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P51809

- VAMP7_HUMAN

UniProt

P51809 - VAMP7_HUMAN

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Protein

Vesicle-associated membrane protein 7

Gene
VAMP7, SYBL1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
  2. SNAP receptor activity Source: RefGenome
  3. SNARE binding Source: RefGenome

GO - Biological processi

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

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; Single-pass type IV membrane protein By similarity. Golgi apparatustrans-Golgi network membrane; Single-pass type IV membrane protein By similarity. Late endosome membrane; Single-pass type IV membrane protein By similarity. Lysosome membrane; Single-pass type IV membrane protein. Endoplasmic reticulum membrane; Single-pass type IV membrane protein By similarity. Cytoplasmic vesiclephagosome membrane; 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.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 188187Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei189 – 20921Helical; Anchor for type IV membrane protein; Reviewed predictionAdd
BLAST
Topological domaini210 – 22011Vesicular Reviewed predictionAdd
BLAST

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
Complete GO annotation...

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 – 1681Phosphoserine By 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.

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.

Miscellaneous databases

EvolutionaryTraceiP51809.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 110104LonginAdd
BLAST
Domaini125 – 18561v-SNARE coiled-coil homologyAdd
BLAST

Sequence similaritiesi

Belongs to the synaptobrevin family.
Contains 1 longin domain.

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei28 – 6841Missing in isoform 3. VSP_017508Add
BLAST
Alternative sequencei145 – 22076DLVAQ…SCVKK → VCHLQNYQQKSCSSHVYEEP QAHYYHHHRINCVHLYHCFT SLWWIYMAKLCEEIGKKKLP LTKDMREQGVKSNPCDSSLS HTDRWYLPVSSTLFSLFKIL FHASRFIFVLSTSLFL in isoform 2. VSP_017509Add
BLAST

Sequence conflict

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

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 142 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

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