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Q9P0L0

- VAPA_HUMAN

UniProt

Q9P0L0 - VAPA_HUMAN

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Protein

Vesicle-associated membrane protein-associated protein A

Gene

VAPA

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

Functioni

May play a role in vesicle trafficking.2 Publications

GO - Molecular functioni

  1. protein heterodimerization activity Source: UniProtKB
  2. signal transducer activity Source: UniProtKB
  3. structural molecule activity Source: InterPro

GO - Biological processi

  1. cell death Source: UniProtKB
  2. membrane fusion Source: ProtInc
  3. neuron projection development Source: UniProtKB
  4. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  5. protein localization to endoplasmic reticulum Source: UniProtKB
  6. signal transduction Source: GOC
  7. small molecule metabolic process Source: Reactome
  8. sphingolipid biosynthetic process Source: Reactome
  9. sphingolipid metabolic process Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_115810. Sphingolipid de novo biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Vesicle-associated membrane protein-associated protein A
Short name:
VAMP-A
Short name:
VAMP-associated protein A
Short name:
VAP-A
Alternative name(s):
33 kDa VAMP-associated protein
Short name:
VAP-33
Gene namesi
Name:VAPA
Synonyms:VAP33
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:12648. VAPA.

Subcellular locationi

Endoplasmic reticulum membrane 2 Publications; Single-pass type IV membrane protein 2 Publications
Note: Present in the plasma membrane and in intracellular vesicles, together with SNARE proteins. May also associate with the cytoskeleton. Colocalizes with OCLN at the tight junction in polarized epithelial cells.

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. endoplasmic reticulum membrane Source: Reactome
  3. integral component of membrane Source: UniProtKB-KW
  4. microtubule cytoskeleton Source: Ensembl
  5. plasma membrane Source: UniProtKB
  6. vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi94 – 941K → D: Alters interaction with ZFYVE27; when associated with D-96. 1 Publication
Mutagenesisi96 – 961M → D: Alters interaction with ZFYVE27; when associated with D-94. 1 Publication

Organism-specific databases

PharmGKBiPA37272.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 249249Vesicle-associated membrane protein-associated protein APRO_0000213470Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei125 – 1251N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9P0L0.
PaxDbiQ9P0L0.
PRIDEiQ9P0L0.

PTM databases

PhosphoSiteiQ9P0L0.

Miscellaneous databases

PMAP-CutDBQ9P0L0.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ9P0L0.
CleanExiHS_VAPA.
ExpressionAtlasiQ9P0L0. baseline and differential.
GenevestigatoriQ9P0L0.

Organism-specific databases

HPAiHPA009174.

Interactioni

Subunit structurei

Homodimer, and heterodimer with VAPB. Interacts with VAMP1, VAMP2, STX1A, BET1, SEC22C and with the C-terminal domain of OCLN. Interacts with OSBPL1A. Interacts (via MSP domain) with ZFYVE27; may retain ZFYVE27 in the endoplasmic reticulum and regulate its function in cell projections formation. Interacts with OSBP. Interacts (via C-terminus) with RSAD2/viperin (via C-terminus). Interacts with HCV protein NS5A and NS5B. Interacts with IFITM3.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P279587EBI-1059156,EBI-8753518From a different organism.
Q034634EBI-1059156,EBI-8803426From a different organism.
EGFRP005332EBI-1059156,EBI-297353
OPRM1P353723EBI-1059156,EBI-2624570
VAPBO95292-12EBI-1059156,EBI-9350848
ZFYVE27Q5T4F45EBI-1059156,EBI-3892947

Protein-protein interaction databases

BioGridi114651. 50 interactions.
DIPiDIP-41135N.
IntActiQ9P0L0. 45 interactions.
MINTiMINT-109415.
STRINGi9606.ENSP00000345656.

Structurei

Secondary structure

1
249
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 218Combined sources
Beta strandi23 – 275Combined sources
Beta strandi33 – 408Combined sources
Beta strandi43 – 453Combined sources
Beta strandi47 – 548Combined sources
Turni56 – 583Combined sources
Beta strandi59 – 635Combined sources
Beta strandi65 – 684Combined sources
Beta strandi73 – 808Combined sources
Beta strandi94 – 1018Combined sources
Helixi109 – 1157Combined sources
Turni118 – 1203Combined sources
Beta strandi122 – 13110Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RR3NMR-A11-135[»]
ProteinModelPortaliQ9P0L0.
SMRiQ9P0L0. Positions 9-135.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9P0L0.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 227227CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei228 – 24821Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 131118MSPPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili169 – 20537Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 MSP domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5066.
GeneTreeiENSGT00390000006947.
HOGENOMiHOG000293182.
HOVERGENiHBG028551.
InParanoidiQ9P0L0.
KOiK06096.
OMAiNPIDELE.
OrthoDBiEOG7CK389.
PhylomeDBiQ9P0L0.
TreeFamiTF317024.

Family and domain databases

Gene3Di2.60.40.360. 1 hit.
InterProiIPR000535. MSP_dom.
IPR008962. PapD-like.
IPR016763. Vesicle-associated_membrane.
[Graphical view]
PfamiPF00635. Motile_Sperm. 1 hit.
[Graphical view]
PIRSFiPIRSF019693. VAMP-associated. 1 hit.
SUPFAMiSSF49354. SSF49354. 1 hit.
PROSITEiPS50202. MSP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9P0L0) [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
MASASGAMAK HEQILVLDPP TDLKFKGPFT DVVTTNLKLR NPSDRKVCFK
60 70 80 90 100
VKTTAPRRYC VRPNSGIIDP GSTVTVSVML QPFDYDPNEK SKHKFMVQTI
110 120 130 140 150
FAPPNTSDME AVWKEAKPDE LMDSKLRCVF EMPNENDKLN DMEPSKAVPL
160 170 180 190 200
NASKQDGPMP KPHSVSLNDT ETRKLMEECK RLQGEMMKLS EENRHLRDEG
210 220 230 240
LRLRKVAHSD KPGSTSTASF RDNVTSPLPS LLVVIAAIFI GFFLGKFIL
Length:249
Mass (Da):27,893
Last modified:January 9, 2007 - v3
Checksum:i68B603F3A9FA5475
GO
Isoform 2 (identifier: Q9P0L0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     139-139: L → LGITPPGNAPTVTSMSSINNTVATPASYHTKDDPRGLSVLKQEKQK

Show »
Length:294
Mass (Da):32,614
Checksum:i8B2D033706621878
GO

Sequence cautioni

The sequence BG488667 differs from that shown. Reason: Frameshift at positions 72, 207 and 241.
The sequence AAD09742.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAF72105.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 112KH → ND in AAC26508. (PubMed:9657962)Curated
Sequence conflicti10 – 112KH → ND in AAV38424. 1 PublicationCurated
Sequence conflicti160 – 1601P → S in AAF72105. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti8 – 81M → T.
Corresponds to variant rs1044163 [ dbSNP | Ensembl ].
VAR_050440
Natural varianti104 – 1041P → L.
Corresponds to variant rs1127666 [ dbSNP | Ensembl ].
VAR_050441

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei139 – 1391L → LGITPPGNAPTVTSMSSINN TVATPASYHTKDDPRGLSVL KQEKQK in isoform 2. 1 PublicationVSP_038648

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF044670 mRNA. Translation: AAD09742.1. Different initiation.
AF154847 mRNA. Translation: AAF72105.1. Different initiation.
AC006238 Genomic DNA. No translation available.
CH471113 Genomic DNA. Translation: EAX01591.1.
CH471113 Genomic DNA. Translation: EAX01592.1.
BC002992 mRNA. Translation: AAH02992.2.
BG488667 mRNA. No translation available.
AF057358 mRNA. Translation: AAC26508.1.
AF086627 mRNA. Translation: AAD13576.1.
BT019618 mRNA. Translation: AAV38424.1.
CCDSiCCDS11847.2. [Q9P0L0-2]
CCDS11848.2. [Q9P0L0-1]
RefSeqiNP_003565.4. NM_003574.5. [Q9P0L0-2]
NP_919415.2. NM_194434.2. [Q9P0L0-1]
UniGeneiHs.165195.

Genome annotation databases

EnsembliENST00000340541; ENSP00000345656; ENSG00000101558. [Q9P0L0-2]
ENST00000400000; ENSP00000382880; ENSG00000101558. [Q9P0L0-1]
GeneIDi9218.
KEGGihsa:9218.
UCSCiuc002koj.3. human. [Q9P0L0-2]
uc002kok.3. human. [Q9P0L0-1]

Polymorphism databases

DMDMi122066680.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF044670 mRNA. Translation: AAD09742.1 . Different initiation.
AF154847 mRNA. Translation: AAF72105.1 . Different initiation.
AC006238 Genomic DNA. No translation available.
CH471113 Genomic DNA. Translation: EAX01591.1 .
CH471113 Genomic DNA. Translation: EAX01592.1 .
BC002992 mRNA. Translation: AAH02992.2 .
BG488667 mRNA. No translation available.
AF057358 mRNA. Translation: AAC26508.1 .
AF086627 mRNA. Translation: AAD13576.1 .
BT019618 mRNA. Translation: AAV38424.1 .
CCDSi CCDS11847.2. [Q9P0L0-2 ]
CCDS11848.2. [Q9P0L0-1 ]
RefSeqi NP_003565.4. NM_003574.5. [Q9P0L0-2 ]
NP_919415.2. NM_194434.2. [Q9P0L0-1 ]
UniGenei Hs.165195.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2RR3 NMR - A 11-135 [» ]
ProteinModelPortali Q9P0L0.
SMRi Q9P0L0. Positions 9-135.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114651. 50 interactions.
DIPi DIP-41135N.
IntActi Q9P0L0. 45 interactions.
MINTi MINT-109415.
STRINGi 9606.ENSP00000345656.

PTM databases

PhosphoSitei Q9P0L0.

Polymorphism databases

DMDMi 122066680.

Proteomic databases

MaxQBi Q9P0L0.
PaxDbi Q9P0L0.
PRIDEi Q9P0L0.

Protocols and materials databases

DNASUi 9218.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000340541 ; ENSP00000345656 ; ENSG00000101558 . [Q9P0L0-2 ]
ENST00000400000 ; ENSP00000382880 ; ENSG00000101558 . [Q9P0L0-1 ]
GeneIDi 9218.
KEGGi hsa:9218.
UCSCi uc002koj.3. human. [Q9P0L0-2 ]
uc002kok.3. human. [Q9P0L0-1 ]

Organism-specific databases

CTDi 9218.
GeneCardsi GC18P009904.
H-InvDB HIX0115359.
HGNCi HGNC:12648. VAPA.
HPAi HPA009174.
MIMi 605703. gene.
neXtProti NX_Q9P0L0.
PharmGKBi PA37272.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5066.
GeneTreei ENSGT00390000006947.
HOGENOMi HOG000293182.
HOVERGENi HBG028551.
InParanoidi Q9P0L0.
KOi K06096.
OMAi NPIDELE.
OrthoDBi EOG7CK389.
PhylomeDBi Q9P0L0.
TreeFami TF317024.

Enzyme and pathway databases

Reactomei REACT_115810. Sphingolipid de novo biosynthesis.

Miscellaneous databases

ChiTaRSi VAPA. human.
EvolutionaryTracei Q9P0L0.
GeneWikii VAPA.
GenomeRNAii 9218.
NextBioi 34557.
PMAP-CutDB Q9P0L0.
PROi Q9P0L0.
SOURCEi Search...

Gene expression databases

Bgeei Q9P0L0.
CleanExi HS_VAPA.
ExpressionAtlasi Q9P0L0. baseline and differential.
Genevestigatori Q9P0L0.

Family and domain databases

Gene3Di 2.60.40.360. 1 hit.
InterProi IPR000535. MSP_dom.
IPR008962. PapD-like.
IPR016763. Vesicle-associated_membrane.
[Graphical view ]
Pfami PF00635. Motile_Sperm. 1 hit.
[Graphical view ]
PIRSFi PIRSF019693. VAMP-associated. 1 hit.
SUPFAMi SSF49354. SSF49354. 1 hit.
PROSITEi PS50202. MSP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "VAP-33 localizes to both an intracellular vesicle population and with occludin at the tight junction."
    Lapierre L.A., Tuma P.L., Navarre J., Goldenring J.R., Anderson J.M.
    J. Cell Sci. 112:3723-3732(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH OCLN.
    Tissue: Liver.
  2. "Cloning and isolating human 33kDa Vamp-associated protein cDNA."
    Zhou H.J., Huang X.W., Zhou Y., Hu S.L., Yuan J.G., Qiang B.Q.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. 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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-199 (ISOFORM 2).
    Tissue: Lung.
  6. "Identification of a human homologue of the vesicle-associated membrane protein (VAMP)-associated protein of 33 kDa (VAP-33): a broadly expressed protein that binds to VAMP."
    Weir M.L., Klip A., Trimble W.S.
    Biochem. J. 333:247-251(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-249 (ISOFORM 1), INTERACTION WITH VAMP1 AND VAMP2.
    Tissue: Pancreatic islet.
  7. "Molecular cloning and characterization of mammalian homologues of vesicle-associated membrane protein-associated (VAMP-associated) proteins."
    Nishimura Y., Hayashi M., Inada H., Tanaka T.
    Biochem. Biophys. Res. Commun. 254:21-26(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-249 (ISOFORM 1).
    Tissue: B-cell.
  8. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-249 (ISOFORM 1).
  9. Cited for: FUNCTION, INTERACTION WITH VAPB; VAMP1; VAMP2; STX1A; BET1 AND SEC22C.
  10. "Promotion of neurite extension by protrudin requires its interaction with vesicle-associated membrane protein-associated protein."
    Saita S., Shirane M., Natume T., Iemura S., Nakayama K.I.
    J. Biol. Chem. 284:13766-13777(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ZFYVE27, MUTAGENESIS OF LYS-94 AND MET-96, SUBCELLULAR LOCATION.
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Viperin inhibits hepatitis C virus replication by interfering with binding of NS5A to host protein hVAP-33."
    Wang S., Wu X., Pan T., Song W., Wang Y., Zhang F., Yuan Z.
    J. Gen. Virol. 93:83-92(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RSAD2 AND HCV PROTEIN NS5A AND NS5B.
  14. "The antiviral effector IFITM3 disrupts intracellular cholesterol homeostasis to block viral entry."
    Amini-Bavil-Olyaee S., Choi Y.J., Lee J.H., Shi M., Huang I.C., Farzan M., Jung J.U.
    Cell Host Microbe 13:452-464(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IFITM3.
  15. "Electrostatic interaction between oxysterol-binding protein and VAMP-associated protein A revealed by NMR and mutagenesis studies."
    Furuita K., Jee J., Fukada H., Mishima M., Kojima C.
    J. Biol. Chem. 285:12961-12970(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 11-135, INTERACTION WITH OSBP.

Entry informationi

Entry nameiVAPA_HUMAN
AccessioniPrimary (citable) accession number: Q9P0L0
Secondary accession number(s): A6NDZ0
, D3DUI3, O75453, Q5U0E7, Q9UBZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: January 9, 2007
Last modified: October 29, 2014
This is version 136 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3