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O00499 (BIN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myc box-dependent-interacting protein 1
Alternative name(s):
Amphiphysin II
Amphiphysin-like protein
Box-dependent myc-interacting protein 1
Bridging integrator 1
Gene names
Name:BIN1
Synonyms:AMPHL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length593 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in regulation of synaptic vesicle endocytosis. May act as a tumor suppressor and inhibits malignant cell transformation.

Subunit structure

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. Ref.5 Ref.14 Ref.16

Subcellular location

Isoform BIN1: Nucleus.

Isoform IIA: Cytoplasm.

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. Ref.14

Post-translational modification

Phosphorylated by protein kinase C By similarity.

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.23

Sequence similarities

Contains 1 BAR domain.

Contains 1 SH3 domain.

Sequence caution

The sequence AAC23441.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processDifferentiation
Endocytosis
Host-virus interaction
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Tumor suppressor
   DomainCoiled coil
SH3 domain
   Molecular functionDevelopmental protein
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell proliferation

Traceable author statement Ref.3. Source: ProtInc

endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

lipid tube assembly

Inferred from mutant phenotype PubMed 19004523. Source: Alzheimers_University_of_Toronto

muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of GTPase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from mutant phenotype PubMed 10412034. Source: Alzheimers_University_of_Toronto

positive regulation of astrocyte differentiation

Inferred from mutant phenotype PubMed 10412034. Source: Alzheimers_University_of_Toronto

positive regulation of endocytosis

Inferred from electronic annotation. Source: Ensembl

regulation of cell cycle arrest

Inferred from direct assay PubMed 10412034. Source: Alzheimers_University_of_Toronto

regulation of neuron differentiation

Inferred from mutant phenotype PubMed 10412034. Source: Alzheimers_University_of_Toronto

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentI band

Inferred from sequence or structural similarity. Source: Alzheimers_University_of_Toronto

T-tubule

Inferred from sequence or structural similarity. Source: Alzheimers_University_of_Toronto

Z disc

Inferred from sequence or structural similarity. Source: Alzheimers_University_of_Toronto

actin cytoskeleton

Traceable author statement Ref.2. Source: ProtInc

axon

Inferred from direct assay PubMed 23399914. Source: Alzheimers_University_of_Toronto

axon initial segment

Inferred from sequence or structural similarity. Source: Alzheimers_University_of_Toronto

axon terminus

Inferred from electronic annotation. Source: Ensembl

cerebellar mossy fiber

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay. Source: LIFEdb

lipid tube

Inferred from mutant phenotype PubMed 19004523. Source: Alzheimers_University_of_Toronto

node of Ranvier

Inferred from sequence or structural similarity. Source: Alzheimers_University_of_Toronto

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

synaptic vesicle

Inferred from electronic annotation. Source: Ensembl

varicosity

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionidentical protein binding

Inferred from physical interaction PubMed 23917616. Source: IntAct

protein binding

Inferred from physical interaction Ref.14PubMed 12604805PubMed 12668730PubMed 16275660PubMed 18647389PubMed 18985028PubMed 23399914PubMed 23917616PubMed 15992821PubMed 15992821PubMed 12604805. Source: IntAct

tau protein binding

Inferred from physical interaction PubMed 23399914. Source: Alzheimers_University_of_Toronto

Complete GO annotation...

Alternative products

This entry describes 11 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform IIA (identifier: O00499-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform IIB (identifier: O00499-2)

The sequence of this isoform differs from the canonical sequence as follows:
     174-204: Missing.
     378-421: Missing.
Isoform IIC1 (identifier: O00499-3)

The sequence of this isoform differs from the canonical sequence as follows:
     335-421: Missing.
Isoform IIC2 (identifier: O00499-4)

The sequence of this isoform differs from the canonical sequence as follows:
     174-204: Missing.
     335-421: Missing.
Isoform IID (identifier: O00499-5)

The sequence of this isoform differs from the canonical sequence as follows:
     335-377: Missing.
Isoform II2 (identifier: O00499-6)

The sequence of this isoform differs from the canonical sequence as follows:
     174-204: Missing.
     378-457: Missing.
Isoform II3 (identifier: O00499-7)

The sequence of this isoform differs from the canonical sequence as follows:
     174-204: Missing.
     335-457: Missing.
Isoform BIN1 (identifier: O00499-8)

The sequence of this isoform differs from the canonical sequence as follows:
     174-204: Missing.
     285-285: P → PRKKSKLFSRLRRKKN
     335-457: Missing.
Isoform BIN1-10-13 (identifier: O00499-9)

The sequence of this isoform differs from the canonical sequence as follows:
     174-204: Missing.
     335-487: Missing.
Isoform BIN1-13 (identifier: O00499-10)

The sequence of this isoform differs from the canonical sequence as follows:
     174-204: Missing.
     285-285: P → PRKKSKLFSRLRRKKN
     335-487: Missing.
Isoform BIN1+12A (identifier: O00499-11)

The sequence of this isoform differs from the canonical sequence as follows:
     174-204: Missing.
     285-285: P → PRKKSKLFSRLRRKKN
     378-457: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.22
Chain2 – 593592Myc box-dependent-interacting protein 1
PRO_0000192951

Regions

Domain29 – 276248BAR
Domain520 – 59273SH3
Region2 – 122121Interaction with BIN2
Region378 – 42144Clathrin-binding
Coiled coil15 – 4228 Potential
Coiled coil193 – 26775 Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.22
Modified residue2961Phosphoserine Ref.18 Ref.21
Modified residue2981Phosphoserine Ref.18
Modified residue3031Phosphoserine Ref.15 Ref.18
Modified residue3071Phosphothreonine Ref.17 Ref.18
Modified residue3231Phosphothreonine Ref.18 Ref.21
Modified residue3311Phosphoserine Ref.18 Ref.21

Natural variations

Alternative sequence174 – 20431Missing in isoform IIB, isoform IIC2, isoform II2, isoform II3, isoform BIN1, isoform BIN1+12A, isoform BIN1-10-13 and isoform BIN1-13.
VSP_000246
Alternative sequence2851P → PRKKSKLFSRLRRKKN in isoform BIN1, isoform BIN1+12A and isoform BIN1-13.
VSP_000247
Alternative sequence335 – 487153Missing in isoform BIN1-10-13 and isoform BIN1-13.
VSP_000251
Alternative sequence335 – 457123Missing in isoform II3 and isoform BIN1.
VSP_000250
Alternative sequence335 – 42187Missing in isoform IIC1 and isoform IIC2.
VSP_000249
Alternative sequence335 – 37743Missing in isoform IID.
VSP_000248
Alternative sequence378 – 45780Missing in isoform II2 and isoform BIN1+12A.
VSP_000253
Alternative sequence378 – 42144Missing in isoform IIB.
VSP_000252
Natural variant351K → N in CNM2; abolishes membrane tubulation. Ref.23
VAR_037425
Natural variant1511D → N in CNM2; abolishes membrane tubulation. Ref.23
VAR_037426

Experimental info

Sequence conflict4741A → P in AAB63263. Ref.2
Sequence conflict4811A → S in AAC24126. Ref.10
Sequence conflict4811A → S in AAC23750. Ref.10
Sequence conflict4811A → S in AAC23751. Ref.10
Sequence conflict5101S → C in AAC23440. Ref.7
Sequence conflict5101S → C in AAC23441. Ref.7
Sequence conflict5281Q → H in AAC23440. Ref.7
Sequence conflict5281Q → H in AAC23441. Ref.7
Sequence conflict5761E → K in AAC23440. Ref.7
Sequence conflict5761E → K in AAC23441. Ref.7

Secondary structure

............................. 593
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform IIA [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 0FF1956F0C7E3B50

FASTA59364,699
        10         20         30         40         50         60 
MAEMGSKGVT AGKIASNVQK KLTRAQEKVL QKLGKADETK DEQFEQCVQN FNKQLTEGTR 

        70         80         90        100        110        120 
LQKDLRTYLA SVKAMHEASK KLNECLQEVY EPDWPGRDEA NKIAENNDLL WMDYHQKLVD 

       130        140        150        160        170        180 
QALLTMDTYL GQFPDIKSRI AKRGRKLVDY DSARHHYESL QTAKKKDEAK IAKPVSLLEK 

       190        200        210        220        230        240 
AAPQWCQGKL QAHLVAQTNL LRNQAEEELI KAQKVFEEMN VDLQEELPSL WNSRVGFYVN 

       250        260        270        280        290        300 
TFQSIAGLEE NFHKEMSKLN QNLNDVLVGL EKQHGSNTFT VKAQPSDNAP AKGNKSPSPP 

       310        320        330        340        350        360 
DGSPAATPEI RVNHEPEPAG GATPGATLPK SPSQLRKGPP VPPPPKHTPS KEVKQEQILS 

       370        380        390        400        410        420 
LFEDTFVPEI SVTTPSQFEA PGPFSEQASL LDLDFDPLPP VTSPVKAPTP SGQSIPWDLW 

       430        440        450        460        470        480 
EPTESPAGSL PSGEPSAAEG TFAVSWPSQT AEPGPAQPAE ASEVAGGTQP AAGAQEPGET 

       490        500        510        520        530        540 
AASEAASSSL PAVVVETFPA TVNGTVEGGS GAGRLDLPPG FMFKVQAQHD YTATDTDELQ 

       550        560        570        580        590 
LKAGDVVLVI PFQNPEEQDE GWLMGVKESD WNQHKELEKC RGVFPENFTE RVP 

« Hide

Isoform IIB [UniParc].

Checksum: 9BEF82FC2C28C845
Show »

FASTA51856,499
Isoform IIC1 [UniParc].

Checksum: F3EA5A2EF666CE59
Show »

FASTA50655,175
Isoform IIC2 [UniParc].

Checksum: 876B8A866F96BA14
Show »

FASTA47551,737
Isoform IID [UniParc].

Checksum: 99FC3F5471E1926B
Show »

FASTA55059,937
Isoform II2 [UniParc].

Checksum: DF00A44348B6F1BF
Show »

FASTA48253,020
Isoform II3 [UniParc].

Checksum: 350E429F13AF49C6
Show »

FASTA43948,258
Isoform BIN1 [UniParc].

Checksum: 7E2ADD14E9D56D9E
Show »

FASTA45450,185
Isoform BIN1-10-13 [UniParc].

Checksum: 08C5B23D79252350
Show »

FASTA40945,563
Isoform BIN1-13 [UniParc].

Checksum: 1C86B9D4C8C204C6
Show »

FASTA42447,491
Isoform BIN1+12A [UniParc].

Checksum: 55E3246DD05172AA
Show »

FASTA49754,948

References

« Hide 'large scale' references
[1]"Identification and characterization of a nerve terminal-enriched amphiphysin isoform."
Ramjaun A.R., Micheva K.D., Bouchelet I., McPherson P.S.
J. Biol. Chem. 272:16700-16706(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IIA).
Tissue: Brain.
[2]"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."
Butler M.H., David C., Ochoa G.-C., Freyberg Z., Daniell L., Grabs D., Cremona O., De Camilli P.
J. Cell Biol. 137:1355-1367(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS IIA AND BIN1).
Tissue: Brain and Skeletal muscle.
[3]"BIN1 is a novel Myc-interacting protein with features of a tumour suppressor."
Sakamuro D., Elliott K.J., Wechsler-Reya R., Prendergast G.C.
Nat. Genet. 14:69-76(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BIN1).
Tissue: Skeletal muscle.
[4]Sakamuro D., Elliott K.J., Wechsler-Reya R., Prendergast G.C.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO N-TERMINUS.
[5]"Multiple amphiphysin II splice variants display differential clathrin binding: identification of two distinct clathrin-binding sites."
Ramjaun A.R., McPherson P.S.
J. Neurochem. 70:2369-2376(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS IIB; IIC1; IIC2 AND IID), INTERACTION WITH CLTC.
Tissue: Brain.
[6]"cDNA cloning of a novel amphiphysin isoform and tissue-specific expression of its multiple splice variants."
Tsutsui K., Maeda Y., Tsutsui K., Seki S., Tokunaga A.
Biochem. Biophys. Res. Commun. 236:178-183(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS II2 AND II3).
Tissue: Brain.
[7]"Structural analysis of the human BIN1 gene. Evidence for tissue-specific transcriptional regulation and alternate RNA splicing."
Wechsler-Reya R.J., Sakamuro D., Zhang J., Duhadaway J., Prendergast G.C.
J. Biol. Chem. 272:31453-31458(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS II3; II3; BIN1-10-13; BIN1-13 AND BIN1+12A).
Tissue: Fibroblast.
[8]Zhang J., Du W., Wechsler-Reya R.J., Duhadaway J., Sakamuro D., Prendergast G.C.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM II2).
[9]"The full-ORF clone resource of the German cDNA consortium."
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.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IIA).
Tissue: Brain.
[10]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
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. expand/collapse author list , 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.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]Yu W., Gibbs R.A.
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 133-593.
Tissue: Brain.
[13]"A role for the putative tumor suppressor Bin1 in muscle cell differentiation."
Wechsler-Reya R.J., Elliott K.J., Prendergast G.C.
Mol. Cell. Biol. 18:566-575(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Tissue: Skeletal muscle.
[14]"Bin2, a functionally nonredundant member of the BAR adaptor gene family."
Ge K., Prendergast G.C.
Genomics 67:210-220(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BIN2, TISSUE SPECIFICITY.
[15]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"The SH3 binding motif of HCV NS5A protein interacts with Bin1 and is important for apoptosis and infectivity."
Nanda S.K., Herion D., Liang T.J.
Gastroenterology 130:794-809(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCV NS5A.
[17]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[18]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-298; SER-303; THR-307; THR-323 AND SER-331, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[21]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; THR-323 AND SER-331, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[23]"Mutations in amphiphysin 2 (BIN1) disrupt interaction with dynamin 2 and cause autosomal recessive centronuclear myopathy."
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.
Nat. Genet. 39:1134-1139(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CNM2 ASN-35 AND ASN-151, CHARACTERIZATION OF VARIANTS CNM2 ASN-35 AND ASN-151.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF004015 mRNA. Translation: AAC51345.1.
AF070576 mRNA. Translation: AAC28646.1.
AF001383 mRNA. Translation: AAB61363.1.
U68485 mRNA. Translation: AAC17461.1.
AF043898 mRNA. Translation: AAC39710.1.
AF043899 mRNA. Translation: AAC39711.1.
AF043900 mRNA. Translation: AAC39712.1.
AF043901 mRNA. Translation: AAC39713.1.
U87558 mRNA. Translation: AAB63263.1.
AF068914 mRNA. Translation: AAC24126.1.
AF068915 mRNA. Translation: AAC24127.1.
AF068916 mRNA. Translation: AAC24128.1.
AF068917 mRNA. Translation: AAC23750.1.
AF068918 mRNA. Translation: AAC23751.1.
U84004 expand/collapse EMBL AC list , U83999, U84001, U84002, U84003 Genomic DNA. Translation: AAC23440.1.
U84004 expand/collapse EMBL AC list , U83999, U84001, U84002, U84003 Genomic DNA. Translation: AAC23441.1. Different initiation.
AL713697 mRNA. Translation: CAD28496.1.
AC012508 Genomic DNA. Translation: AAY24328.1.
CH471103 Genomic DNA. Translation: EAW95302.1.
CCDSCCDS2137.1. [O00499-8]
CCDS2138.1. [O00499-1]
CCDS2139.1. [O00499-5]
CCDS2140.1. [O00499-3]
CCDS2141.1. [O00499-11]
CCDS2142.1. [O00499-2]
CCDS2143.1. [O00499-9]
CCDS42743.1. [O00499-4]
CCDS42744.1. [O00499-6]
CCDS46403.1. [O00499-7]
PIRJC5593.
RefSeqNP_004296.1. NM_004305.3. [O00499-8]
NP_647593.1. NM_139343.2. [O00499-1]
NP_647594.1. NM_139344.2. [O00499-5]
NP_647595.1. NM_139345.2. [O00499-3]
NP_647596.1. NM_139346.2. [O00499-11]
NP_647597.1. NM_139347.2. [O00499-2]
NP_647598.1. NM_139348.2. [O00499-6]
NP_647599.1. NM_139349.2. [O00499-4]
NP_647600.1. NM_139350.2. [O00499-7]
NP_647601.1. NM_139351.2. [O00499-9]
XP_005263704.1. XM_005263647.1. [O00499-10]
UniGeneHs.193163.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MUZNMR-A513-593[»]
1MV0NMR-B513-593[»]
1MV3NMR-A301-593[»]
2FICX-ray1.99A/B1-272[»]
2RMYNMR-A1-33[»]
2RNDNMR-A1-33[»]
ProteinModelPortalO00499.
SMRO00499. Positions 1-33, 40-271, 301-377, 455-593.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106771. 39 interactions.
DIPDIP-41480N.
IntActO00499. 16 interactions.
MINTMINT-258326.

PTM databases

PhosphoSiteO00499.

2D gel databases

UCD-2DPAGEO00499.

Proteomic databases

MaxQBO00499.
PaxDbO00499.
PRIDEO00499.

Protocols and materials databases

DNASU274.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000259238; ENSP00000259238; ENSG00000136717. [O00499-11]
ENST00000316724; ENSP00000316779; ENSG00000136717. [O00499-1]
ENST00000346226; ENSP00000315411; ENSG00000136717. [O00499-2]
ENST00000348750; ENSP00000259237; ENSG00000136717. [O00499-9]
ENST00000351659; ENSP00000315388; ENSG00000136717. [O00499-3]
ENST00000352848; ENSP00000315284; ENSG00000136717. [O00499-8]
ENST00000357970; ENSP00000350654; ENSG00000136717. [O00499-5]
ENST00000376113; ENSP00000365281; ENSG00000136717. [O00499-10]
ENST00000393040; ENSP00000376760; ENSG00000136717. [O00499-6]
ENST00000393041; ENSP00000376761; ENSG00000136717. [O00499-4]
ENST00000409400; ENSP00000386797; ENSG00000136717. [O00499-7]
GeneID274.
KEGGhsa:274.
UCSCuc002tns.2. human. [O00499-1]
uc002tnt.2. human. [O00499-9]
uc002tnu.2. human. [O00499-10]
uc002tnv.2. human. [O00499-5]
uc002tnw.2. human. [O00499-11]
uc002tnx.2. human. [O00499-8]
uc002tny.2. human. [O00499-3]
uc002tnz.2. human. [O00499-2]
uc002toa.2. human. [O00499-6]
uc002tob.2. human. [O00499-7]
uc002toc.2. human. [O00499-4]

Organism-specific databases

CTD274.
GeneCardsGC02M127898.
HGNCHGNC:1052. BIN1.
HPACAB001945.
HPA003894.
HPA005437.
MIM255200. phenotype.
601248. gene.
neXtProtNX_O00499.
Orphanet169186. Autosomal recessive centronuclear myopathy.
PharmGKBPA25355.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG264615.
HOVERGENHBG004224.
InParanoidO00499.
OMAVYEPEWP.
OrthoDBEOG7XWPND.
PhylomeDBO00499.
TreeFamTF313542.

Gene expression databases

BgeeO00499.
GenevestigatorO00499.

Family and domain databases

Gene3D1.20.1270.60. 2 hits.
InterProIPR027267. AH/BAR-dom.
IPR003005. Amphiphysin.
IPR003023. Amphiphysin_2.
IPR004148. BAR_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamPF03114. BAR. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSPR01251. AMPHIPHYSIN.
PR01253. AMPHIPHYSIN2.
PR00452. SH3DOMAIN.
SMARTSM00721. BAR. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS51021. BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBIN1. human.
EvolutionaryTraceO00499.
GeneWikiBIN1.
GenomeRNAi274.
NextBio1087.
PROO00499.
SOURCESearch...

Entry information

Entry nameBIN1_HUMAN
AccessionPrimary (citable) accession number: O00499
Secondary accession number(s): O00297 expand/collapse secondary AC list , O00545, O43867, O60552, O60553, O60554, O60555, O75514, O75515, O75516, O75517, O75518, Q659B7, Q92944, Q99688
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: July 1, 1997
Last modified: July 9, 2014
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM