Full text data of VPS37C
VPS37C
(PML39)
[Confidence: low (only semi-automatic identification from reviews)]
Vacuolar protein sorting-associated protein 37C; hVps37C (ESCRT-I complex subunit VPS37C)
Vacuolar protein sorting-associated protein 37C; hVps37C (ESCRT-I complex subunit VPS37C)
UniProt
A5D8V6
ID VP37C_HUMAN Reviewed; 355 AA.
AC A5D8V6; Q8N3K4;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 30-NOV-2010, sequence version 2.
DT 22-JAN-2014, entry version 59.
DE RecName: Full=Vacuolar protein sorting-associated protein 37C;
DE Short=hVps37C;
DE AltName: Full=ESCRT-I complex subunit VPS37C;
GN Name=VPS37C; Synonyms=PML39;
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 [LARGE SCALE MRNA], AND VARIANT ASP-182.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-198.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-198.
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 [5]
RP FUNCTION, INTERACTION WITH HGS; STAM2 AND TSG101, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15509564; DOI=10.1074/jbc.M410384200;
RA Eastman S.W., Martin-Serrano J., Chung W., Zang T., Bieniasz P.D.;
RT "Identification of human VPS37C, a component of endosomal sorting
RT complex required for transport-I important for viral budding.";
RL J. Biol. Chem. 280:628-636(2005).
RN [6]
RP INTERACTION WITH TSG101; VPS28; MVB12A AND MVB12B, AND MASS
RP SPECTROMETRY.
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 [7]
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 [8]
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 [9]
RP PHOSPHORYLATION BY TBK1.
RX PubMed=21270402; DOI=10.4049/jimmunol.1000262;
RA Da Q., Yang X., Xu Y., Gao G., Cheng G., Tang H.;
RT "TANK-binding kinase 1 attenuates PTAP-dependent retroviral budding
RT through targeting endosomal sorting complex required for transport-
RT I.";
RL J. Immunol. 186:3023-3030(2011).
RN [10]
RP IDENTIFICATION IN AN ESCRT-I COMPLEX WITH UBAP1, AND SUBUNIT.
RX PubMed=22405001; DOI=10.1016/j.str.2011.12.013;
RA Agromayor M., Soler N., Caballe A., Kueck T., Freund S.M., Allen M.D.,
RA Bycroft M., Perisic O., Ye Y., McDonald B., Scheel H., Hofmann K.,
RA Neil S.J., Martin-Serrano J., Williams R.L.;
RT "The UBAP1 subunit of ESCRT-I interacts with ubiquitin via a SOUBA
RT domain.";
RL Structure 20:414-428(2012).
CC -!- FUNCTION: Component of the ESCRT-I complex, a regulator of
CC vesicular trafficking process. Required for the sorting of
CC endocytic ubiquitinated cargos into multivesicular bodies. May be
CC involved in cell growth and differentiation.
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, VPS28, MVB12A and MVB12B.
CC Component of the ESCRT-I complex (endosomal sorting complex
CC required for transport I) which consists of TSG101, VPS28, a VPS37
CC protein (VPS37A to -D) and UBAP1 in a 1:1:1:1 stoechiometry.
CC Interacts with HGS and STAM2. Interacts with CEP55.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane; Peripheral membrane
CC protein (Probable). Note=Probably associates with membranes.
CC Recruited to the plasma membrane by HIV-1.
CC -!- PTM: Phosphorylated by TBK1.
CC -!- SIMILARITY: Belongs to the VPS37 family.
CC -!- SIMILARITY: Contains 1 VPS37 C-terminal domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD38936.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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; AL834261; CAD38936.1; ALT_INIT; mRNA.
DR EMBL; AP000437; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW73925.1; -; Genomic_DNA.
DR EMBL; BC141827; AAI41828.1; -; mRNA.
DR EMBL; BC142702; AAI42703.1; -; mRNA.
DR RefSeq; NP_060436.4; NM_017966.4.
DR RefSeq; XP_005274134.1; XM_005274077.1.
DR RefSeq; XP_005274135.1; XM_005274078.1.
DR RefSeq; XP_005274136.1; XM_005274079.1.
DR UniGene; Hs.523715; -.
DR ProteinModelPortal; A5D8V6; -.
DR SMR; A5D8V6; 109-150.
DR IntAct; A5D8V6; 5.
DR MINT; MINT-6173488; -.
DR STRING; 9606.ENSP00000301765; -.
DR PhosphoSite; A5D8V6; -.
DR PaxDb; A5D8V6; -.
DR PRIDE; A5D8V6; -.
DR Ensembl; ENST00000301765; ENSP00000301765; ENSG00000167987.
DR GeneID; 55048; -.
DR KEGG; hsa:55048; -.
DR UCSC; uc001nqv.1; human.
DR CTD; 55048; -.
DR GeneCards; GC11M060897; -.
DR H-InvDB; HIX0009681; -.
DR HGNC; HGNC:26097; VPS37C.
DR HPA; HPA043348; -.
DR MIM; 610038; gene.
DR neXtProt; NX_A5D8V6; -.
DR PharmGKB; PA142670617; -.
DR eggNOG; NOG311749; -.
DR HOGENOM; HOG000234744; -.
DR HOVERGEN; HBG073355; -.
DR InParanoid; A5D8V6; -.
DR KO; K12185; -.
DR OMA; GYSWSPQ; -.
DR OrthoDB; EOG7KQ22B; -.
DR PhylomeDB; A5D8V6; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR ChiTaRS; VPS37C; human.
DR GenomeRNAi; 55048; -.
DR NextBio; 58505; -.
DR PRO; PR:A5D8V6; -.
DR ArrayExpress; A5D8V6; -.
DR Bgee; A5D8V6; -.
DR CleanEx; HS_VPS37C; -.
DR Genevestigator; A5D8V6; -.
DR GO; GO:0000813; C:ESCRT I complex; IDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0016197; P:endosomal transport; TAS:Reactome.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0019082; P:viral protein processing; TAS:Reactome.
DR GO; GO:0019068; P:virion assembly; TAS:Reactome.
DR InterPro; IPR009851; Mod_r.
DR Pfam; PF07200; Mod_r; 1.
DR PROSITE; PS51314; VPS37_C; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Endosome; Membrane; Polymorphism;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1 355 Vacuolar protein sorting-associated
FT protein 37C.
FT /FTId=PRO_0000312198.
FT DOMAIN 78 167 VPS37 C-terminal.
FT COMPBIAS 171 353 Pro-rich.
FT VARIANT 182 182 V -> D (in dbSNP:rs2232142).
FT /FTId=VAR_037451.
FT VARIANT 198 198 L -> S (in dbSNP:rs754382).
FT /FTId=VAR_037452.
FT VARIANT 261 261 S -> A (in dbSNP:rs4297482).
FT /FTId=VAR_037453.
SQ SEQUENCE 355 AA; 38659 MW; 1DE18F0E4C7C7E2E CRC64;
METLKDKTLQ ELEELQNDSE AIDQLALESP EVQDLQLERE MALATNRSLA ERNLEFQGPL
EISRSNLSDR YQELRKLVER CQEQKAKLEK FSSALQPGTL LDLLQVEGMK IEEESEAMAE
KFLEGEVPLE TFLENFSSMR MLSHLRRVRV EKLQEVVRKP RASQELAGDA PPPRPPPPVR
PVPQGTPPVV EEQPQPPLAM PPYPLPYSPS PSLPVGPTAH GALPPAPFPV VSQPSFYSGP
LGPTYPAAQL GPRGAAGYSW SPQRSMPPRP GYPGTPMGAS GPGYPLRGGR APSPGYPQQS
PYPATGGKPP YPIQPQLPSF PGQPQPSVPL QPPYPPGPAP PYGFPPPPGP AWPGY
//
ID VP37C_HUMAN Reviewed; 355 AA.
AC A5D8V6; Q8N3K4;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 30-NOV-2010, sequence version 2.
DT 22-JAN-2014, entry version 59.
DE RecName: Full=Vacuolar protein sorting-associated protein 37C;
DE Short=hVps37C;
DE AltName: Full=ESCRT-I complex subunit VPS37C;
GN Name=VPS37C; Synonyms=PML39;
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 [LARGE SCALE MRNA], AND VARIANT ASP-182.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-198.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-198.
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 [5]
RP FUNCTION, INTERACTION WITH HGS; STAM2 AND TSG101, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15509564; DOI=10.1074/jbc.M410384200;
RA Eastman S.W., Martin-Serrano J., Chung W., Zang T., Bieniasz P.D.;
RT "Identification of human VPS37C, a component of endosomal sorting
RT complex required for transport-I important for viral budding.";
RL J. Biol. Chem. 280:628-636(2005).
RN [6]
RP INTERACTION WITH TSG101; VPS28; MVB12A AND MVB12B, AND MASS
RP SPECTROMETRY.
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 [7]
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 [8]
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 [9]
RP PHOSPHORYLATION BY TBK1.
RX PubMed=21270402; DOI=10.4049/jimmunol.1000262;
RA Da Q., Yang X., Xu Y., Gao G., Cheng G., Tang H.;
RT "TANK-binding kinase 1 attenuates PTAP-dependent retroviral budding
RT through targeting endosomal sorting complex required for transport-
RT I.";
RL J. Immunol. 186:3023-3030(2011).
RN [10]
RP IDENTIFICATION IN AN ESCRT-I COMPLEX WITH UBAP1, AND SUBUNIT.
RX PubMed=22405001; DOI=10.1016/j.str.2011.12.013;
RA Agromayor M., Soler N., Caballe A., Kueck T., Freund S.M., Allen M.D.,
RA Bycroft M., Perisic O., Ye Y., McDonald B., Scheel H., Hofmann K.,
RA Neil S.J., Martin-Serrano J., Williams R.L.;
RT "The UBAP1 subunit of ESCRT-I interacts with ubiquitin via a SOUBA
RT domain.";
RL Structure 20:414-428(2012).
CC -!- FUNCTION: Component of the ESCRT-I complex, a regulator of
CC vesicular trafficking process. Required for the sorting of
CC endocytic ubiquitinated cargos into multivesicular bodies. May be
CC involved in cell growth and differentiation.
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, VPS28, MVB12A and MVB12B.
CC Component of the ESCRT-I complex (endosomal sorting complex
CC required for transport I) which consists of TSG101, VPS28, a VPS37
CC protein (VPS37A to -D) and UBAP1 in a 1:1:1:1 stoechiometry.
CC Interacts with HGS and STAM2. Interacts with CEP55.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane; Peripheral membrane
CC protein (Probable). Note=Probably associates with membranes.
CC Recruited to the plasma membrane by HIV-1.
CC -!- PTM: Phosphorylated by TBK1.
CC -!- SIMILARITY: Belongs to the VPS37 family.
CC -!- SIMILARITY: Contains 1 VPS37 C-terminal domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD38936.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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; AL834261; CAD38936.1; ALT_INIT; mRNA.
DR EMBL; AP000437; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW73925.1; -; Genomic_DNA.
DR EMBL; BC141827; AAI41828.1; -; mRNA.
DR EMBL; BC142702; AAI42703.1; -; mRNA.
DR RefSeq; NP_060436.4; NM_017966.4.
DR RefSeq; XP_005274134.1; XM_005274077.1.
DR RefSeq; XP_005274135.1; XM_005274078.1.
DR RefSeq; XP_005274136.1; XM_005274079.1.
DR UniGene; Hs.523715; -.
DR ProteinModelPortal; A5D8V6; -.
DR SMR; A5D8V6; 109-150.
DR IntAct; A5D8V6; 5.
DR MINT; MINT-6173488; -.
DR STRING; 9606.ENSP00000301765; -.
DR PhosphoSite; A5D8V6; -.
DR PaxDb; A5D8V6; -.
DR PRIDE; A5D8V6; -.
DR Ensembl; ENST00000301765; ENSP00000301765; ENSG00000167987.
DR GeneID; 55048; -.
DR KEGG; hsa:55048; -.
DR UCSC; uc001nqv.1; human.
DR CTD; 55048; -.
DR GeneCards; GC11M060897; -.
DR H-InvDB; HIX0009681; -.
DR HGNC; HGNC:26097; VPS37C.
DR HPA; HPA043348; -.
DR MIM; 610038; gene.
DR neXtProt; NX_A5D8V6; -.
DR PharmGKB; PA142670617; -.
DR eggNOG; NOG311749; -.
DR HOGENOM; HOG000234744; -.
DR HOVERGEN; HBG073355; -.
DR InParanoid; A5D8V6; -.
DR KO; K12185; -.
DR OMA; GYSWSPQ; -.
DR OrthoDB; EOG7KQ22B; -.
DR PhylomeDB; A5D8V6; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR ChiTaRS; VPS37C; human.
DR GenomeRNAi; 55048; -.
DR NextBio; 58505; -.
DR PRO; PR:A5D8V6; -.
DR ArrayExpress; A5D8V6; -.
DR Bgee; A5D8V6; -.
DR CleanEx; HS_VPS37C; -.
DR Genevestigator; A5D8V6; -.
DR GO; GO:0000813; C:ESCRT I complex; IDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0016197; P:endosomal transport; TAS:Reactome.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0019082; P:viral protein processing; TAS:Reactome.
DR GO; GO:0019068; P:virion assembly; TAS:Reactome.
DR InterPro; IPR009851; Mod_r.
DR Pfam; PF07200; Mod_r; 1.
DR PROSITE; PS51314; VPS37_C; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Endosome; Membrane; Polymorphism;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1 355 Vacuolar protein sorting-associated
FT protein 37C.
FT /FTId=PRO_0000312198.
FT DOMAIN 78 167 VPS37 C-terminal.
FT COMPBIAS 171 353 Pro-rich.
FT VARIANT 182 182 V -> D (in dbSNP:rs2232142).
FT /FTId=VAR_037451.
FT VARIANT 198 198 L -> S (in dbSNP:rs754382).
FT /FTId=VAR_037452.
FT VARIANT 261 261 S -> A (in dbSNP:rs4297482).
FT /FTId=VAR_037453.
SQ SEQUENCE 355 AA; 38659 MW; 1DE18F0E4C7C7E2E CRC64;
METLKDKTLQ ELEELQNDSE AIDQLALESP EVQDLQLERE MALATNRSLA ERNLEFQGPL
EISRSNLSDR YQELRKLVER CQEQKAKLEK FSSALQPGTL LDLLQVEGMK IEEESEAMAE
KFLEGEVPLE TFLENFSSMR MLSHLRRVRV EKLQEVVRKP RASQELAGDA PPPRPPPPVR
PVPQGTPPVV EEQPQPPLAM PPYPLPYSPS PSLPVGPTAH GALPPAPFPV VSQPSFYSGP
LGPTYPAAQL GPRGAAGYSW SPQRSMPPRP GYPGTPMGAS GPGYPLRGGR APSPGYPQQS
PYPATGGKPP YPIQPQLPSF PGQPQPSVPL QPPYPPGPAP PYGFPPPPGP AWPGY
//
MIM
610038
*RECORD*
*FIELD* NO
610038
*FIELD* TI
*610038 VACUOLAR PROTEIN SORTING 37, YEAST, HOMOLOG OF, C; VPS37C
*FIELD* TX
DESCRIPTION
read more
VPS37C is a subunit of ESCRT-I (endosomal sorting complex required for
transport I), a complex in the class E vacuolar protein sorting (VPS)
pathway required for sorting ubiquitinated transmembrane proteins into
internal vesicles of multivesicular bodies (Eastman et al., 2005).
CLONING
By searching a database for sequences homologous to yeast Vps37,
Stuchell et al. (2004) identified human VPS37C. The deduced 523-amino
acid protein contains a central mod(r) (modifier of rudimentary) domain
and 2 coiled-coil regions, one overlapping the N-terminal border of the
mod(r) domain and the other within the mod(r) domain.
Using TSG101 (601387) as bait in a yeast 2-hybrid screen of a peripheral
mononuclear lymphocyte cDNA library, Eastman et al. (2005) cloned
VPS37C. The deduced 355-amino acid protein contains an N-terminal mod(r)
domain and a C-terminal proline-rich domain.
GENE FUNCTION
Eastman et al. (2005) found that VPS37C formed a ternary complex with
TSG101 and VPS28 (601387) by binding a C-terminal domain of TSG101.
VPS37C also bound HRS (HGS; 604375), another class E VPS factor. VPS37C
was recruited to aberrant endosomes induced by overexpression of TSG101,
HRS, or a dominant-negative form of VPS4 (VPS4A; 609982). Enveloped
viruses that encode PTAP motifs to facilitate budding, like human
immunodeficiency virus (HIV)-1 Gag protein, exploit ESCRT-I as an
interface with the class E VPS pathway. VPS37C was recruited to the
plasma membrane along with TSG101 by HIV-1 Gag. Moreover, direct fusion
of VPS37C to HIV-1 Gag obviated the requirement for a PTAP motif to
induce virion release. Depletion of VPS37C from human embryonic kidney
cells did not inhibit murine leukemia virus budding, which is not
mediated by ESCRT-I. However, if murine leukemia virus budding was
engineered to be ESCRT-I-dependent, it was inhibited by VPS37C
depletion, and the inhibition was accentuated if VPS37B (610037) was
simultaneously depleted. Eastman et al. (2005) concluded that VPS37C is
a functional component of mammalian ESCRT-I.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the VPS37C
gene to chromosome 11 (TMAP SHGC-31731).
*FIELD* RF
1. Eastman, S. W.; Martin-Serrano, J.; Chung, W.; Zang, T.; Bieniasz,
P. D.: Identification of human VPS37C, a component of endosomal sorting
complex required for transport-I important for viral budding. J.
Biol. Chem. 280: 628-636, 2005.
2. Stuchell, M. D.; Garrus, J. E.; Muller, B.; Stray, K. M.; Ghaffarian,
S.; McKinnon, R.; Krausslich, 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.
*FIELD* CD
Patricia A. Hartz: 4/10/2006
*FIELD* ED
mgross: 04/14/2008
mgross: 4/10/2006
*RECORD*
*FIELD* NO
610038
*FIELD* TI
*610038 VACUOLAR PROTEIN SORTING 37, YEAST, HOMOLOG OF, C; VPS37C
*FIELD* TX
DESCRIPTION
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VPS37C is a subunit of ESCRT-I (endosomal sorting complex required for
transport I), a complex in the class E vacuolar protein sorting (VPS)
pathway required for sorting ubiquitinated transmembrane proteins into
internal vesicles of multivesicular bodies (Eastman et al., 2005).
CLONING
By searching a database for sequences homologous to yeast Vps37,
Stuchell et al. (2004) identified human VPS37C. The deduced 523-amino
acid protein contains a central mod(r) (modifier of rudimentary) domain
and 2 coiled-coil regions, one overlapping the N-terminal border of the
mod(r) domain and the other within the mod(r) domain.
Using TSG101 (601387) as bait in a yeast 2-hybrid screen of a peripheral
mononuclear lymphocyte cDNA library, Eastman et al. (2005) cloned
VPS37C. The deduced 355-amino acid protein contains an N-terminal mod(r)
domain and a C-terminal proline-rich domain.
GENE FUNCTION
Eastman et al. (2005) found that VPS37C formed a ternary complex with
TSG101 and VPS28 (601387) by binding a C-terminal domain of TSG101.
VPS37C also bound HRS (HGS; 604375), another class E VPS factor. VPS37C
was recruited to aberrant endosomes induced by overexpression of TSG101,
HRS, or a dominant-negative form of VPS4 (VPS4A; 609982). Enveloped
viruses that encode PTAP motifs to facilitate budding, like human
immunodeficiency virus (HIV)-1 Gag protein, exploit ESCRT-I as an
interface with the class E VPS pathway. VPS37C was recruited to the
plasma membrane along with TSG101 by HIV-1 Gag. Moreover, direct fusion
of VPS37C to HIV-1 Gag obviated the requirement for a PTAP motif to
induce virion release. Depletion of VPS37C from human embryonic kidney
cells did not inhibit murine leukemia virus budding, which is not
mediated by ESCRT-I. However, if murine leukemia virus budding was
engineered to be ESCRT-I-dependent, it was inhibited by VPS37C
depletion, and the inhibition was accentuated if VPS37B (610037) was
simultaneously depleted. Eastman et al. (2005) concluded that VPS37C is
a functional component of mammalian ESCRT-I.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the VPS37C
gene to chromosome 11 (TMAP SHGC-31731).
*FIELD* RF
1. Eastman, S. W.; Martin-Serrano, J.; Chung, W.; Zang, T.; Bieniasz,
P. D.: Identification of human VPS37C, a component of endosomal sorting
complex required for transport-I important for viral budding. J.
Biol. Chem. 280: 628-636, 2005.
2. Stuchell, M. D.; Garrus, J. E.; Muller, B.; Stray, K. M.; Ghaffarian,
S.; McKinnon, R.; Krausslich, 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.
*FIELD* CD
Patricia A. Hartz: 4/10/2006
*FIELD* ED
mgross: 04/14/2008
mgross: 4/10/2006