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Vacuolar protein sorting-associated protein 51 homolog (Another new gene 2 protein) (Protein fat-free homolog)

 VPS51_HUMAN             Reviewed;         782 AA.
Q9UID3; Q6PJV5; Q7L8A6; Q8WZ35; Q96DF4; Q96GR3;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 2.
25-OCT-2017, entry version 125.
RecName: Full=Vacuolar protein sorting-associated protein 51 homolog;
AltName: Full=Another new gene 2 protein;
AltName: Full=Protein fat-free homolog;
Name=VPS51; Synonyms=ANG2, C11orf2, C11orf3, FFR; ORFNames=PP5382;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9615229; DOI=10.1006/geno.1998.5296;
Lemmens I.H., Kas K., Merregaert J., Van de Ven W.J.M.;
"Identification and molecular characterization of TM7SF2 in the FAUNA
gene cluster on human chromosome 11q13.";
Genomics 49:437-442(1998).
[2]
SEQUENCE REVISION.
Lemmens I.H., Kas K., Merregaert J., Van de Ven W.J.M.;
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=15498874; DOI=10.1073/pnas.0404089101;
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., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
Gu J.;
"Large-scale cDNA transfection screening for genes related to cancer
development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
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., 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.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cervix, Eye, Lung, and Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 120-782 (ISOFORM 1).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
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.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH VPS52; VPS53;
VPS54 AND STX6.
PubMed=20685960; DOI=10.1091/mbc.E10-05-0392;
Perez-Victoria F.J., Schindler C., Magadan J.G., Mardones G.A.,
Delevoye C., Romao M., Raposo G., Bonifacino J.S.;
"Ang2/fat-free is a conserved subunit of the Golgi-associated
retrograde protein complex.";
Mol. Biol. Cell 21:3386-3395(2010).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
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.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-649, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE EARP
COMPLEX.
PubMed=25799061; DOI=10.1038/ncb3129;
Schindler C., Chen Y., Pu J., Guo X., Bonifacino J.S.;
"EARP is a multisubunit tethering complex involved in endocytic
recycling.";
Nat. Cell Biol. 17:639-650(2015).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Acts as component of the GARP complex that is involved
in retrograde transport from early and late endosomes to the
trans-Golgi network (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
(PubMed:20685960). Acts as component of the EARP complex that is
involved in endocytic recycling. The EARP complex associates with
Rab4-positive endosomes and promotes recycling of internalized
transferrin receptor (TFRC) to the plasma membrane
(PubMed:25799061). {ECO:0000269|PubMed:20685960,
ECO:0000269|PubMed:25799061}.
-!- SUBUNIT: Component of the Golgi-associated retrograde protein
(GARP) complex, also called VFT (VPS fifty-three) complex,
composed of VPS51, VPS52, VPS53 and VPS54 (PubMed:20685960).
Component of the endosome-associated retrograde protein (EARP)
complex, composed of VPS51, VPS52, VPS53 and VPS50/Syndetin
(PubMed:25799061). Interacts with STX6 (PubMed:20685960).
{ECO:0000269|PubMed:20685960, ECO:0000269|PubMed:25799061}.
-!- INTERACTION:
O60499-1:STX10; NbExp=5; IntAct=EBI-16067837, EBI-16067850;
O43752:STX6; NbExp=8; IntAct=EBI-16067837, EBI-2695795;
Q96JG6:VPS50; NbExp=6; IntAct=EBI-16067837, EBI-11044388;
Q8N1B4:VPS52; NbExp=4; IntAct=EBI-16067837, EBI-2799833;
-!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
{ECO:0000269|PubMed:20685960}. Recycling endosome
{ECO:0000269|PubMed:25799061}. Note=Localizes to the trans-Golgi
network as part of the GARP complex, while it localizes to
recycling endosomes as part of the EARP complex (PubMed:25799061).
{ECO:0000269|PubMed:25799061}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9UID3-1; Sequence=Displayed;
Name=2;
IsoId=Q9UID3-2; Sequence=VSP_014700;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the VPS51 family. {ECO:0000305}.
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EMBL; AF024631; AAF21627.2; -; mRNA.
EMBL; AF289557; AAL55741.1; -; mRNA.
EMBL; AL833818; CAD38681.2; -; mRNA.
EMBL; AP003068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC006555; AAH06555.2; -; mRNA.
EMBL; BC007198; AAH07198.1; -; mRNA.
EMBL; BC009285; AAH09285.2; -; mRNA.
EMBL; BC010540; AAH10540.1; -; mRNA.
EMBL; BC017438; AAH17438.1; -; mRNA.
CCDS; CCDS8093.1; -. [Q9UID3-1]
RefSeq; NP_037397.2; NM_013265.3. [Q9UID3-1]
UniGene; Hs.277517; -.
UniGene; Hs.732951; -.
PDB; 4J2C; X-ray; 1.80 A; B/D=33-49.
PDBsum; 4J2C; -.
ProteinModelPortal; Q9UID3; -.
SMR; Q9UID3; -.
BioGrid; 107197; 51.
CORUM; Q9UID3; -.
DIP; DIP-60562N; -.
IntAct; Q9UID3; 25.
MINT; MINT-3080728; -.
STRING; 9606.ENSP00000279281; -.
iPTMnet; Q9UID3; -.
PhosphoSitePlus; Q9UID3; -.
DMDM; 71153003; -.
EPD; Q9UID3; -.
PaxDb; Q9UID3; -.
PeptideAtlas; Q9UID3; -.
PRIDE; Q9UID3; -.
Ensembl; ENST00000279281; ENSP00000279281; ENSG00000149823. [Q9UID3-1]
GeneID; 738; -.
KEGG; hsa:738; -.
UCSC; uc001ocr.3; human. [Q9UID3-1]
CTD; 738; -.
DisGeNET; 738; -.
EuPathDB; HostDB:ENSG00000149823.7; -.
GeneCards; VPS51; -.
HGNC; HGNC:1172; VPS51.
HPA; HPA039650; -.
HPA; HPA061447; -.
MIM; 615738; gene.
neXtProt; NX_Q9UID3; -.
OpenTargets; ENSG00000149823; -.
PharmGKB; PA25485; -.
eggNOG; KOG2346; Eukaryota.
eggNOG; ENOG410XPIF; LUCA.
GeneTree; ENSGT00390000001738; -.
HOGENOM; HOG000046877; -.
HOVERGEN; HBG107916; -.
InParanoid; Q9UID3; -.
KO; K20296; -.
OMA; CEEFLAH; -.
OrthoDB; EOG091G0321; -.
PhylomeDB; Q9UID3; -.
TreeFam; TF314825; -.
Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
GenomeRNAi; 738; -.
PRO; PR:Q9UID3; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000149823; -.
CleanEx; HS_C11orf2; -.
ExpressionAtlas; Q9UID3; baseline and differential.
Genevisible; Q9UID3; HS.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:1990745; C:EARP complex; IDA:UniProtKB.
GO; GO:0000938; C:GARP complex; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
GO; GO:0006914; P:autophagy; IMP:UniProtKB.
GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
GO; GO:0048193; P:Golgi vesicle transport; IBA:GO_Central.
GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
GO; GO:0007041; P:lysosomal transport; IMP:MGI.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:UniProtKB.
Gene3D; 1.20.900.10; -; 1.
InterPro; IPR016159; Cullin_repeat-like_dom.
InterPro; IPR035899; DBL_dom_sf.
InterPro; IPR014812; Vps51.
PANTHER; PTHR15954; PTHR15954; 1.
SUPFAM; SSF74788; SSF74788; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Coiled coil;
Complete proteome; Endosome; Golgi apparatus; Lipid transport;
Phosphoprotein; Protein transport; Reference proteome; Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
CHAIN 2 782 Vacuolar protein sorting-associated
protein 51 homolog.
/FTId=PRO_0000089831.
COILED 116 147 {ECO:0000255}.
COILED 270 292 {ECO:0000255}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 18 18 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163}.
MOD_RES 44 44 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UVL4}.
MOD_RES 649 649 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 124 Missing (in isoform 2).
{ECO:0000303|PubMed:15498874}.
/FTId=VSP_014700.
HELIX 34 41 {ECO:0000244|PDB:4J2C}.
SEQUENCE 782 AA; 86042 MW; 0E858672E4C656DD CRC64;
MAAAAAAGPS PGSGPGDSPE GPEGEAPERR RKAHGMLKLY YGLSEGEAAG RPAGPDPLDP
TDLNGAHFDP EVYLDKLRRE CPLAQLMDSE TDMVRQIRAL DSDMQTLVYE NYNKFISATD
TIRKMKNDFR KMEDEMDRLA TNMAVITDFS ARISATLQDR HERITKLAGV HALLRKLQFL
FELPSRLTKC VELGAYGQAV RYQGRAQAVL QQYQHLPSFR AIQDDCQVIT ARLAQQLRQR
FREGGSGAPE QAECVELLLA LGEPAEELCE EFLAHARGRL EKELRNLEAE LGPSPPAPDV
LEFTDHGGSG FVGGLCQVAA AYQELFAAQG PAGAEKLAAF ARQLGSRYFA LVERRLAQEQ
GGGDNSLLVR ALDRFHRRLR APGALLAAAG LADAATEIVE RVARERLGHH LQGLRAAFLG
CLTDVRQALA APRVAGKEGP GLAELLANVA SSILSHIKAS LAAVHLFTAK EVSFSNKPYF
RGEFCSQGVR EGLIVGFVHS MCQTAQSFCD SPGEKGGATP PALLLLLSRL CLDYETATIS
YILTLTDEQF LVQDQFPVTP VSTLCAEARE TARRLLTHYV KVQGLVISQM LRKSVETRDW
LSTLEPRNVR AVMKRVVEDT TAIDVQVGLL YEEGVRKAQS SDSSKRTFSV YSSSRQQGRY
APSYTPSAPM DTNLLSNIQK LFSERIDVFS PVEFNKVSVL TGIIKISLKT LLECVRLRTF
GRFGLQQVQV DCHFLQLYLW RFVADEELVH LLLDEVVASA ALRCPDPVPM EPSVVEVICE
RG


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