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O08838

- AMPH_RAT

UniProt

O08838 - AMPH_RAT

Protein

Amphiphysin

Gene

Amph

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    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 binding Source: IntAct
    2. protein complex binding Source: RGD
    3. protein C-terminus binding Source: RGD
    4. protein heterodimerization activity Source: RGD

    GO - Biological processi

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

    Names & Taxonomyi

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

    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:
    PDBe
    RCSB PDB
    PDBj
    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

    MADIKTGIFA KNVQKRLNRA QEKVLQKLGK ADETKDEQFE EYVQNFKRQE    50
    AEGTRLQREL RGYLAAIKGM QEASMKLTES LHEVYEPDWY GREDVKMVGE 100
    KCDVLWEDFH QKLVDGSLLT LDTYLGQFPD IKNRIAKRSR KLVDYDSARH 150
    HLEALQSSKR KDESRISKAE EEFQKAQKVF EEFNVDLQEE LPSLWSRRVG 200
    FYVNTFKNVS SLEAKFHKEI AVLCHKLYEV MTKLGDQHAD KAFSIQGAPS 250
    DSGPLRIAKT PSPPEEASPL PSPTASPNHT LAPASPAPVR PRSPSQTRKG 300
    PPVPPLPKVT PTKELQQENI INFFEDNFVP EINVTTPSQN EVLEVKKEET 350
    LLDLDFDPFK PDVTPAGSAA ATHSPMSQTL PWDLWTTSTD LVQPASGGSF 400
    NDFTQPQDTS LFTMQTDQNM AETEQALPTE PQAEEPPTTA AAPTAGLDLG 450
    LEMEEPKEEA AIPPGTDAGE TVGTEGSTGE EAEAEKAALP AGEGESPEGA 500
    KIDVESTELA SSESPQAAEL EAGAPQEKVI PSVVIEPASN HEGEEHQETT 550
    TGTETREATE DVAPQGPAGE KQELATEPTP LDSQAATPAP AGAVDASLSA 600
    GDAAQELPPG FLYKVETLHD FEAANSDELT LQRGDVVLVV PSDSEADQDA 650
    GWLVGVKESD WLQYRDLATY KGLFPENFTR HLE 683
    Length:683
    Mass (Da):74,878
    Last modified:July 1, 1997 - v1
    Checksum:i7FEA4A9E5A1F6631
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y13381 mRNA. Translation: CAA73808.1 .
    RefSeqi NP_071553.1. NM_022217.1.
    UniGenei Rn.44463.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2VJ0 X-ray 1.60 Q 324-330 [» ]
    ProteinModelPortali O08838.
    SMRi O08838. Positions 35-234, 604-683.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 248889. 18 interactions.
    DIPi DIP-30977N.
    IntActi O08838. 7 interactions.
    MINTi MINT-101171.
    STRINGi 10116.ENSRNOP00000017102.

    PTM databases

    PhosphoSitei O08838.

    Proteomic databases

    PaxDbi O08838.
    PRIDEi O08838.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 60668.
    KEGGi rno:60668.
    UCSCi RGD:620274. rat.

    Organism-specific databases

    CTDi 273.
    RGDi 620274. Amph.

    Phylogenomic databases

    eggNOGi NOG264615.
    HOGENOMi HOG000252987.
    HOVERGENi HBG004224.
    InParanoidi O08838.
    KOi K12562.
    PhylomeDBi O08838.

    Miscellaneous databases

    EvolutionaryTracei O08838.
    NextBioi 612393.
    PROi O08838.

    Gene expression databases

    Genevestigatori O08838.

    Family and domain databases

    Gene3Di 1.20.1270.60. 1 hit.
    InterProi IPR027267. AH/BAR-dom.
    IPR003005. Amphiphysin.
    IPR003017. Amphiphysin_1.
    IPR004148. BAR_dom.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF03114. BAR. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view ]
    PRINTSi PR01251. AMPHIPHYSIN.
    PR01252. AMPHIPHYSIN1.
    PR00452. SH3DOMAIN.
    SMARTi SM00721. BAR. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    PROSITEi PS51021. BAR. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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(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.

    Entry informationi

    Entry nameiAMPH_RAT
    AccessioniPrimary (citable) accession number: O08838
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2001
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 116 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