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Protein

Vesicle-associated membrane protein 7

Gene

VAMP7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

GO - Biological processi

  • calcium ion-dependent exocytosis Source: UniProtKB
  • endosome to lysosome transport Source: UniProtKB
  • eosinophil degranulation Source: UniProtKB
  • ER to Golgi vesicle-mediated transport Source: UniProtKB
  • Golgi to plasma membrane protein transport Source: Ensembl
  • membrane organization Source: Reactome
  • natural killer cell degranulation Source: UniProtKB
  • neutrophil degranulation Source: UniProtKB
  • phagocytosis, engulfment Source: UniProtKB
  • positive regulation of histamine secretion by mast cell Source: UniProtKB
  • post-Golgi vesicle-mediated transport Source: Reactome
  • regulation of protein targeting to vacuolar membrane Source: Ensembl
  • SNARE complex assembly Source: Ensembl
  • triglyceride transport Source: Ensembl
  • vesicle fusion Source: UniProtKB
  • vesicle fusion with Golgi apparatus Source: Ensembl
  • 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 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:11486. VAMP7.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 188187CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei189 – 20921Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
BLAST
Topological domaini210 – 22011VesicularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • apical part of cell Source: Ensembl
  • azurophil granule membrane Source: UniProtKB
  • cell junction Source: UniProtKB-KW
  • cell surface Source: Ensembl
  • cytoplasm Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • Golgi apparatus Source: HPA
  • integral component of membrane Source: UniProtKB-KW
  • intracellular membrane-bounded organelle Source: HPA
  • lamellipodium Source: UniProtKB
  • late endosome membrane Source: UniProtKB
  • lysosomal membrane Source: UniProtKB
  • membrane Source: UniProtKB
  • neuron projection Source: UniProtKB
  • perinuclear region of cytoplasm Source: Ensembl
  • phagocytic vesicle Source: UniProtKB
  • phagocytic vesicle membrane Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
  • platelet alpha granule Source: UniProtKB
  • pseudopodium Source: UniProtKB
  • secretory granule Source: UniProtKB
  • secretory granule membrane Source: UniProtKB
  • SNARE complex Source: UniProtKB
  • synapse Source: UniProtKB-KW
  • trans-Golgi network Source: UniProtKB
  • 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

Orphaneti251510. 46,XY partial gonadal dysgenesis.
PharmGKBiPA162408786.

Polymorphism and mutation databases

BioMutaiVAMP7.
DMDMi1723133.

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

BgeeiP51809.
CleanExiHS_VAMP7.
ExpressionAtlasiP51809. baseline and differential.
GenevisibleiP51809. HS.

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. 16 interactions.
IntActiP51809. 7 interactions.
STRINGi9606.ENSP00000262640.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP51809.

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.
GeneTreeiENSGT00510000047733.
HOGENOMiHOG000042711.
HOVERGENiHBG006675.
InParanoidiP51809.
KOiK08515.
OMAiCHDRIIY.
OrthoDBiEOG75B87Z.
PhylomeDBiP51809.
TreeFamiTF323448.

Family and domain databases

Gene3Di1.10.3840.10. 1 hit.
3.30.450.50. 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. AlignAdd to basket

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

        10         20         30         40         50
MAILFAVVAR GTTILAKHAW CGGNFLEVTE QILAKIPSEN NKLTYSHGNY
60 70 80 90 100
LFHYICQDRI VYLCITDDDF ERSRAFNFLN EIKKRFQTTY GSRAQTALPY
110 120 130 140 150
AMNSEFSSVL AAQLKHHSEN KGLDKVMETQ AQVDELKGIM VRNIDLVAQR
160 170 180 190 200
GERLELLIDK TENLVDSSVT FKTTSRNLAR AMCMKNLKLT IIIIIVSIVF
210 220
IYIIVSPLCG GFTWPSCVKK
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.Sequence of unknown origin in the C-terminal part.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti98 – 981L → P in BAD96514 (Ref. 5) Curated

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:
EMBLi
GenBanki
DDBJi
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]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi112712. 16 interactions.
IntActiP51809. 7 interactions.
STRINGi9606.ENSP00000262640.

PTM databases

PhosphoSiteiP51809.

Polymorphism and mutation databases

BioMutaiVAMP7.
DMDMi1723133.

Proteomic databases

MaxQBiP51809.
PaxDbiP51809.
PRIDEiP51809.

Protocols and materials databases

DNASUi6845.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi6845.
GeneCardsiGC0XP155110.
HGNCiHGNC:11486. VAMP7.
HPAiHPA036733.
MIMi300053. gene.
neXtProtiNX_P51809.
Orphaneti251510. 46,XY partial gonadal dysgenesis.
PharmGKBiPA162408786.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5143.
GeneTreeiENSGT00510000047733.
HOGENOMiHOG000042711.
HOVERGENiHBG006675.
InParanoidiP51809.
KOiK08515.
OMAiCHDRIIY.
OrthoDBiEOG75B87Z.
PhylomeDBiP51809.
TreeFamiTF323448.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP51809.
GeneWikiiSYBL1.
GenomeRNAii6845.
NextBioi26723.
PROiP51809.
SOURCEiSearch...

Gene expression databases

BgeeiP51809.
CleanExiHS_VAMP7.
ExpressionAtlasiP51809. baseline and differential.
GenevisibleiP51809. HS.

Family and domain databases

Gene3Di1.10.3840.10. 1 hit.
3.30.450.50. 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]
ProtoNetiSearch...

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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. "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: June 24, 2015
This is version 151 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

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.