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Q9UEU0 (VTI1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vesicle transport through interaction with t-SNAREs homolog 1B
Alternative name(s):
Vesicle transport v-SNARE protein Vti1-like 1
Vti1-rp1
Gene names
Name:VTI1B
Synonyms:VTI1, VTI1L, VTI1L1, VTI2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length232 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

V-SNARE that mediates vesicle transport pathways through interactions with t-SNAREs on the target membrane. These interactions are proposed to mediate aspects of the specificity of vesicle trafficking and to promote fusion of the lipid bilayers. May be concerned with increased secretion of cytokines associated with cellular senescence.

Subunit structure

Forms a SNARE complex with STX7, STX8 and VAMP8 which functions in the homotypic fusion of late endosomes. Component of the SNARE complex composed of STX7, STX8, VAMP7 and VIT1B that is required for heterotypic fusion of late endosomes with lysosomes By similarity. May interact with STX17.

Subcellular location

Late endosome membrane; Single-pass type IV membrane protein. Lysosome membrane. Cytoplasmic granule Ref.10.

Tissue specificity

Expressed in all tissues examined.

Sequence similarities

Belongs to the VTI1 family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: Q9UEU0-1)

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 Short (identifier: Q9UEU0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 232231Vesicle transport through interaction with t-SNAREs homolog 1B
PRO_0000218228

Regions

Topological domain2 – 208207Cytoplasmic Potential
Transmembrane209 – 22921Helical; Anchor for type IV membrane protein; Potential
Topological domain230 – 2323Vesicular Potential
Coiled coil35 – 9864 Potential
Coiled coil161 – 19838 Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.11
Modified residue1381Phosphoserine By similarity

Natural variations

Alternative sequence1 – 6161Missing in isoform Short.
VSP_006753

Experimental info

Sequence conflict241D → N in AAC52016. Ref.1

Secondary structure

............ 232
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified February 20, 2007. Version 3.
Checksum: B421C2863235B9B1

FASTA23226,688
        10         20         30         40         50         60 
MASSAASSEH FEKLHEIFRG LHEDLQGVPE RLLGTAGTEE KKKLIRDFDE KQQEANETLA 

        70         80         90        100        110        120 
EMEEELRYAP LSFRNPMMSK LRNYRKDLAK LHREVRSTPL TATPGGRGDM KYGIYAVENE 

       130        140        150        160        170        180 
HMNRLQSQRA MLLQGTESLN RATQSIERSH RIATETDQIG SEIIEELGEQ RDQLERTKSR 

       190        200        210        220        230 
LVNTSENLSK SRKILRSMSR KVTTNKLLLS IIILLELAIL GGLVYYKFFR SH 

« Hide

Isoform Short [UniParc].

Checksum: 7BC64529E0DBE12C
Show »

FASTA17119,810

References

« Hide 'large scale' references
[1]"A human homolog can functionally replace the yeast vesicle-associated SNARE Vti1p in two vesicle transport pathways."
Fischer von Mollard G., Stevens T.H.
J. Biol. Chem. 273:2624-2630(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
Tissue: Glioblastoma and Hypothalamus.
[2]"A hVti1 homologue: its expression depends on population doubling levels in both normal and SV40-transformed human fibroblasts."
Li H.-C., Tahara H., Tsuyama N., Ide T.
Biochem. Biophys. Res. Commun. 247:70-74(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
Tissue: Fibroblast.
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
[5]"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] (ISOFORM LONG).
[6]"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 LONG).
Tissue: Kidney.
[7]"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.
[8]"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].
[9]"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].
[10]"The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes."
Itakura E., Kishi-Itakura C., Mizushima N.
Cell 151:1256-1269(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH STX17.
[11]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF035824 mRNA. Translation: AAC52016.1.
AF060902 mRNA. Translation: AAC73059.1.
CR456757 mRNA. Translation: CAG33038.1.
CR542095 mRNA. Translation: CAG46892.1.
BT019348 mRNA. Translation: AAV38155.1.
BC003142 mRNA. Translation: AAH03142.1.
CCDSCCDS9786.1. [Q9UEU0-1]
RefSeqNP_006361.1. NM_006370.2. [Q9UEU0-1]
UniGeneHs.741177.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2V8SX-ray2.22V1-96[»]
ProteinModelPortalQ9UEU0.
SMRQ9UEU0. Positions 2-94, 139-197.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115753. 7 interactions.
IntActQ9UEU0. 5 interactions.
MINTMINT-1429590.
STRING9606.ENSP00000216456.

PTM databases

PhosphoSiteQ9UEU0.

Polymorphism databases

DMDM126302613.

Proteomic databases

MaxQBQ9UEU0.
PaxDbQ9UEU0.
PRIDEQ9UEU0.

Protocols and materials databases

DNASU10490.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000554659; ENSP00000450731; ENSG00000100568. [Q9UEU0-1]
GeneID10490.
KEGGhsa:10490.
UCSCuc001xjt.3. human. [Q9UEU0-1]

Organism-specific databases

CTD10490.
GeneCardsGC14M068117.
HGNCHGNC:17793. VTI1B.
HPAHPA044121.
MIM603207. gene.
neXtProtNX_Q9UEU0.
PharmGKBPA134861090.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG291765.
HOGENOMHOG000116573.
HOVERGENHBG058837.
InParanoidQ9UEU0.
KOK08493.
OMAYYKFFHK.
OrthoDBEOG70KGQQ.
PhylomeDBQ9UEU0.
TreeFamTF312874.

Gene expression databases

ArrayExpressQ9UEU0.
BgeeQ9UEU0.
GenevestigatorQ9UEU0.

Family and domain databases

InterProIPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
IPR007705. Vesicle_trsprt_v-SNARE_N.
[Graphical view]
PfamPF05008. V-SNARE. 1 hit.
[Graphical view]
SMARTSM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMSSF47661. SSF47661. 1 hit.
ProtoNetSearch...

Other

ChiTaRSVTI1B. human.
EvolutionaryTraceQ9UEU0.
GeneWikiVTI1B.
GenomeRNAi10490.
NextBio39804.
PROQ9UEU0.
SOURCESearch...

Entry information

Entry nameVTI1B_HUMAN
AccessionPrimary (citable) accession number: Q9UEU0
Secondary accession number(s): O43547, Q96J28
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: February 20, 2007
Last modified: July 9, 2014
This is version 127 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 chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM