myopathy.";
Nat. Genet. 39:1134-1139(2007).
-!- FUNCTION: May be involved in regulation of synaptic vesicle
endocytosis. May act as a tumor suppressor and inhibits malignant
cell transformation.
-!- SUBUNIT: Heterodimer with AMPH. Binds SH3GLB1 (By similarity).
Interacts (via SH3 domain) with SYNJ1. Interacts (via SH3 domain)
with DNM1. Isoform IIA interacts with CLTC. Isoform IIB does not
interact with CLTC. Isoform IIC1 does not interact with CLTC.
Isoform IIC2 does not interact with CLTC. Interacts with AP2A2.
Interacts with AP2B1. Interacts with MYC (via N-terminal
transactivation domain); the interaction requires the integrity of
the conserved MYC box regions 1 and 2. Interacts with BIN2.
Interacts (SH3 domain) with HCV NS5A. {ECO:0000250,
ECO:0000269|PubMed:10903846, ECO:0000269|PubMed:16530520,
ECO:0000269|PubMed:9603201}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-719094, EBI-719094;
P27958:- (xeno); NbExp=2; IntAct=EBI-8870146, EBI-8753518;
Q9WMX2:- (xeno); NbExp=5; IntAct=EBI-719094, EBI-6863748;
Q9UBW5:BIN2; NbExp=2; IntAct=EBI-719094, EBI-2042570;
Q9Y2H0:DLGAP4; NbExp=4; IntAct=EBI-719094, EBI-722139;
P09467:FBP1; NbExp=4; IntAct=EBI-719094, EBI-712740;
P10636-7:MAPT; NbExp=5; IntAct=EBI-6926280, EBI-6926270;
Q13496:MTM1; NbExp=6; IntAct=EBI-719094, EBI-2864109;
P01106:MYC; NbExp=3; IntAct=EBI-7689134, EBI-447544;
Q8NFH8-2:REPS2; NbExp=6; IntAct=EBI-719094, EBI-8029141;
O95219:SNX4; NbExp=3; IntAct=EBI-719094, EBI-724909;
Q13426:XRCC4; NbExp=4; IntAct=EBI-719094, EBI-717592;
-!- SUBCELLULAR LOCATION: Isoform BIN1: Nucleus.
-!- SUBCELLULAR LOCATION: Isoform IIA: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=11;
Comment=Additional isoforms seem to exist.;
Name=IIA;
IsoId=O00499-1; Sequence=Displayed;
Name=IIB;
IsoId=O00499-2; Sequence=VSP_000246, VSP_000252;
Name=IIC1;
IsoId=O00499-3; Sequence=VSP_000249;
Name=IIC2;
IsoId=O00499-4; Sequence=VSP_000246, VSP_000249;
Name=IID;
IsoId=O00499-5; Sequence=VSP_000248;
Name=II2;
IsoId=O00499-6; Sequence=VSP_000246, VSP_000253;
Name=II3;
IsoId=O00499-7; Sequence=VSP_000246, VSP_000250;
Name=BIN1;
IsoId=O00499-8; Sequence=VSP_000246, VSP_000247, VSP_000250;
Name=BIN1-10-13;
IsoId=O00499-9; Sequence=VSP_000246, VSP_000251;
Name=BIN1-13;
IsoId=O00499-10; Sequence=VSP_000246, VSP_000247, VSP_000251;
Name=BIN1+12A;
IsoId=O00499-11; Sequence=VSP_000246, VSP_000247, VSP_000253;
-!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in the brain
and muscle. Isoform IIA is expressed only in the brain where it is
concentrated in axon initial segments and nodes of Ranvier.
Isoform BIN1 is widely expressed with highest expression in
skeletal muscle. {ECO:0000269|PubMed:10903846}.
-!- PTM: Phosphorylated by protein kinase C. {ECO:0000250}.
-!- DISEASE: Myopathy, centronuclear, 2 (CNM2) [MIM:255200]: A
congenital muscle disorder characterized by progressive muscular
weakness and wasting involving mainly limb girdle, trunk, and neck
muscles. It may also affect distal muscles. Weakness may be
present during childhood or adolescence or may not become evident
until the third decade of life. Ptosis is a frequent clinical
feature. The most prominent histopathologic features include high
frequency of centrally located nuclei in muscle fibers not
secondary to regeneration, radial arrangement of sarcoplasmic
strands around the central nuclei, and predominance and hypotrophy
of type 1 fibers. {ECO:0000269|PubMed:17676042}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- SEQUENCE CAUTION:
Sequence=AAC23441.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BIN1ID794ch2q14.html";
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EMBL; AF004015; AAC51345.1; -; mRNA.
EMBL; AF070576; AAC28646.1; -; mRNA.
EMBL; AF001383; AAB61363.1; -; mRNA.
EMBL; U68485; AAC17461.1; -; mRNA.
EMBL; AF043898; AAC39710.1; -; mRNA.
EMBL; AF043899; AAC39711.1; -; mRNA.
EMBL; AF043900; AAC39712.1; -; mRNA.
EMBL; AF043901; AAC39713.1; -; mRNA.
EMBL; U87558; AAB63263.1; -; mRNA.
EMBL; AF068914; AAC24126.1; -; mRNA.
EMBL; AF068915; AAC24127.1; -; mRNA.
EMBL; AF068916; AAC24128.1; -; mRNA.
EMBL; AF068917; AAC23750.1; -; mRNA.
EMBL; AF068918; AAC23751.1; -; mRNA.
EMBL; U84004; AAC23440.1; -; Genomic_DNA.
EMBL; U83999; AAC23440.1; JOINED; Genomic_DNA.
EMBL; U84001; AAC23440.1; JOINED; Genomic_DNA.
EMBL; U84002; AAC23440.1; JOINED; Genomic_DNA.
EMBL; U84003; AAC23440.1; JOINED; Genomic_DNA.
EMBL; U84004; AAC23441.1; ALT_INIT; Genomic_DNA.
EMBL; U83999; AAC23441.1; JOINED; Genomic_DNA.
EMBL; U84001; AAC23441.1; JOINED; Genomic_DNA.
EMBL; U84002; AAC23441.1; JOINED; Genomic_DNA.
EMBL; U84003; AAC23441.1; JOINED; Genomic_DNA.
EMBL; AL713697; CAD28496.1; -; mRNA.
EMBL; AC012508; AAY24328.1; -; Genomic_DNA.
EMBL; CH471103; EAW95302.1; -; Genomic_DNA.
CCDS; CCDS2137.1; -. [O00499-8]
CCDS; CCDS2138.1; -. [O00499-1]
CCDS; CCDS2139.1; -. [O00499-5]
CCDS; CCDS2140.1; -. [O00499-3]
CCDS; CCDS2141.1; -. [O00499-11]
CCDS; CCDS2142.1; -. [O00499-2]
CCDS; CCDS2143.1; -. [O00499-9]
CCDS; CCDS42743.1; -. [O00499-4]
CCDS; CCDS42744.1; -. [O00499-6]
CCDS; CCDS46403.1; -. [O00499-7]
CCDS; CCDS82508.1; -. [O00499-10]
PIR; JC5593; JC5593.
RefSeq; NP_001307561.1; NM_001320632.1. [O00499-10]
RefSeq; NP_001307562.1; NM_001320633.1.
RefSeq; NP_001307569.1; NM_001320640.1.
RefSeq; NP_001307570.1; NM_001320641.1.
RefSeq; NP_001307571.1; NM_001320642.1.
RefSeq; NP_004296.1; NM_004305.3. [O00499-8]
RefSeq; NP_647593.1; NM_139343.2. [O00499-1]
RefSeq; NP_647594.1; NM_139344.2. [O00499-5]
RefSeq; NP_647595.1; NM_139345.2. [O00499-3]
RefSeq; NP_647596.1; NM_139346.2. [O00499-11]
RefSeq; NP_647597.1; NM_139347.2. [O00499-2]
RefSeq; NP_647598.1; NM_139348.2. [O00499-6]
RefSeq; NP_647599.1; NM_139349.2. [O00499-4]
RefSeq; NP_647600.1; NM_139350.2. [O00499-7]
RefSeq; NP_647601.1; NM_139351.2. [O00499-9]
UniGene; Hs.193163; -.
PDB; 1MUZ; NMR; -; A=513-593.
PDB; 1MV0; NMR; -; B=513-593.
PDB; 1MV3; NMR; -; A=301-593.
PDB; 2FIC; X-ray; 1.99 A; A/B=1-272.
PDB; 2RMY; NMR; -; A=1-33.
PDB; 2RND; NMR; -; A=1-33.
PDB; 5I22; NMR; -; A=513-593.
PDBsum; 1MUZ; -.
PDBsum; 1MV0; -.
PDBsum; 1MV3; -.
PDBsum; 2FIC; -.
PDBsum; 2RMY; -.
PDBsum; 2RND; -.
PDBsum; 5I22; -.
ProteinModelPortal; O00499; -.
SMR; O00499; -.
BioGrid; 106771; 63.
DIP; DIP-41480N; -.
ELM; O00499; -.
IntAct; O00499; 24.
MINT; MINT-258326; -.
STRING; 9606.ENSP00000316779; -.
iPTMnet; O00499; -.
PhosphoSitePlus; O00499; -.
BioMuta; BIN1; -.
UCD-2DPAGE; O00499; -.
EPD; O00499; -.
MaxQB; O00499; -.
PaxDb; O00499; -.
PeptideAtlas; O00499; -.
PRIDE; O00499; -.
DNASU; 274; -.
Ensembl; ENST00000259238; ENSP00000259238; ENSG00000136717. [O00499-11]
Ensembl; ENST00000316724; ENSP00000316779; ENSG00000136717. [O00499-1]
Ensembl; ENST00000346226; ENSP00000315411; ENSG00000136717. [O00499-2]
Ensembl; ENST00000348750; ENSP00000259237; ENSG00000136717. [O00499-9]
Ensembl; ENST00000351659; ENSP00000315388; ENSG00000136717. [O00499-3]
Ensembl; ENST00000352848; ENSP00000315284; ENSG00000136717. [O00499-8]
Ensembl; ENST00000357970; ENSP00000350654; ENSG00000136717. [O00499-5]
Ensembl; ENST00000376113; ENSP00000365281; ENSG00000136717. [O00499-10]
Ensembl; ENST00000393040; ENSP00000376760; ENSG00000136717. [O00499-6]
Ensembl; ENST00000393041; ENSP00000376761; ENSG00000136717. [O00499-4]
Ensembl; ENST00000409400; ENSP00000386797; ENSG00000136717. [O00499-7]
GeneID; 274; -.
KEGG; hsa:274; -.
UCSC; uc002tns.3; human. [O00499-1]
CTD; 274; -.
DisGeNET; 274; -.
EuPathDB; HostDB:ENSG00000136717.14; -.
GeneCards; BIN1; -.
HGNC; HGNC:1052; BIN1.
HPA; CAB001945; -.
HPA; HPA003894; -.
HPA; HPA005437; -.
MalaCards; BIN1; -.
MIM; 255200; phenotype.
MIM; 601248; gene.
neXtProt; NX_O00499; -.
OpenTargets; ENSG00000136717; -.
Orphanet; 169189; Autosomal dominant centronuclear myopathy.
Orphanet; 169186; Autosomal recessive centronuclear myopathy.
PharmGKB; PA25355; -.
eggNOG; ENOG410ITR4; Eukaryota.
eggNOG; ENOG410XQXT; LUCA.
GeneTree; ENSGT00390000017588; -.
HOVERGEN; HBG004224; -.
InParanoid; O00499; -.
KO; K12562; -.
OMA; NKNPFED; -.
OrthoDB; EOG091G07IE; -.
PhylomeDB; O00499; -.
TreeFam; TF313542; -.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
SIGNOR; O00499; -.
ChiTaRS; BIN1; human.
EvolutionaryTrace; O00499; -.
GeneWiki; BIN1; -.
GenomeRNAi; 274; -.
PRO; PR:O00499; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000136717; -.
ExpressionAtlas; O00499; baseline and differential.
Genevisible; O00499; HS.
GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
GO; GO:0030424; C:axon; IDA:Alzheimers_University_of_Toronto.
GO; GO:0043194; C:axon initial segment; ISS:Alzheimers_University_of_Toronto.
GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0031674; C:I band; ISS:Alzheimers_University_of_Toronto.
GO; GO:0060987; C:lipid tube; IMP:Alzheimers_University_of_Toronto.
GO; GO:0016020; C:membrane; IDA:AgBase.
GO; GO:0033268; C:node of Ranvier; ISS:Alzheimers_University_of_Toronto.
GO; GO:0005635; C:nuclear envelope; IEA:Ensembl.
GO; GO:0030315; C:T-tubule; ISS:Alzheimers_University_of_Toronto.
GO; GO:0030018; C:Z disc; ISS:Alzheimers_University_of_Toronto.
GO; GO:0051015; F:actin filament binding; IDA:WormBase.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0070063; F:RNA polymerase binding; IPI:AgBase.
GO; GO:0048156; F:tau protein binding; IPI:Alzheimers_University_of_Toronto.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0060988; P:lipid tube assembly; IMP:Alzheimers_University_of_Toronto.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0042692; P:muscle cell differentiation; IEA:Ensembl.
GO; GO:0051647; P:nucleus localization; IEA:Ensembl.
GO; GO:0006997; P:nucleus organization; IMP:WormBase.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:AgBase.
GO; GO:0048711; P:positive regulation of astrocyte differentiation; IMP:Alzheimers_University_of_Toronto.
GO; GO:0071156; P:regulation of cell cycle arrest; IDA:Alzheimers_University_of_Toronto.
GO; GO:0030100; P:regulation of endocytosis; IEA:InterPro.
GO; GO:0045664; P:regulation of neuron differentiation; IMP:Alzheimers_University_of_Toronto.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd12139; SH3_Bin1; 1.
Gene3D; 1.20.1270.60; -; 1.
InterPro; IPR027267; AH/BAR-dom.
InterPro; IPR003005; Amphiphysin.
InterPro; IPR035471; Amphiphysin-2_SH3.
InterPro; IPR003023; Amphiphysin_2.
InterPro; IPR004148; BAR_dom.
InterPro; IPR036028; SH3-like_dom.
InterPro; IPR001452; SH3_domain.
Pfam; PF03114; BAR; 1.
Pfam; PF14604; SH3_9; 1.
PRINTS; PR01251; AMPHIPHYSIN.
PRINTS; PR01253; AMPHIPHYSIN2.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00721; BAR; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF103657; SSF103657; 3.
SUPFAM; SSF50044; SSF50044; 1.
PROSITE; PS51021; BAR; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Coiled coil;
Complete proteome; Cytoplasm; Developmental protein; Differentiation;
Disease mutation; Endocytosis; Host-virus interaction; Nucleus;
Phosphoprotein; Reference proteome; SH3 domain; Tumor suppressor.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 593 Myc box-dependent-interacting protein 1.
/FTId=PRO_0000192951.
DOMAIN 29 276 BAR. {ECO:0000255|PROSITE-
ProRule:PRU00361}.
DOMAIN 520 592 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
REGION 2 122 Interaction with BIN2.
{ECO:0000269|PubMed:10903846}.
REGION 378 421 Clathrin-binding.
COILED 15 42 {ECO:0000255}.
COILED 193 267 {ECO:0000255}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 296 296 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 298 298 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 303 303 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 307 307 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19367720}.
MOD_RES 323 323 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 331 331 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
VAR_SEQ 174 204 Missing (in isoform IIB, isoform IIC2,
isoform II2, isoform II3, isoform BIN1,
isoform BIN1+12A, isoform BIN1-10-13 and
isoform BIN1-13).
{ECO:0000303|PubMed:8782822,
ECO:0000303|PubMed:9182667,
ECO:0000303|PubMed:9223448,
ECO:0000303|PubMed:9395479,
ECO:0000303|PubMed:9603201}.
/FTId=VSP_000246.
VAR_SEQ 285 285 P -> PRKKSKLFSRLRRKKN (in isoform BIN1,
isoform BIN1+12A and isoform BIN1-13).
{ECO:0000303|PubMed:8782822,
ECO:0000303|PubMed:9182667,
ECO:0000303|PubMed:9395479}.
/FTId=VSP_000247.
VAR_SEQ 335 487 Missing (in isoform BIN1-10-13 and
isoform BIN1-13).
{ECO:0000303|PubMed:9395479}.
/FTId=VSP_000251.
VAR_SEQ 335 457 Missing (in isoform II3 and isoform
BIN1). {ECO:0000303|PubMed:8782822,
ECO:0000303|PubMed:9182667,
ECO:0000303|PubMed:9223448,
ECO:0000303|PubMed:9395479}.
/FTId=VSP_000250.
VAR_SEQ 335 421 Missing (in isoform IIC1 and isoform
IIC2). {ECO:0000303|PubMed:9603201}.
/FTId=VSP_000249.
VAR_SEQ 335 377 Missing (in isoform IID).
{ECO:0000303|PubMed:9603201}.
/FTId=VSP_000248.
VAR_SEQ 378 457 Missing (in isoform II2 and isoform
BIN1+12A). {ECO:0000303|PubMed:9223448,
ECO:0000303|PubMed:9395479}.
/FTId=VSP_000253.
VAR_SEQ 378 421 Missing (in isoform IIB).
{ECO:0000303|PubMed:9603201}.
/FTId=VSP_000252.
VARIANT 35 35 K -> N (in CNM2; abolishes membrane
tubulation; dbSNP:rs121909273).
{ECO:0000269|PubMed:17676042}.
/FTId=VAR_037425.
VARIANT 151 151 D -> N (in CNM2; abolishes membrane
tubulation; dbSNP:rs121909274).
{ECO:0000269|PubMed:17676042}.
/FTId=VAR_037426.
CONFLICT 474 474 A -> P (in Ref. 2; AAB63263).
{ECO:0000305}.
CONFLICT 481 481 A -> S (in Ref. 10; AAC24126/AAC23750/
AAC23751). {ECO:0000305}.
CONFLICT 510 510 S -> C (in Ref. 7; AAC23440/AAC23441).
{ECO:0000305}.
CONFLICT 528 528 Q -> H (in Ref. 7; AAC23440/AAC23441).
{ECO:0000305}.
CONFLICT 576 576 E -> K (in Ref. 7; AAC23440/AAC23441).
{ECO:0000305}.
HELIX 8 33 {ECO:0000244|PDB:2RMY}.
HELIX 43 89 {ECO:0000244|PDB:2FIC}.
HELIX 97 121 {ECO:0000244|PDB:2FIC}.
HELIX 123 131 {ECO:0000244|PDB:2FIC}.
HELIX 133 161 {ECO:0000244|PDB:2FIC}.
STRAND 163 165 {ECO:0000244|PDB:2FIC}.
HELIX 205 268 {ECO:0000244|PDB:2FIC}.
STRAND 523 527 {ECO:0000244|PDB:1MUZ}.
STRAND 535 537 {ECO:0000244|PDB:1MUZ}.
STRAND 546 549 {ECO:0000244|PDB:1MUZ}.
HELIX 555 557 {ECO:0000244|PDB:1MUZ}.
STRAND 562 567 {ECO:0000244|PDB:1MUZ}.
HELIX 568 572 {ECO:0000244|PDB:1MUZ}.
HELIX 573 579 {ECO:0000244|PDB:1MUZ}.
STRAND 582 585 {ECO:0000244|PDB:1MUZ}.
HELIX 586 588 {ECO:0000244|PDB:1MUZ}.
STRAND 589 591 {ECO:0000244|PDB:1MUZ}.
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


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