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Q9P0L0

- VAPA_HUMAN

UniProt

Q9P0L0 - VAPA_HUMAN

Protein

Vesicle-associated membrane protein-associated protein A

Gene

VAPA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 3 (09 Jan 2007)
      Previous versions | rss
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    Functioni

    May play a role in vesicle trafficking.2 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein heterodimerization activity Source: UniProtKB
    3. signal transducer activity Source: UniProtKB
    4. structural molecule activity Source: InterPro

    GO - Biological processi

    1. cell death Source: UniProtKB
    2. membrane fusion Source: ProtInc
    3. neuron projection development Source: UniProtKB
    4. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    5. protein localization to endoplasmic reticulum Source: UniProtKB
    6. signal transduction Source: GOC
    7. small molecule metabolic process Source: Reactome
    8. sphingolipid biosynthetic process Source: Reactome
    9. sphingolipid metabolic process Source: Reactome

    Enzyme and pathway databases

    ReactomeiREACT_115810. Sphingolipid de novo biosynthesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Vesicle-associated membrane protein-associated protein A
    Short name:
    VAMP-A
    Short name:
    VAMP-associated protein A
    Short name:
    VAP-A
    Alternative name(s):
    33 kDa VAMP-associated protein
    Short name:
    VAP-33
    Gene namesi
    Name:VAPA
    Synonyms:VAP33
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:12648. VAPA.

    Subcellular locationi

    Endoplasmic reticulum membrane 2 Publications; Single-pass type IV membrane protein 2 Publications
    Note: Present in the plasma membrane and in intracellular vesicles, together with SNARE proteins. May also associate with the cytoskeleton. Colocalizes with OCLN at the tight junction in polarized epithelial cells.

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. endoplasmic reticulum membrane Source: Reactome
    3. integral component of membrane Source: UniProtKB-KW
    4. microtubule Source: Ensembl
    5. plasma membrane Source: UniProtKB
    6. vesicle Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi94 – 941K → D: Alters interaction with ZFYVE27; when associated with D-96. 1 Publication
    Mutagenesisi96 – 961M → D: Alters interaction with ZFYVE27; when associated with D-94. 1 Publication

    Organism-specific databases

    PharmGKBiPA37272.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 249249Vesicle-associated membrane protein-associated protein APRO_0000213470Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei125 – 1251N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9P0L0.
    PaxDbiQ9P0L0.
    PRIDEiQ9P0L0.

    PTM databases

    PhosphoSiteiQ9P0L0.

    Miscellaneous databases

    PMAP-CutDBQ9P0L0.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ9P0L0.
    BgeeiQ9P0L0.
    CleanExiHS_VAPA.
    GenevestigatoriQ9P0L0.

    Organism-specific databases

    HPAiHPA009174.

    Interactioni

    Subunit structurei

    Homodimer, and heterodimer with VAPB. Interacts with VAMP1, VAMP2, STX1A, BET1, SEC22C and with the C-terminal domain of OCLN. Interacts with OSBPL1A. Interacts (via MSP domain) with ZFYVE27; may retain ZFYVE27 in the endoplasmic reticulum and regulate its function in cell projections formation. Interacts with OSBP. Interacts (via C-terminus) with RSAD2/viperin (via C-terminus). Interacts with HCV protein NS5A and NS5B. Interacts with IFITM3.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P279585EBI-1059156,EBI-6904388From a different organism.
    Q034634EBI-1059156,EBI-8803426From a different organism.
    EGFRP005332EBI-1059156,EBI-297353
    OPRM1P353723EBI-1059156,EBI-2624570
    VAPBO95292-12EBI-1059156,EBI-9350848
    ZFYVE27Q5T4F45EBI-1059156,EBI-3892947

    Protein-protein interaction databases

    BioGridi114651. 40 interactions.
    DIPiDIP-41135N.
    IntActiQ9P0L0. 45 interactions.
    MINTiMINT-109415.
    STRINGi9606.ENSP00000345656.

    Structurei

    Secondary structure

    1
    249
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi14 – 218
    Beta strandi23 – 275
    Beta strandi33 – 408
    Beta strandi43 – 453
    Beta strandi47 – 548
    Turni56 – 583
    Beta strandi59 – 635
    Beta strandi65 – 684
    Beta strandi73 – 808
    Beta strandi94 – 1018
    Helixi109 – 1157
    Turni118 – 1203
    Beta strandi122 – 13110

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2RR3NMR-A11-135[»]
    ProteinModelPortaliQ9P0L0.
    SMRiQ9P0L0. Positions 9-135.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9P0L0.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 227227CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei228 – 24821Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini14 – 131118MSPPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili169 – 20537Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 MSP domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5066.
    HOGENOMiHOG000293182.
    HOVERGENiHBG028551.
    KOiK06096.
    OMAiNPIDELE.
    OrthoDBiEOG7CK389.
    PhylomeDBiQ9P0L0.
    TreeFamiTF317024.

    Family and domain databases

    Gene3Di2.60.40.360. 1 hit.
    InterProiIPR000535. MSP_dom.
    IPR008962. PapD-like.
    IPR016763. Vesicle-associated_membrane.
    [Graphical view]
    PfamiPF00635. Motile_Sperm. 1 hit.
    [Graphical view]
    PIRSFiPIRSF019693. VAMP-associated. 1 hit.
    SUPFAMiSSF49354. SSF49354. 1 hit.
    PROSITEiPS50202. MSP. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9P0L0-1) [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

    MASASGAMAK HEQILVLDPP TDLKFKGPFT DVVTTNLKLR NPSDRKVCFK    50
    VKTTAPRRYC VRPNSGIIDP GSTVTVSVML QPFDYDPNEK SKHKFMVQTI 100
    FAPPNTSDME AVWKEAKPDE LMDSKLRCVF EMPNENDKLN DMEPSKAVPL 150
    NASKQDGPMP KPHSVSLNDT ETRKLMEECK RLQGEMMKLS EENRHLRDEG 200
    LRLRKVAHSD KPGSTSTASF RDNVTSPLPS LLVVIAAIFI GFFLGKFIL 249
    Length:249
    Mass (Da):27,893
    Last modified:January 9, 2007 - v3
    Checksum:i68B603F3A9FA5475
    GO
    Isoform 2 (identifier: Q9P0L0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         139-139: L → LGITPPGNAPTVTSMSSINNTVATPASYHTKDDPRGLSVLKQEKQK

    Show »
    Length:294
    Mass (Da):32,614
    Checksum:i8B2D033706621878
    GO

    Sequence cautioni

    The sequence BG488667 differs from that shown. Reason: Frameshift at positions 72, 207 and 241.
    The sequence AAD09742.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAF72105.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 112KH → ND in AAC26508. (PubMed:9657962)Curated
    Sequence conflicti10 – 112KH → ND in AAV38424. 1 PublicationCurated
    Sequence conflicti160 – 1601P → S in AAF72105. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti8 – 81M → T.
    Corresponds to variant rs1044163 [ dbSNP | Ensembl ].
    VAR_050440
    Natural varianti104 – 1041P → L.
    Corresponds to variant rs1127666 [ dbSNP | Ensembl ].
    VAR_050441

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei139 – 1391L → LGITPPGNAPTVTSMSSINN TVATPASYHTKDDPRGLSVL KQEKQK in isoform 2. 1 PublicationVSP_038648

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF044670 mRNA. Translation: AAD09742.1. Different initiation.
    AF154847 mRNA. Translation: AAF72105.1. Different initiation.
    AC006238 Genomic DNA. No translation available.
    CH471113 Genomic DNA. Translation: EAX01591.1.
    CH471113 Genomic DNA. Translation: EAX01592.1.
    BC002992 mRNA. Translation: AAH02992.2.
    BG488667 mRNA. No translation available.
    AF057358 mRNA. Translation: AAC26508.1.
    AF086627 mRNA. Translation: AAD13576.1.
    BT019618 mRNA. Translation: AAV38424.1.
    CCDSiCCDS11847.2. [Q9P0L0-2]
    CCDS11848.2. [Q9P0L0-1]
    RefSeqiNP_003565.4. NM_003574.5. [Q9P0L0-2]
    NP_919415.2. NM_194434.2. [Q9P0L0-1]
    UniGeneiHs.165195.

    Genome annotation databases

    EnsembliENST00000340541; ENSP00000345656; ENSG00000101558. [Q9P0L0-2]
    ENST00000400000; ENSP00000382880; ENSG00000101558. [Q9P0L0-1]
    GeneIDi9218.
    KEGGihsa:9218.
    UCSCiuc002koj.3. human. [Q9P0L0-2]
    uc002kok.3. human. [Q9P0L0-1]

    Polymorphism databases

    DMDMi122066680.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF044670 mRNA. Translation: AAD09742.1 . Different initiation.
    AF154847 mRNA. Translation: AAF72105.1 . Different initiation.
    AC006238 Genomic DNA. No translation available.
    CH471113 Genomic DNA. Translation: EAX01591.1 .
    CH471113 Genomic DNA. Translation: EAX01592.1 .
    BC002992 mRNA. Translation: AAH02992.2 .
    BG488667 mRNA. No translation available.
    AF057358 mRNA. Translation: AAC26508.1 .
    AF086627 mRNA. Translation: AAD13576.1 .
    BT019618 mRNA. Translation: AAV38424.1 .
    CCDSi CCDS11847.2. [Q9P0L0-2 ]
    CCDS11848.2. [Q9P0L0-1 ]
    RefSeqi NP_003565.4. NM_003574.5. [Q9P0L0-2 ]
    NP_919415.2. NM_194434.2. [Q9P0L0-1 ]
    UniGenei Hs.165195.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2RR3 NMR - A 11-135 [» ]
    ProteinModelPortali Q9P0L0.
    SMRi Q9P0L0. Positions 9-135.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114651. 40 interactions.
    DIPi DIP-41135N.
    IntActi Q9P0L0. 45 interactions.
    MINTi MINT-109415.
    STRINGi 9606.ENSP00000345656.

    PTM databases

    PhosphoSitei Q9P0L0.

    Polymorphism databases

    DMDMi 122066680.

    Proteomic databases

    MaxQBi Q9P0L0.
    PaxDbi Q9P0L0.
    PRIDEi Q9P0L0.

    Protocols and materials databases

    DNASUi 9218.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000340541 ; ENSP00000345656 ; ENSG00000101558 . [Q9P0L0-2 ]
    ENST00000400000 ; ENSP00000382880 ; ENSG00000101558 . [Q9P0L0-1 ]
    GeneIDi 9218.
    KEGGi hsa:9218.
    UCSCi uc002koj.3. human. [Q9P0L0-2 ]
    uc002kok.3. human. [Q9P0L0-1 ]

    Organism-specific databases

    CTDi 9218.
    GeneCardsi GC18P009904.
    H-InvDB HIX0115359.
    HGNCi HGNC:12648. VAPA.
    HPAi HPA009174.
    MIMi 605703. gene.
    neXtProti NX_Q9P0L0.
    PharmGKBi PA37272.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5066.
    HOGENOMi HOG000293182.
    HOVERGENi HBG028551.
    KOi K06096.
    OMAi NPIDELE.
    OrthoDBi EOG7CK389.
    PhylomeDBi Q9P0L0.
    TreeFami TF317024.

    Enzyme and pathway databases

    Reactomei REACT_115810. Sphingolipid de novo biosynthesis.

    Miscellaneous databases

    ChiTaRSi VAPA. human.
    EvolutionaryTracei Q9P0L0.
    GeneWikii VAPA.
    GenomeRNAii 9218.
    NextBioi 34557.
    PMAP-CutDB Q9P0L0.
    PROi Q9P0L0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9P0L0.
    Bgeei Q9P0L0.
    CleanExi HS_VAPA.
    Genevestigatori Q9P0L0.

    Family and domain databases

    Gene3Di 2.60.40.360. 1 hit.
    InterProi IPR000535. MSP_dom.
    IPR008962. PapD-like.
    IPR016763. Vesicle-associated_membrane.
    [Graphical view ]
    Pfami PF00635. Motile_Sperm. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF019693. VAMP-associated. 1 hit.
    SUPFAMi SSF49354. SSF49354. 1 hit.
    PROSITEi PS50202. MSP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "VAP-33 localizes to both an intracellular vesicle population and with occludin at the tight junction."
      Lapierre L.A., Tuma P.L., Navarre J., Goldenring J.R., Anderson J.M.
      J. Cell Sci. 112:3723-3732(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH OCLN.
      Tissue: Liver.
    2. "Cloning and isolating human 33kDa Vamp-associated protein cDNA."
      Zhou H.J., Huang X.W., Zhou Y., Hu S.L., Yuan J.G., Qiang B.Q.
      Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-199 (ISOFORM 2).
      Tissue: Lung.
    6. "Identification of a human homologue of the vesicle-associated membrane protein (VAMP)-associated protein of 33 kDa (VAP-33): a broadly expressed protein that binds to VAMP."
      Weir M.L., Klip A., Trimble W.S.
      Biochem. J. 333:247-251(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-249 (ISOFORM 1), INTERACTION WITH VAMP1 AND VAMP2.
      Tissue: Pancreatic islet.
    7. "Molecular cloning and characterization of mammalian homologues of vesicle-associated membrane protein-associated (VAMP-associated) proteins."
      Nishimura Y., Hayashi M., Inada H., Tanaka T.
      Biochem. Biophys. Res. Commun. 254:21-26(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-249 (ISOFORM 1).
      Tissue: B-cell.
    8. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-249 (ISOFORM 1).
    9. Cited for: FUNCTION, INTERACTION WITH VAPB; VAMP1; VAMP2; STX1A; BET1 AND SEC22C.
    10. "Promotion of neurite extension by protrudin requires its interaction with vesicle-associated membrane protein-associated protein."
      Saita S., Shirane M., Natume T., Iemura S., Nakayama K.I.
      J. Biol. Chem. 284:13766-13777(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ZFYVE27, MUTAGENESIS OF LYS-94 AND MET-96, SUBCELLULAR LOCATION.
    11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Viperin inhibits hepatitis C virus replication by interfering with binding of NS5A to host protein hVAP-33."
      Wang S., Wu X., Pan T., Song W., Wang Y., Zhang F., Yuan Z.
      J. Gen. Virol. 93:83-92(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RSAD2 AND HCV PROTEIN NS5A AND NS5B.
    14. "The antiviral effector IFITM3 disrupts intracellular cholesterol homeostasis to block viral entry."
      Amini-Bavil-Olyaee S., Choi Y.J., Lee J.H., Shi M., Huang I.C., Farzan M., Jung J.U.
      Cell Host Microbe 13:452-464(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IFITM3.
    15. "Electrostatic interaction between oxysterol-binding protein and VAMP-associated protein A revealed by NMR and mutagenesis studies."
      Furuita K., Jee J., Fukada H., Mishima M., Kojima C.
      J. Biol. Chem. 285:12961-12970(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 11-135, INTERACTION WITH OSBP.

    Entry informationi

    Entry nameiVAPA_HUMAN
    AccessioniPrimary (citable) accession number: Q9P0L0
    Secondary accession number(s): A6NDZ0
    , D3DUI3, O75453, Q5U0E7, Q9UBZ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 2002
    Last sequence update: January 9, 2007
    Last modified: October 1, 2014
    This is version 135 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3