[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). TISSUE=Brain, and Heart; DOI=10.1006/bbrc.1998.9876; PubMed=9920726 [NCBI, ExPASy, EBI, Israel, Japan] Nishimura Y., Hayashi M., Inada H., Tanaka T.; "Molecular cloning and characterization of mammalian homologues of vesicle-associated membrane protein-associated (VAMP-associated) proteins."; Biochem. Biophys. Res. Commun. 254:21-26(1999).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Adrenal gland; DOI=10.1073/pnas.160270997; PubMed=10931946 [NCBI, ExPASy, EBI, Israel, Japan] 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., 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.; "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."; Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). DOI=10.1101/gr.1293003; PubMed=12975309 [NCBI, ExPASy, EBI, Israel, Japan] 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., 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.; "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."; Genome Res. 13:2265-2270(2003).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1038/414865a; PubMed=11780052 [NCBI, ExPASy, EBI, Israel, Japan] 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., 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.; "The DNA sequence and comparative analysis of human chromosome 20."; Nature 414:865-871(2001).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Lymph; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[6]	PROTEIN SEQUENCE OF 2-19. TISSUE=Platelet; DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan] Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.; "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."; Nat. Biotechnol. 21:566-569(2003).
[7]	INTERACTION WITH HCV NS5A AND NS5B. DOI=10.1128/JVI.79.21.13473-13482.2005; PubMed=16227268 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Human VAP-B is involved in hepatitis C virus replication through interaction with NS5A and NS5B."; J. Virol. 79:13473-13482(2005).
[8]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159 AND SER-160, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."; Cell 127:635-648(2006).
[9]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1073/pnas.0507066103; PubMed=16565220 [NCBI, ExPASy, EBI, Israel, Japan] Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; "Phosphoproteome analysis of the human mitotic spindle."; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
[10]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-150; SER-156 AND SER-160, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan] Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.; "A quantitative atlas of mitotic phosphorylation."; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.
[12]	VARIANT ALS8/SMAF SER-56. DOI=10.1086/425287; PubMed=15372378 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "A mutation in the vesicle-trafficking protein VAPB causes late-onset spinal muscular atrophy and amyotrophic lateral sclerosis."; Am. J. Hum. Genet. 75:822-831(2004).

Comments

FUNCTION: May play a role in vesicle trafficking.
SUBUNIT: Homodimer, and heterodimer with VAPA. Interacts with VAMP1 and VAMP2. Interacts with HCV NS5A and NS5B.
INTERACTION:
Q03137:Epha4 (xeno); NbExp=1; IntAct=EBI-1188298, EBI-1539152;
SUBCELLULAR LOCATION: Cell membrane; Single-pass type IV membrane protein (By similarity). Endomembrane system; Single-pass type IV membrane protein (By similarity). Note=Present in the plasma membrane and in intracellular vesicles (By similarity).

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	1
Synonyms	VAP-B
Isoform ID	O95292-1
This is the isoform sequence displayed in this entry.

Name	2
Synonyms	VAP-C
Isoform ID	O95292-2
Features which should be applied to build the isoform sequence: VSP_003277, VSP_003278.

TISSUE SPECIFICITY: Ubiquitous. Isoform 1 predominates.
DISEASE: Defects in VAPB are the cause of amyotrophic lateral sclerosis type 8 (ALS8) [MIM:608627]. ALS8 is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. 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 cases leading to familial forms.
DISEASE: Defects in VAPB are a cause of spinal muscular atrophy autosomal dominant Finkel type (SMAF) [MIM:182980]; also called late-onset spinal muscular atrophy Finkel type or spinal muscular atrophy proximal adult autosomal dominant. Spinal muscular atrophy refers to a group of neuromuscular disorders characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. SMAF 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.
SIMILARITY: Contains 1 MSP domain.
WEB RESOURCE: Name=Alsod; Note=ALS genetic mutations db; URL="http://alsod.iop.kcl.ac.uk/Als/";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=VAPB";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF086628; AAD13577.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF086629; AAD13578.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF160212; AAF67013.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY358464; AAQ88829.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL035455; CAC15021.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL035455; CAM27023.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001712; AAH01712.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00006211; -.
IPI00748221; -.

JG0186; JG0186.

NP_004729.1; -.

3D structure databases

SMR

O95292; 1-134.

ModBase

O95292.

Protein-protein interaction databases

IntAct

O95292; 2.

Protein family/group databases

TCDB

9.B.17.1.1; VAMP-associated protein (VAP) family.

PTM databases

PhosphoSite

O95292; -.

Organism-specific databases

GC20P056397; -.

HIX0015950; -.

HGNC:12649; VAPB.

CAB013722; -.
HPA013144; -.

MIM

182980; phenotype. [NCBI / EBI]
605704; gene. [NCBI / EBI]
608627; phenotype. [NCBI / EBI]

Orphanet

803; Amyotrophic lateral sclerosis.
70; Proximal spinal muscular atrophy.

PharmGKB

PA37273; -.

Gene expression databases

O95292; -.

O95292; -.

HS_VAPB; -.

ENSG00000124164; Homo sapiens.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from direct assay from UniProtKB).
GO:0005794;	Cellular component: Golgi apparatus (inferred from direct assay from UniProtKB).
GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0048487;	Molecular function: beta-tubulin binding (inferred from direct assay from UniProtKB).
GO:0019899;	Molecular function: enzyme binding (inferred from physical interaction from UniProtKB).
GO:0046982;	Molecular function: protein heterodimerization activity (inferred from physical interaction from UniProtKB).
GO:0042803;	Molecular function: protein homodimerization activity (inferred from physical interaction from UniProtKB).
GO:0005198;	Molecular function: structural molecule activity (inferred from electronic annotation from InterPro).
GO:0008219;	Biological process: cell death (inferred from electronic annotation from UniProtKB-KW).
GO:0030968;	Biological process: endoplasmic reticulum unfolded protein response (inferred from mutant phenotype from UniProtKB).
GO:0045070;	Biological process: positive regulation of viral genome replication (inferred from mutant phenotype from UniProtKB).
GO:0019048;	Biological process: virus-host interaction (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR000535; Major_sperm.
IPR008962; PapD-like.
IPR016763; Vesicle-associated_membrane.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.40.360; MSP; 1.

Pfam

PF00635; Motile_Sperm; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF019693; VAMP-associated; 1.

PROSITE

PS50202; MSP; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

O95292; -.

Genome annotation databases

Ensembl

ENSG00000124164; Homo sapiens. [Contig view]

GeneID

9217; -.

KEGG

hsa:9217; -.

Phylogenomic databases

HOGENOM

O95292; -.

HOVERGEN

O95292; -.

OMA

O95292; KTAQSNS.

Other

34553; -.

VAPB; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; Amyotrophic lateral sclerosis; Cell membrane; Coiled coil; Direct protein sequencing; Disease mutation; Host-virus interaction; Membrane; Neurodegeneration; Phosphoprotein; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 243`	`242`	`Vesicle-associated membrane protein-associated protein B/C.`	`PRO_0000213473`
`TOPO_DOM`	`2 222`	`221`	`Cytoplasmic (Potential).`
`TRANSMEM`	`223 243`	`21`	`Anchor for type IV membrane protein (Potential).`
`DOMAIN`	`7 124`	`118`	`MSP.`
`COILED`	`159 196`	`38`	`Potential.`
`MOD_RES`	`150 150`		`Phosphothreonine.`
`MOD_RES`	`156 156`		`Phosphoserine.`
`MOD_RES`	`159 159`		`Phosphoserine.`
`MOD_RES`	`160 160`		`Phosphoserine.`
`MOD_RES`	`206 206`		`Phosphoserine.`
`VAR_SEQ`	`71 99`		`VMLQPFDYDPNEKSKHKFMVQSMFAPTDT -> GRRWTADEEDSAEQQPHFSISPNWEGRRP (in isoform 2).`	`VSP_003277`
`VAR_SEQ`	`100 243`		`Missing (in isoform 2).`	`VSP_003278`
`VARIANT`	`56 56`	`1`	`P -> S (in ALS8 and SMAF).`	`VAR_026743 [3D]`
`CONFLICT`	`60 60`		`I -> V (in Ref. 2; AAF67013).`
`CONFLICT`	`67 67`		`I -> L (in Ref. 2; AAF67013).`
`CONFLICT`	`97 97`		`T -> P (in Ref. 2; AAF67013).`
`CONFLICT`	`103 106`		`EAVW -> DGTR (in Ref. 2; AAF67013).`

Sequence information

Length: 243 AA [This is the length of the unprocessed precursor]

Molecular weight: 27228 Da [This is the MW of the unprocessed precursor]

CRC64: 22AEEF9EC7FC0B3F [This is a checksum on the sequence]

        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

O95292 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools