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O08838 (AMPH_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Amphiphysin
Gene names
Name:Amph
Synonyms:Amph1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length683 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May participate in mechanisms of regulated exocytosis in synapses and certain endocrine cell types. May control the properties of the membrane associated cytoskeleton By similarity.

Subunit structure

Heterodimer with BIN1. Binds SH3GLB1 By similarity. Interacts with REPS1 and SGIP1; may be involved in clathrin-mediated endocytosis By similarity. Binds AP2A2. Interacts with AP2B1. Ref.3 Ref.4 Ref.5 Ref.6

Subcellular location

Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasmcytoskeleton By similarity.

Sequence similarities

Contains 1 BAR domain.

Contains 1 SH3 domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Bin1O088392EBI-80080,EBI-80095
Dnm1P215753EBI-80080,EBI-80070
Dnm2P390522EBI-80080,EBI-349613
Necap1Q9CR957EBI-80080,EBI-7592476From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 683683Amphiphysin
PRO_0000192949

Regions

Domain24 – 240217BAR
Domain610 – 68374SH3
Coiled coil10 – 8374 Potential
Coiled coil144 – 19148 Potential

Amino acid modifications

Modified residue4961Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
O08838 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 7FEA4A9E5A1F6631

FASTA68374,878
        10         20         30         40         50         60 
MADIKTGIFA KNVQKRLNRA QEKVLQKLGK ADETKDEQFE EYVQNFKRQE AEGTRLQREL 

        70         80         90        100        110        120 
RGYLAAIKGM QEASMKLTES LHEVYEPDWY GREDVKMVGE KCDVLWEDFH QKLVDGSLLT 

       130        140        150        160        170        180 
LDTYLGQFPD IKNRIAKRSR KLVDYDSARH HLEALQSSKR KDESRISKAE EEFQKAQKVF 

       190        200        210        220        230        240 
EEFNVDLQEE LPSLWSRRVG FYVNTFKNVS SLEAKFHKEI AVLCHKLYEV MTKLGDQHAD 

       250        260        270        280        290        300 
KAFSIQGAPS DSGPLRIAKT PSPPEEASPL PSPTASPNHT LAPASPAPVR PRSPSQTRKG 

       310        320        330        340        350        360 
PPVPPLPKVT PTKELQQENI INFFEDNFVP EINVTTPSQN EVLEVKKEET LLDLDFDPFK 

       370        380        390        400        410        420 
PDVTPAGSAA ATHSPMSQTL PWDLWTTSTD LVQPASGGSF NDFTQPQDTS LFTMQTDQNM 

       430        440        450        460        470        480 
AETEQALPTE PQAEEPPTTA AAPTAGLDLG LEMEEPKEEA AIPPGTDAGE TVGTEGSTGE 

       490        500        510        520        530        540 
EAEAEKAALP AGEGESPEGA KIDVESTELA SSESPQAAEL EAGAPQEKVI PSVVIEPASN 

       550        560        570        580        590        600 
HEGEEHQETT TGTETREATE DVAPQGPAGE KQELATEPTP LDSQAATPAP AGAVDASLSA 

       610        620        630        640        650        660 
GDAAQELPPG FLYKVETLHD FEAANSDELT LQRGDVVLVV PSDSEADQDA GWLVGVKESD 

       670        680 
WLQYRDLATY KGLFPENFTR HLE 

« Hide

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].
Strain: Sprague-Dawley.
Tissue: Brain cortex.
[2]Lubec G., Chen W.-Q.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 198-207; 242-256 AND 615-633, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus.
[3]"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.
[4]"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.
[5]"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.
[6]"Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly."
Schmid E.M., Ford M.G.J., Burtey A., Praefcke G.J.K., Peak-Chew S.-Y., Mills I.G., Benmerah A., McMahon H.T.
PLoS Biol. 4:E262-E262(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AP2B1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y13381 mRNA. Translation: CAA73808.1.
RefSeqNP_071553.1. NM_022217.1.
UniGeneRn.44463.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2VJ0X-ray1.60Q324-330[»]
ProteinModelPortalO08838.
SMRO08838. Positions 35-234, 604-683.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248889. 18 interactions.
DIPDIP-30977N.
IntActO08838. 7 interactions.
MINTMINT-101171.
STRING10116.ENSRNOP00000017102.

PTM databases

PhosphoSiteO08838.

Proteomic databases

PaxDbO08838.
PRIDEO08838.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID60668.
KEGGrno:60668.
UCSCRGD:620274. rat.

Organism-specific databases

CTD273.
RGD620274. Amph.

Phylogenomic databases

eggNOGNOG264615.
HOGENOMHOG000252987.
HOVERGENHBG004224.
InParanoidO08838.
KOK12562.
PhylomeDBO08838.

Gene expression databases

GenevestigatorO08838.

Family and domain databases

Gene3D1.20.1270.60. 1 hit.
InterProIPR027267. AH/BAR-dom.
IPR003005. Amphiphysin.
IPR003017. Amphiphysin_1.
IPR004148. BAR_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamPF03114. BAR. 1 hit.
[Graphical view]
PRINTSPR01251. AMPHIPHYSIN.
PR01252. AMPHIPHYSIN1.
PR00452. SH3DOMAIN.
SMARTSM00721. BAR. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS51021. BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO08838.
NextBio612393.
PROO08838.

Entry information

Entry nameAMPH_RAT
AccessionPrimary (citable) accession number: O08838
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: July 1, 1997
Last modified: April 16, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references