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Q9NP79

- VTA1_HUMAN

UniProt

Q9NP79 - VTA1_HUMAN

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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

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 - 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
Complete GO annotation...

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 Source: UniProtKB-KW
  3. extracellular vesicular exosome Source: UniProtKB
  4. membrane Source: UniProtKB-KW
Complete GO annotation...

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

BgeeiQ9NP79.
CleanExiHS_VTA1.
ExpressionAtlasiQ9NP79. baseline and differential.
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. 33 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 – 143Combined sources
Beta strandi15 – 173Combined sources
Helixi18 – 3013Combined sources
Helixi32 – 4918Combined sources
Helixi56 – 7419Combined sources
Helixi78 – 814Combined sources
Helixi83 – 10624Combined sources
Helixi112 – 12918Combined sources
Helixi136 – 15722Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000011342.
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

        10         20         30         40         50
MAALAPLPPL PAQFKSIQHH LRTAQEHDKR DPVVAYYCRL YAMQTGMKID
60 70 80 90 100
SKTPECRKFL SKLMDQLEAL KKQLGDNEAI TQEIVGCAHL ENYALKMFLY
110 120 130 140 150
ADNEDRAGRF HKNMIKSFYT ASLLIDVITV FGELTDENVK HRKYARWKAT
160 170 180 190 200
YIHNCLKNGE TPQAGPVGIE EDNDIEENED AGAASLPTQP TQPSSSSTYD
210 220 230 240 250
PSNMPSGNYT GIQIPPGAHA PANTPAEVPH STGVASNTIQ PTPQTIPAID
260 270 280 290 300
PALFNTISQG DVRLTPEDFA RAQKYCKYAG SALQYEDVST AVQNLQKALK

LLTTGRE
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. Curated
The sequence AAG43125.1 differs from that shown. Reason: Frameshift at position 269. Curated

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:
EMBLi
GenBanki
DDBJi
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. [Q9NP79-1]
RefSeqiNP_001273300.1. NM_001286371.1.
NP_001273301.1. NM_001286372.1. [Q9NP79-2]
NP_057569.2. NM_016485.4. [Q9NP79-1]
UniGeneiHs.431367.

Genome annotation databases

EnsembliENST00000367630; ENSP00000356602; ENSG00000009844. [Q9NP79-1]
ENST00000452973; ENSP00000395767; ENSG00000009844. [Q9NP79-2]
GeneIDi51534.
KEGGihsa:51534.
UCSCiuc003qiw.3. human. [Q9NP79-1]

Polymorphism databases

DMDMi30580379.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [Q9NP79-1 ]
RefSeqi NP_001273300.1. NM_001286371.1.
NP_001273301.1. NM_001286372.1. [Q9NP79-2 ]
NP_057569.2. NM_016485.4. [Q9NP79-1 ]
UniGenei Hs.431367.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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. 33 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 . [Q9NP79-1 ]
ENST00000452973 ; ENSP00000395767 ; ENSG00000009844 . [Q9NP79-2 ]
GeneIDi 51534.
KEGGi hsa:51534.
UCSCi uc003qiw.3. human. [Q9NP79-1 ]

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.
GeneTreei ENSGT00390000011342.
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 35475634.
PROi Q9NP79.
SOURCEi Search...

Gene expression databases

Bgeei Q9NP79.
CleanExi HS_VTA1.
ExpressionAtlasi Q9NP79. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 117 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

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    Human chromosome 6: entries, gene names and cross-references to MIM
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    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

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