HUMAN:VAPA

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	VAPA (synonyms: VAP33)
Protein Name(s)	Vesicle-associated membrane protein-associated protein A VAMP-A VAMP-associated protein A VAP-A 33 kDa VAMP-associated protein VAP-33
External Links
UniProt	Q9P0L0
EMBL	AF044670 AF154847 AC006238 CH471113 CH471113 BC002992 BG488667 AF057358 AF086627 BT019618
CCDS	CCDS11847.2 CCDS11848.2
RefSeq	NP_003565.4 NP_919415.2
UniGene	Hs.165195
PDB	2RR3
PDBsum	2RR3
ProteinModelPortal	Q9P0L0
SMR	Q9P0L0
BioGrid	114651
DIP	DIP-41135N
IntAct	Q9P0L0
MINT	MINT-109415
STRING	9606.ENSP00000345656
PhosphoSite	Q9P0L0
DMDM	122066680
MaxQB	Q9P0L0
PaxDb	Q9P0L0
PRIDE	Q9P0L0
DNASU	9218
Ensembl	ENST00000340541 ENST00000400000
GeneID	9218
KEGG	hsa:9218
UCSC	uc002koj.3 uc002kok.3
CTD	9218
GeneCards	GC18P009904
H-InvDB	HIX0115359
HGNC	HGNC:12648
HPA	HPA009174
MIM	605703
neXtProt	NX_Q9P0L0
PharmGKB	PA37272
eggNOG	COG5066
GeneTree	ENSGT00390000006947
HOGENOM	HOG000293182
HOVERGEN	HBG028551
InParanoid	Q9P0L0
KO	K06096
OMA	FEMPSEN
OrthoDB	EOG7CK389
PhylomeDB	Q9P0L0
TreeFam	TF317024
Reactome	REACT_115810
ChiTaRS	VAPA
EvolutionaryTrace	Q9P0L0
GeneWiki	VAPA
GenomeRNAi	9218
NextBio	34557
PMAP-CutDB	Q9P0L0
PRO	PR:Q9P0L0
Proteomes	UP000005640
Bgee	Q9P0L0
CleanEx	HS_VAPA
ExpressionAtlas	Q9P0L0
Genevestigator	Q9P0L0
GO	GO:0005783 GO:0005789 GO:0016021 GO:0015630 GO:0005886 GO:0031982 GO:0046982 GO:0004871 GO:0005198 GO:0008219 GO:0061025 GO:0031175 GO:0043123 GO:0070972 GO:0007165 GO:0044281 GO:0030148 GO:0006665
Gene3D	2.60.40.360
InterPro	IPR000535 IPR008962 IPR016763 IPR030229
PANTHER	PTHR10809 PTHR10809:SF40
Pfam	PF00635
PIRSF	PIRSF019693
SUPFAM	SSF49354
PROSITE	PS50202

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0006944	cellular membrane fusion	PMID:23142642^[1]	ECO:0000314			P		Table 1 shows the VAPA protein and its involvement in cellular membrane fusion and lipid metabolism.	complete CACAO 5759
enables	GO:0045296	cadherin binding	PMID:25468996^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:16791210^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0019904	protein domain specific binding	PMID:20178991^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P22059	F		Seeded From UniProt	complete
enables	GO:0008017	microtubule binding	PMID:18713837^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0090114	COPII-coated vesicle budding	PMID:18713837^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
NOT\|involved_in	GO:0034975	protein folding in endoplasmic reticulum	PMID:18713837^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0033149	FFAT motif binding	PMID:18713837^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006888	endoplasmic reticulum to Golgi vesicle-mediated transport	PMID:18713837^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
NOT\|involved_in	GO:0007029	endoplasmic reticulum organization	PMID:18713837^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
NOT\|part_of	GO:0070971	endoplasmic reticulum exit site	PMID:18713837^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:18713837^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0044829	positive regulation by host of viral genome replication	PMID:19515777^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	has_input:(UniProtKB:Q99IB8)	Seeded From UniProt	complete
involved_in	GO:0044828	negative regulation by host of viral genome replication	PMID:19515777^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	has_input:(UniProtKB:Q9WMX2)	Seeded From UniProt	complete
involved_in	GO:0044791	positive regulation by host of viral release from host cell	PMID:19515777^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	has_input:(UniProtKB:Q99IB8)	Seeded From UniProt	complete
involved_in	GO:0070972	protein localization to endoplasmic reticulum	PMID:19289470^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
colocalizes_with	GO:0048471	perinuclear region of cytoplasm	PMID:16895911^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:9920726^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O95292	F		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:16227268^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O95292	F		Seeded From UniProt	complete
involved_in	GO:0043123	positive regulation of I-kappaB kinase/NF-kappaB signaling	PMID:12761501^[11]	ECO:0007001	high throughput mutant phenotypic evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0031982	vesicle	PMID:10523508^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0031175	neuron projection development	PMID:19289470^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0008219	cell death	PMID:19289470^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
colocalizes_with	GO:0005923	bicellular tight junction	PMID:10523508^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:10523508^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:19289470^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0000139	Golgi membrane	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0090114	C		Seeded From UniProt	complete
part_of	GO:0015630	microtubule cytoskeleton	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WV55 ensembl:ENSMUSP00000024897	C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9WV55 ensembl:ENSMUSP00000024897	C		Seeded From UniProt	complete
part_of	GO:0005789	endoplasmic reticulum membrane	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR016763 InterPro:IPR030229	C		Seeded From UniProt	complete
enables	GO:0033149	FFAT motif binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR030229	F		Seeded From UniProt	complete
involved_in	GO:0070972	protein localization to endoplasmic reticulum	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR030229	P		Seeded From UniProt	complete
involved_in	GO:0061025	membrane fusion	PMID:9657962^[13]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043312	neutrophil degranulation	Reactome:R-HSA-6798695	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0035577	azurophil granule membrane	Reactome:R-HSA-6798739	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0030148	sphingolipid biosynthetic process	Reactome:R-HSA-1660661	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	Reactome:R-HSA-6798739	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005789	endoplasmic reticulum membrane	Reactome:R-HSA-429732 Reactome:R-HSA-429730 Reactome:R-HSA-429699 Reactome:R-HSA-429694 Reactome:R-HSA-429683	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
part_of	GO:0030054	cell junction	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0965	C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0256	C		Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0812	C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0039	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539	C		Seeded From UniProt	complete
part_of	GO:0005923	bicellular tight junction	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0796 UniProtKB-SubCell:SL-0265	C		Seeded From UniProt	complete
part_of	GO:0005789	endoplasmic reticulum membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0097	C		Seeded From UniProt	complete
part_of	GO:0031965	nuclear membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0182	C		Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ Passantino, R et al. (2013) Identifying protein partners of CLN8, an ER-resident protein involved in neuronal ceroid lipofuscinosis. Biochim. Biophys. Acta 1833 529-40 PubMed GONUTS page
↑ Guo, Z et al. (2014) E-cadherin interactome complexity and robustness resolved by quantitative proteomics. Sci Signal 7 rs7 PubMed GONUTS page
↑ Sigal, A et al. (2006) Dynamic proteomics in individual human cells uncovers widespread cell-cycle dependence of nuclear proteins. Nat. Methods 3 525-31 PubMed GONUTS page
↑ Furuita, K et al. (2010) Electrostatic interaction between oxysterol-binding protein and VAMP-associated protein A revealed by NMR and mutagenesis studies. J. Biol. Chem. 285 12961-70 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 ^5.7 Prosser, DC et al. (2008) FFAT rescues VAPA-mediated inhibition of ER-to-Golgi transport and VAPB-mediated ER aggregation. J. Cell. Sci. 121 3052-61 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Kukihara, H et al. (2009) Human VAP-C negatively regulates hepatitis C virus propagation. J. Virol. 83 7959-69 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 Saita, S et al. (2009) Promotion of neurite extension by protrudin requires its interaction with vesicle-associated membrane protein-associated protein. J. Biol. Chem. 284 13766-77 PubMed GONUTS page
↑ Kawano, M et al. (2006) Efficient trafficking of ceramide from the endoplasmic reticulum to the Golgi apparatus requires a VAMP-associated protein-interacting FFAT motif of CERT. J. Biol. Chem. 281 30279-88 PubMed GONUTS page
↑ Nishimura, Y et al. (1999) Molecular cloning and characterization of mammalian homologues of vesicle-associated membrane protein-associated (VAMP-associated) proteins. Biochem. Biophys. Res. Commun. 254 21-6 PubMed GONUTS page
↑ Hamamoto, I et al. (2005) Human VAP-B is involved in hepatitis C virus replication through interaction with NS5A and NS5B. J. Virol. 79 13473-82 PubMed GONUTS page
↑ Matsuda, A et al. (2003) Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. Oncogene 22 3307-18 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 Lapierre, LA et al. (1999) VAP-33 localizes to both an intracellular vesicle population and with occludin at the tight junction. J. Cell. Sci. 112 ( Pt 21) 3723-32 PubMed GONUTS page
↑ Weir, ML et al. (1998) 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. Biochem. J. 333 ( Pt 2) 247-51 PubMed GONUTS page

[PMID:23142642-1] Passantino, R et al. (2013) Identifying protein partners of CLN8, an ER-resident protein involved in neuronal ceroid lipofuscinosis. Biochim. Biophys. Acta 1833 529-40 PubMed GONUTS page

[PMID:25468996-2] Guo, Z et al. (2014) E-cadherin interactome complexity and robustness resolved by quantitative proteomics. Sci Signal 7 rs7 PubMed GONUTS page

[PMID:16791210-3] Sigal, A et al. (2006) Dynamic proteomics in individual human cells uncovers widespread cell-cycle dependence of nuclear proteins. Nat. Methods 3 525-31 PubMed GONUTS page

[PMID:20178991-4] Furuita, K et al. (2010) Electrostatic interaction between oxysterol-binding protein and VAMP-associated protein A revealed by NMR and mutagenesis studies. J. Biol. Chem. 285 12961-70 PubMed GONUTS page

[PMID:18713837-5] 5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 ^5.7 Prosser, DC et al. (2008) FFAT rescues VAPA-mediated inhibition of ER-to-Golgi transport and VAPB-mediated ER aggregation. J. Cell. Sci. 121 3052-61 PubMed GONUTS page

[PMID:19515777-6] 6.0 ^6.1 ^6.2 Kukihara, H et al. (2009) Human VAP-C negatively regulates hepatitis C virus propagation. J. Virol. 83 7959-69 PubMed GONUTS page

[PMID:19289470-7] 7.0 ^7.1 ^7.2 ^7.3 Saita, S et al. (2009) Promotion of neurite extension by protrudin requires its interaction with vesicle-associated membrane protein-associated protein. J. Biol. Chem. 284 13766-77 PubMed GONUTS page

[PMID:16895911-8] Kawano, M et al. (2006) Efficient trafficking of ceramide from the endoplasmic reticulum to the Golgi apparatus requires a VAMP-associated protein-interacting FFAT motif of CERT. J. Biol. Chem. 281 30279-88 PubMed GONUTS page

[PMID:9920726-9] Nishimura, Y et al. (1999) Molecular cloning and characterization of mammalian homologues of vesicle-associated membrane protein-associated (VAMP-associated) proteins. Biochem. Biophys. Res. Commun. 254 21-6 PubMed GONUTS page

[PMID:16227268-10] Hamamoto, I et al. (2005) Human VAP-B is involved in hepatitis C virus replication through interaction with NS5A and NS5B. J. Virol. 79 13473-82 PubMed GONUTS page

[PMID:12761501-11] Matsuda, A et al. (2003) Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. Oncogene 22 3307-18 PubMed GONUTS page

[PMID:10523508-12] 12.0 ^12.1 ^12.2 Lapierre, LA et al. (1999) VAP-33 localizes to both an intracellular vesicle population and with occludin at the tight junction. J. Cell. Sci. 112 ( Pt 21) 3723-32 PubMed GONUTS page

[PMID:9657962-13] Weir, ML et al. (1998) 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. Biochem. J. 333 ( Pt 2) 247-51 PubMed GONUTS page

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

[13]

HUMAN:VAPA

Contents

Annotations

Notes

References

a

b

c

e

f

g

h

i

m

n

o

p

s

v

Navigation menu

Personal tools

Namespaces

Variants

Views

More

Search

Navigation

Cacao

Links

Tools