Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O95292 (VAPB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vesicle-associated membrane protein-associated protein B/C

Short name=VAMP-B/VAMP-C
Short name=VAMP-associated protein B/C
Short name=VAP-B/VAP-C
Gene names
Name:VAPB
ORF Names:UNQ484/PRO983
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length243 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Participates in the endoplasmic reticulum unfolded protein response (UPR) by inducing ERN1/IRE1 activity. Involved in cellular calcium homeostasis regulation. Ref.9 Ref.14 Ref.18

Subunit structure

Homodimer, and heterodimer with VAPA. Interacts with VAMP1 and VAMP2. Interacts with HCV NS5A and NS5B. Interacts (via MSP domain) with ZFYVE27. Interacts with RMDN3. Ref.7 Ref.13 Ref.18

Subcellular location

Endoplasmic reticulum membrane; Single-pass type IV membrane protein By similarity. Note: Present in mitochondria-associated membranes that are endoplasmic reticulum membrane regions closely apposed to the outer mitochondrial membrane. Ref.18

Tissue specificity

Ubiquitous. Isoform 1 predominates.

Involvement in disease

Amyotrophic lateral sclerosis 8 (ALS8) [MIM:608627]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.14 Ref.18 Ref.19

Spinal muscular atrophy, proximal, adult, autosomal dominant (SMAPAD) [MIM:182980]: A form of spinal muscular atrophy, a neuromuscular disorder characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. SMAPAD is characterized by proximal muscle weakness that begins in the lower limbs and then progresses to upper limbs, onset in late adulthood (after third decade) and a benign course. Most of the patients remain ambulatory 10 to 40 years after clinical onset.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19

Sequence similarities

Belongs to the VAMP-associated protein (VAP) (TC 9.B.17) family. [View classification]

Contains 1 MSP domain.

Ontologies

Keywords
   Biological processHost-virus interaction
Unfolded protein response
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
   DiseaseAmyotrophic lateral sclerosis
Disease mutation
Neurodegeneration
   DomainCoiled coil
Transmembrane
Transmembrane helix
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of signaling protein activity involved in unfolded protein response

Inferred from direct assay Ref.14. Source: UniProtKB

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

cellular calcium ion homeostasis

Inferred from mutant phenotype Ref.18. Source: UniProtKB

endoplasmic reticulum unfolded protein response

Inferred from mutant phenotype Ref.9. Source: UniProtKB

modulation by virus of host morphology or physiology

Inferred from direct assay Ref.7. Source: UniProtKB

positive regulation of viral genome replication

Inferred from mutant phenotype Ref.7. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

sphingolipid biosynthetic process

Traceable author statement. Source: Reactome

sphingolipid metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.7. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay Ref.19Ref.9. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from direct assay Ref.7. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionbeta-tubulin binding

Inferred from direct assay PubMed 17540579. Source: UniProtKB

enzyme binding

Inferred from physical interaction PubMed 17540579. Source: UniProtKB

protein heterodimerization activity

Inferred from physical interaction Ref.7Ref.1. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction Ref.7PubMed 17540579Ref.1. Source: UniProtKB

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q034636EBI-1188298,EBI-8803426From a different organism.
Epha4Q031372EBI-1188298,EBI-1539152From a different organism.
YIF1AO950709EBI-1188298,EBI-2799703
ZFYVE27Q5T4F42EBI-1188298,EBI-3892947

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O95292-1)

Also known as: VAP-B;

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: O95292-2)

Also known as: VAP-C;

The sequence of this isoform differs from the canonical sequence as follows:
     71-99: VMLQPFDYDPNEKSKHKFMVQSMFAPTDT → GRRWTADEEDSAEQQPHFSISPNWEGRRP
     100-243: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6 Ref.12
Chain2 – 243242Vesicle-associated membrane protein-associated protein B/C
PRO_0000213473

Regions

Topological domain2 – 222221Cytoplasmic Potential
Transmembrane223 – 24321Helical; Anchor for type IV membrane protein; Potential
Domain7 – 124118MSP
Coiled coil159 – 19638 Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.12
Modified residue1501Phosphothreonine Ref.11 Ref.15
Modified residue1561Phosphoserine Ref.11 Ref.15
Modified residue1601Phosphoserine Ref.11 Ref.15

Natural variations

Alternative sequence71 – 9929VMLQP…APTDT → GRRWTADEEDSAEQQPHFSI SPNWEGRRP in isoform 2.
VSP_003277
Alternative sequence100 – 243144Missing in isoform 2.
VSP_003278
Natural variant461T → I in ALS8; it forms insoluble cytosolic aggregates; cannot activate the UPR pathway through ERN1/IRE1 induction; results in ubiquitinated aggregates accumulation and cell death. Ref.14
Corresponds to variant rs281875284 [ dbSNP | Ensembl ].
VAR_067964
Natural variant561P → S in ALS8 and SMAPAD; it forms insoluble cytosolic aggregates; cannot activate the UPR pathway; affects interaction with RMDN3; affects cellular calcium homeostasis. Ref.9 Ref.14 Ref.18 Ref.19
Corresponds to variant rs74315431 [ dbSNP | Ensembl ].
VAR_026743

Experimental info

Sequence conflict601I → V in AAF67013. Ref.2
Sequence conflict671I → L in AAF67013. Ref.2
Sequence conflict971T → P in AAF67013. Ref.2
Sequence conflict103 – 1064EAVW → DGTR in AAF67013. Ref.2

Secondary structure

......................... 243
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (VAP-B) [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 22AEEF9EC7FC0B3F

FASTA24327,228
        10         20         30         40         50         60 
MAKVEQVLSL EPQHELKFRG PFTDVVTTNL KLGNPTDRNV CFKVKTTAPR RYCVRPNSGI 

        70         80         90        100        110        120 
IDAGASINVS VMLQPFDYDP NEKSKHKFMV QSMFAPTDTS DMEAVWKEAK PEDLMDSKLR 

       130        140        150        160        170        180 
CVFELPAEND KPHDVEINKI ISTTASKTET PIVSKSLSSS LDDTEVKKVM EECKRLQGEV 

       190        200        210        220        230        240 
QRLREENKQF KEEDGLRMRK TVQSNSPISA LAPTGKEEGL STRLLALVVL FFIVGVIIGK 


IAL 

« Hide

Isoform 2 (VAP-C) [UniParc].

Checksum: 042285C56B89CCDC
Show »

FASTA9911,152

References

« Hide 'large scale' references
[1]"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] (ISOFORMS 1 AND 2).
Tissue: Brain and Heart.
[2]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Adrenal gland.
[3]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
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).
Tissue: Lymph.
[6]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-19.
Tissue: Platelet.
[7]"Human VAP-B is involved in hepatitis C virus replication through interaction with NS5A and NS5B."
Hamamoto I., Nishimura Y., Okamoto T., Aizaki H., Liu M., Mori Y., Abe T., Suzuki T., Lai M.M., Miyamura T., Moriishi K., Matsuura Y.
J. Virol. 79:13473-13482(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCV NS5A AND NS5B.
[8]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Characterization of amyotrophic lateral sclerosis-linked P56S mutation of vesicle-associated membrane protein-associated protein B (VAPB/ALS8)."
Kanekura K., Nishimoto I., Aiso S., Matsuoka M.
J. Biol. Chem. 281:30223-30233(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ENDOPLASMIC RETICULUM UNFOLDED PROTEIN RESPONSE, CHARACTERIZATION OF VARIANT ALS8 SER-56.
[10]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-150; SER-156 AND SER-160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[13]"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: INTERACTION WITH ZFYVE27.
[14]"Characterization of the properties of a novel mutation in VAPB in familial amyotrophic lateral sclerosis."
Chen H.J., Anagnostou G., Chai A., Withers J., Morris A., Adhikaree J., Pennetta G., de Belleroche J.S.
J. Biol. Chem. 285:40266-40281(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ENDOPLASMIC RETICULUM UNFOLDED PROTEIN RESPONSE, VARIANT ALS8 ILE-46, CHARACTERIZATION OF VARIANTS ALS8 ILE-46 AND SER-56.
[15]"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 THR-150; SER-156 AND SER-160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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].
[17]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"VAPB interacts with the mitochondrial protein PTPIP51 to regulate calcium homeostasis."
De Vos K.J., Morotz G.M., Stoica R., Tudor E.L., Lau K.F., Ackerley S., Warley A., Shaw C.E., Miller C.C.
Hum. Mol. Genet. 21:1299-1311(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELLULAR CALCIUM HOMEOSTASIS REGULATION, SUBCELLULAR LOCATION, INTERACTION WITH RMDN3, CHARACTERIZATION OF VARIANT ALS8 SER-56.
[19]"A mutation in the vesicle-trafficking protein VAPB causes late-onset spinal muscular atrophy and amyotrophic lateral sclerosis."
Nishimura A.L., Mitne-Neto M., Silva H.C., Richieri-Costa A., Middleton S., Cascio D., Kok F., Oliveira J.R., Gillingwater T., Webb J., Skehel P., Zatz M.
Am. J. Hum. Genet. 75:822-831(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALS8 SER-56, VARIANT SMAPAD SER-56.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF086628 mRNA. Translation: AAD13577.1.
AF086629 mRNA. Translation: AAD13578.1.
AF160212 mRNA. Translation: AAF67013.1.
AY358464 mRNA. Translation: AAQ88829.1.
AL035455 Genomic DNA. Translation: CAC15021.1.
AL035455 Genomic DNA. Translation: CAM27023.1.
BC001712 mRNA. Translation: AAH01712.1.
PIRJG0186.
RefSeqNP_001182606.1. NM_001195677.1.
NP_004729.1. NM_004738.4.
UniGeneHs.182625.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2MDKNMR-A1-125[»]
3IKKX-ray2.50A/B1-125[»]
ProteinModelPortalO95292.
SMRO95292. Positions 1-125.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114650. 35 interactions.
IntActO95292. 23 interactions.
STRING9606.ENSP00000417175.

Protein family/group databases

TCDB9.B.17.1.1. the vamp-associated protein (vap) family.

PTM databases

PhosphoSiteO95292.

Proteomic databases

PaxDbO95292.
PRIDEO95292.

Protocols and materials databases

DNASU9217.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000395802; ENSP00000379147; ENSG00000124164. [O95292-2]
ENST00000475243; ENSP00000417175; ENSG00000124164. [O95292-1]
GeneID9217.
KEGGhsa:9217.
UCSCuc002xza.3. human. [O95292-1]
uc002xzd.2. human. [O95292-2]

Organism-specific databases

CTD9217.
GeneCardsGC20P056964.
HGNCHGNC:12649. VAPB.
HPACAB013722.
HPA013144.
MIM182980. phenotype.
605704. gene.
608627. phenotype.
neXtProtNX_O95292.
Orphanet209335. Adult-onset proximal spinal muscular atrophy, autosomal dominant.
803. Amyotrophic lateral sclerosis.
PharmGKBPA37273.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5066.
HOGENOMHOG000293182.
HOVERGENHBG028551.
InParanoidO95292.
KOK10707.
OMAGLRMRKA.
OrthoDBEOG7CK389.
PhylomeDBO95292.
TreeFamTF317024.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressO95292.
BgeeO95292.
CleanExHS_VAPB.
GenevestigatorO95292.

Family and domain databases

Gene3D2.60.40.360. 1 hit.
InterProIPR000535. MSP_dom.
IPR008962. PapD-like.
IPR016763. Vesicle-associated_membrane.
[Graphical view]
PfamPF00635. Motile_Sperm. 1 hit.
[Graphical view]
PIRSFPIRSF019693. VAMP-associated. 1 hit.
SUPFAMSSF49354. SSF49354. 1 hit.
PROSITEPS50202. MSP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSVAPB. human.
EvolutionaryTraceO95292.
GeneWikiVAPB.
GenomeRNAi9217.
NextBio34553.
PROO95292.
SOURCESearch...

Entry information

Entry nameVAPB_HUMAN
AccessionPrimary (citable) accession number: O95292
Secondary accession number(s): A2A2F2, O95293, Q9P0H0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 135 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM