Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9NP79

- VTA1_HUMAN

UniProt

Q9NP79 - VTA1_HUMAN

Protein

Vacuolar protein sorting-associated protein VTA1 homolog

Gene

VTA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Involved in the endosomal multivesicular bodies (MVB) pathway. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. Thought to be a cofactor of VPS4A/B, which catalyzes disassembles membrane-associated ESCRT-III assemblies. Involved in the sorting and down-regulation of EGFR By similarity. Involved in HIV-1 budding.By similarity1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. endosomal transport Source: Reactome
    2. membrane organization Source: Reactome
    3. protein transport Source: UniProtKB-KW
    4. viral life cycle Source: Reactome
    5. viral process Source: Reactome

    Keywords - Biological processi

    Protein transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_27258. Endosomal Sorting Complex Required For Transport (ESCRT).
    REACT_6359. Budding and maturation of HIV virion.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Vacuolar protein sorting-associated protein VTA1 homolog
    Alternative name(s):
    Dopamine-responsive gene 1 protein
    Short name:
    DRG-1
    LYST-interacting protein 5
    Short name:
    LIP5
    SKD1-binding protein 1
    Short name:
    SBP1
    Gene namesi
    Name:VTA1
    Synonyms:C6orf55
    ORF Names:HSPC228, My012
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:20954. VTA1.

    Subcellular locationi

    Cytoplasm 1 Publication. Endosome membrane 1 Publication; Peripheral membrane protein 1 Publication

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. endosome membrane Source: UniProtKB-SubCell
    3. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm, Endosome, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162408932.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 307306Vacuolar protein sorting-associated protein VTA1 homologPRO_0000089509Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9NP79.
    PaxDbiQ9NP79.
    PRIDEiQ9NP79.

    PTM databases

    PhosphoSiteiQ9NP79.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9NP79.
    BgeeiQ9NP79.
    CleanExiHS_VTA1.
    GenevestigatoriQ9NP79.

    Organism-specific databases

    HPAiHPA030968.

    Interactioni

    Subunit structurei

    Interacts with VPS4B. Interacts with CHMP1B. Interacts with CHMP2A; the interaction probably involves the open conformation of (polymerized) CHMP2A. Interacts with CHMP3. Interacts with CHMP5; the interaction involves soluble CHMP5. Interacts with IST1.6 Publications

    Protein-protein interaction databases

    BioGridi119595. 30 interactions.
    IntActiQ9NP79. 17 interactions.
    MINTiMINT-1438279.
    STRINGi9606.ENSP00000356602.

    Structurei

    Secondary structure

    1
    307
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi12 – 143
    Beta strandi15 – 173
    Helixi18 – 3013
    Helixi32 – 4918
    Helixi56 – 7419
    Helixi78 – 814
    Helixi83 – 10624
    Helixi112 – 12918
    Helixi136 – 15722

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LXLNMR-A1-183[»]
    2LXMNMR-A1-168[»]
    ProteinModelPortaliQ9NP79.
    SMRiQ9NP79. Positions 13-163.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 186185Interaction with IST1Add
    BLAST
    Regioni2 – 7574Interaction with CHMP5Add
    BLAST
    Regioni198 – 307110Interaction with VPS4BBy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the VTA1 family.Curated

    Phylogenomic databases

    eggNOGiNOG127441.
    HOGENOMiHOG000265547.
    HOVERGENiHBG050907.
    InParanoidiQ9NP79.
    KOiK12199.
    OMAiTPQPGPI.
    OrthoDBiEOG7JHM66.
    PhylomeDBiQ9NP79.
    TreeFamiTF105917.

    Family and domain databases

    Gene3Di1.25.40.270. 1 hit.
    InterProiIPR023175. VPS_Vta1/CALS_N-dom.
    [Graphical view]

    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 1 (identifier: Q9NP79-1) [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

    MAALAPLPPL PAQFKSIQHH LRTAQEHDKR DPVVAYYCRL YAMQTGMKID    50
    SKTPECRKFL SKLMDQLEAL KKQLGDNEAI TQEIVGCAHL ENYALKMFLY 100
    ADNEDRAGRF HKNMIKSFYT ASLLIDVITV FGELTDENVK HRKYARWKAT 150
    YIHNCLKNGE TPQAGPVGIE EDNDIEENED AGAASLPTQP TQPSSSSTYD 200
    PSNMPSGNYT GIQIPPGAHA PANTPAEVPH STGVASNTIQ PTPQTIPAID 250
    PALFNTISQG DVRLTPEDFA RAQKYCKYAG SALQYEDVST AVQNLQKALK 300
    LLTTGRE 307
    Length:307
    Mass (Da):33,879
    Last modified:October 1, 2000 - v1
    Checksum:iC7DE611E50B58BF9
    GO
    Isoform 2 (identifier: Q9NP79-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-69: MAALAPLPPL...LSKLMDQLEA → MTSETLWWLIT
         234-260: Missing.

    Show »
    Length:222
    Mass (Da):24,553
    Checksum:iCEF86AF60A37B628
    GO

    Sequence cautioni

    The sequence AAF36148.1 differs from that shown. Reason: Frameshift at positions 131 and 140.
    The sequence AAG43125.1 differs from that shown. Reason: Frameshift at position 269.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 141F → L in CAB66619. (PubMed:11230166)Curated
    Sequence conflicti155 – 1562CL → V in AAF36148. (PubMed:11042152)Curated
    Sequence conflicti282 – 2821A → V in BAG62917. (PubMed:14702039)Curated
    Sequence conflicti307 – 3071E → D in CAG33488. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti239 – 2391I → M.
    Corresponds to variant rs2232307 [ dbSNP | Ensembl ].
    VAR_053917

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6969MAALA…DQLEA → MTSETLWWLIT in isoform 2. 1 PublicationVSP_056727Add
    BLAST
    Alternative sequencei234 – 26027Missing in isoform 2. 1 PublicationVSP_056728Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF271994 mRNA. Translation: AAF76210.1.
    AF060225 mRNA. Translation: AAG43125.1. Frameshift.
    AF151062 mRNA. Translation: AAF36148.1. Frameshift.
    AL136684 mRNA. Translation: CAB66619.1.
    AK000051 mRNA. Translation: BAA90909.1.
    AK301376 mRNA. Translation: BAG62917.1.
    CR457207 mRNA. Translation: CAG33488.1.
    AL033522 Genomic DNA. Translation: CAI21072.1.
    CH471051 Genomic DNA. Translation: EAW47883.1.
    CH471051 Genomic DNA. Translation: EAW47885.1.
    BC005937 mRNA. Translation: AAH05937.1.
    BC006989 mRNA. Translation: AAH06989.1.
    BC022536 mRNA. Translation: AAH22536.1.
    CCDSiCCDS5197.1.
    RefSeqiNP_001273300.1. NM_001286371.1.
    NP_001273301.1. NM_001286372.1.
    NP_057569.2. NM_016485.4.
    UniGeneiHs.431367.

    Genome annotation databases

    EnsembliENST00000367630; ENSP00000356602; ENSG00000009844.
    ENST00000452973; ENSP00000395767; ENSG00000009844.
    GeneIDi51534.
    KEGGihsa:51534.
    UCSCiuc003qiw.3. human.
    uc011edu.2. human.

    Polymorphism databases

    DMDMi30580379.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF271994 mRNA. Translation: AAF76210.1 .
    AF060225 mRNA. Translation: AAG43125.1 . Frameshift.
    AF151062 mRNA. Translation: AAF36148.1 . Frameshift.
    AL136684 mRNA. Translation: CAB66619.1 .
    AK000051 mRNA. Translation: BAA90909.1 .
    AK301376 mRNA. Translation: BAG62917.1 .
    CR457207 mRNA. Translation: CAG33488.1 .
    AL033522 Genomic DNA. Translation: CAI21072.1 .
    CH471051 Genomic DNA. Translation: EAW47883.1 .
    CH471051 Genomic DNA. Translation: EAW47885.1 .
    BC005937 mRNA. Translation: AAH05937.1 .
    BC006989 mRNA. Translation: AAH06989.1 .
    BC022536 mRNA. Translation: AAH22536.1 .
    CCDSi CCDS5197.1.
    RefSeqi NP_001273300.1. NM_001286371.1.
    NP_001273301.1. NM_001286372.1.
    NP_057569.2. NM_016485.4.
    UniGenei Hs.431367.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LXL NMR - A 1-183 [» ]
    2LXM NMR - A 1-168 [» ]
    ProteinModelPortali Q9NP79.
    SMRi Q9NP79. Positions 13-163.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119595. 30 interactions.
    IntActi Q9NP79. 17 interactions.
    MINTi MINT-1438279.
    STRINGi 9606.ENSP00000356602.

    PTM databases

    PhosphoSitei Q9NP79.

    Polymorphism databases

    DMDMi 30580379.

    Proteomic databases

    MaxQBi Q9NP79.
    PaxDbi Q9NP79.
    PRIDEi Q9NP79.

    Protocols and materials databases

    DNASUi 51534.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367630 ; ENSP00000356602 ; ENSG00000009844 .
    ENST00000452973 ; ENSP00000395767 ; ENSG00000009844 .
    GeneIDi 51534.
    KEGGi hsa:51534.
    UCSCi uc003qiw.3. human.
    uc011edu.2. human.

    Organism-specific databases

    CTDi 51534.
    GeneCardsi GC06P142468.
    H-InvDB HIX0006262.
    HGNCi HGNC:20954. VTA1.
    HPAi HPA030968.
    MIMi 610902. gene.
    neXtProti NX_Q9NP79.
    PharmGKBi PA162408932.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG127441.
    HOGENOMi HOG000265547.
    HOVERGENi HBG050907.
    InParanoidi Q9NP79.
    KOi K12199.
    OMAi TPQPGPI.
    OrthoDBi EOG7JHM66.
    PhylomeDBi Q9NP79.
    TreeFami TF105917.

    Enzyme and pathway databases

    Reactomei REACT_27258. Endosomal Sorting Complex Required For Transport (ESCRT).
    REACT_6359. Budding and maturation of HIV virion.

    Miscellaneous databases

    GeneWikii VTA1.
    GenomeRNAii 51534.
    NextBioi 55284.
    PROi Q9NP79.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NP79.
    Bgeei Q9NP79.
    CleanExi HS_VTA1.
    Genevestigatori Q9NP79.

    Family and domain databases

    Gene3Di 1.25.40.270. 1 hit.
    InterProi IPR023175. VPS_Vta1/CALS_N-dom.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of dopamine responsive genes in glial cells by subtractive hybridization."
      Shi J., Cai W., Xie Y.
      Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Mao Y.M., Xie Y., Zheng Z.H., Gu S.H., Ying K., Lin Q., Dai J.L., Tang R., Dong H., Wu X.Z.
      Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Fetal brain.
    3. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Umbilical cord blood.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Colon and Synovial cell.
    6. "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 1).
    7. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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 1).
      Tissue: Brain and Urinary bladder.
    10. Bienvenut W.V., Zebisch A., Kolch W.
      Submitted (OCT-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-15 AND 30-39, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma.
    11. "The role of LIP5 and CHMP5 in multivesicular body formation and HIV-1 budding in mammalian cells."
      Ward D.M., Vaughn M.B., Shiflett S.L., White P.L., Pollock A.L., Hill J., Schnegelberger R., Sundquist W.I., Kaplan J.
      J. Biol. Chem. 280:10548-10555(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CHMP5.
    12. "Targeting of AMSH to endosomes is required for epidermal growth factor receptor degradation."
      Ma Y.M., Boucrot E., Villen J., Affar el B., Gygi S.P., Goettlinger H.G., Kirchhausen T.
      J. Biol. Chem. 282:9805-9812(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CHMP5.
    13. "Novel interactions of ESCRT-III with LIP5 and VPS4 and their implications for ESCRT-III disassembly."
      Shim S., Merrill S.A., Hanson P.I.
      Mol. Biol. Cell 19:2661-2672(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CHMP1B; CHMP2A; CHMP3; CHMP5 AND VPS4B.
    14. "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].
    15. Cited for: INTERACTION WITH IST1.
    16. "Biochemical analyses of human IST1 and its function in cytokinesis."
      Bajorek M., Morita E., Skalicky J.J., Morham S.G., Babst M., Sundquist W.I.
      Mol. Biol. Cell 20:1360-1373(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IST1.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Mechanism of inhibition of retrovirus release from cells by interferon-induced gene ISG15."
      Kuang Z., Seo E.J., Leis J.
      J. Virol. 85:7153-7161(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CHMP2A; CHMP3 AND CHMP5.
    19. "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 nameiVTA1_HUMAN
    AccessioniPrimary (citable) accession number: Q9NP79
    Secondary accession number(s): B4DW55
    , E1P594, E7ETQ7, Q5TGM1, Q6IAE8, Q9H0R2, Q9H3K9, Q9P0Q0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 9, 2003
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 115 of the entry and version 1 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3