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Protein

Amphiphysin

Gene

Amph

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  1. protein complex binding Source: RGD
  2. protein C-terminus binding Source: RGD
  3. protein heterodimerization activity Source: RGD

GO - Biological processi

  1. positive regulation of endocytosis Source: RGD
  2. positive regulation of GTPase activity Source: RGD
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Amphiphysin
Gene namesi
Name:Amph
Synonyms:Amph1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620274. Amph.

Subcellular locationi

GO - Cellular componenti

  1. axon terminus Source: RGD
  2. cell junction Source: UniProtKB-KW
  3. cytoskeleton Source: UniProtKB-SubCell
  4. synaptic vesicle membrane Source: UniProtKB-SubCell
  5. terminal bouton Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 683683AmphiphysinPRO_0000192949Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei496 – 4961PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO08838.
PRIDEiO08838.

PTM databases

PhosphoSiteiO08838.

Expressioni

Gene expression databases

GenevestigatoriO08838.

Interactioni

Subunit structurei

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.By similarity4 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi248889. 18 interactions.
DIPiDIP-30977N.
IntActiO08838. 7 interactions.
MINTiMINT-101171.
STRINGi10116.ENSRNOP00000017102.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VJ0X-ray1.60Q324-330[»]
ProteinModelPortaliO08838.
SMRiO08838. Positions 35-234, 604-683.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO08838.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 240217BARPROSITE-ProRule annotationAdd
BLAST
Domaini610 – 68374SH3PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili10 – 8374Sequence AnalysisAdd
BLAST
Coiled coili144 – 19148Sequence 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.
HOGENOMiHOG000252987.
HOVERGENiHBG004224.
InParanoidiO08838.
KOiK12562.
PhylomeDBiO08838.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR003005. Amphiphysin.
IPR003017. Amphiphysin_1.
IPR004148. BAR_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF03114. BAR. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR01251. AMPHIPHYSIN.
PR01252. AMPHIPHYSIN1.
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]

Sequencei

Sequence statusi: Complete.

O08838-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADIKTGIFA KNVQKRLNRA QEKVLQKLGK ADETKDEQFE EYVQNFKRQE
60 70 80 90 100
AEGTRLQREL RGYLAAIKGM QEASMKLTES LHEVYEPDWY GREDVKMVGE
110 120 130 140 150
KCDVLWEDFH QKLVDGSLLT LDTYLGQFPD IKNRIAKRSR KLVDYDSARH
160 170 180 190 200
HLEALQSSKR KDESRISKAE EEFQKAQKVF EEFNVDLQEE LPSLWSRRVG
210 220 230 240 250
FYVNTFKNVS SLEAKFHKEI AVLCHKLYEV MTKLGDQHAD KAFSIQGAPS
260 270 280 290 300
DSGPLRIAKT PSPPEEASPL PSPTASPNHT LAPASPAPVR PRSPSQTRKG
310 320 330 340 350
PPVPPLPKVT PTKELQQENI INFFEDNFVP EINVTTPSQN EVLEVKKEET
360 370 380 390 400
LLDLDFDPFK PDVTPAGSAA ATHSPMSQTL PWDLWTTSTD LVQPASGGSF
410 420 430 440 450
NDFTQPQDTS LFTMQTDQNM AETEQALPTE PQAEEPPTTA AAPTAGLDLG
460 470 480 490 500
LEMEEPKEEA AIPPGTDAGE TVGTEGSTGE EAEAEKAALP AGEGESPEGA
510 520 530 540 550
KIDVESTELA SSESPQAAEL EAGAPQEKVI PSVVIEPASN HEGEEHQETT
560 570 580 590 600
TGTETREATE DVAPQGPAGE KQELATEPTP LDSQAATPAP AGAVDASLSA
610 620 630 640 650
GDAAQELPPG FLYKVETLHD FEAANSDELT LQRGDVVLVV PSDSEADQDA
660 670 680
GWLVGVKESD WLQYRDLATY KGLFPENFTR HLE
Length:683
Mass (Da):74,878
Last modified:June 30, 1997 - v1
Checksum:i7FEA4A9E5A1F6631
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13381 mRNA. Translation: CAA73808.1.
RefSeqiNP_071553.1. NM_022217.1.
UniGeneiRn.44463.

Genome annotation databases

GeneIDi60668.
KEGGirno:60668.
UCSCiRGD:620274. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13381 mRNA. Translation: CAA73808.1.
RefSeqiNP_071553.1. NM_022217.1.
UniGeneiRn.44463.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VJ0X-ray1.60Q324-330[»]
ProteinModelPortaliO08838.
SMRiO08838. Positions 35-234, 604-683.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248889. 18 interactions.
DIPiDIP-30977N.
IntActiO08838. 7 interactions.
MINTiMINT-101171.
STRINGi10116.ENSRNOP00000017102.

PTM databases

PhosphoSiteiO08838.

Proteomic databases

PaxDbiO08838.
PRIDEiO08838.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi60668.
KEGGirno:60668.
UCSCiRGD:620274. rat.

Organism-specific databases

CTDi273.
RGDi620274. Amph.

Phylogenomic databases

eggNOGiNOG264615.
HOGENOMiHOG000252987.
HOVERGENiHBG004224.
InParanoidiO08838.
KOiK12562.
PhylomeDBiO08838.

Miscellaneous databases

EvolutionaryTraceiO08838.
NextBioi612393.
PROiO08838.

Gene expression databases

GenevestigatoriO08838.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR003005. Amphiphysin.
IPR003017. Amphiphysin_1.
IPR004148. BAR_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF03114. BAR. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR01251. AMPHIPHYSIN.
PR01252. AMPHIPHYSIN1.
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

  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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brain cortex.
  2. Lubec G., Chen W.-Q.
    Submitted (MAR-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(1998) [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(1998) [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(2005) [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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AP2B1.

Entry informationi

Entry nameiAMPH_RAT
AccessioniPrimary (citable) accession number: O08838
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2001
Last sequence update: June 30, 1997
Last modified: March 3, 2015
This is version 119 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

External Data

Dasty 3

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 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.