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Protein

Vesicle-associated membrane protein 4

Gene

VAMP4

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

Functioni

Involved in the pathway that functions to remove an inhibitor (probably synaptotagmin-4) of calcium-triggered exocytosis during the maturation of secretory granules. May be a marker for this sorting pathway that is critical for remodeling the secretory response of granule.

GO - Molecular functioni

GO - Biological processi

  • exocytosis Source: GO_Central
  • Golgi ribbon formation Source: UniProtKB
  • microtubule cytoskeleton organization Source: UniProtKB
  • SNARE complex assembly Source: BHF-UCL
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-HSA-6811440. Retrograde transport at the Trans-Golgi-Network.
SIGNORiO75379.

Names & Taxonomyi

Protein namesi
Recommended name:
Vesicle-associated membrane protein 4
Short name:
VAMP-4
Gene namesi
Name:VAMP4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:12645. VAMP4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 115115CytoplasmicSequence analysisAdd
BLAST
Transmembranei116 – 13621Helical; Anchor for type IV membrane proteinSequence analysisAdd
BLAST
Topological domaini137 – 1415VesicularSequence analysis

GO - Cellular componenti

  • cell surface Source: BHF-UCL
  • endosome Source: ProtInc
  • Golgi apparatus Source: UniProtKB
  • Golgi membrane Source: ProtInc
  • integral component of membrane Source: UniProtKB-KW
  • lysosome Source: ProtInc
  • SNARE complex Source: GO_Central
  • trans-Golgi network membrane Source: Reactome
  • transport vesicle Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37269.

Polymorphism and mutation databases

BioMutaiVAMP4.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 141141Vesicle-associated membrane protein 4PRO_0000206731Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171PhosphoserineBy similarity
Modified residuei30 – 301PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO75379.
PaxDbiO75379.
PRIDEiO75379.

PTM databases

iPTMnetiO75379.
PhosphoSiteiO75379.
SwissPalmiO75379.

Expressioni

Gene expression databases

BgeeiO75379.
CleanExiHS_VAMP4.
ExpressionAtlasiO75379. baseline and differential.
GenevisibleiO75379. HS.

Organism-specific databases

HPAiHPA050418.

Interactioni

Subunit structurei

Identified in a complex containing STX6, STX12, VAMP4 and VTI1A.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
BCL2L13Q9BXK53EBI-10187996,EBI-747430
CCDC155Q8N6L03EBI-744953,EBI-749265
SNAP29O957213EBI-10187996,EBI-490676
SNAP47Q5SQN12EBI-744953,EBI-10244848
STX4Q128464EBI-744953,EBI-744942

GO - Molecular functioni

Protein-protein interaction databases

BioGridi114222. 48 interactions.
DIPiDIP-44226N.
IntActiO75379. 19 interactions.
MINTiMINT-1469104.
STRINGi9606.ENSP00000236192.

Structurei

3D structure databases

ProteinModelPortaliO75379.
SMRiO75379. Positions 49-111.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini52 – 11261v-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0860. Eukaryota.
COG5143. LUCA.
GeneTreeiENSGT00550000074449.
HOGENOMiHOG000042711.
HOVERGENiHBG061695.
InParanoidiO75379.
KOiK08513.
OMAiWRGCKMK.
OrthoDBiEOG7J182W.
PhylomeDBiO75379.
TreeFamiTF313666.

Family and domain databases

Gene3Di1.10.3840.10. 1 hit.
InterProiIPR001388. Synaptobrevin.
[Graphical view]
PfamiPF00957. Synaptobrevin. 1 hit.
[Graphical view]
PRINTSiPR00219. SYNAPTOBREVN.
PROSITEiPS00417. SYNAPTOBREVIN. 1 hit.
PS50892. V_SNARE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O75379-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPPKFKRHLN DDDVTGSVKS ERRNLLEDDS DEEEDFFLRG PSGPRFGPRN
60 70 80 90 100
DKIKHVQNQV DEVIDVMQEN ITKVIERGER LDELQDKSES LSDNATAFSN
110 120 130 140
RSKQLRRQMW WRGCKIKAIM ALVAAILLLV IIILIVMKYR T
Length:141
Mass (Da):16,397
Last modified:April 3, 2002 - v2
Checksum:i556CC682D26CF91E
GO
Isoform 2 (identifier: O75379-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     39-39: Missing.

Note: No experimental confirmation available.
Show »
Length:140
Mass (Da):16,241
Checksum:iA2D4E66093D57837
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681Q → P in AAC24032 (PubMed:9553086).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei39 – 391Missing in isoform 2. 1 PublicationVSP_006326

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF044310 mRNA. Translation: AAC24032.1.
AL035296 mRNA. Translation: CAA22896.1.
Z98751 Genomic DNA. Translation: CAM28272.1.
CH471067 Genomic DNA. Translation: EAW90904.1.
BC005974 mRNA. Translation: AAH05974.1.
BC007019 mRNA. Translation: AAH07019.1.
BC031264 mRNA. Translation: AAH31264.1.
CCDSiCCDS1298.1. [O75379-1]
CCDS53430.1. [O75379-2]
RefSeqiNP_001172056.1. NM_001185127.1. [O75379-2]
NP_003753.2. NM_003762.4. [O75379-1]
UniGeneiHs.6651.

Genome annotation databases

EnsembliENST00000236192; ENSP00000236192; ENSG00000117533. [O75379-1]
ENST00000367740; ENSP00000356714; ENSG00000117533. [O75379-2]
ENST00000474047; ENSP00000435933; ENSG00000117533. [O75379-1]
GeneIDi8674.
KEGGihsa:8674.
UCSCiuc001ghy.3. human. [O75379-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF044310 mRNA. Translation: AAC24032.1.
AL035296 mRNA. Translation: CAA22896.1.
Z98751 Genomic DNA. Translation: CAM28272.1.
CH471067 Genomic DNA. Translation: EAW90904.1.
BC005974 mRNA. Translation: AAH05974.1.
BC007019 mRNA. Translation: AAH07019.1.
BC031264 mRNA. Translation: AAH31264.1.
CCDSiCCDS1298.1. [O75379-1]
CCDS53430.1. [O75379-2]
RefSeqiNP_001172056.1. NM_001185127.1. [O75379-2]
NP_003753.2. NM_003762.4. [O75379-1]
UniGeneiHs.6651.

3D structure databases

ProteinModelPortaliO75379.
SMRiO75379. Positions 49-111.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114222. 48 interactions.
DIPiDIP-44226N.
IntActiO75379. 19 interactions.
MINTiMINT-1469104.
STRINGi9606.ENSP00000236192.

PTM databases

iPTMnetiO75379.
PhosphoSiteiO75379.
SwissPalmiO75379.

Polymorphism and mutation databases

BioMutaiVAMP4.

Proteomic databases

EPDiO75379.
PaxDbiO75379.
PRIDEiO75379.

Protocols and materials databases

DNASUi8674.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000236192; ENSP00000236192; ENSG00000117533. [O75379-1]
ENST00000367740; ENSP00000356714; ENSG00000117533. [O75379-2]
ENST00000474047; ENSP00000435933; ENSG00000117533. [O75379-1]
GeneIDi8674.
KEGGihsa:8674.
UCSCiuc001ghy.3. human. [O75379-1]

Organism-specific databases

CTDi8674.
GeneCardsiVAMP4.
HGNCiHGNC:12645. VAMP4.
HPAiHPA050418.
MIMi606909. gene.
neXtProtiNX_O75379.
PharmGKBiPA37269.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0860. Eukaryota.
COG5143. LUCA.
GeneTreeiENSGT00550000074449.
HOGENOMiHOG000042711.
HOVERGENiHBG061695.
InParanoidiO75379.
KOiK08513.
OMAiWRGCKMK.
OrthoDBiEOG7J182W.
PhylomeDBiO75379.
TreeFamiTF313666.

Enzyme and pathway databases

ReactomeiR-HSA-6811440. Retrograde transport at the Trans-Golgi-Network.
SIGNORiO75379.

Miscellaneous databases

GeneWikiiVAMP4.
GenomeRNAii8674.
PROiO75379.
SOURCEiSearch...

Gene expression databases

BgeeiO75379.
CleanExiHS_VAMP4.
ExpressionAtlasiO75379. baseline and differential.
GenevisibleiO75379. HS.

Family and domain databases

Gene3Di1.10.3840.10. 1 hit.
InterProiIPR001388. Synaptobrevin.
[Graphical view]
PfamiPF00957. Synaptobrevin. 1 hit.
[Graphical view]
PRINTSiPR00219. SYNAPTOBREVN.
PROSITEiPS00417. SYNAPTOBREVIN. 1 hit.
PS50892. V_SNARE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Seven novel mammalian SNARE proteins localize to distinct membrane compartments."
    Advani R.J., Bae H.-R., Bock J.B., Chao D.S., Doung Y.-C., Prekeris R., Yoo J.-S., Scheller R.H.
    J. Biol. Chem. 273:10317-10324(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: B-cell.
  2. Rhodes S.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Bone marrow and Urinary bladder.
  6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiVAMP4_HUMAN
AccessioniPrimary (citable) accession number: O75379
Secondary accession number(s): A2IDD8
, Q96IY9, Q96J20, Q9UEL7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: April 3, 2002
Last modified: June 8, 2016
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.