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P51809 (VAMP7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:VAMP7
Synonyms:SYBL1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length220 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.10 Ref.12

Subunit structure

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.

Subcellular location

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. Ref.11

Tissue specificity

Detected in all tissues tested.

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.

Sequence similarities

Belongs to the synaptobrevin family.

Contains 1 longin domain.

Contains 1 v-SNARE coiled-coil homology domain.

Sequence caution

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

Ontologies

Keywords
   Biological processExocytosis
Protein transport
Transport
   Cellular componentCell junction
Cytoplasmic vesicle
Endoplasmic reticulum
Endosome
Golgi apparatus
Lysosome
Membrane
Synapse
Synaptosome
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Signal-anchor
Transmembrane
Transmembrane helix
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processER to Golgi vesicle-mediated transport

Inferred from sequence or structural similarity PubMed 16495485. Source: UniProtKB

Golgi to plasma membrane protein transport

Inferred from electronic annotation. Source: Ensembl

calcium ion-dependent exocytosis

Inferred from sequence or structural similarity PubMed 14993220. Source: UniProtKB

endocytosis

Inferred from Biological aspect of Ancestor. Source: RefGenome

endosome to lysosome transport

Inferred from direct assay Ref.9. Source: UniProtKB

eosinophil degranulation

Inferred from sequence or structural similarity PubMed 14993220. Source: UniProtKB

exocytosis

Inferred from Biological aspect of Ancestor. Source: RefGenome

membrane organization

Traceable author statement. Source: Reactome

neutrophil degranulation

Inferred from sequence or structural similarity PubMed 14993220. Source: UniProtKB

phagocytosis, engulfment

Inferred from sequence or structural similarity PubMed 15133481. Source: UniProtKB

post-Golgi vesicle-mediated transport

Traceable author statement. Source: Reactome

regulation of protein targeting to vacuolar membrane

Inferred from electronic annotation. Source: Ensembl

triglyceride transport

Inferred from electronic annotation. Source: Ensembl

vesicle fusion

Inferred from direct assay Ref.9. Source: UniProtKB

vesicle fusion with Golgi apparatus

Inferred from electronic annotation. Source: Ensembl

vesicle-mediated transport

Inferred from direct assay Ref.9. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

SNARE complex

Inferred from sequence or structural similarity PubMed 15133481. Source: UniProtKB

apical part of cell

Inferred from electronic annotation. Source: Ensembl

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from direct assay. Source: HPA

endoplasmic reticulum membrane

Inferred from sequence or structural similarity PubMed 16495485. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

late endosome membrane

Inferred from sequence or structural similarity PubMed 10459012. Source: UniProtKB

lysosomal membrane

Inferred from direct assay Ref.11. Source: UniProtKB

neuron projection

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

phagocytic vesicle

Inferred from sequence or structural similarity PubMed 15470500. Source: UniProtKB

phagocytic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Traceable author statement. Source: Reactome

synapse

Inferred from electronic annotation. Source: UniProtKB-KW

transport vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionSNAP receptor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

SNARE binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AGFG1P525947EBI-1052205,EBI-996560

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P51809-1)

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.
Isoform 2 (identifier: P51809-2)

Also known as: Ti-VAMPb/VAMP7b;

The sequence of this isoform differs from the canonical sequence as follows:
     145-220: DLVAQRGERL...GFTWPSCVKK → VCHLQNYQQK...IFVLSTSLFL
Isoform 3 (identifier: P51809-3)

Also known as: Ti-VAMPc/VAMP7c;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 220219Vesicle-associated membrane protein 7
PRO_0000206761

Regions

Topological domain2 – 188187Cytoplasmic Potential
Transmembrane189 – 20921Helical; Anchor for type IV membrane protein; Potential
Topological domain210 – 22011Vesicular Potential
Domain7 – 110104Longin
Domain125 – 18561v-SNARE coiled-coil homology

Amino acid modifications

Modified residue21N-acetylalanine; partial Ref.8
Modified residue1681Phosphoserine By similarity

Natural variations

Alternative sequence28 – 6841Missing in isoform 3.
VSP_017508
Alternative sequence145 – 22076DLVAQ…SCVKK → VCHLQNYQQKSCSSHVYEEP QAHYYHHHRINCVHLYHCFT SLWWIYMAKLCEEIGKKKLP LTKDMREQGVKSNPCDSSLS HTDRWYLPVSSTLFSLFKIL FHASRFIFVLSTSLFL in isoform 2.
VSP_017509

Experimental info

Sequence conflict981L → P in BAD96514. Ref.5

Secondary structure

....................... 220
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Ti-VAMPa/VAMP7a) [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 9C1AA5C590375CEF

FASTA22024,935
        10         20         30         40         50         60 
MAILFAVVAR GTTILAKHAW CGGNFLEVTE QILAKIPSEN NKLTYSHGNY LFHYICQDRI 

        70         80         90        100        110        120 
VYLCITDDDF ERSRAFNFLN EIKKRFQTTY GSRAQTALPY AMNSEFSSVL AAQLKHHSEN 

       130        140        150        160        170        180 
KGLDKVMETQ AQVDELKGIM VRNIDLVAQR GERLELLIDK TENLVDSSVT FKTTSRNLAR 

       190        200        210        220 
AMCMKNLKLT IIIIIVSIVF IYIIVSPLCG GFTWPSCVKK 

« Hide

Isoform 2 (Ti-VAMPb/VAMP7b) [UniParc].

Checksum: AB6942EF4ACD2978
Show »

FASTA26030,217
Isoform 3 (Ti-VAMPc/VAMP7c) [UniParc].

Checksum: FE272984659C2B96
Show »

FASTA17920,121

References

« Hide 'large scale' references
[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]"Differentially regulated and evolved genes in the fully sequenced Xq/Yq pseudoautosomal region."
Ciccodicola A., D'Esposito M., Esposito T., Gianfrancesco F., Migliaccio C., Miano M.G., Matarazzo M.R., Vacca M., Franze A., Cuccurese M., Cocchia M., Curci A., Terracciano A., Torino A., Cocchia S., Mercadante G., Pannone E., Archidiacono N. expand/collapse author list , Rocchi M., Schlessinger D., D'Urso M.
Hum. Mol. Genet. 9:395-401(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"A dual mechanism controlling the localization and function of exocytic v-SNARE."
Martinez-Arca S., Rudge R., Vacca M., Camonis J., Daviet L., Formstecher E., Hamburger A., Filippini F., D'Esposito M., Galli T.
Proc. Natl. Acad. Sci. U.S.A. 100:9011-9016(2003) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Integral and associated lysosomal membrane proteins."
Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H., Elsaesser H.-P., Mann M., Hasilik A.
Traffic 8:1676-1686(2007) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001138621.1. NM_001145149.2.
NP_001172112.1. NM_001185183.1.
NP_005629.1. NM_005638.5.
UniGeneHs.24167.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DMWNMR-A1-118[»]
ProteinModelPortalP51809.
SMRP51809. Positions 1-193.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112712. 10 interactions.
IntActP51809. 7 interactions.
STRING9606.ENSP00000286448.

PTM databases

PhosphoSiteP51809.

Polymorphism databases

DMDM1723133.

Proteomic databases

PaxDbP51809.
PRIDEP51809.

Protocols and materials databases

DNASU6845.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262640; ENSP00000262640; ENSG00000124333. [P51809-2]
ENST00000286448; ENSP00000286448; ENSG00000124333. [P51809-1]
ENST00000460621; ENSP00000427822; ENSG00000124333. [P51809-3]
GeneID6845.
KEGGhsa:6845.
UCSCuc004fnr.3. human. [P51809-1]
uc004fns.3. human. [P51809-2]
uc004fnt.3. human. [P51809-3]

Organism-specific databases

CTD6845.
GeneCardsGC0XP155110.
HGNCHGNC:11486. VAMP7.
HPAHPA036733.
MIM300053. gene.
neXtProtNX_P51809.
PharmGKBPA162408786.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5143.
HOGENOMHOG000042711.
HOVERGENHBG006675.
KOK08515.
OMAMKHYSES.
OrthoDBEOG75B87Z.
PhylomeDBP51809.
TreeFamTF323448.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.

Gene expression databases

ArrayExpressP51809.
BgeeP51809.
CleanExHS_VAMP7.
GenevestigatorP51809.

Family and domain databases

Gene3D3.30.450.50. 1 hit.
InterProIPR011012. Longin-like_dom.
IPR010908. Longin_dom.
IPR001388. Synaptobrevin.
[Graphical view]
PfamPF13774. Longin. 1 hit.
PF00957. Synaptobrevin. 1 hit.
[Graphical view]
PRINTSPR00219. SYNAPTOBREVN.
SUPFAMSSF64356. SSF64356. 1 hit.
PROSITEPS50859. LONGIN. 1 hit.
PS00417. SYNAPTOBREVIN. 1 hit.
PS50892. V_SNARE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP51809.
GeneWikiSYBL1.
GenomeRNAi6845.
NextBio26723.
PROP51809.
SOURCESearch...

Entry information

Entry nameVAMP7_HUMAN
AccessionPrimary (citable) accession number: P51809
Secondary accession number(s): Q53GY7, Q7Z409, Q9H4A7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM