Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P51809

- VAMP7_HUMAN

UniProt

P51809 - VAMP7_HUMAN

Protein

Vesicle-associated membrane protein 7

Gene

VAMP7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Involved in the targeting and/or fusion of transport vesicles to their target membrane during transport of proteins from the early endosome to the lysosome. Required for heterotypic fusion of late endosomes with lysosomes and homotypic lysosomal fusion. Required for calcium regulated lysosomal exocytosis. Involved in the export of chylomicrons from the endoplasmic reticulum to the cis Golgi. Required for exocytosis of mediators during eosinophil and neutrophil degranulation, and target cell killing by natural killer cells. Required for focal exocytosis of late endocytic vesicles during phagosome formation.3 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. calcium ion-dependent exocytosis Source: UniProtKB
    2. endosome to lysosome transport Source: UniProtKB
    3. eosinophil degranulation Source: UniProtKB
    4. ER to Golgi vesicle-mediated transport Source: UniProtKB
    5. Golgi to plasma membrane protein transport Source: Ensembl
    6. membrane organization Source: Reactome
    7. neutrophil degranulation Source: UniProtKB
    8. phagocytosis, engulfment Source: UniProtKB
    9. post-Golgi vesicle-mediated transport Source: Reactome
    10. regulation of protein targeting to vacuolar membrane Source: Ensembl
    11. triglyceride transport Source: Ensembl
    12. vesicle fusion Source: UniProtKB
    13. vesicle fusion with Golgi apparatus Source: Ensembl
    14. vesicle-mediated transport Source: UniProtKB

    Keywords - Biological processi

    Exocytosis, Protein transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_19187. Clathrin derived vesicle budding.
    REACT_19287. Lysosome Vesicle Biogenesis.
    REACT_19400. Golgi Associated Vesicle Biogenesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Vesicle-associated membrane protein 7
    Short name:
    VAMP-7
    Alternative name(s):
    Synaptobrevin-like protein 1
    Tetanus-insensitive VAMP
    Short name:
    Ti-VAMP
    Gene namesi
    Name:VAMP7
    Synonyms:SYBL1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:11486. VAMP7.

    Subcellular locationi

    Cytoplasmic vesiclesecretory vesicle membrane By similarity; Single-pass type IV membrane protein By similarity. Golgi apparatustrans-Golgi network membrane By similarity; Single-pass type IV membrane protein By similarity. Late endosome membrane By similarity; Single-pass type IV membrane protein By similarity. Lysosome membrane 1 Publication; Single-pass type IV membrane protein 1 Publication. Endoplasmic reticulum membrane By similarity; Single-pass type IV membrane protein By similarity. Cytoplasmic vesiclephagosome membrane By similarity; Single-pass type IV membrane protein By similarity. Cell junctionsynapsesynaptosome By similarity
    Note: In immature neurons expression is localized in vesicular structures in axons and dendrites while in mature neurons it is localized to the somatodendritic region. Colocalizes with LAMP1 in kidney cells. Localization to the endoplasmic reticulum membrane was observed in the intestine but not in liver or kidney By similarity.By similarity

    GO - Cellular componenti

    1. apical part of cell Source: Ensembl
    2. cell junction Source: UniProtKB-KW
    3. cytoplasm Source: HPA
    4. endoplasmic reticulum membrane Source: UniProtKB
    5. extracellular vesicular exosome Source: UniProt
    6. Golgi apparatus Source: HPA
    7. integral component of membrane Source: UniProtKB-KW
    8. intracellular membrane-bounded organelle Source: HPA
    9. late endosome membrane Source: UniProtKB
    10. lysosomal membrane Source: UniProtKB
    11. neuron projection Source: UniProtKB
    12. perinuclear region of cytoplasm Source: Ensembl
    13. phagocytic vesicle Source: UniProtKB
    14. phagocytic vesicle membrane Source: UniProtKB-SubCell
    15. plasma membrane Source: Reactome
    16. SNARE complex Source: UniProtKB
    17. synapse Source: UniProtKB-KW
    18. transport vesicle membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Golgi apparatus, Lysosome, Membrane, Synapse, Synaptosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162408786.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 220219Vesicle-associated membrane protein 7PRO_0000206761Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine; partial1 Publication
    Modified residuei168 – 1681PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP51809.
    PaxDbiP51809.
    PRIDEiP51809.

    PTM databases

    PhosphoSiteiP51809.

    Expressioni

    Tissue specificityi

    Detected in all tissues tested.

    Gene expression databases

    ArrayExpressiP51809.
    BgeeiP51809.
    CleanExiHS_VAMP7.
    GenevestigatoriP51809.

    Organism-specific databases

    HPAiHPA036733.

    Interactioni

    Subunit structurei

    Component of the SNARE complex composed of STX4, SNAP23 and VAMP7 that binds SYT7 during lysosomal exocytosis. Component of the SNARE complex composed of STX7, STX8, VAMP7 and VTI1B that is required for heterotypic fusion of late endosomes with lysosomes. May interact with STX17 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AGFG1P525947EBI-1052205,EBI-996560

    Protein-protein interaction databases

    BioGridi112712. 10 interactions.
    IntActiP51809. 7 interactions.
    STRINGi9606.ENSP00000286448.

    Structurei

    Secondary structure

    1
    220
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 106
    Beta strandi13 – 197
    Beta strandi21 – 233
    Helixi26 – 338
    Beta strandi38 – 403
    Beta strandi42 – 476
    Beta strandi50 – 578
    Beta strandi60 – 7011
    Helixi72 – 8918
    Helixi91 – 955
    Helixi103 – 11715

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DMWNMR-A1-118[»]
    ProteinModelPortaliP51809.
    SMRiP51809. Positions 1-193.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP51809.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 188187CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini210 – 22011VesicularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei189 – 20921Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini7 – 110104LonginPROSITE-ProRule annotationAdd
    BLAST
    Domaini125 – 18561v-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the synaptobrevin family.Curated
    Contains 1 longin domain.PROSITE-ProRule annotation
    Contains 1 v-SNARE coiled-coil homology domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5143.
    HOGENOMiHOG000042711.
    HOVERGENiHBG006675.
    KOiK08515.
    OMAiMKHYSES.
    OrthoDBiEOG75B87Z.
    PhylomeDBiP51809.
    TreeFamiTF323448.

    Family and domain databases

    Gene3Di3.30.450.50. 1 hit.
    InterProiIPR011012. Longin-like_dom.
    IPR010908. Longin_dom.
    IPR001388. Synaptobrevin.
    [Graphical view]
    PfamiPF13774. Longin. 1 hit.
    PF00957. Synaptobrevin. 1 hit.
    [Graphical view]
    PRINTSiPR00219. SYNAPTOBREVN.
    SUPFAMiSSF64356. SSF64356. 1 hit.
    PROSITEiPS50859. LONGIN. 1 hit.
    PS00417. SYNAPTOBREVIN. 1 hit.
    PS50892. V_SNARE. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P51809-1) [UniParc]FASTAAdd to Basket

    Also known as: Ti-VAMPa/VAMP7a

    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

    MAILFAVVAR GTTILAKHAW CGGNFLEVTE QILAKIPSEN NKLTYSHGNY    50
    LFHYICQDRI VYLCITDDDF ERSRAFNFLN EIKKRFQTTY GSRAQTALPY 100
    AMNSEFSSVL AAQLKHHSEN KGLDKVMETQ AQVDELKGIM VRNIDLVAQR 150
    GERLELLIDK TENLVDSSVT FKTTSRNLAR AMCMKNLKLT IIIIIVSIVF 200
    IYIIVSPLCG GFTWPSCVKK 220
    Length:220
    Mass (Da):24,935
    Last modified:January 23, 2007 - v3
    Checksum:i9C1AA5C590375CEF
    GO
    Isoform 2 (identifier: P51809-2) [UniParc]FASTAAdd to Basket

    Also known as: Ti-VAMPb/VAMP7b

    The sequence of this isoform differs from the canonical sequence as follows:
         145-220: DLVAQRGERL...GFTWPSCVKK → VCHLQNYQQK...IFVLSTSLFL

    Show »
    Length:260
    Mass (Da):30,217
    Checksum:iAB6942EF4ACD2978
    GO
    Isoform 3 (identifier: P51809-3) [UniParc]FASTAAdd to Basket

    Also known as: Ti-VAMPc/VAMP7c

    The sequence of this isoform differs from the canonical sequence as follows:
         28-68: Missing.

    Show »
    Length:179
    Mass (Da):20,121
    Checksum:iFE272984659C2B96
    GO

    Sequence cautioni

    The sequence BI547528 differs from that shown. Reason: Sequence of unknown origin in the C-terminal part.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti98 – 981L → P in BAD96514. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei28 – 6841Missing in isoform 3. 1 PublicationVSP_017508Add
    BLAST
    Alternative sequencei145 – 22076DLVAQ…SCVKK → VCHLQNYQQKSCSSHVYEEP QAHYYHHHRINCVHLYHCFT SLWWIYMAKLCEEIGKKKLP LTKDMREQGVKSNPCDSSLS HTDRWYLPVSSTLFSLFKIL FHASRFIFVLSTSLFL in isoform 2. 1 PublicationVSP_017509Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X92396 mRNA. Translation: CAA63133.1.
    AJ271736 Genomic DNA. Translation: CAB96816.1.
    AJ549301 mRNA. Translation: CAD70593.2.
    AJ295938 mRNA. Translation: CAC16891.1.
    AK222794 mRNA. Translation: BAD96514.1.
    BC056141 mRNA. Translation: AAH56141.1.
    BI547528 mRNA. No translation available.
    CCDSiCCDS14770.4. [P51809-1]
    CCDS48199.1. [P51809-3]
    CCDS55548.1. [P51809-2]
    RefSeqiNP_001138621.1. NM_001145149.2. [P51809-3]
    NP_001172112.1. NM_001185183.1. [P51809-2]
    NP_005629.1. NM_005638.5. [P51809-1]
    UniGeneiHs.24167.

    Genome annotation databases

    EnsembliENST00000262640; ENSP00000262640; ENSG00000124333. [P51809-2]
    ENST00000286448; ENSP00000286448; ENSG00000124333. [P51809-1]
    ENST00000460621; ENSP00000427822; ENSG00000124333. [P51809-3]
    GeneIDi6845.
    KEGGihsa:6845.
    UCSCiuc004fnr.3. human. [P51809-1]
    uc004fns.3. human. [P51809-2]
    uc004fnt.3. human. [P51809-3]

    Polymorphism databases

    DMDMi1723133.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X92396 mRNA. Translation: CAA63133.1 .
    AJ271736 Genomic DNA. Translation: CAB96816.1 .
    AJ549301 mRNA. Translation: CAD70593.2 .
    AJ295938 mRNA. Translation: CAC16891.1 .
    AK222794 mRNA. Translation: BAD96514.1 .
    BC056141 mRNA. Translation: AAH56141.1 .
    BI547528 mRNA. No translation available.
    CCDSi CCDS14770.4. [P51809-1 ]
    CCDS48199.1. [P51809-3 ]
    CCDS55548.1. [P51809-2 ]
    RefSeqi NP_001138621.1. NM_001145149.2. [P51809-3 ]
    NP_001172112.1. NM_001185183.1. [P51809-2 ]
    NP_005629.1. NM_005638.5. [P51809-1 ]
    UniGenei Hs.24167.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DMW NMR - A 1-118 [» ]
    ProteinModelPortali P51809.
    SMRi P51809. Positions 1-193.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112712. 10 interactions.
    IntActi P51809. 7 interactions.
    STRINGi 9606.ENSP00000286448.

    PTM databases

    PhosphoSitei P51809.

    Polymorphism databases

    DMDMi 1723133.

    Proteomic databases

    MaxQBi P51809.
    PaxDbi P51809.
    PRIDEi P51809.

    Protocols and materials databases

    DNASUi 6845.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262640 ; ENSP00000262640 ; ENSG00000124333 . [P51809-2 ]
    ENST00000286448 ; ENSP00000286448 ; ENSG00000124333 . [P51809-1 ]
    ENST00000460621 ; ENSP00000427822 ; ENSG00000124333 . [P51809-3 ]
    GeneIDi 6845.
    KEGGi hsa:6845.
    UCSCi uc004fnr.3. human. [P51809-1 ]
    uc004fns.3. human. [P51809-2 ]
    uc004fnt.3. human. [P51809-3 ]

    Organism-specific databases

    CTDi 6845.
    GeneCardsi GC0XP155110.
    HGNCi HGNC:11486. VAMP7.
    HPAi HPA036733.
    MIMi 300053. gene.
    neXtProti NX_P51809.
    PharmGKBi PA162408786.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5143.
    HOGENOMi HOG000042711.
    HOVERGENi HBG006675.
    KOi K08515.
    OMAi MKHYSES.
    OrthoDBi EOG75B87Z.
    PhylomeDBi P51809.
    TreeFami TF323448.

    Enzyme and pathway databases

    Reactomei REACT_19187. Clathrin derived vesicle budding.
    REACT_19287. Lysosome Vesicle Biogenesis.
    REACT_19400. Golgi Associated Vesicle Biogenesis.

    Miscellaneous databases

    EvolutionaryTracei P51809.
    GeneWikii SYBL1.
    GenomeRNAii 6845.
    NextBioi 26723.
    PROi P51809.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51809.
    Bgeei P51809.
    CleanExi HS_VAMP7.
    Genevestigatori P51809.

    Family and domain databases

    Gene3Di 3.30.450.50. 1 hit.
    InterProi IPR011012. Longin-like_dom.
    IPR010908. Longin_dom.
    IPR001388. Synaptobrevin.
    [Graphical view ]
    Pfami PF13774. Longin. 1 hit.
    PF00957. Synaptobrevin. 1 hit.
    [Graphical view ]
    PRINTSi PR00219. SYNAPTOBREVN.
    SUPFAMi SSF64356. SSF64356. 1 hit.
    PROSITEi PS50859. LONGIN. 1 hit.
    PS00417. SYNAPTOBREVIN. 1 hit.
    PS50892. V_SNARE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A synaptobrevin-like gene in the Xq28 pseudoautosomal region undergoes X inactivation."
      D'Esposito M., Ciccodicola A., Gianfrancesco F., Esposito T., Flagiello L., Mazzarella R., Schlessinger D., D'Urso M.
      Nat. Genet. 13:227-229(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Tissue: Brain.
    4. "Alternative splicing of SYBL1 gene."
      D'Esposito M., Filippini F., Rossi V., D'Urso M.
      Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Liver.
    6. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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).
      Tissue: Hippocampus and Uterus.
    8. Bienvenut W.V.
      Submitted (JUN-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-10; 126-137 AND 143-150, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    9. "Syntaxin 7 and VAMP-7 are soluble N-ethylmaleimide-sensitive factor attachment protein receptors required for late endosome-lysosome and homotypic lysosome fusion in alveolar macrophages."
      Ward D.M., Pevsner J., Scullion M.A., Vaughn M., Kaplan J.
      Mol. Biol. Cell 11:2327-2333(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "A critical role for vesicle-associated membrane protein-7 in exocytosis from human eosinophils and neutrophils."
      Logan M.R., Lacy P., Odemuyiwa S.O., Steward M., Davoine F., Kita H., Moqbel R.
      Allergy 61:777-784(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Placenta.
    12. "Vesicle-associated membrane protein 7 (VAMP-7) is essential for target cell killing in a natural killer cell line."
      Marcet-Palacios M., Odemuyiwa S.O., Coughlin J.J., Garofoli D., Ewen C., Davidson C.E., Ghaffari M., Kane K.P., Lacy P., Logan M.R., Befus A.D., Bleackley R.C., Moqbel R.
      Biochem. Biophys. Res. Commun. 366:617-623(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Solution structure of the longin domain of synaptobrevin-like protein 1."
      RIKEN structural genomics initiative (RSGI)
      Submitted (OCT-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1-118.

    Entry informationi

    Entry nameiVAMP7_HUMAN
    AccessioniPrimary (citable) accession number: P51809
    Secondary accession number(s): Q53GY7, Q7Z409, Q9H4A7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 143 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

    Miscellaneous

    The gene coding for this protein is located in the pseudoautosomal region 2 (PAR2) of X and Y chromosomes.
    Loss-of-function mutant (antisense inhibition) displays impaired granzyme B release and target cell killing by natural killer cells.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3