ID   BIN3_HUMAN              Reviewed;         253 AA.
AC   Q9NQY0; Q9BVG2; Q9NVY9;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=Bridging integrator 3;
GN   Name=BIN3;
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 1), AND TISSUE SPECIFICITY.
RX   PubMed=11274158; DOI=10.1074/jbc.m101096200;
RA   Routhier E.L., Burn T.C., Abbaszade I., Summers M., Albright C.F.,
RA   Prendergast G.C.;
RT   "Human BIN3 complements the F-actin localization defects caused by loss of
RT   Hob3p, the fission yeast homolog of Rvs161p.";
RL   J. Biol. Chem. 276:21670-21677(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung, and Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
CC   -!- FUNCTION: Involved in cytokinesis and septation where it has a role in
CC       the localization of F-actin.
CC   -!- INTERACTION:
CC       Q9NQY0; Q9NYB9-2: ABI2; NbExp=7; IntAct=EBI-2653038, EBI-11096309;
CC       Q9NQY0; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-2653038, EBI-725606;
CC       Q9NQY0; Q6XZF7: DNMBP; NbExp=2; IntAct=EBI-2653038, EBI-2483419;
CC       Q9NQY0; Q9BRT9: GINS4; NbExp=3; IntAct=EBI-2653038, EBI-747500;
CC       Q9NQY0; Q9UBU9: NXF1; NbExp=3; IntAct=EBI-2653038, EBI-398874;
CC       Q9NQY0; O15160: POLR1C; NbExp=3; IntAct=EBI-2653038, EBI-1055079;
CC       Q9NQY0; Q9NQG5: RPRD1B; NbExp=3; IntAct=EBI-2653038, EBI-747925;
CC       Q9NQY0; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-2653038, EBI-11525489;
CC       Q9NQY0; P40222: TXLNA; NbExp=3; IntAct=EBI-2653038, EBI-359793;
CC       Q9NQY0; Q9BZL1: UBL5; NbExp=3; IntAct=EBI-2653038, EBI-607755;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9NQY0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NQY0-2; Sequence=VSP_013465;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed except in brain.
CC       {ECO:0000269|PubMed:11274158}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH01223.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF271732; AAF76218.1; -; mRNA.
DR   EMBL; AK001289; BAA91603.1; -; mRNA.
DR   EMBL; AK023980; BAB14751.1; -; mRNA.
DR   EMBL; BC001223; AAH01223.1; ALT_INIT; mRNA.
DR   EMBL; BC009824; AAH09824.1; -; mRNA.
DR   CCDS; CCDS47825.1; -. [Q9NQY0-1]
DR   RefSeq; NP_061158.1; NM_018688.4. [Q9NQY0-1]
DR   RefSeq; XP_011542888.1; XM_011544586.2.
DR   AlphaFoldDB; Q9NQY0; -.
DR   SMR; Q9NQY0; -.
DR   BioGRID; 120995; 46.
DR   IntAct; Q9NQY0; 34.
DR   MINT; Q9NQY0; -.
DR   STRING; 9606.ENSP00000276416; -.
DR   ChEMBL; CHEMBL4295959; -.
DR   GlyGen; Q9NQY0; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9NQY0; -.
DR   PhosphoSitePlus; Q9NQY0; -.
DR   BioMuta; BIN3; -.
DR   DMDM; 30912742; -.
DR   EPD; Q9NQY0; -.
DR   jPOST; Q9NQY0; -.
DR   MassIVE; Q9NQY0; -.
DR   MaxQB; Q9NQY0; -.
DR   PaxDb; 9606-ENSP00000276416; -.
DR   PeptideAtlas; Q9NQY0; -.
DR   ProteomicsDB; 82229; -. [Q9NQY0-1]
DR   ProteomicsDB; 82230; -. [Q9NQY0-2]
DR   Pumba; Q9NQY0; -.
DR   Antibodypedia; 5285; 395 antibodies from 26 providers.
DR   DNASU; 55909; -.
DR   Ensembl; ENST00000276416.11; ENSP00000276416.6; ENSG00000147439.14. [Q9NQY0-1]
DR   Ensembl; ENST00000519513.5; ENSP00000430423.1; ENSG00000147439.14. [Q9NQY0-2]
DR   GeneID; 55909; -.
DR   KEGG; hsa:55909; -.
DR   MANE-Select; ENST00000276416.11; ENSP00000276416.6; NM_018688.6; NP_061158.1.
DR   UCSC; uc003xcl.5; human. [Q9NQY0-1]
DR   AGR; HGNC:1054; -.
DR   CTD; 55909; -.
DR   DisGeNET; 55909; -.
DR   GeneCards; BIN3; -.
DR   HGNC; HGNC:1054; BIN3.
DR   HPA; ENSG00000147439; Low tissue specificity.
DR   MIM; 606396; gene.
DR   neXtProt; NX_Q9NQY0; -.
DR   OpenTargets; ENSG00000147439; -.
DR   PharmGKB; PA25357; -.
DR   VEuPathDB; HostDB:ENSG00000147439; -.
DR   eggNOG; KOG3771; Eukaryota.
DR   GeneTree; ENSGT00950000182882; -.
DR   HOGENOM; CLU_090113_1_0_1; -.
DR   InParanoid; Q9NQY0; -.
DR   OMA; TRFCAYF; -.
DR   OrthoDB; 3075274at2759; -.
DR   PhylomeDB; Q9NQY0; -.
DR   TreeFam; TF331711; -.
DR   PathwayCommons; Q9NQY0; -.
DR   SignaLink; Q9NQY0; -.
DR   BioGRID-ORCS; 55909; 13 hits in 1162 CRISPR screens.
DR   ChiTaRS; BIN3; human.
DR   GeneWiki; BIN3; -.
DR   GenomeRNAi; 55909; -.
DR   Pharos; Q9NQY0; Tbio.
DR   PRO; PR:Q9NQY0; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q9NQY0; Protein.
DR   Bgee; ENSG00000147439; Expressed in sural nerve and 180 other cell types or tissues.
DR   ExpressionAtlas; Q9NQY0; baseline and differential.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0008093; F:cytoskeletal anchor activity; NAS:UniProtKB.
DR   GO; GO:0051666; P:actin cortical patch localization; IBA:GO_Central.
DR   GO; GO:0007015; P:actin filament organization; NAS:UniProtKB.
DR   GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; NAS:UniProtKB.
DR   GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0014839; P:myoblast migration involved in skeletal muscle regeneration; IEA:Ensembl.
DR   GO; GO:0097320; P:plasma membrane tubulation; IBA:GO_Central.
DR   GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR   GO; GO:0010591; P:regulation of lamellipodium assembly; IEA:Ensembl.
DR   GO; GO:0048741; P:skeletal muscle fiber development; IEA:Ensembl.
DR   GO; GO:0009826; P:unidimensional cell growth; IMP:UniProtKB.
DR   CDD; cd07590; BAR_Bin3; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR004148; BAR_dom.
DR   InterPro; IPR046982; BIN3/RVS161-like.
DR   InterPro; IPR037428; Bin3_BAR.
DR   PANTHER; PTHR47174; BRIDGING INTEGRATOR 3; 1.
DR   PANTHER; PTHR47174:SF3; BRIDGING INTEGRATOR 3; 1.
DR   Pfam; PF03114; BAR; 1.
DR   SMART; SM00721; BAR; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   PROSITE; PS51021; BAR; 1.
DR   Genevisible; Q9NQY0; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Reference proteome; Septation.
FT   CHAIN           1..253
FT                   /note="Bridging integrator 3"
FT                   /id="PRO_0000192955"
FT   DOMAIN          9..232
FT                   /note="BAR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT   REGION          220..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          18..51
FT                   /evidence="ECO:0000255"
FT   COILED          120..152
FT                   /evidence="ECO:0000255"
FT   COILED          231..247
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        224..240
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..54
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_013465"
FT   CONFLICT        122
FT                   /note="N -> I (in Ref. 2; BAA91603)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   253 AA;  29665 MW;  254CC7113749C584 CRC64;
     MSWIPFKIGQ PKKQIVPKTV ERDFEREYGK LQQLEEQTRR LQKDMKKSTD ADLAMSKSAV
     KISLDLLSNP LCEQDQDLLN MVTALDTAMK RMDAFNQEKV NQIQKTVIEP LKKFGSVFPS
     LNMAVKRREQ ALQDYRRLQA KVEKYEEKEK TGPVLAKLHQ AREELRPVRE DFEAKNRQLL
     EEMPRFYGSR LDYFQPSFES LIRAQVVYYS EMHKIFGDLS HQLDQPGHSD EQRERENEAK
     LSELRALSIV ADD
//