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Q9UEU0

- VTI1B_HUMAN

UniProt

Q9UEU0 - VTI1B_HUMAN

Protein

Vesicle transport through interaction with t-SNAREs homolog 1B

Gene

VTI1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 3 (20 Feb 2007)
      Previous versions | rss
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    Functioni

    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.

    GO - Molecular functioni

    1. SNARE binding Source: MGI

    GO - Biological processi

    1. cell proliferation Source: ProtInc
    2. intracellular protein transport Source: InterPro
    3. membrane fusion Source: ProtInc
    4. vesicle docking involved in exocytosis Source: ProtInc
    5. vesicle-mediated transport Source: ProtInc

    Keywords - Biological processi

    Protein transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Vesicle transport through interaction with t-SNAREs homolog 1B
    Alternative name(s):
    Vesicle transport v-SNARE protein Vti1-like 1
    Vti1-rp1
    Gene namesi
    Name:VTI1B
    Synonyms:VTI1, VTI1L, VTI1L1, VTI2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:17793. VTI1B.

    Subcellular locationi

    Late endosome membrane 1 Publication; Single-pass type IV membrane protein 1 Publication. Lysosome membrane 1 Publication. Cytoplasmic granule 1 Publication

    GO - Cellular componenti

    1. Golgi apparatus Source: UniProtKB
    2. integral component of membrane Source: UniProtKB-KW
    3. late endosome membrane Source: UniProtKB
    4. lysosomal membrane Source: UniProtKB
    5. neuronal cell body Source: ParkinsonsUK-UCL
    6. perinuclear region of cytoplasm Source: Ensembl
    7. SNARE complex Source: Ensembl
    8. synaptic vesicle Source: ParkinsonsUK-UCL

    Keywords - Cellular componenti

    Endosome, Lysosome, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134861090.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 232231Vesicle transport through interaction with t-SNAREs homolog 1BPRO_0000218228Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei138 – 1381PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9UEU0.
    PaxDbiQ9UEU0.
    PRIDEiQ9UEU0.

    PTM databases

    PhosphoSiteiQ9UEU0.

    Expressioni

    Tissue specificityi

    Expressed in all tissues examined.

    Gene expression databases

    ArrayExpressiQ9UEU0.
    BgeeiQ9UEU0.
    GenevestigatoriQ9UEU0.

    Organism-specific databases

    HPAiHPA044121.

    Interactioni

    Subunit structurei

    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.By similarity

    Protein-protein interaction databases

    BioGridi115753. 7 interactions.
    IntActiQ9UEU0. 5 interactions.
    MINTiMINT-1429590.
    STRINGi9606.ENSP00000216456.

    Structurei

    Secondary structure

    1
    232
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni4 – 63
    Helixi9 – 2618
    Turni29 – 313
    Beta strandi32 – 343
    Helixi39 – 6628
    Helixi71 – 9323

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2V8SX-ray2.22V1-96[»]
    ProteinModelPortaliQ9UEU0.
    SMRiQ9UEU0. Positions 2-94, 139-197.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UEU0.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 208207CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini230 – 2323VesicularSequence Analysis

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei209 – 22921Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili35 – 9864Sequence AnalysisAdd
    BLAST
    Coiled coili161 – 19838Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the VTI1 family.Curated

    Keywords - Domaini

    Coiled coil, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG291765.
    HOGENOMiHOG000116573.
    HOVERGENiHBG058837.
    InParanoidiQ9UEU0.
    KOiK08493.
    OMAiYYKFFHK.
    OrthoDBiEOG70KGQQ.
    PhylomeDBiQ9UEU0.
    TreeFamiTF312874.

    Family and domain databases

    InterProiIPR010989. t-SNARE.
    IPR000727. T_SNARE_dom.
    IPR007705. Vesicle_trsprt_v-SNARE_N.
    [Graphical view]
    PfamiPF05008. V-SNARE. 1 hit.
    [Graphical view]
    SMARTiSM00397. t_SNARE. 1 hit.
    [Graphical view]
    SUPFAMiSSF47661. SSF47661. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: Q9UEU0-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MASSAASSEH FEKLHEIFRG LHEDLQGVPE RLLGTAGTEE KKKLIRDFDE    50
    KQQEANETLA EMEEELRYAP LSFRNPMMSK LRNYRKDLAK LHREVRSTPL 100
    TATPGGRGDM KYGIYAVENE HMNRLQSQRA MLLQGTESLN RATQSIERSH 150
    RIATETDQIG SEIIEELGEQ RDQLERTKSR LVNTSENLSK SRKILRSMSR 200
    KVTTNKLLLS IIILLELAIL GGLVYYKFFR SH 232
    Length:232
    Mass (Da):26,688
    Last modified:February 20, 2007 - v3
    Checksum:iB421C2863235B9B1
    GO
    Isoform Short (identifier: Q9UEU0-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:171
    Mass (Da):19,810
    Checksum:i7BC64529E0DBE12C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti24 – 241D → N in AAC52016. (PubMed:9446565)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6161Missing in isoform Short. 1 PublicationVSP_006753Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS9786.1. [Q9UEU0-1]
    RefSeqiNP_006361.1. NM_006370.2. [Q9UEU0-1]
    UniGeneiHs.741177.

    Genome annotation databases

    EnsembliENST00000554659; ENSP00000450731; ENSG00000100568. [Q9UEU0-1]
    GeneIDi10490.
    KEGGihsa:10490.
    UCSCiuc001xjt.3. human. [Q9UEU0-1]

    Polymorphism databases

    DMDMi126302613.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS9786.1. [Q9UEU0-1 ]
    RefSeqi NP_006361.1. NM_006370.2. [Q9UEU0-1 ]
    UniGenei Hs.741177.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2V8S X-ray 2.22 V 1-96 [» ]
    ProteinModelPortali Q9UEU0.
    SMRi Q9UEU0. Positions 2-94, 139-197.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115753. 7 interactions.
    IntActi Q9UEU0. 5 interactions.
    MINTi MINT-1429590.
    STRINGi 9606.ENSP00000216456.

    PTM databases

    PhosphoSitei Q9UEU0.

    Polymorphism databases

    DMDMi 126302613.

    Proteomic databases

    MaxQBi Q9UEU0.
    PaxDbi Q9UEU0.
    PRIDEi Q9UEU0.

    Protocols and materials databases

    DNASUi 10490.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000554659 ; ENSP00000450731 ; ENSG00000100568 . [Q9UEU0-1 ]
    GeneIDi 10490.
    KEGGi hsa:10490.
    UCSCi uc001xjt.3. human. [Q9UEU0-1 ]

    Organism-specific databases

    CTDi 10490.
    GeneCardsi GC14M068117.
    HGNCi HGNC:17793. VTI1B.
    HPAi HPA044121.
    MIMi 603207. gene.
    neXtProti NX_Q9UEU0.
    PharmGKBi PA134861090.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG291765.
    HOGENOMi HOG000116573.
    HOVERGENi HBG058837.
    InParanoidi Q9UEU0.
    KOi K08493.
    OMAi YYKFFHK.
    OrthoDBi EOG70KGQQ.
    PhylomeDBi Q9UEU0.
    TreeFami TF312874.

    Miscellaneous databases

    ChiTaRSi VTI1B. human.
    EvolutionaryTracei Q9UEU0.
    GeneWikii VTI1B.
    GenomeRNAii 10490.
    NextBioi 39804.
    PROi Q9UEU0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UEU0.
    Bgeei Q9UEU0.
    Genevestigatori Q9UEU0.

    Family and domain databases

    InterProi IPR010989. t-SNARE.
    IPR000727. T_SNARE_dom.
    IPR007705. Vesicle_trsprt_v-SNARE_N.
    [Graphical view ]
    Pfami PF05008. V-SNARE. 1 hit.
    [Graphical view ]
    SMARTi SM00397. t_SNARE. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47661. SSF47661. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. 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].

    Entry informationi

    Entry nameiVTI1B_HUMAN
    AccessioniPrimary (citable) accession number: Q9UEU0
    Secondary accession number(s): O43547, Q96J28
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: February 20, 2007
    Last modified: October 1, 2014
    This is version 128 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3