VTI1B

Protein-coding gene in the species Homo sapiens

VTI1B

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
2V8S

Identifiers

Aliases

VTI1B, VTI1, VTI1-LIKE, VTI1L, VTI2, v-SNARE, vti1-rp1, vesicle transport through interaction with t-SNAREs 1B

External IDs

OMIM: 603207; MGI: 1855688; HomoloGene: 38178; GeneCards: VTI1B; OMA:VTI1B - orthologs

Gene location (Human)

Chr.	Chromosome 14 (human)^[1]

Band	14q24.1	Start	67,647,085 bp^[1]
Band	14q24.1	End	67,674,820 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 12 (mouse)^[2]

Band	12\|12 C3	Start	79,202,791 bp^[2]
Band	12\|12 C3	End	79,219,441 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

C1 segment

amygdala

anterior cingulate cortex

nucleus accumbens

prefrontal cortex

right frontal lobe

putamen

caudate nucleus

hypothalamus

optic nerve

Top expressed in

dorsal striatum

globus pallidus

olfactory tubercle

amygdala

nucleus accumbens

transitional epithelium of urinary bladder

cingulate gyrus

arcuate nucleus

prefrontal cortex

paraventricular nucleus of hypothalamus

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	SNAP receptor activity protein binding chloride channel inhibitor activity SNARE binding
Cellular component	integral component of membrane recycling endosome vesicle endosome Golgi apparatus intracellular membrane-bounded organelle late endosome membrane synaptic vesicle membrane lysosomal membrane neuronal cell body perinuclear region of cytoplasm lysosome ER to Golgi transport vesicle membrane SNARE complex endoplasmic reticulum membrane extracellular region cytosol platelet alpha granule lumen early endosome membrane recycling endosome membrane
Biological process	membrane fusion vesicle docking involved in exocytosis autophagosome maturation protein transport cell population proliferation intracellular protein transport vesicle-mediated transport regulation of protein localization to plasma membrane Golgi to vacuole transport vesicle fusion with Golgi apparatus endoplasmic reticulum to Golgi vesicle-mediated transport intra-Golgi vesicle-mediated transport protein targeting to vacuole retrograde transport, endosome to Golgi platelet degranulation
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


10490


53612

Ensembl


ENSG00000100568


ENSMUSG00000021124

UniProt


Q9UEU0


O88384

RefSeq (mRNA)


NM_006370


NM_016800 NM_001364374

RefSeq (protein)


NP_006361


n/a

Location (UCSC)

Chr 14: 67.65 – 67.67 Mb

Chr 12: 79.2 – 79.22 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Vesicle transport through interaction with t-SNAREs homolog 1B is a protein that in humans is encoded by the VTI1B gene.^[5]^[6]^[7]

Interactions

VTI1B has been shown to interact with STX8.^[8]^[9]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000100568 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000021124 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Li HC, Tahara H, Tsuyama N, Ide T (July 1998). "A hVti1 homologue: its expression depends on population doubling levels in both normal and SV40-transformed human fibroblasts". Biochem Biophys Res Commun. 247 (1): 70–4. doi:10.1006/bbrc.1998.8737. PMID 9636656.
^ Fischer von Mollard G, Stevens TH (February 1998). "A human homolog can functionally replace the yeast vesicle-associated SNARE Vti1p in two vesicle transport pathways". J Biol Chem. 273 (5): 2624–30. doi:10.1074/jbc.273.5.2624. PMID 9446565.
^ "Entrez Gene: VTI1B vesicle transport through interaction with t-SNAREs homolog 1B (yeast)".
^ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
^ Subramaniam VN, Loh E, Horstmann H, Habermann A, Xu Y, Coe J, Griffiths G, Hong W (March 2000). "Preferential association of syntaxin 8 with the early endosome" (PDF). J. Cell Sci. 113 (6): 997–1008. doi:10.1242/jcs.113.6.997. PMID 10683148.

Subramaniam VN, Loh E, Horstmann H, Habermann A, Xu Y, Coe J, Griffiths G, Hong W (2000). "Preferential association of syntaxin 8 with the early endosome" (PDF). J. Cell Sci. 113 (6): 997–1008. doi:10.1242/jcs.113.6.997. PMID 10683148.
Antonin W, Holroyd C, Fasshauer D, Pabst S, Von Mollard GF, Jahn R (2001). "A SNARE complex mediating fusion of late endosomes defines conserved properties of SNARE structure and function". EMBO J. 19 (23): 6453–64. doi:10.1093/emboj/19.23.6453. PMC 305878. PMID 11101518.
Wade N, Bryant NJ, Connolly LM, Simpson RJ, Luzio JP, Piper RC, James DE (2001). "Syntaxin 7 complexes with mouse Vps10p tail interactor 1b, syntaxin 6, vesicle-associated membrane protein (VAMP)8, and VAMP7 in b16 melanoma cells". J. Biol. Chem. 276 (23): 19820–7. doi:10.1074/jbc.M010838200. PMID 11278762.
Antonin W, Fasshauer D, Becker S, Jahn R, Schneider TR (2002). "Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs". Nat. Struct. Biol. 9 (2): 107–11. doi:10.1038/nsb746. hdl:11858/00-001M-0000-0012-F459-F. PMID 11786915. S2CID 17724790.
Kreykenbohm V, Wenzel D, Antonin W, Atlachkine V, von Mollard GF (2003). "The SNAREs vti1a and vti1b have distinct localization and SNARE complex partners". Eur. J. Cell Biol. 81 (5): 273–80. doi:10.1078/0171-9335-00247. hdl:11858/00-001M-0000-0012-F3DF-D. PMID 12067063.
Antonin W, Dulubova I, Arac D, Pabst S, Plitzner J, Rizo J, Jahn R (2002). "The N-terminal domains of syntaxin 7 and vti1b form three-helix bundles that differ in their ability to regulate SNARE complex assembly". J. Biol. Chem. 277 (39): 36449–56. doi:10.1074/jbc.M204369200. hdl:11858/00-001M-0000-0012-F2E6-3. PMID 12114520.
Bogdanovic A, Bennett N, Kieffer S, Louwagie M, Morio T, Garin J, Satre M, Bruckert F (2002). "Syntaxin 7, syntaxin 8, Vti1 and VAMP7 (vesicle-associated membrane protein 7) form an active SNARE complex for early macropinocytic compartment fusion in Dictyostelium discoideum". Biochem. J. 368 (Pt 1): 29–39. doi:10.1042/BJ20020845. PMC 1222979. PMID 12175335.
Martinez-Arca S, Rudge R, Vacca M, Raposo G, Camonis J, Proux-Gillardeaux V, Daviet L, Formstecher E, Hamburger A, Filippini F, D'Esposito M, Galli T (2003). "A dual mechanism controlling the localization and function of exocytic v-SNAREs". Proc. Natl. Acad. Sci. U.S.A. 100 (15): 9011–6. Bibcode:2003PNAS..100.9011M. doi:10.1073/pnas.1431910100. PMC 166429. PMID 12853575.
Yan Q, Sun W, McNew JA, Vida TA, Bean AJ (2004). "Ca2+ and N-ethylmaleimide-sensitive factor differentially regulate disassembly of SNARE complexes on early endosomes". J. Biol. Chem. 279 (18): 18270–6. doi:10.1074/jbc.M400093200. PMID 14769786.
Hirst J, Miller SE, Taylor MJ, von Mollard GF, Robinson MS (2005). "EpsinR is an adaptor for the SNARE protein Vti1b". Mol. Biol. Cell. 15 (12): 5593–602. doi:10.1091/mbc.E04-06-0468. PMC 532037. PMID 15371541.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.