Amphiphysin - Rattus norvegicus (Rat)

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O08838 (AMPH_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 107. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Amphiphysin

Gene names

Name:	Amph
Synonyms:	Amph1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	683 AA.
Sequence status	Complete.
Protein existence	Evidence 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 vesicle › secretory vesicle › synaptic vesicle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasm › cytoskeleton By similarity.
Sequence similarities	Contains 1 BAR domain. Contains 1 SH3 domain.

Ontologies

Keywords
Cellular component	Cell junction Cytoplasm Cytoplasmic vesicle Cytoskeleton Membrane Synapse
Domain	Coiled coil SH3 domain
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of GTPase activity Inferred from direct assay Ref.1. Source: RGD positive regulation of endocytosis Inferred from mutant phenotype Ref.1. Source: RGD
Cellular_component	axon terminus Inferred from direct assay Ref.1. Source: RGD cell junction Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell synaptic vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Bin1	O08839	2	EBI-80080,EBI-80095

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 683

683

Amphiphysin

PRO_0000192949

Regions

Domain

24 – 240

217

BAR

Domain

610 – 683

SH3

Coiled coil

10 – 83

Potential

Coiled coil

144 – 191

Potential

Amino acid modifications

Modified residue

250

Phosphoserine By similarity

Modified residue

295

Phosphoserine By similarity

Modified residue

297

Phosphothreonine By similarity

Modified residue

496

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

O08838 [UniParc].

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

FASTA

683

74,878

        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, 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.

IPI

IPI00196508.

RefSeq

NP_071553.1. NM_022217.1.

UniGene

Rn.44463.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2VJ0	X-ray	1.60	Q	324-330	[»]

ProteinModelPortal

O08838.

SMR

O08838. Positions 35-234, 604-683.

ModBase

Search...

Protein-protein interaction databases

IntAct

O08838. 2 interactions.

MINT

MINT-101171.

STRING

10116.ENSRNOP00000017102.

PTM databases

PhosphoSite

O08838.

Proteomic databases

PaxDb

O08838.

PRIDE

O08838.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

60668.

KEGG

rno:60668.

UCSC

RGD:620274. rat.

Organism-specific databases

CTD

273.

RGD

620274. Amph.

Phylogenomic databases

eggNOG

NOG264615.

HOGENOM

HOG000252987.

HOVERGEN

HBG004224.

InParanoid

O08838.

K12562.

OrthoDB

EOG49078R.

Gene expression databases

ArrayExpress

O08838.

Genevestigator

O08838.

GermOnline

ENSRNOG00000012490. Rattus norvegicus.

Family and domain databases

Gene3D

1.20.1270.60. 1 hit.

InterPro

IPR027267. AH/BAR-dom.
IPR003005. Amphiphysin.
IPR003017. Amphiphysin_1.
IPR004148. BAR_dom.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]

Pfam

PF03114. BAR. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]

PRINTS

PR01251. AMPHIPHYSIN.
PR01252. AMPHIPHYSIN1.
PR00452. SH3DOMAIN.

SMART

SM00721. BAR. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF50044. SH3. 1 hit.

PROSITE

PS51021. BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O08838.

NextBio

612393.

Entry information

Entry name

AMPH_RAT

Accession

Primary (citable) accession number: O08838

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2001
Last sequence update:	July 1, 1997
Last modified:	May 1, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents