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Vacuolar protein sorting-associated protein 28 homolog (H-Vps28) (ESCRT-I complex subunit VPS28)

 VPS28_HUMAN             Reviewed;         221 AA.
Q9UK41; Q86VK0;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
23-MAY-2018, entry version 149.
RecName: Full=Vacuolar protein sorting-associated protein 28 homolog;
Short=H-Vps28;
AltName: Full=ESCRT-I complex subunit VPS28;
Name=VPS28;
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).
Hunt P.R., Pevsner J.;
"H-vps28, a human homolog of yeast class E protein Vps28p localizes to
an abnormal compartment in I-cell fibroblasts.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Lung;
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).
[4]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11916981; DOI=10.1083/jcb.200112080;
Bishop N., Horman A., Woodman P.;
"Mammalian class E vps proteins recognize ubiquitin and act in the
removal of endosomal protein-ubiquitin conjugates.";
J. Cell Biol. 157:91-101(2002).
[5]
INTERACTION WITH TSG101.
PubMed=14505570; DOI=10.1016/S0092-8674(03)00714-1;
von Schwedler U.K., Stuchell M., Mueller B., Ward D.M., Chung H.-Y.,
Morita E., Wang H.E., Davis T., He G.P., Cimbora D.M., Scott A.,
Kraeusslich H.-G., Kaplan J., Morham S.G., Sundquist W.I.;
"The protein network of HIV budding.";
Cell 114:701-713(2003).
[6]
INTERACTION WITH VPS37B.
PubMed=15218037; DOI=10.1074/jbc.M405226200;
Stuchell M.D., Garrus J.E., Mueller B., Stray K.M., Ghaffarian S.,
McKinnon R., Kraeusslich H.-G., Morham S.G., Sundquist W.I.;
"The human endosomal sorting complex required for transport (ESCRT-I)
and its role in HIV-1 budding.";
J. Biol. Chem. 279:36059-36071(2004).
[7]
INTERACTION WITH TSG101; VPS37B; VPS37C; MVB12A AND MVB12B, AND
RECONSTITUTION OF THE ESCRT-I COMPLEX.
PubMed=18005716; DOI=10.1016/j.chom.2007.06.003;
Morita E., Sandrin V., Alam S.L., Eckert D.M., Gygi S.P.,
Sundquist W.I.;
"Identification of human MVB12 proteins as ESCRT-I subunits that
function in HIV budding.";
Cell Host Microbe 2:41-53(2007).
[8]
INTERACTION WITH CEP55.
PubMed=17853893; DOI=10.1038/sj.emboj.7601850;
Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P.,
Rodesch C.K., Sundquist W.I.;
"Human ESCRT and ALIX proteins interact with proteins of the midbody
and function in cytokinesis.";
EMBO J. 26:4215-4227(2007).
[9]
INTERACTION WITH VPS36; SNF8 AND VPS25.
PubMed=18539118; DOI=10.1016/j.devcel.2008.04.004;
Im Y.J., Hurley J.H.;
"Integrated structural model and membrane targeting mechanism of the
human ESCRT-II complex.";
Dev. Cell 14:902-913(2008).
[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]
IDENTIFICATION IN AN ESCRT-I COMPLEX WITH UBAP1, AND SUBUNIT.
PubMed=21757351; DOI=10.1016/j.cub.2011.06.028;
Stefani F., Zhang L., Taylor S., Donovan J., Rollinson S., Doyotte A.,
Brownhill K., Bennion J., Pickering-Brown S., Woodman P.;
"UBAP1 is a component of an endosome-specific ESCRT-I complex that is
essential for MVB sorting.";
Curr. Biol. 21:1245-1250(2011).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND 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: Component of the ESCRT-I complex, a regulator of
vesicular trafficking process. {ECO:0000269|PubMed:11916981}.
-!- SUBUNIT: Component of the ESCRT-I complex (endosomal sorting
complex required for transport I) which consists of TSG101, VPS28,
a VPS37 protein (VPS37A to -D) and MVB12A or MVB12B in a 1:1:1:1
stoichiometry. Interacts with TSG101, VPS37B, VPS37C, MVB12A and
MVB12B. Component of an ESCRT-I complex (endosomal sorting complex
required for transport I) which consists of TSG101, VPS28, VPS37A
and UBAP1 in a 1:1:1:1 stoichiometry. Interacts WITH VPS36; the
interaction mediates the association with the ESCRT-II complex.
Interacts with SNF8 and VPS25. Interacts with CEP55.
{ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:15218037,
ECO:0000269|PubMed:17853893, ECO:0000269|PubMed:18005716,
ECO:0000269|PubMed:18539118, ECO:0000269|PubMed:21757351}.
-!- INTERACTION:
Q9H2G9:BLZF1; NbExp=3; IntAct=EBI-727424, EBI-2548012;
Q9H257-2:CARD9; NbExp=4; IntAct=EBI-727424, EBI-11530605;
Q9H257-3:CARD9; NbExp=3; IntAct=EBI-727424, EBI-16431743;
Q08379:GOLGA2; NbExp=6; IntAct=EBI-727424, EBI-618309;
Q9NS73-5:MBIP; NbExp=3; IntAct=EBI-727424, EBI-10182361;
Q8WWW0-2:RASSF5; NbExp=3; IntAct=EBI-727424, EBI-960502;
Q8IYX7:SAXO1; NbExp=3; IntAct=EBI-727424, EBI-3957636;
P12757:SKIL; NbExp=4; IntAct=EBI-727424, EBI-2902468;
Q16637:SMN2; NbExp=5; IntAct=EBI-727424, EBI-395421;
Q16637-3:SMN2; NbExp=3; IntAct=EBI-727424, EBI-395447;
Q99081-3:TCF12; NbExp=3; IntAct=EBI-727424, EBI-11952764;
P14373:TRIM27; NbExp=3; IntAct=EBI-727424, EBI-719493;
Q99816:TSG101; NbExp=9; IntAct=EBI-727424, EBI-346882;
Q8N6Y0:USHBP1; NbExp=6; IntAct=EBI-727424, EBI-739895;
Q9H9H4:VPS37B; NbExp=4; IntAct=EBI-727424, EBI-4400866;
Q8N1B4:VPS52; NbExp=4; IntAct=EBI-727424, EBI-2799833;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11916981}.
Late endosome membrane {ECO:0000269|PubMed:11916981}; Peripheral
membrane protein {ECO:0000269|PubMed:11916981}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9UK41-1; Sequence=Displayed;
Name=2;
IsoId=Q9UK41-2; Sequence=VSP_042028;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the VPS28 family. {ECO:0000255|PROSITE-
ProRule:PRU00642, ECO:0000255|PROSITE-ProRule:PRU00645}.
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EMBL; AF182844; AAF00499.1; -; mRNA.
EMBL; AF205589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC006485; AAH06485.1; -; mRNA.
EMBL; BC019321; AAH19321.1; -; mRNA.
EMBL; BC050713; AAH50713.1; -; mRNA.
CCDS; CCDS34967.1; -. [Q9UK41-2]
CCDS; CCDS6425.1; -. [Q9UK41-1]
RefSeq; NP_057292.1; NM_016208.3. [Q9UK41-1]
RefSeq; NP_898880.1; NM_183057.2. [Q9UK41-2]
UniGene; Hs.418175; -.
UniGene; Hs.650693; -.
ProteinModelPortal; Q9UK41; -.
SMR; Q9UK41; -.
BioGrid; 119341; 63.
CORUM; Q9UK41; -.
IntAct; Q9UK41; 29.
MINT; Q9UK41; -.
STRING; 9606.ENSP00000366565; -.
iPTMnet; Q9UK41; -.
PhosphoSitePlus; Q9UK41; -.
DMDM; 13124619; -.
EPD; Q9UK41; -.
PaxDb; Q9UK41; -.
PeptideAtlas; Q9UK41; -.
PRIDE; Q9UK41; -.
TopDownProteomics; Q9UK41-1; -. [Q9UK41-1]
DNASU; 51160; -.
Ensembl; ENST00000292510; ENSP00000292510; ENSG00000160948. [Q9UK41-1]
Ensembl; ENST00000377348; ENSP00000366565; ENSG00000160948. [Q9UK41-2]
Ensembl; ENST00000526054; ENSP00000434064; ENSG00000160948. [Q9UK41-1]
Ensembl; ENST00000529182; ENSP00000434556; ENSG00000160948. [Q9UK41-2]
GeneID; 51160; -.
KEGG; hsa:51160; -.
UCSC; uc003zcs.2; human. [Q9UK41-1]
CTD; 51160; -.
EuPathDB; HostDB:ENSG00000160948.13; -.
GeneCards; VPS28; -.
HGNC; HGNC:18178; VPS28.
HPA; HPA024688; -.
HPA; HPA024745; -.
MIM; 611952; gene.
neXtProt; NX_Q9UK41; -.
OpenTargets; ENSG00000160948; -.
PharmGKB; PA38512; -.
eggNOG; KOG3284; Eukaryota.
eggNOG; ENOG4111IQ4; LUCA.
GeneTree; ENSGT00390000007486; -.
HOGENOM; HOG000203818; -.
HOVERGEN; HBG054248; -.
InParanoid; Q9UK41; -.
KO; K12184; -.
OMA; KYRLDCP; -.
OrthoDB; EOG091G0LT0; -.
PhylomeDB; Q9UK41; -.
TreeFam; TF313364; -.
Reactome; R-HSA-162588; Budding and maturation of HIV virion.
Reactome; R-HSA-174490; Membrane binding and targetting of GAG proteins.
Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
ChiTaRS; VPS28; human.
GeneWiki; VPS28; -.
GenomeRNAi; 51160; -.
PRO; PR:Q9UK41; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000160948; -.
CleanEx; HS_VPS28; -.
ExpressionAtlas; Q9UK41; baseline and differential.
Genevisible; Q9UK41; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
GO; GO:0000813; C:ESCRT I complex; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
GO; GO:0016197; P:endosomal transport; TAS:Reactome.
GO; GO:0016236; P:macroautophagy; TAS:ParkinsonsUK-UCL.
GO; GO:0036258; P:multivesicular body assembly; TAS:ParkinsonsUK-UCL.
GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:UniProtKB.
GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:UniProtKB.
GO; GO:2000397; P:positive regulation of ubiquitin-dependent endocytosis; IMP:UniProtKB.
GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central.
GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:UniProtKB.
GO; GO:0039702; P:viral budding via host ESCRT complex; TAS:ParkinsonsUK-UCL.
GO; GO:0019058; P:viral life cycle; TAS:Reactome.
Gene3D; 1.20.120.1130; -; 1.
Gene3D; 1.20.1440.200; -; 1.
InterPro; IPR037202; ESCRT_assembly_dom.
InterPro; IPR007143; Vps28.
InterPro; IPR017899; VPS28_C.
InterPro; IPR037206; VPS28_C_sf.
InterPro; IPR017898; VPS28_N.
InterPro; IPR038358; VPS28_N_sf.
PANTHER; PTHR12937; PTHR12937; 1.
Pfam; PF03997; VPS28; 1.
PIRSF; PIRSF017535; VPS28; 1.
SUPFAM; SSF140111; SSF140111; 1.
SUPFAM; SSF140427; SSF140427; 1.
PROSITE; PS51310; VPS28_C; 1.
PROSITE; PS51313; VPS28_N; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell membrane; Complete proteome;
Endosome; Membrane; Protein transport; Reference proteome; Transport.
CHAIN 1 221 Vacuolar protein sorting-associated
protein 28 homolog.
/FTId=PRO_0000120951.
DOMAIN 13 120 VPS28 N-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00645}.
DOMAIN 124 220 VPS28 C-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00642}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:25944712}.
VAR_SEQ 184 221 LQTLSGMSASDELDDSQVRQMLFDLESAYNAFNRFLHA ->
WVSLPARQSPAVPETLPARRSPAVPLRPSAPTCPVLHSQAA
DPERHVGVR (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_042028.
SEQUENCE 221 AA; 25425 MW; B2E1697B82D02AB8 CRC64;
MFHGIPATPG IGAPGNKPEL YEEVKLYKNA REREKYDNMA ELFAVVKTMQ ALEKAYIKDC
VSPSEYTAAC SRLLVQYKAA FRQVQGSEIS SIDEFCRKFR LDCPLAMERI KEDRPITIKD
DKGNLNRCIA DVVSLFITVM DKLRLEIRAM DEIQPDLREL METMHRMSHL PPDFEGRQTV
SQWLQTLSGM SASDELDDSQ VRQMLFDLES AYNAFNRFLH A


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