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O00499

- BIN1_HUMAN

UniProt

O00499 - BIN1_HUMAN

Protein

Myc box-dependent-interacting protein 1

Gene

BIN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

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

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. protein binding Source: IntAct
    3. tau protein binding Source: Alzheimers_University_of_Toronto

    GO - Biological processi

    1. cell proliferation Source: ProtInc
    2. endocytosis Source: UniProtKB-KW
    3. lipid tube assembly Source: Alzheimers_University_of_Toronto
    4. muscle cell differentiation Source: Ensembl
    5. positive regulation of apoptotic process Source: Alzheimers_University_of_Toronto
    6. positive regulation of astrocyte differentiation Source: Alzheimers_University_of_Toronto
    7. positive regulation of endocytosis Source: Ensembl
    8. positive regulation of GTPase activity Source: Ensembl
    9. regulation of cell cycle arrest Source: Alzheimers_University_of_Toronto
    10. regulation of neuron differentiation Source: Alzheimers_University_of_Toronto
    11. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Differentiation, Endocytosis, Host-virus interaction

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:BIN1
    Synonyms:AMPHL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:1052. BIN1.

    Subcellular locationi

    GO - Cellular componenti

    1. actin cytoskeleton Source: ProtInc
    2. axon Source: Alzheimers_University_of_Toronto
    3. axon initial segment Source: Alzheimers_University_of_Toronto
    4. axon terminus Source: Ensembl
    5. cerebellar mossy fiber Source: Ensembl
    6. cytoplasm Source: LIFEdb
    7. I band Source: Alzheimers_University_of_Toronto
    8. lipid tube Source: Alzheimers_University_of_Toronto
    9. node of Ranvier Source: Alzheimers_University_of_Toronto
    10. nucleus Source: UniProtKB-SubCell
    11. synaptic vesicle Source: Ensembl
    12. T-tubule Source: Alzheimers_University_of_Toronto
    13. varicosity Source: Ensembl
    14. Z disc Source: Alzheimers_University_of_Toronto

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti35 – 351K → N in CNM2; abolishes membrane tubulation. 1 Publication
    VAR_037425
    Natural varianti151 – 1511D → N in CNM2; abolishes membrane tubulation. 1 Publication
    VAR_037426

    Keywords - Diseasei

    Disease mutation, Tumor suppressor

    Organism-specific databases

    MIMi255200. phenotype.
    Orphaneti169186. Autosomal recessive centronuclear myopathy.
    PharmGKBiPA25355.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 593592Myc box-dependent-interacting protein 1PRO_0000192951Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei296 – 2961Phosphoserine2 Publications
    Modified residuei298 – 2981Phosphoserine1 Publication
    Modified residuei303 – 3031Phosphoserine2 Publications
    Modified residuei307 – 3071Phosphothreonine2 Publications
    Modified residuei323 – 3231Phosphothreonine2 Publications
    Modified residuei331 – 3311Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated by protein kinase C.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO00499.
    PaxDbiO00499.
    PRIDEiO00499.

    2D gel databases

    UCD-2DPAGEO00499.

    PTM databases

    PhosphoSiteiO00499.

    Expressioni

    Tissue specificityi

    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.1 Publication

    Gene expression databases

    BgeeiO00499.
    GenevestigatoriO00499.

    Organism-specific databases

    HPAiCAB001945.
    HPA003894.
    HPA005437.

    Interactioni

    Subunit structurei

    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.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-719094,EBI-719094
    P279582EBI-8870146,EBI-8753518From a different organism.
    Q9WMX24EBI-719094,EBI-6863748From a different organism.
    BIN2Q9UBW52EBI-719094,EBI-2042570
    DLGAP4Q9Y2H04EBI-719094,EBI-722139
    FBP1P094674EBI-719094,EBI-712740
    MAPTP10636-75EBI-6926280,EBI-6926270
    MTM1Q134966EBI-719094,EBI-2864109
    MYCP011063EBI-7689134,EBI-447544
    REPS2Q8NFH8-26EBI-719094,EBI-8029141
    SNX4O952193EBI-719094,EBI-724909
    XRCC4Q134264EBI-719094,EBI-717592

    Protein-protein interaction databases

    BioGridi106771. 40 interactions.
    DIPiDIP-41480N.
    IntActiO00499. 18 interactions.
    MINTiMINT-258326.

    Structurei

    Secondary structure

    1
    593
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 3326
    Helixi43 – 8947
    Helixi97 – 12125
    Helixi123 – 1319
    Helixi133 – 16129
    Helixi205 – 26864
    Beta strandi523 – 5275
    Beta strandi535 – 5373
    Beta strandi546 – 5494
    Helixi555 – 5573
    Beta strandi562 – 5676
    Helixi568 – 5725
    Helixi573 – 5797
    Beta strandi582 – 5854
    Helixi586 – 5883
    Beta strandi589 – 5913

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MUZNMR-A513-593[»]
    1MV0NMR-B513-593[»]
    1MV3NMR-A301-593[»]
    2FICX-ray1.99A/B1-272[»]
    2RMYNMR-A1-33[»]
    2RNDNMR-A1-33[»]
    ProteinModelPortaliO00499.
    SMRiO00499. Positions 1-33, 40-271, 301-377, 455-593.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00499.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini29 – 276248BARPROSITE-ProRule annotationAdd
    BLAST
    Domaini520 – 59273SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 122121Interaction with BIN2Add
    BLAST
    Regioni378 – 42144Clathrin-bindingAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili15 – 4228Sequence AnalysisAdd
    BLAST
    Coiled coili193 – 26775Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 BAR domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, SH3 domain

    Phylogenomic databases

    eggNOGiNOG264615.
    HOVERGENiHBG004224.
    InParanoidiO00499.
    OMAiVYEPEWP.
    OrthoDBiEOG7XWPND.
    PhylomeDBiO00499.
    TreeFamiTF313542.

    Family and domain databases

    Gene3Di1.20.1270.60. 2 hits.
    InterProiIPR027267. AH/BAR-dom.
    IPR003005. Amphiphysin.
    IPR003023. Amphiphysin_2.
    IPR004148. BAR_dom.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF03114. BAR. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view]
    PRINTSiPR01251. AMPHIPHYSIN.
    PR01253. AMPHIPHYSIN2.
    PR00452. SH3DOMAIN.
    SMARTiSM00721. BAR. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    PROSITEiPS51021. BAR. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (11)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 11 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform IIA (identifier: O00499-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAEMGSKGVT AGKIASNVQK KLTRAQEKVL QKLGKADETK DEQFEQCVQN    50
    FNKQLTEGTR LQKDLRTYLA SVKAMHEASK KLNECLQEVY EPDWPGRDEA 100
    NKIAENNDLL WMDYHQKLVD QALLTMDTYL GQFPDIKSRI AKRGRKLVDY 150
    DSARHHYESL QTAKKKDEAK IAKPVSLLEK AAPQWCQGKL QAHLVAQTNL 200
    LRNQAEEELI KAQKVFEEMN VDLQEELPSL WNSRVGFYVN TFQSIAGLEE 250
    NFHKEMSKLN QNLNDVLVGL EKQHGSNTFT VKAQPSDNAP AKGNKSPSPP 300
    DGSPAATPEI RVNHEPEPAG GATPGATLPK SPSQLRKGPP VPPPPKHTPS 350
    KEVKQEQILS LFEDTFVPEI SVTTPSQFEA PGPFSEQASL LDLDFDPLPP 400
    VTSPVKAPTP SGQSIPWDLW EPTESPAGSL PSGEPSAAEG TFAVSWPSQT 450
    AEPGPAQPAE ASEVAGGTQP AAGAQEPGET AASEAASSSL PAVVVETFPA 500
    TVNGTVEGGS GAGRLDLPPG FMFKVQAQHD YTATDTDELQ LKAGDVVLVI 550
    PFQNPEEQDE GWLMGVKESD WNQHKELEKC RGVFPENFTE RVP 593
    Length:593
    Mass (Da):64,699
    Last modified:July 1, 1997 - v1
    Checksum:i0FF1956F0C7E3B50
    GO
    Isoform IIB (identifier: O00499-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         174-204: Missing.
         378-421: Missing.

    Show »
    Length:518
    Mass (Da):56,499
    Checksum:i9BEF82FC2C28C845
    GO
    Isoform IIC1 (identifier: O00499-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         335-421: Missing.

    Show »
    Length:506
    Mass (Da):55,175
    Checksum:iF3EA5A2EF666CE59
    GO
    Isoform IIC2 (identifier: O00499-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         174-204: Missing.
         335-421: Missing.

    Show »
    Length:475
    Mass (Da):51,737
    Checksum:i876B8A866F96BA14
    GO
    Isoform IID (identifier: O00499-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         335-377: Missing.

    Show »
    Length:550
    Mass (Da):59,937
    Checksum:i99FC3F5471E1926B
    GO
    Isoform II2 (identifier: O00499-6) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:482
    Mass (Da):53,020
    Checksum:iDF00A44348B6F1BF
    GO
    Isoform II3 (identifier: O00499-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         174-204: Missing.
         335-457: Missing.

    Show »
    Length:439
    Mass (Da):48,258
    Checksum:i350E429F13AF49C6
    GO
    Isoform BIN1 (identifier: O00499-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         174-204: Missing.
         285-285: P → PRKKSKLFSRLRRKKN
         335-457: Missing.

    Show »
    Length:454
    Mass (Da):50,185
    Checksum:i7E2ADD14E9D56D9E
    GO
    Isoform BIN1-10-13 (identifier: O00499-9) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         174-204: Missing.
         335-487: Missing.

    Show »
    Length:409
    Mass (Da):45,563
    Checksum:i08C5B23D79252350
    GO
    Isoform BIN1-13 (identifier: O00499-10) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         174-204: Missing.
         285-285: P → PRKKSKLFSRLRRKKN
         335-487: Missing.

    Show »
    Length:424
    Mass (Da):47,491
    Checksum:i1C86B9D4C8C204C6
    GO
    Isoform BIN1+12A (identifier: O00499-11) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:497
    Mass (Da):54,948
    Checksum:i55E3246DD05172AA
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti474 – 4741A → P in AAB63263. (PubMed:9182667)Curated
    Sequence conflicti481 – 4811A → S in AAC24126. (PubMed:15815621)Curated
    Sequence conflicti481 – 4811A → S in AAC23750. (PubMed:15815621)Curated
    Sequence conflicti481 – 4811A → S in AAC23751. (PubMed:15815621)Curated
    Sequence conflicti510 – 5101S → C in AAC23440. (PubMed:9395479)Curated
    Sequence conflicti510 – 5101S → C in AAC23441. (PubMed:9395479)Curated
    Sequence conflicti528 – 5281Q → H in AAC23440. (PubMed:9395479)Curated
    Sequence conflicti528 – 5281Q → H in AAC23441. (PubMed:9395479)Curated
    Sequence conflicti576 – 5761E → K in AAC23440. (PubMed:9395479)Curated
    Sequence conflicti576 – 5761E → K in AAC23441. (PubMed:9395479)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti35 – 351K → N in CNM2; abolishes membrane tubulation. 1 Publication
    VAR_037425
    Natural varianti151 – 1511D → N in CNM2; abolishes membrane tubulation. 1 Publication
    VAR_037426

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei174 – 20431Missing in isoform IIB, isoform IIC2, isoform II2, isoform II3, isoform BIN1, isoform BIN1+12A, isoform BIN1-10-13 and isoform BIN1-13. 5 PublicationsVSP_000246Add
    BLAST
    Alternative sequencei285 – 2851P → PRKKSKLFSRLRRKKN in isoform BIN1, isoform BIN1+12A and isoform BIN1-13. 3 PublicationsVSP_000247
    Alternative sequencei335 – 487153Missing in isoform BIN1-10-13 and isoform BIN1-13. 1 PublicationVSP_000251Add
    BLAST
    Alternative sequencei335 – 457123Missing in isoform II3 and isoform BIN1. 4 PublicationsVSP_000250Add
    BLAST
    Alternative sequencei335 – 42187Missing in isoform IIC1 and isoform IIC2. 1 PublicationVSP_000249Add
    BLAST
    Alternative sequencei335 – 37743Missing in isoform IID. 1 PublicationVSP_000248Add
    BLAST
    Alternative sequencei378 – 45780Missing in isoform II2 and isoform BIN1+12A. 2 PublicationsVSP_000253Add
    BLAST
    Alternative sequencei378 – 42144Missing in isoform IIB. 1 PublicationVSP_000252Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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
    , U83999, U84001, U84002, U84003 Genomic DNA. Translation: AAC23440.1.
    U84004
    , 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.
    CCDSiCCDS2137.1. [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]
    PIRiJC5593.
    RefSeqiNP_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]
    UniGeneiHs.193163.

    Genome annotation databases

    EnsembliENST00000259238; 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]
    GeneIDi274.
    KEGGihsa:274.
    UCSCiuc002tns.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]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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
    , U83999 , U84001 , U84002 , U84003 Genomic DNA. Translation: AAC23440.1 .
    U84004
    , 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 .
    CCDSi CCDS2137.1. [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 ]
    PIRi JC5593.
    RefSeqi NP_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 ]
    UniGenei Hs.193163.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MUZ NMR - A 513-593 [» ]
    1MV0 NMR - B 513-593 [» ]
    1MV3 NMR - A 301-593 [» ]
    2FIC X-ray 1.99 A/B 1-272 [» ]
    2RMY NMR - A 1-33 [» ]
    2RND NMR - A 1-33 [» ]
    ProteinModelPortali O00499.
    SMRi O00499. Positions 1-33, 40-271, 301-377, 455-593.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106771. 40 interactions.
    DIPi DIP-41480N.
    IntActi O00499. 18 interactions.
    MINTi MINT-258326.

    PTM databases

    PhosphoSitei O00499.

    2D gel databases

    UCD-2DPAGE O00499.

    Proteomic databases

    MaxQBi O00499.
    PaxDbi O00499.
    PRIDEi O00499.

    Protocols and materials databases

    DNASUi 274.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000259238 ; 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 ]
    GeneIDi 274.
    KEGGi hsa:274.
    UCSCi uc002tns.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

    CTDi 274.
    GeneCardsi GC02M127898.
    HGNCi HGNC:1052. BIN1.
    HPAi CAB001945.
    HPA003894.
    HPA005437.
    MIMi 255200. phenotype.
    601248. gene.
    neXtProti NX_O00499.
    Orphaneti 169186. Autosomal recessive centronuclear myopathy.
    PharmGKBi PA25355.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG264615.
    HOVERGENi HBG004224.
    InParanoidi O00499.
    OMAi VYEPEWP.
    OrthoDBi EOG7XWPND.
    PhylomeDBi O00499.
    TreeFami TF313542.

    Miscellaneous databases

    ChiTaRSi BIN1. human.
    EvolutionaryTracei O00499.
    GeneWikii BIN1.
    GenomeRNAii 274.
    NextBioi 1087.
    PROi O00499.
    SOURCEi Search...

    Gene expression databases

    Bgeei O00499.
    Genevestigatori O00499.

    Family and domain databases

    Gene3Di 1.20.1270.60. 2 hits.
    InterProi IPR027267. AH/BAR-dom.
    IPR003005. Amphiphysin.
    IPR003023. Amphiphysin_2.
    IPR004148. BAR_dom.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF03114. BAR. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view ]
    PRINTSi PR01251. AMPHIPHYSIN.
    PR01253. AMPHIPHYSIN2.
    PR00452. SH3DOMAIN.
    SMARTi SM00721. BAR. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    PROSITEi PS51021. BAR. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.
      , 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. 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. 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. 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.

    Entry informationi

    Entry nameiBIN1_HUMAN
    AccessioniPrimary (citable) accession number: O00499
    Secondary accession number(s): O00297
    , O00545, O43867, O60552, O60553, O60554, O60555, O75514, O75515, O75516, O75517, O75518, Q659B7, Q92944, Q99688
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2001
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 156 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3