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Q9UID3 (VPS51_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. 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:
Vacuolar protein sorting-associated protein 51 homolog
Alternative name(s):
Another new gene 2 protein
Protein fat-free homolog
Gene names
Name:VPS51
Synonyms:ANG2, C11orf2, C11orf3, FFR
ORF Names:PP5382
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length782 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi networkl (TGN). The GARP complex is required for the maintenance of protein retrieval from endosomes to the TGN, acid hydrolase sorting, lysosome function, endosomal cholesterol traffic and autophagy. VPS51 participates in retrograde transport of acid hydrolase receptors, likely by promoting tethering and SNARE-dependent fusion of endosome-derived carriers to the TGN. Ref.9

Subunit structure

Component of the Golgi-associated retrograde protein (GARP) complex, also called VFT (VPS fifty-three) complex, composed of VPS51, VPS52, VPS53 and VPS54. Interacts with STX6. Ref.9

Subcellular location

Golgi apparatustrans-Golgi network Ref.9.

Sequence similarities

Belongs to the VPS51 family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UID3-1)

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 2 (identifier: Q9UID3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-124: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 782781Vacuolar protein sorting-associated protein 51 homolog
PRO_0000089831

Regions

Coiled coil116 – 14732 Potential
Coiled coil270 – 29223 Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.11 Ref.12
Modified residue181Phosphoserine Ref.7

Natural variations

Alternative sequence1 – 124124Missing in isoform 2.
VSP_014700

Secondary structure

... 782
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 2.
Checksum: 0E858672E4C656DD

FASTA78286,042
        10         20         30         40         50         60 
MAAAAAAGPS PGSGPGDSPE GPEGEAPERR RKAHGMLKLY YGLSEGEAAG RPAGPDPLDP 

        70         80         90        100        110        120 
TDLNGAHFDP EVYLDKLRRE CPLAQLMDSE TDMVRQIRAL DSDMQTLVYE NYNKFISATD 

       130        140        150        160        170        180 
TIRKMKNDFR KMEDEMDRLA TNMAVITDFS ARISATLQDR HERITKLAGV HALLRKLQFL 

       190        200        210        220        230        240 
FELPSRLTKC VELGAYGQAV RYQGRAQAVL QQYQHLPSFR AIQDDCQVIT ARLAQQLRQR 

       250        260        270        280        290        300 
FREGGSGAPE QAECVELLLA LGEPAEELCE EFLAHARGRL EKELRNLEAE LGPSPPAPDV 

       310        320        330        340        350        360 
LEFTDHGGSG FVGGLCQVAA AYQELFAAQG PAGAEKLAAF ARQLGSRYFA LVERRLAQEQ 

       370        380        390        400        410        420 
GGGDNSLLVR ALDRFHRRLR APGALLAAAG LADAATEIVE RVARERLGHH LQGLRAAFLG 

       430        440        450        460        470        480 
CLTDVRQALA APRVAGKEGP GLAELLANVA SSILSHIKAS LAAVHLFTAK EVSFSNKPYF 

       490        500        510        520        530        540 
RGEFCSQGVR EGLIVGFVHS MCQTAQSFCD SPGEKGGATP PALLLLLSRL CLDYETATIS 

       550        560        570        580        590        600 
YILTLTDEQF LVQDQFPVTP VSTLCAEARE TARRLLTHYV KVQGLVISQM LRKSVETRDW 

       610        620        630        640        650        660 
LSTLEPRNVR AVMKRVVEDT TAIDVQVGLL YEEGVRKAQS SDSSKRTFSV YSSSRQQGRY 

       670        680        690        700        710        720 
APSYTPSAPM DTNLLSNIQK LFSERIDVFS PVEFNKVSVL TGIIKISLKT LLECVRLRTF 

       730        740        750        760        770        780 
GRFGLQQVQV DCHFLQLYLW RFVADEELVH LLLDEVVASA ALRCPDPVPM EPSVVEVICE 


RG 

« Hide

Isoform 2 [UniParc].

Checksum: A887B9E4D045BAE6
Show »

FASTA65872,655

References

« Hide 'large scale' references
[1]"Identification and molecular characterization of TM7SF2 in the FAUNA gene cluster on human chromosome 11q13."
Lemmens I.H., Kas K., Merregaert J., Van de Ven W.J.M.
Genomics 49:437-442(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]Lemmens I.H., Kas K., Merregaert J., Van de Ven W.J.M.
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Large-scale cDNA transfection screening for genes related to cancer development and progression."
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. expand/collapse author list , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[4]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Cervix, Eye, Lung and Muscle.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 120-782 (ISOFORM 1).
Tissue: Testis.
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, 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]"Ang2/fat-free is a conserved subunit of the Golgi-associated retrograde protein complex."
Perez-Victoria F.J., Schindler C., Magadan J.G., Mardones G.A., Delevoye C., Romao M., Raposo G., Bonifacino J.S.
Mol. Biol. Cell 21:3386-3395(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VPS52; VPS53; VPS54 AND STX6.
[10]"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].
[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].
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(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
AF024631 mRNA. Translation: AAF21627.2.
AF289557 mRNA. Translation: AAL55741.1.
AL833818 mRNA. Translation: CAD38681.2.
AP003068 Genomic DNA. No translation available.
BC006555 mRNA. Translation: AAH06555.2.
BC007198 mRNA. Translation: AAH07198.1.
BC009285 mRNA. Translation: AAH09285.2.
BC010540 mRNA. Translation: AAH10540.1.
BC017438 mRNA. Translation: AAH17438.1.
CCDSCCDS8093.1. [Q9UID3-1]
RefSeqNP_037397.2. NM_013265.3. [Q9UID3-1]
UniGeneHs.277517.
Hs.732951.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4J2CX-ray1.80B/D33-49[»]
ProteinModelPortalQ9UID3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107197. 11 interactions.
DIPDIP-60562N.
IntActQ9UID3. 7 interactions.
MINTMINT-3080728.
STRING9606.ENSP00000279281.

PTM databases

PhosphoSiteQ9UID3.

Polymorphism databases

DMDM71153003.

Proteomic databases

MaxQBQ9UID3.
PaxDbQ9UID3.
PRIDEQ9UID3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000279281; ENSP00000279281; ENSG00000149823. [Q9UID3-1]
GeneID738.
KEGGhsa:738.
UCSCuc001ocr.2. human. [Q9UID3-1]

Organism-specific databases

CTD738.
GeneCardsGC11P064864.
HGNCHGNC:1172. VPS51.
HPAHPA039650.
MIM615738. gene.
neXtProtNX_Q9UID3.
PharmGKBPA25485.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG127717.
HOGENOMHOG000046877.
HOVERGENHBG107916.
InParanoidQ9UID3.
OMAPYFRGEF.
OrthoDBEOG7D59MX.
PhylomeDBQ9UID3.
TreeFamTF314825.

Gene expression databases

ArrayExpressQ9UID3.
BgeeQ9UID3.
CleanExHS_C11orf2.
GenevestigatorQ9UID3.

Family and domain databases

InterProIPR016159. Cullin_repeat-like_dom.
[Graphical view]
SUPFAMSSF74788. SSF74788. 1 hit.
ProtoNetSearch...

Other

ChiTaRSC11orf2. human.
GenomeRNAi738.
NextBio2996.
PROQ9UID3.
SOURCESearch...

Entry information

Entry nameVPS51_HUMAN
AccessionPrimary (citable) accession number: Q9UID3
Secondary accession number(s): Q6PJV5 expand/collapse secondary AC list , Q7L8A6, Q8WZ35, Q96DF4, Q96GR3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 96 of the entry and version 2 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 11

Human chromosome 11: entries, gene names and cross-references to MIM