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O00499

- BIN1_HUMAN

UniProt

O00499 - BIN1_HUMAN

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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

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. 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
Complete GO annotation...

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-KW
  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
Complete GO annotation...

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
P2795811EBI-719094,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. 44 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 – 3326Combined sources
Helixi43 – 8947Combined sources
Helixi97 – 12125Combined sources
Helixi123 – 1319Combined sources
Helixi133 – 16129Combined sources
Helixi205 – 26864Combined sources
Beta strandi523 – 5275Combined sources
Beta strandi535 – 5373Combined sources
Beta strandi546 – 5494Combined sources
Helixi555 – 5573Combined sources
Beta strandi562 – 5676Combined sources
Helixi568 – 5725Combined sources
Helixi573 – 5797Combined sources
Beta strandi582 – 5854Combined sources
Helixi586 – 5883Combined sources
Beta strandi589 – 5913Combined sources

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.
GeneTreeiENSGT00390000017588.
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

        10         20         30         40         50
MAEMGSKGVT AGKIASNVQK KLTRAQEKVL QKLGKADETK DEQFEQCVQN
60 70 80 90 100
FNKQLTEGTR LQKDLRTYLA SVKAMHEASK KLNECLQEVY EPDWPGRDEA
110 120 130 140 150
NKIAENNDLL WMDYHQKLVD QALLTMDTYL GQFPDIKSRI AKRGRKLVDY
160 170 180 190 200
DSARHHYESL QTAKKKDEAK IAKPVSLLEK AAPQWCQGKL QAHLVAQTNL
210 220 230 240 250
LRNQAEEELI KAQKVFEEMN VDLQEELPSL WNSRVGFYVN TFQSIAGLEE
260 270 280 290 300
NFHKEMSKLN QNLNDVLVGL EKQHGSNTFT VKAQPSDNAP AKGNKSPSPP
310 320 330 340 350
DGSPAATPEI RVNHEPEPAG GATPGATLPK SPSQLRKGPP VPPPPKHTPS
360 370 380 390 400
KEVKQEQILS LFEDTFVPEI SVTTPSQFEA PGPFSEQASL LDLDFDPLPP
410 420 430 440 450
VTSPVKAPTP SGQSIPWDLW EPTESPAGSL PSGEPSAAEG TFAVSWPSQT
460 470 480 490 500
AEPGPAQPAE ASEVAGGTQP AAGAQEPGET AASEAASSSL PAVVVETFPA
510 520 530 540 550
TVNGTVEGGS GAGRLDLPPG FMFKVQAQHD YTATDTDELQ LKAGDVVLVI
560 570 580 590
PFQNPEEQDE GWLMGVKESD WNQHKELEKC RGVFPENFTE RVP
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. 44 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 GC02M127805.
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.
GeneTreei ENSGT00390000017588.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 157 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