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Protein

Myc box-dependent-interacting protein 1

Gene

Bin1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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.1 Publication

GO - Molecular functioni

  • GTPase binding Source: RGD
  • protein complex binding Source: RGD
  • protein heterodimerization activity Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Endocytosis

Names & Taxonomyi

Protein namesi
Recommended name:
Myc box-dependent-interacting protein 1
Alternative name(s):
Amphiphysin II
Amphiphysin-like protein
Bridging integrator 1
Gene namesi
Name:Bin1
Synonyms:Amph2, Amphl
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621786. Bin1.

Subcellular locationi

GO - Cellular componenti

  • axon Source: Alzheimers_University_of_Toronto
  • axon initial segment Source: Alzheimers_University_of_Toronto
  • axon terminus Source: RGD
  • cerebellar mossy fiber Source: RGD
  • I band Source: Alzheimers_University_of_Toronto
  • lipid tube Source: Alzheimers_University_of_Toronto
  • microtubule Source: Alzheimers_University_of_Toronto
  • node of Ranvier Source: Alzheimers_University_of_Toronto
  • nucleus Source: UniProtKB-SubCell
  • synaptic vesicle Source: RGD
  • T-tubule Source: Alzheimers_University_of_Toronto
  • varicosity Source: RGD
  • Z disc Source: Alzheimers_University_of_Toronto
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 588587Myc box-dependent-interacting protein 1PRO_0000192953Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei296 – 2961PhosphoserineBy similarity
Modified residuei298 – 2981PhosphoserineCombined sources
Modified residuei304 – 3041PhosphoserineCombined sources
Modified residuei308 – 3081PhosphothreonineCombined sources
Modified residuei324 – 3241PhosphoserineCombined sources
Modified residuei332 – 3321PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by protein kinase C.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiO08839.
PRIDEiO08839.

PTM databases

iPTMnetiO08839.
PhosphoSiteiO08839.

Expressioni

Tissue specificityi

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

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
AmphO088382EBI-80095,EBI-80080
Dnm1P215752EBI-80095,EBI-80070
Necap1Q9CR958EBI-80095,EBI-7592476From a different organism.

GO - Molecular functioni

  • GTPase binding Source: RGD
  • protein complex binding Source: RGD
  • protein heterodimerization activity Source: RGD

Protein-protein interaction databases

BioGridi250629. 13 interactions.
DIPiDIP-30979N.
IntActiO08839. 8 interactions.
MINTiMINT-101225.
STRINGi10116.ENSRNOP00000017573.

Structurei

Secondary structure

1
588
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi518 – 5247Combined sources
Beta strandi541 – 5455Combined sources
Helixi550 – 5523Combined sources
Beta strandi557 – 5626Combined sources
Helixi563 – 5675Combined sources
Helixi572 – 5754Combined sources
Beta strandi577 – 5804Combined sources
Helixi581 – 5833Combined sources
Beta strandi584 – 5874Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BB9X-ray2.20A495-588[»]
ProteinModelPortaliO08839.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO08839.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 276248BARPROSITE-ProRule annotationAdd
BLAST
Domaini515 – 58874SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 122121Interaction with BIN2By similarityAdd
BLAST
Regioni379 – 42244Clathrin-bindingBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili15 – 4228Sequence analysisAdd
BLAST
Coiled coili193 – 27482Sequence 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

eggNOGiENOG410ITR4. Eukaryota.
ENOG410XQXT. LUCA.
HOGENOMiHOG000252987.
HOVERGENiHBG004224.
InParanoidiO08839.
KOiK12562.
PhylomeDBiO08839.

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 (6)i

Sequence statusi: Complete.

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

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform AMPH2-1 (identifier: O08839-1) [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 KLSECLQEVY EPEWPGRDEA
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 QNLNDVLVSL EKQHGSNTFT VKAQPSDSAP EKGNKSPSPP
310 320 330 340 350
PDGSPAATPE IRVNHEPEPA SGASPGATIP KSPSQLRKGP PVPPPPKHTP
360 370 380 390 400
SKEMKQEQIL SLFDDAFVPE ISVTTPSQFE APGPFSEQAS LLDLDFEPLP
410 420 430 440 450
PVASPVKAPT PSGQSIPWDL WEPTESQAGV LPSGEPSSAE GSFAVAWPSQ
460 470 480 490 500
TAEPGPAQPA EASEVVGGTQ EPGETAASEA TSSSLPAVVV ETFSATVNGA
510 520 530 540 550
VEGSTTTGRL DLPPGFMFKV QAQHDYTATD TDELQLKAGD VVLVIPFQNP
560 570 580
EEQDEGWLMG VKESDWNQHK ELEKCRGVFP ENFTERVQ
Length:588
Mass (Da):64,533
Last modified:July 1, 1997 - v1
Checksum:i164AC90E09547F1A
GO
Isoform AMPH2-2 (identifier: O08839-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     423-460: Missing.

Show »
Length:550
Mass (Da):60,857
Checksum:iEABCC9BFA01853A3
GO
Isoform AMPH2-3 (identifier: O08839-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     335-588: Missing.

Show »
Length:334
Mass (Da):37,377
Checksum:i7DFCA41A3235D22E
GO
Isoform AMPH2-4 (identifier: O08839-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     173-205: Missing.
     253-588: Missing.

Show »
Length:219
Mass (Da):25,238
Checksum:iA780685B678CD85B
GO
Isoform AMPH2-5 (identifier: O08839-5) [UniParc]FASTAAdd to basket

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

Show »
Length:440
Mass (Da):49,143
Checksum:i63E65E87050D4DF4
GO
Isoform AMPH2-6 (identifier: O08839-6) [UniParc]FASTAAdd to basket

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

Show »
Length:407
Mass (Da):45,506
Checksum:i046474D7A2E23EDB
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei173 – 20533Missing in isoform AMPH2-4 and isoform AMPH2-6. CuratedVSP_000256Add
BLAST
Alternative sequencei253 – 588336Missing in isoform AMPH2-4. CuratedVSP_000257Add
BLAST
Alternative sequencei335 – 588254Missing in isoform AMPH2-3. CuratedVSP_000258Add
BLAST
Alternative sequencei335 – 482148Missing in isoform AMPH2-5 and isoform AMPH2-6. CuratedVSP_000259Add
BLAST
Alternative sequencei423 – 46038Missing in isoform AMPH2-2. CuratedVSP_000260Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13380 mRNA. Translation: CAA73807.1.
RefSeqiNP_446411.1. NM_053959.1. [O08839-1]
UniGeneiRn.17098.

Genome annotation databases

GeneIDi117028.
KEGGirno:117028.
UCSCiRGD:621786. rat. [O08839-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13380 mRNA. Translation: CAA73807.1.
RefSeqiNP_446411.1. NM_053959.1. [O08839-1]
UniGeneiRn.17098.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BB9X-ray2.20A495-588[»]
ProteinModelPortaliO08839.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250629. 13 interactions.
DIPiDIP-30979N.
IntActiO08839. 8 interactions.
MINTiMINT-101225.
STRINGi10116.ENSRNOP00000017573.

PTM databases

iPTMnetiO08839.
PhosphoSiteiO08839.

Proteomic databases

PaxDbiO08839.
PRIDEiO08839.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi117028.
KEGGirno:117028.
UCSCiRGD:621786. rat. [O08839-1]

Organism-specific databases

CTDi274.
RGDi621786. Bin1.

Phylogenomic databases

eggNOGiENOG410ITR4. Eukaryota.
ENOG410XQXT. LUCA.
HOGENOMiHOG000252987.
HOVERGENiHBG004224.
InParanoidiO08839.
KOiK12562.
PhylomeDBiO08839.

Miscellaneous databases

EvolutionaryTraceiO08839.
PROiO08839.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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, IDENTIFICATION BY 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. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298; SER-304; THR-308 AND SER-324, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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.

Entry informationi

Entry nameiBIN1_RAT
AccessioniPrimary (citable) accession number: O08839
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: July 1, 1997
Last modified: June 8, 2016
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.