Full text data of VPS28
VPS28
[Confidence: low (only semi-automatic identification from reviews)]
Vacuolar protein sorting-associated protein 28 homolog; H-Vps28 (ESCRT-I complex subunit VPS28)
Vacuolar protein sorting-associated protein 28 homolog; H-Vps28 (ESCRT-I complex subunit VPS28)
UniProt
Q9UK41
ID VPS28_HUMAN Reviewed; 221 AA.
AC Q9UK41; Q86VK0;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 110.
DE RecName: Full=Vacuolar protein sorting-associated protein 28 homolog;
DE Short=H-Vps28;
DE AltName: Full=ESCRT-I complex subunit VPS28;
GN Name=VPS28;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Hunt P.R., Pevsner J.;
RT "H-vps28, a human homolog of yeast class E protein Vps28p localizes to
RT an abnormal compartment in I-cell fibroblasts.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
RA Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
RA Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11916981; DOI=10.1083/jcb.200112080;
RA Bishop N., Horman A., Woodman P.;
RT "Mammalian class E vps proteins recognize ubiquitin and act in the
RT removal of endosomal protein-ubiquitin conjugates.";
RL J. Cell Biol. 157:91-101(2002).
RN [5]
RP INTERACTION WITH TSG101.
RX PubMed=14505570; DOI=10.1016/S0092-8674(03)00714-1;
RA von Schwedler U.K., Stuchell M., Mueller B., Ward D.M., Chung H.-Y.,
RA Morita E., Wang H.E., Davis T., He G.P., Cimbora D.M., Scott A.,
RA Kraeusslich H.-G., Kaplan J., Morham S.G., Sundquist W.I.;
RT "The protein network of HIV budding.";
RL Cell 114:701-713(2003).
RN [6]
RP INTERACTION WITH VPS37B.
RX PubMed=15218037; DOI=10.1074/jbc.M405226200;
RA Stuchell M.D., Garrus J.E., Mueller B., Stray K.M., Ghaffarian S.,
RA McKinnon R., Kraeusslich H.-G., Morham S.G., Sundquist W.I.;
RT "The human endosomal sorting complex required for transport (ESCRT-I)
RT and its role in HIV-1 budding.";
RL J. Biol. Chem. 279:36059-36071(2004).
RN [7]
RP INTERACTION WITH TSG101; VPS37B; VPS37C; MVB12A AND MVB12B, AND
RP RECONSTITUTION OF THE ESCRT-I COMPLEX.
RX PubMed=18005716; DOI=10.1016/j.chom.2007.06.003;
RA Morita E., Sandrin V., Alam S.L., Eckert D.M., Gygi S.P.,
RA Sundquist W.I.;
RT "Identification of human MVB12 proteins as ESCRT-I subunits that
RT function in HIV budding.";
RL Cell Host Microbe 2:41-53(2007).
RN [8]
RP INTERACTION WITH CEP55.
RX PubMed=17853893; DOI=10.1038/sj.emboj.7601850;
RA Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P.,
RA Rodesch C.K., Sundquist W.I.;
RT "Human ESCRT and ALIX proteins interact with proteins of the midbody
RT and function in cytokinesis.";
RL EMBO J. 26:4215-4227(2007).
RN [9]
RP INTERACTION WITH VPS36; SNF8 AND VPS25.
RX PubMed=18539118; DOI=10.1016/j.devcel.2008.04.004;
RA Im Y.J., Hurley J.H.;
RT "Integrated structural model and membrane targeting mechanism of the
RT human ESCRT-II complex.";
RL Dev. Cell 14:902-913(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP IDENTIFICATION IN AN ESCRT-I COMPLEX WITH UBAP1, AND SUBUNIT.
RX PubMed=21757351; DOI=10.1016/j.cub.2011.06.028;
RA Stefani F., Zhang L., Taylor S., Donovan J., Rollinson S., Doyotte A.,
RA Brownhill K., Bennion J., Pickering-Brown S., Woodman P.;
RT "UBAP1 is a component of an endosome-specific ESCRT-I complex that is
RT essential for MVB sorting.";
RL Curr. Biol. 21:1245-1250(2011).
CC -!- FUNCTION: Component of the ESCRT-I complex, a regulator of
CC vesicular trafficking process.
CC -!- SUBUNIT: Component of the ESCRT-I complex (endosomal sorting
CC complex required for transport I) which consists of TSG101, VPS28,
CC a VPS37 protein (VPS37A to -D) and MVB12A or MVB12B in a 1:1:1:1
CC stoechiometry. Interacts with TSG101, VPS37B, VPS37C, MVB12A and
CC MVB12B. Component of an ESCRT-I complex (endosomal sorting complex
CC required for transport I) which consists of TSG101, VPS28, VPS37A
CC and UBAP1 in a 1:1:1:1 stoechiometry. Interacts WITH VPS36; the
CC interaction mediates the association with the ESCRT-II complex.
CC Interacts with SNF8 and VPS25. Interacts with CEP55.
CC -!- INTERACTION:
CC Q99816:TSG101; NbExp=3; IntAct=EBI-727424, EBI-346882;
CC -!- SUBCELLULAR LOCATION: Cell membrane. Late endosome membrane;
CC Peripheral membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UK41-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UK41-2; Sequence=VSP_042028;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the VPS28 family.
CC -!- SIMILARITY: Contains 1 VPS28 C-terminal domain.
CC -!- SIMILARITY: Contains 1 VPS28 N-terminal domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF182844; AAF00499.1; -; mRNA.
DR EMBL; AF205589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006485; AAH06485.1; -; mRNA.
DR EMBL; BC019321; AAH19321.1; -; mRNA.
DR EMBL; BC050713; AAH50713.1; -; mRNA.
DR RefSeq; NP_057292.1; NM_016208.3.
DR RefSeq; NP_898880.1; NM_183057.2.
DR RefSeq; XP_005272379.1; XM_005272322.1.
DR UniGene; Hs.418175; -.
DR ProteinModelPortal; Q9UK41; -.
DR SMR; Q9UK41; 24-117, 123-220.
DR IntAct; Q9UK41; 14.
DR MINT; MINT-234404; -.
DR STRING; 9606.ENSP00000366565; -.
DR PhosphoSite; Q9UK41; -.
DR DMDM; 13124619; -.
DR PaxDb; Q9UK41; -.
DR PRIDE; Q9UK41; -.
DR DNASU; 51160; -.
DR Ensembl; ENST00000292510; ENSP00000292510; ENSG00000160948.
DR Ensembl; ENST00000377348; ENSP00000366565; ENSG00000160948.
DR Ensembl; ENST00000526054; ENSP00000434064; ENSG00000160948.
DR Ensembl; ENST00000529182; ENSP00000434556; ENSG00000160948.
DR Ensembl; ENST00000562786; ENSP00000457919; ENSG00000260313.
DR Ensembl; ENST00000565984; ENSP00000456843; ENSG00000260313.
DR GeneID; 51160; -.
DR KEGG; hsa:51160; -.
DR UCSC; uc003zcs.1; human.
DR CTD; 51160; -.
DR GeneCards; GC08M145649; -.
DR HGNC; HGNC:18178; VPS28.
DR HPA; HPA024688; -.
DR HPA; HPA024745; -.
DR MIM; 611952; gene.
DR neXtProt; NX_Q9UK41; -.
DR PharmGKB; PA38512; -.
DR eggNOG; NOG276841; -.
DR HOGENOM; HOG000203818; -.
DR HOVERGEN; HBG054248; -.
DR KO; K12184; -.
DR OMA; YDNMADL; -.
DR PhylomeDB; Q9UK41; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR ChiTaRS; VPS28; human.
DR GeneWiki; VPS28; -.
DR GenomeRNAi; 51160; -.
DR NextBio; 54073; -.
DR PRO; PR:Q9UK41; -.
DR ArrayExpress; Q9UK41; -.
DR Bgee; Q9UK41; -.
DR CleanEx; HS_VPS28; -.
DR Genevestigator; Q9UK41; -.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0000813; C:ESCRT I complex; IDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016197; P:endosomal transport; TAS:Reactome.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:UniProtKB.
DR GO; GO:0019082; P:viral protein processing; TAS:Reactome.
DR GO; GO:0019068; P:virion assembly; TAS:Reactome.
DR InterPro; IPR007143; VPS28.
DR InterPro; IPR017899; VPS28_C.
DR InterPro; IPR017898; VPS28_N.
DR PANTHER; PTHR12937; PTHR12937; 1.
DR Pfam; PF03997; VPS28; 1.
DR PIRSF; PIRSF017535; VPS28; 1.
DR PROSITE; PS51310; VPS28_C; 1.
DR PROSITE; PS51313; VPS28_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Complete proteome; Endosome;
KW Membrane; Protein transport; Reference proteome; Transport.
FT CHAIN 1 221 Vacuolar protein sorting-associated
FT protein 28 homolog.
FT /FTId=PRO_0000120951.
FT DOMAIN 13 120 VPS28 N-terminal.
FT DOMAIN 124 220 VPS28 C-terminal.
FT VAR_SEQ 184 221 LQTLSGMSASDELDDSQVRQMLFDLESAYNAFNRFLHA ->
FT WVSLPARQSPAVPETLPARRSPAVPLRPSAPTCPVLHSQAA
FT DPERHVGVR (in isoform 2).
FT /FTId=VSP_042028.
SQ 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
//
ID VPS28_HUMAN Reviewed; 221 AA.
AC Q9UK41; Q86VK0;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 110.
DE RecName: Full=Vacuolar protein sorting-associated protein 28 homolog;
DE Short=H-Vps28;
DE AltName: Full=ESCRT-I complex subunit VPS28;
GN Name=VPS28;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Hunt P.R., Pevsner J.;
RT "H-vps28, a human homolog of yeast class E protein Vps28p localizes to
RT an abnormal compartment in I-cell fibroblasts.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
RA Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
RA Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11916981; DOI=10.1083/jcb.200112080;
RA Bishop N., Horman A., Woodman P.;
RT "Mammalian class E vps proteins recognize ubiquitin and act in the
RT removal of endosomal protein-ubiquitin conjugates.";
RL J. Cell Biol. 157:91-101(2002).
RN [5]
RP INTERACTION WITH TSG101.
RX PubMed=14505570; DOI=10.1016/S0092-8674(03)00714-1;
RA von Schwedler U.K., Stuchell M., Mueller B., Ward D.M., Chung H.-Y.,
RA Morita E., Wang H.E., Davis T., He G.P., Cimbora D.M., Scott A.,
RA Kraeusslich H.-G., Kaplan J., Morham S.G., Sundquist W.I.;
RT "The protein network of HIV budding.";
RL Cell 114:701-713(2003).
RN [6]
RP INTERACTION WITH VPS37B.
RX PubMed=15218037; DOI=10.1074/jbc.M405226200;
RA Stuchell M.D., Garrus J.E., Mueller B., Stray K.M., Ghaffarian S.,
RA McKinnon R., Kraeusslich H.-G., Morham S.G., Sundquist W.I.;
RT "The human endosomal sorting complex required for transport (ESCRT-I)
RT and its role in HIV-1 budding.";
RL J. Biol. Chem. 279:36059-36071(2004).
RN [7]
RP INTERACTION WITH TSG101; VPS37B; VPS37C; MVB12A AND MVB12B, AND
RP RECONSTITUTION OF THE ESCRT-I COMPLEX.
RX PubMed=18005716; DOI=10.1016/j.chom.2007.06.003;
RA Morita E., Sandrin V., Alam S.L., Eckert D.M., Gygi S.P.,
RA Sundquist W.I.;
RT "Identification of human MVB12 proteins as ESCRT-I subunits that
RT function in HIV budding.";
RL Cell Host Microbe 2:41-53(2007).
RN [8]
RP INTERACTION WITH CEP55.
RX PubMed=17853893; DOI=10.1038/sj.emboj.7601850;
RA Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P.,
RA Rodesch C.K., Sundquist W.I.;
RT "Human ESCRT and ALIX proteins interact with proteins of the midbody
RT and function in cytokinesis.";
RL EMBO J. 26:4215-4227(2007).
RN [9]
RP INTERACTION WITH VPS36; SNF8 AND VPS25.
RX PubMed=18539118; DOI=10.1016/j.devcel.2008.04.004;
RA Im Y.J., Hurley J.H.;
RT "Integrated structural model and membrane targeting mechanism of the
RT human ESCRT-II complex.";
RL Dev. Cell 14:902-913(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP IDENTIFICATION IN AN ESCRT-I COMPLEX WITH UBAP1, AND SUBUNIT.
RX PubMed=21757351; DOI=10.1016/j.cub.2011.06.028;
RA Stefani F., Zhang L., Taylor S., Donovan J., Rollinson S., Doyotte A.,
RA Brownhill K., Bennion J., Pickering-Brown S., Woodman P.;
RT "UBAP1 is a component of an endosome-specific ESCRT-I complex that is
RT essential for MVB sorting.";
RL Curr. Biol. 21:1245-1250(2011).
CC -!- FUNCTION: Component of the ESCRT-I complex, a regulator of
CC vesicular trafficking process.
CC -!- SUBUNIT: Component of the ESCRT-I complex (endosomal sorting
CC complex required for transport I) which consists of TSG101, VPS28,
CC a VPS37 protein (VPS37A to -D) and MVB12A or MVB12B in a 1:1:1:1
CC stoechiometry. Interacts with TSG101, VPS37B, VPS37C, MVB12A and
CC MVB12B. Component of an ESCRT-I complex (endosomal sorting complex
CC required for transport I) which consists of TSG101, VPS28, VPS37A
CC and UBAP1 in a 1:1:1:1 stoechiometry. Interacts WITH VPS36; the
CC interaction mediates the association with the ESCRT-II complex.
CC Interacts with SNF8 and VPS25. Interacts with CEP55.
CC -!- INTERACTION:
CC Q99816:TSG101; NbExp=3; IntAct=EBI-727424, EBI-346882;
CC -!- SUBCELLULAR LOCATION: Cell membrane. Late endosome membrane;
CC Peripheral membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UK41-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UK41-2; Sequence=VSP_042028;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the VPS28 family.
CC -!- SIMILARITY: Contains 1 VPS28 C-terminal domain.
CC -!- SIMILARITY: Contains 1 VPS28 N-terminal domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF182844; AAF00499.1; -; mRNA.
DR EMBL; AF205589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006485; AAH06485.1; -; mRNA.
DR EMBL; BC019321; AAH19321.1; -; mRNA.
DR EMBL; BC050713; AAH50713.1; -; mRNA.
DR RefSeq; NP_057292.1; NM_016208.3.
DR RefSeq; NP_898880.1; NM_183057.2.
DR RefSeq; XP_005272379.1; XM_005272322.1.
DR UniGene; Hs.418175; -.
DR ProteinModelPortal; Q9UK41; -.
DR SMR; Q9UK41; 24-117, 123-220.
DR IntAct; Q9UK41; 14.
DR MINT; MINT-234404; -.
DR STRING; 9606.ENSP00000366565; -.
DR PhosphoSite; Q9UK41; -.
DR DMDM; 13124619; -.
DR PaxDb; Q9UK41; -.
DR PRIDE; Q9UK41; -.
DR DNASU; 51160; -.
DR Ensembl; ENST00000292510; ENSP00000292510; ENSG00000160948.
DR Ensembl; ENST00000377348; ENSP00000366565; ENSG00000160948.
DR Ensembl; ENST00000526054; ENSP00000434064; ENSG00000160948.
DR Ensembl; ENST00000529182; ENSP00000434556; ENSG00000160948.
DR Ensembl; ENST00000562786; ENSP00000457919; ENSG00000260313.
DR Ensembl; ENST00000565984; ENSP00000456843; ENSG00000260313.
DR GeneID; 51160; -.
DR KEGG; hsa:51160; -.
DR UCSC; uc003zcs.1; human.
DR CTD; 51160; -.
DR GeneCards; GC08M145649; -.
DR HGNC; HGNC:18178; VPS28.
DR HPA; HPA024688; -.
DR HPA; HPA024745; -.
DR MIM; 611952; gene.
DR neXtProt; NX_Q9UK41; -.
DR PharmGKB; PA38512; -.
DR eggNOG; NOG276841; -.
DR HOGENOM; HOG000203818; -.
DR HOVERGEN; HBG054248; -.
DR KO; K12184; -.
DR OMA; YDNMADL; -.
DR PhylomeDB; Q9UK41; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR ChiTaRS; VPS28; human.
DR GeneWiki; VPS28; -.
DR GenomeRNAi; 51160; -.
DR NextBio; 54073; -.
DR PRO; PR:Q9UK41; -.
DR ArrayExpress; Q9UK41; -.
DR Bgee; Q9UK41; -.
DR CleanEx; HS_VPS28; -.
DR Genevestigator; Q9UK41; -.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0000813; C:ESCRT I complex; IDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016197; P:endosomal transport; TAS:Reactome.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:UniProtKB.
DR GO; GO:0019082; P:viral protein processing; TAS:Reactome.
DR GO; GO:0019068; P:virion assembly; TAS:Reactome.
DR InterPro; IPR007143; VPS28.
DR InterPro; IPR017899; VPS28_C.
DR InterPro; IPR017898; VPS28_N.
DR PANTHER; PTHR12937; PTHR12937; 1.
DR Pfam; PF03997; VPS28; 1.
DR PIRSF; PIRSF017535; VPS28; 1.
DR PROSITE; PS51310; VPS28_C; 1.
DR PROSITE; PS51313; VPS28_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Complete proteome; Endosome;
KW Membrane; Protein transport; Reference proteome; Transport.
FT CHAIN 1 221 Vacuolar protein sorting-associated
FT protein 28 homolog.
FT /FTId=PRO_0000120951.
FT DOMAIN 13 120 VPS28 N-terminal.
FT DOMAIN 124 220 VPS28 C-terminal.
FT VAR_SEQ 184 221 LQTLSGMSASDELDDSQVRQMLFDLESAYNAFNRFLHA ->
FT WVSLPARQSPAVPETLPARRSPAVPLRPSAPTCPVLHSQAA
FT DPERHVGVR (in isoform 2).
FT /FTId=VSP_042028.
SQ 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
//
MIM
611952
*RECORD*
*FIELD* NO
611952
*FIELD* TI
*611952 VACUOLAR PROTEIN SORTING 28, YEAST, HOMOLOG OF; VPS28
*FIELD* TX
DESCRIPTION
read more
Class E vacuolar protein sorting (VPS) proteins, such as VPS28, are
required for appropriate sorting of receptors within the endocytic
pathway (Bishop and Woodman, 2001).
CLONING
By searching EST databases for homologs of yeast Vps28, Bishop and
Woodman (2001) identified human VPS28 and several invertebrate homologs.
The 221-amino acid human protein shares 28% amino acid identity with
yeast Vps28. RT-PCR analysis revealed ubiquitous expression of a single
VPS28 transcript in human tissues. Immunofluorescence and confocal
microscopy showed that VPS28 was exclusively cytosolic.
GENE FUNCTION
Using coimmunoprecipitation and crosslinking analysis, Bishop and
Woodman (2001) found that human VPS28 interacted with the coiled-coil
C-terminal portion of TSG101 (601387). Expression of ATPase-defective
VPS4 (609983) shifted a portion of TSG101 and VPS28 from the cytosol to
endosomal vacuoles. Bishop and Woodman (2001) concluded that TSG101 and
VPS28 are directly involved in endosomal sorting.
Philips et al. (2008) showed that the avirulent Mycobacterium smegmatis
species could multiply in Drosophila S2 cells or murine macrophages in
which small interfering RNA had disrupted components of the ESCRT
(endosomal sorting complex required for transport) complex, including
Tsg101 and Vps28, by modulating the phagosome induced by mycobacteria.
Immunofluorescence and confocal microscopy showed that Tsg101- or
Vps28-depleted cells harbored mycobacteria in a heavily ubiquitinated
vacuolar location. Philips et al. (2008) concluded that ESCRT machinery
is critical for containment of mycobacterial proliferation.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the VPS28
gene to chromosome 8 (TMAP A006J21).
*FIELD* RF
1. Bishop, N.; Woodman, P.: TSG101/mammalian VPS23 and mammalian
VPS28 interact directly and are recruited to VPS4-induced endosomes. J.
Biol. Chem. 276: 11735-11742, 2001.
2. Philips, J. A.; Porto, M. C.; Wang, H.; Rubin, E. J.; Perrimon,
N.: ESCRT factors restrict mycobacterial growth. Proc. Nat. Acad.
Sci. 105: 3070-3075, 2008.
*FIELD* CD
Paul J. Converse: 4/14/2008
*FIELD* ED
mgross: 04/14/2008
*RECORD*
*FIELD* NO
611952
*FIELD* TI
*611952 VACUOLAR PROTEIN SORTING 28, YEAST, HOMOLOG OF; VPS28
*FIELD* TX
DESCRIPTION
read more
Class E vacuolar protein sorting (VPS) proteins, such as VPS28, are
required for appropriate sorting of receptors within the endocytic
pathway (Bishop and Woodman, 2001).
CLONING
By searching EST databases for homologs of yeast Vps28, Bishop and
Woodman (2001) identified human VPS28 and several invertebrate homologs.
The 221-amino acid human protein shares 28% amino acid identity with
yeast Vps28. RT-PCR analysis revealed ubiquitous expression of a single
VPS28 transcript in human tissues. Immunofluorescence and confocal
microscopy showed that VPS28 was exclusively cytosolic.
GENE FUNCTION
Using coimmunoprecipitation and crosslinking analysis, Bishop and
Woodman (2001) found that human VPS28 interacted with the coiled-coil
C-terminal portion of TSG101 (601387). Expression of ATPase-defective
VPS4 (609983) shifted a portion of TSG101 and VPS28 from the cytosol to
endosomal vacuoles. Bishop and Woodman (2001) concluded that TSG101 and
VPS28 are directly involved in endosomal sorting.
Philips et al. (2008) showed that the avirulent Mycobacterium smegmatis
species could multiply in Drosophila S2 cells or murine macrophages in
which small interfering RNA had disrupted components of the ESCRT
(endosomal sorting complex required for transport) complex, including
Tsg101 and Vps28, by modulating the phagosome induced by mycobacteria.
Immunofluorescence and confocal microscopy showed that Tsg101- or
Vps28-depleted cells harbored mycobacteria in a heavily ubiquitinated
vacuolar location. Philips et al. (2008) concluded that ESCRT machinery
is critical for containment of mycobacterial proliferation.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the VPS28
gene to chromosome 8 (TMAP A006J21).
*FIELD* RF
1. Bishop, N.; Woodman, P.: TSG101/mammalian VPS23 and mammalian
VPS28 interact directly and are recruited to VPS4-induced endosomes. J.
Biol. Chem. 276: 11735-11742, 2001.
2. Philips, J. A.; Porto, M. C.; Wang, H.; Rubin, E. J.; Perrimon,
N.: ESCRT factors restrict mycobacterial growth. Proc. Nat. Acad.
Sci. 105: 3070-3075, 2008.
*FIELD* CD
Paul J. Converse: 4/14/2008
*FIELD* ED
mgross: 04/14/2008