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O08839 (BIN1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·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
Bridging integrator 1
Gene names
Name:Bin1
Synonyms:Amph2, Amphl
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length588 AA.
Sequence statusComplete.
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. Ref.7

Subunit structure

Heterodimer with AMPH. Binds SH3GLB1 By similarity. Interacts (via SH3 domain) with SYNJ1. Interacts (via SH3 domain) with DNM1. Interacts 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 By similarity. Ref.1 Ref.4 Ref.5 Ref.6 Ref.7

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Tissue specificity

Isoform AMPH2-1 is expressed in brain, concentrated at nerve terminals. Isoform AMPH2-2 is widely expressed.

Post-translational modification

Phosphorylated by protein kinase C.

Sequence similarities

Contains 1 BAR domain.

Contains 1 SH3 domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AmphO088382EBI-80095,EBI-80080
Dnm1P215752EBI-80095,EBI-80070

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform AMPH2-1 (identifier: O08839-1)

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 AMPH2-2 (identifier: O08839-2)

The sequence of this isoform differs from the canonical sequence as follows:
     423-460: Missing.
Isoform AMPH2-3 (identifier: O08839-3)

The sequence of this isoform differs from the canonical sequence as follows:
     335-588: Missing.
Isoform AMPH2-4 (identifier: O08839-4)

The sequence of this isoform differs from the canonical sequence as follows:
     173-205: Missing.
     253-588: Missing.
Isoform AMPH2-5 (identifier: O08839-5)

The sequence of this isoform differs from the canonical sequence as follows:
     335-482: Missing.
Isoform AMPH2-6 (identifier: O08839-6)

The sequence of this isoform differs from the canonical sequence as follows:
     173-205: Missing.
     335-482: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 588588Myc box-dependent-interacting protein 1
PRO_0000192953

Regions

Domain29 – 276248BAR
Domain515 – 58874SH3
Region1 – 122122Interaction with BIN2 By similarity
Region379 – 42244Clathrin-binding By similarity
Coiled coil15 – 4228 Potential
Coiled coil193 – 27482 Potential

Amino acid modifications

Modified residue2961Phosphoserine By similarity
Modified residue2981Phosphoserine By similarity
Modified residue3041Phosphoserine By similarity
Modified residue3081Phosphothreonine By similarity
Modified residue3241Phosphoserine By similarity
Modified residue3321Phosphoserine By similarity

Natural variations

Alternative sequence173 – 20533Missing in isoform AMPH2-4 and isoform AMPH2-6.
VSP_000256
Alternative sequence253 – 588336Missing in isoform AMPH2-4.
VSP_000257
Alternative sequence335 – 588254Missing in isoform AMPH2-3.
VSP_000258
Alternative sequence335 – 482148Missing in isoform AMPH2-5 and isoform AMPH2-6.
VSP_000259
Alternative sequence423 – 46038Missing in isoform AMPH2-2.
VSP_000260

Secondary structure

1 ................ 588
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform AMPH2-1 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 164AC90E09547F1A

FASTA58864,533
        10         20         30         40         50         60 
MAEMGSKGVT AGKIASNVQK KLTRAQEKVL QKLGKADETK DEQFEQCVQN FNKQLTEGTR 

        70         80         90        100        110        120 
LQKDLRTYLA SVKAMHEASK KLSECLQEVY EPEWPGRDEA 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 QNLNDVLVSL EKQHGSNTFT VKAQPSDSAP EKGNKSPSPP 

       310        320        330        340        350        360 
PDGSPAATPE IRVNHEPEPA SGASPGATIP KSPSQLRKGP PVPPPPKHTP SKEMKQEQIL 

       370        380        390        400        410        420 
SLFDDAFVPE ISVTTPSQFE APGPFSEQAS LLDLDFEPLP PVASPVKAPT PSGQSIPWDL 

       430        440        450        460        470        480 
WEPTESQAGV LPSGEPSSAE GSFAVAWPSQ TAEPGPAQPA EASEVVGGTQ EPGETAASEA 

       490        500        510        520        530        540 
TSSSLPAVVV ETFSATVNGA VEGSTTTGRL DLPPGFMFKV QAQHDYTATD TDELQLKAGD 

       550        560        570        580 
VVLVIPFQNP EEQDEGWLMG VKESDWNQHK ELEKCRGVFP ENFTERVQ

« Hide

Isoform AMPH2-2 [UniParc].

Checksum: EABCC9BFA01853A3
Show »

FASTA55060,857
Isoform AMPH2-3 [UniParc].

Checksum: 7DFCA41A3235D22E
Show »

FASTA33437,377
Isoform AMPH2-4 [UniParc].

Checksum: A780685B678CD85B
Show »

FASTA21925,238
Isoform AMPH2-5 [UniParc].

Checksum: 63E65E87050D4DF4
Show »

FASTA44049,143
Isoform AMPH2-6 [UniParc].

Checksum: 046474D7A2E23EDB
Show »

FASTA40745,506

References

[1]"Amphiphysin heterodimers: potential role in clathrin-mediated endocytosis."
Wigge P., Koehler K., Vallis Y., Doyle C., Owen D., Hunt S.P., McMahon H.T.
Mol. Biol. Cell 8:2003-2015(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, ALTERNATIVE SPLICING.
Strain: Sprague-Dawley.
Tissue: Brain cortex and Kidney.
[2]"Clathrin interacts specifically with amphiphysin and is displaced by dynamin."
McMahon H.T., Wigge P., Smith C.
FEBS Lett. 413:319-322(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM AMPH2-1).
Strain: Sprague-Dawley.
Tissue: Brain cortex.
[3]Lubec G., Chen W.-Q., Kang S.U., Lubec S.
Submitted (SEP-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 155-164; 190-202; 510-537 AND 577-586, MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain and Hippocampus.
[4]"A structural explanation for the binding of multiple ligands by the alpha-adaptin appendage domain."
Owen D.J., Vallis Y., Noble M.E.M., Hunter J.B., Dafforn T.R., Evans P.R., McMahon H.T.
Cell 97:805-815(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AP2A2.
[5]"Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly."
Traub L.M., Downs M.A., Westrich J.L., Fremont D.H.
Proc. Natl. Acad. Sci. U.S.A. 96:8907-8912(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AP2A2.
[6]"Molecular switches involving the AP-2 beta2 appendage regulate endocytic cargo selection and clathrin coat assembly."
Edeling M.A., Mishra S.K., Keyel P.A., Steinhauser A.L., Collins B.M., Roth R., Heuser J.E., Owen D.J., Traub L.M.
Dev. Cell 10:329-342(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AP2B1.
[7]"Crystal structure of the amphiphysin-2 SH3 domain and its role in the prevention of dynamin ring formation."
Owen D.J., Wigge P., Vallis Y., Moore J.D.A., Evans P.R., McMahon H.T.
EMBO J. 17:5273-5285(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 506-588, FUNCTION, INTERACTION WITH DNM1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y13380 mRNA. Translation: CAA73807.1.
IPIIPI00196509.
IPI00231388.
IPI00231389.
IPI00231390.
IPI00231391.
IPI00555232.
RefSeqNP_446411.1. NM_053959.1.
UniGeneRn.17098.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BB9X-ray2.20A495-588[»]
ProteinModelPortalO08839.
ModBaseSearch...

Protein-protein interaction databases

IntActO08839. 3 interactions.
MINTMINT-101225.
STRING10116.ENSRNOP00000017573.

PTM databases

PhosphoSiteO08839.

Proteomic databases

PaxDbO08839.
PRIDEO08839.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID117028.
KEGGrno:117028.
UCSCRGD:621786. rat.

Organism-specific databases

CTD274.
RGD621786. Bin1.

Phylogenomic databases

eggNOGNOG264615.
HOGENOMHOG000252987.
HOVERGENHBG004224.
InParanoidO08839.
OrthoDBEOG4G4GQ2.

Gene expression databases

ArrayExpressO08839.
GenevestigatorO08839.
GermOnlineENSRNOG00000012852. Rattus norvegicus.

Family and domain databases

Gene3D1.20.1270.60. 2 hits.
InterProIPR027267. AH/BAR-dom.
IPR003005. Amphiphysin.
IPR003023. Amphiphysin_2.
IPR004148. BAR_dom.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamPF03114. BAR. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
PRINTSPR01251. AMPHIPHYSIN.
PR01253. AMPHIPHYSIN2.
PR00452. SH3DOMAIN.
SMARTSM00721. BAR. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SH3. 1 hit.
PROSITEPS51021. BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO08839.
NextBio619805.

Entry information

Entry nameBIN1_RAT
AccessionPrimary (citable) accession number: O08839
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: July 1, 1997
Last modified: May 1, 2013
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents