Full text data of CHMP5
CHMP5
(C9orf83, SNF7DC2)
[Confidence: low (only semi-automatic identification from reviews)]
Charged multivesicular body protein 5 (Chromatin-modifying protein 5; SNF7 domain-containing protein 2; Vacuolar protein sorting-associated protein 60; Vps60; hVps60)
Charged multivesicular body protein 5 (Chromatin-modifying protein 5; SNF7 domain-containing protein 2; Vacuolar protein sorting-associated protein 60; Vps60; hVps60)
UniProt
Q9NZZ3
ID CHMP5_HUMAN Reviewed; 219 AA.
AC Q9NZZ3; B2RD95; B4DIR6; Q5VXW2; Q96AV2; Q9HB68; Q9NYS4; Q9Y323;
read moreDT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 108.
DE RecName: Full=Charged multivesicular body protein 5;
DE AltName: Full=Chromatin-modifying protein 5;
DE AltName: Full=SNF7 domain-containing protein 2;
DE AltName: Full=Vacuolar protein sorting-associated protein 60;
DE Short=Vps60;
DE Short=hVps60;
GN Name=CHMP5; Synonyms=C9orf83, SNF7DC2;
GN ORFNames=CGI-34, HSPC177, PNAS-114, PNAS-2;
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] (ISOFORM 1).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow, Brain, Kidney, and Urinary bladder;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 81-219 (ISOFORM 1).
RC TISSUE=Promyelocytic leukemia;
RA Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F.,
RA Yan W., Yang H., Zhao Z.-L.;
RT "Human acute promyelocytic leukemia cell line NB4's apoptosis related
RT genes.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION IN HIV-1 BUDDING, AND INTERACTION WITH CHMP2A.
RX PubMed=14519844; DOI=10.1073/pnas.2133846100;
RA Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.;
RT "Divergent retroviral late-budding domains recruit vacuolar protein
RT sorting factors by using alternative adaptor proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003).
RN [9]
RP ERRATUM.
RA Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.;
RL Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH VTA1.
RX PubMed=15644320; DOI=10.1074/jbc.M413734200;
RA Ward D.M., Vaughn M.B., Shiflett S.L., White P.L., Pollock A.L.,
RA Hill J., Schnegelberger R., Sundquist W.I., Kaplan J.;
RT "The role of LIP5 and CHMP5 in multivesicular body formation and HIV-1
RT budding in mammalian cells.";
RL J. Biol. Chem. 280:10548-10555(2005).
RN [11]
RP SUBCELLULAR LOCATION.
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 [12]
RP INTERACTION WITH VTA1, AND MASS SPECTROMETRY.
RX PubMed=17261583; DOI=10.1074/jbc.M611635200;
RA Ma Y.M., Boucrot E., Villen J., Affar el B., Gygi S.P.,
RA Goettlinger H.G., Kirchhausen T.;
RT "Targeting of AMSH to endosomes is required for epidermal growth
RT factor receptor degradation.";
RL J. Biol. Chem. 282:9805-9812(2007).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
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 [16]
RP ISGYLATION, AND INTERACTION WITH VTA1.
RX PubMed=21543490; DOI=10.1128/JVI.02610-10;
RA Kuang Z., Seo E.J., Leis J.;
RT "Mechanism of inhibition of retrovirus release from cells by
RT interferon-induced gene ISG15.";
RL J. Virol. 85:7153-7161(2011).
CC -!- FUNCTION: Probable peripherally associated component of the
CC endosomal sorting required for transport complex III (ESCRT-III)
CC which is involved in multivesicular bodies (MVBs) formation and
CC sorting of endosomal cargo proteins into MVBs. MVBs contain
CC intraluminal vesicles (ILVs) that are generated by invagination
CC and scission from the limiting membrane of the endosome and mostly
CC are delivered to lysosomes enabling degradation of membrane
CC proteins, such as stimulated growth factor receptors, lysosomal
CC enzymes and lipids. The MVB pathway appears to require the
CC sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-
CC III proteins mostly dissociate from the invaginating membrane
CC before the ILV is released. The ESCRT machinery also functions in
CC topologically equivalent membrane fission events, such as the
CC terminal stages of cytokinesis and the budding of enveloped
CC viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are
CC believed to mediate the necessary vesicle extrusion and/or
CC membrane fission activities, possibly in conjunction with the AAA
CC ATPase VPS4. Involved in HIV-1 p6- and p9-dependent virus release.
CC -!- SUBUNIT: Probable peripherally associated component of the
CC endosomal sorting required for transport complex III (ESCRT-III).
CC ESCRT-III components are thought to multimerize to form a flat
CC lattice on the perimeter membrane of the endosome. Several
CC assembly forms of ESCRT-III may exist that interact and act
CC sequentally. Interacts with VTA1. Interacts with CHMP2A. Interacts
CC with VTA1; the interaction involves soluble CHMP5.
CC -!- INTERACTION:
CC O95630:STAMBP; NbExp=2; IntAct=EBI-751303, EBI-396676;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Endosome membrane;
CC Peripheral membrane protein (Probable). Note=Localizes to the
CC midbody of dividing cells. Localized in two distinct rings on
CC either side of the Fleming body.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NZZ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NZZ3-2; Sequence=VSP_042556;
CC Note=No experimental confirmation available;
CC -!- PTM: ISGylated. Isgylation inhibits its interaction with VTA1.
CC -!- SIMILARITY: Belongs to the SNF7 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG23821.1; Type=Erroneous initiation;
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DR EMBL; AF132968; AAD27743.1; -; mRNA.
DR EMBL; AF161525; AAF29140.1; -; mRNA.
DR EMBL; AK295744; BAG58578.1; -; mRNA.
DR EMBL; AK315455; BAG37842.1; -; mRNA.
DR EMBL; AL356472; CAH72744.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58512.1; -; Genomic_DNA.
DR EMBL; BC006974; AAH06974.1; -; mRNA.
DR EMBL; BC007457; AAH07457.1; -; mRNA.
DR EMBL; BC016698; AAH16698.1; -; mRNA.
DR EMBL; BC020796; AAH20796.1; -; mRNA.
DR EMBL; BC021168; AAH21168.1; -; mRNA.
DR EMBL; AF275810; AAG23821.1; ALT_INIT; mRNA.
DR EMBL; AF229832; AAF42917.1; -; mRNA.
DR RefSeq; NP_001182465.1; NM_001195536.1.
DR RefSeq; NP_057494.3; NM_016410.5.
DR UniGene; Hs.635313; -.
DR PDB; 2LXM; NMR; -; B=139-195.
DR PDB; 3ULY; X-ray; 2.60 A; B=151-219.
DR PDB; 3UM0; X-ray; 3.10 A; B=200-219.
DR PDB; 3UM1; X-ray; 2.71 A; B/E=151-219.
DR PDB; 3UM2; X-ray; 2.59 A; B/E=200-219.
DR PDBsum; 2LXM; -.
DR PDBsum; 3ULY; -.
DR PDBsum; 3UM0; -.
DR PDBsum; 3UM1; -.
DR PDBsum; 3UM2; -.
DR ProteinModelPortal; Q9NZZ3; -.
DR SMR; Q9NZZ3; 154-189.
DR DIP; DIP-50420N; -.
DR IntAct; Q9NZZ3; 5.
DR MINT; MINT-1466639; -.
DR STRING; 9606.ENSP00000223500; -.
DR PhosphoSite; Q9NZZ3; -.
DR DMDM; 51702157; -.
DR PaxDb; Q9NZZ3; -.
DR PeptideAtlas; Q9NZZ3; -.
DR PRIDE; Q9NZZ3; -.
DR DNASU; 51510; -.
DR Ensembl; ENST00000223500; ENSP00000223500; ENSG00000086065.
DR Ensembl; ENST00000419016; ENSP00000442725; ENSG00000086065.
DR GeneID; 51510; -.
DR KEGG; hsa:51510; -.
DR UCSC; uc003zsm.4; human.
DR CTD; 51510; -.
DR GeneCards; GC09P033257; -.
DR HGNC; HGNC:26942; CHMP5.
DR HPA; CAB033874; -.
DR HPA; HPA042883; -.
DR HPA; HPA056437; -.
DR MIM; 610900; gene.
DR neXtProt; NX_Q9NZZ3; -.
DR PharmGKB; PA134903143; -.
DR eggNOG; NOG300000; -.
DR HOGENOM; HOG000191086; -.
DR HOVERGEN; HBG055759; -.
DR InParanoid; Q9NZZ3; -.
DR KO; K12198; -.
DR OMA; ARYKEQM; -.
DR OrthoDB; EOG7JMGFX; -.
DR PhylomeDB; Q9NZZ3; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR ChiTaRS; CHMP5; human.
DR GeneWiki; CHMP5; -.
DR GenomeRNAi; 51510; -.
DR NextBio; 55198; -.
DR PRO; PR:Q9NZZ3; -.
DR Bgee; Q9NZZ3; -.
DR CleanEx; HS_CHMP5; -.
DR Genevestigator; Q9NZZ3; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0016197; P:endosomal transport; TAS:Reactome.
DR GO; GO:0008333; P:endosome to lysosome transport; IEA:Ensembl.
DR GO; GO:0007040; P:lysosome organization; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0001919; P:regulation of receptor recycling; IEA:Ensembl.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR005024; Snf7.
DR Pfam; PF03357; Snf7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; Endosome; Membrane; Phosphoprotein; Polymorphism;
KW Protein transport; Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1 219 Charged multivesicular body protein 5.
FT /FTId=PRO_0000211500.
FT REGION 121 158 Interaction with VTA1.
FT COILED 26 179 Potential.
FT MOD_RES 86 86 Phosphoserine.
FT VAR_SEQ 166 219 ELDALGDELLADEDSSYLDEAASAPAIPEGVPTDTKNKDGV
FT LVDEFGLPQIPAS -> GWSSGG (in isoform 2).
FT /FTId=VSP_042556.
FT VARIANT 86 86 S -> P (in dbSNP:rs11540558).
FT /FTId=VAR_052029.
FT CONFLICT 14 14 P -> R (in Ref. 1; AAD27743).
FT CONFLICT 19 19 D -> G (in Ref. 6; AAH16698).
FT CONFLICT 84 93 QQSFNMEQAN -> NSHSTWTGH (in Ref. 1;
FT AAD27743).
FT CONFLICT 122 122 Q -> P (in Ref. 1; AAD27743).
FT HELIX 160 176
FT HELIX 181 188
SQ SEQUENCE 219 AA; 24571 MW; C99695F66FD7E126 CRC64;
MNRLFGKAKP KAPPPSLTDC IGTVDSRAES IDKKISRLDA ELVKYKDQIK KMREGPAKNM
VKQKALRVLK QKRMYEQQRD NLAQQSFNME QANYTIQSLK DTKTTVDAMK LGVKEMKKAY
KQVKIDQIED LQDQLEDMME DANEIQEALS RSYGTPELDE DDLEAELDAL GDELLADEDS
SYLDEAASAP AIPEGVPTDT KNKDGVLVDE FGLPQIPAS
//
ID CHMP5_HUMAN Reviewed; 219 AA.
AC Q9NZZ3; B2RD95; B4DIR6; Q5VXW2; Q96AV2; Q9HB68; Q9NYS4; Q9Y323;
read moreDT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 108.
DE RecName: Full=Charged multivesicular body protein 5;
DE AltName: Full=Chromatin-modifying protein 5;
DE AltName: Full=SNF7 domain-containing protein 2;
DE AltName: Full=Vacuolar protein sorting-associated protein 60;
DE Short=Vps60;
DE Short=hVps60;
GN Name=CHMP5; Synonyms=C9orf83, SNF7DC2;
GN ORFNames=CGI-34, HSPC177, PNAS-114, PNAS-2;
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] (ISOFORM 1).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow, Brain, Kidney, and Urinary bladder;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 81-219 (ISOFORM 1).
RC TISSUE=Promyelocytic leukemia;
RA Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F.,
RA Yan W., Yang H., Zhao Z.-L.;
RT "Human acute promyelocytic leukemia cell line NB4's apoptosis related
RT genes.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION IN HIV-1 BUDDING, AND INTERACTION WITH CHMP2A.
RX PubMed=14519844; DOI=10.1073/pnas.2133846100;
RA Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.;
RT "Divergent retroviral late-budding domains recruit vacuolar protein
RT sorting factors by using alternative adaptor proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003).
RN [9]
RP ERRATUM.
RA Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.;
RL Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH VTA1.
RX PubMed=15644320; DOI=10.1074/jbc.M413734200;
RA Ward D.M., Vaughn M.B., Shiflett S.L., White P.L., Pollock A.L.,
RA Hill J., Schnegelberger R., Sundquist W.I., Kaplan J.;
RT "The role of LIP5 and CHMP5 in multivesicular body formation and HIV-1
RT budding in mammalian cells.";
RL J. Biol. Chem. 280:10548-10555(2005).
RN [11]
RP SUBCELLULAR LOCATION.
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 [12]
RP INTERACTION WITH VTA1, AND MASS SPECTROMETRY.
RX PubMed=17261583; DOI=10.1074/jbc.M611635200;
RA Ma Y.M., Boucrot E., Villen J., Affar el B., Gygi S.P.,
RA Goettlinger H.G., Kirchhausen T.;
RT "Targeting of AMSH to endosomes is required for epidermal growth
RT factor receptor degradation.";
RL J. Biol. Chem. 282:9805-9812(2007).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
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 [16]
RP ISGYLATION, AND INTERACTION WITH VTA1.
RX PubMed=21543490; DOI=10.1128/JVI.02610-10;
RA Kuang Z., Seo E.J., Leis J.;
RT "Mechanism of inhibition of retrovirus release from cells by
RT interferon-induced gene ISG15.";
RL J. Virol. 85:7153-7161(2011).
CC -!- FUNCTION: Probable peripherally associated component of the
CC endosomal sorting required for transport complex III (ESCRT-III)
CC which is involved in multivesicular bodies (MVBs) formation and
CC sorting of endosomal cargo proteins into MVBs. MVBs contain
CC intraluminal vesicles (ILVs) that are generated by invagination
CC and scission from the limiting membrane of the endosome and mostly
CC are delivered to lysosomes enabling degradation of membrane
CC proteins, such as stimulated growth factor receptors, lysosomal
CC enzymes and lipids. The MVB pathway appears to require the
CC sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-
CC III proteins mostly dissociate from the invaginating membrane
CC before the ILV is released. The ESCRT machinery also functions in
CC topologically equivalent membrane fission events, such as the
CC terminal stages of cytokinesis and the budding of enveloped
CC viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are
CC believed to mediate the necessary vesicle extrusion and/or
CC membrane fission activities, possibly in conjunction with the AAA
CC ATPase VPS4. Involved in HIV-1 p6- and p9-dependent virus release.
CC -!- SUBUNIT: Probable peripherally associated component of the
CC endosomal sorting required for transport complex III (ESCRT-III).
CC ESCRT-III components are thought to multimerize to form a flat
CC lattice on the perimeter membrane of the endosome. Several
CC assembly forms of ESCRT-III may exist that interact and act
CC sequentally. Interacts with VTA1. Interacts with CHMP2A. Interacts
CC with VTA1; the interaction involves soluble CHMP5.
CC -!- INTERACTION:
CC O95630:STAMBP; NbExp=2; IntAct=EBI-751303, EBI-396676;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Endosome membrane;
CC Peripheral membrane protein (Probable). Note=Localizes to the
CC midbody of dividing cells. Localized in two distinct rings on
CC either side of the Fleming body.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NZZ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NZZ3-2; Sequence=VSP_042556;
CC Note=No experimental confirmation available;
CC -!- PTM: ISGylated. Isgylation inhibits its interaction with VTA1.
CC -!- SIMILARITY: Belongs to the SNF7 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG23821.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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DR EMBL; AF132968; AAD27743.1; -; mRNA.
DR EMBL; AF161525; AAF29140.1; -; mRNA.
DR EMBL; AK295744; BAG58578.1; -; mRNA.
DR EMBL; AK315455; BAG37842.1; -; mRNA.
DR EMBL; AL356472; CAH72744.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58512.1; -; Genomic_DNA.
DR EMBL; BC006974; AAH06974.1; -; mRNA.
DR EMBL; BC007457; AAH07457.1; -; mRNA.
DR EMBL; BC016698; AAH16698.1; -; mRNA.
DR EMBL; BC020796; AAH20796.1; -; mRNA.
DR EMBL; BC021168; AAH21168.1; -; mRNA.
DR EMBL; AF275810; AAG23821.1; ALT_INIT; mRNA.
DR EMBL; AF229832; AAF42917.1; -; mRNA.
DR RefSeq; NP_001182465.1; NM_001195536.1.
DR RefSeq; NP_057494.3; NM_016410.5.
DR UniGene; Hs.635313; -.
DR PDB; 2LXM; NMR; -; B=139-195.
DR PDB; 3ULY; X-ray; 2.60 A; B=151-219.
DR PDB; 3UM0; X-ray; 3.10 A; B=200-219.
DR PDB; 3UM1; X-ray; 2.71 A; B/E=151-219.
DR PDB; 3UM2; X-ray; 2.59 A; B/E=200-219.
DR PDBsum; 2LXM; -.
DR PDBsum; 3ULY; -.
DR PDBsum; 3UM0; -.
DR PDBsum; 3UM1; -.
DR PDBsum; 3UM2; -.
DR ProteinModelPortal; Q9NZZ3; -.
DR SMR; Q9NZZ3; 154-189.
DR DIP; DIP-50420N; -.
DR IntAct; Q9NZZ3; 5.
DR MINT; MINT-1466639; -.
DR STRING; 9606.ENSP00000223500; -.
DR PhosphoSite; Q9NZZ3; -.
DR DMDM; 51702157; -.
DR PaxDb; Q9NZZ3; -.
DR PeptideAtlas; Q9NZZ3; -.
DR PRIDE; Q9NZZ3; -.
DR DNASU; 51510; -.
DR Ensembl; ENST00000223500; ENSP00000223500; ENSG00000086065.
DR Ensembl; ENST00000419016; ENSP00000442725; ENSG00000086065.
DR GeneID; 51510; -.
DR KEGG; hsa:51510; -.
DR UCSC; uc003zsm.4; human.
DR CTD; 51510; -.
DR GeneCards; GC09P033257; -.
DR HGNC; HGNC:26942; CHMP5.
DR HPA; CAB033874; -.
DR HPA; HPA042883; -.
DR HPA; HPA056437; -.
DR MIM; 610900; gene.
DR neXtProt; NX_Q9NZZ3; -.
DR PharmGKB; PA134903143; -.
DR eggNOG; NOG300000; -.
DR HOGENOM; HOG000191086; -.
DR HOVERGEN; HBG055759; -.
DR InParanoid; Q9NZZ3; -.
DR KO; K12198; -.
DR OMA; ARYKEQM; -.
DR OrthoDB; EOG7JMGFX; -.
DR PhylomeDB; Q9NZZ3; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR ChiTaRS; CHMP5; human.
DR GeneWiki; CHMP5; -.
DR GenomeRNAi; 51510; -.
DR NextBio; 55198; -.
DR PRO; PR:Q9NZZ3; -.
DR Bgee; Q9NZZ3; -.
DR CleanEx; HS_CHMP5; -.
DR Genevestigator; Q9NZZ3; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0016197; P:endosomal transport; TAS:Reactome.
DR GO; GO:0008333; P:endosome to lysosome transport; IEA:Ensembl.
DR GO; GO:0007040; P:lysosome organization; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0001919; P:regulation of receptor recycling; IEA:Ensembl.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR005024; Snf7.
DR Pfam; PF03357; Snf7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; Endosome; Membrane; Phosphoprotein; Polymorphism;
KW Protein transport; Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1 219 Charged multivesicular body protein 5.
FT /FTId=PRO_0000211500.
FT REGION 121 158 Interaction with VTA1.
FT COILED 26 179 Potential.
FT MOD_RES 86 86 Phosphoserine.
FT VAR_SEQ 166 219 ELDALGDELLADEDSSYLDEAASAPAIPEGVPTDTKNKDGV
FT LVDEFGLPQIPAS -> GWSSGG (in isoform 2).
FT /FTId=VSP_042556.
FT VARIANT 86 86 S -> P (in dbSNP:rs11540558).
FT /FTId=VAR_052029.
FT CONFLICT 14 14 P -> R (in Ref. 1; AAD27743).
FT CONFLICT 19 19 D -> G (in Ref. 6; AAH16698).
FT CONFLICT 84 93 QQSFNMEQAN -> NSHSTWTGH (in Ref. 1;
FT AAD27743).
FT CONFLICT 122 122 Q -> P (in Ref. 1; AAD27743).
FT HELIX 160 176
FT HELIX 181 188
SQ SEQUENCE 219 AA; 24571 MW; C99695F66FD7E126 CRC64;
MNRLFGKAKP KAPPPSLTDC IGTVDSRAES IDKKISRLDA ELVKYKDQIK KMREGPAKNM
VKQKALRVLK QKRMYEQQRD NLAQQSFNME QANYTIQSLK DTKTTVDAMK LGVKEMKKAY
KQVKIDQIED LQDQLEDMME DANEIQEALS RSYGTPELDE DDLEAELDAL GDELLADEDS
SYLDEAASAP AIPEGVPTDT KNKDGVLVDE FGLPQIPAS
//
MIM
610900
*RECORD*
*FIELD* NO
610900
*FIELD* TI
*610900 CHMP FAMILY, MEMBER 5; CHMP5
;;CHROMATIN-MODIFYING PROTEIN 5;;
CHARGED MULTIVESICULAR BODY PROTEIN 5;;
read moreHSPC177
*FIELD* TX
DESCRIPTION
CHMP5 belongs to the chromatin-modifying protein/charged multivesicular
body protein (CHMP) family. These proteins are components of ESCRT-III
(endosomal sorting complex required for transport III), a complex
involved in degradation of surface receptor proteins and formation of
endocytic multivesicular bodies (MVBs). Some CHMPs have both nuclear and
cytoplasmic/vesicular distributions, and one such CHMP, CHMP1A (164010),
is required for both MVB formation and regulation of cell cycle
progression (Tsang et al., 2006).
CLONING
Ward et al. (2005) stated that CHMP5 is a small coiled-coil protein.
Cell fractionation of COS-7 cells followed by Western blot analysis
showed that endogenous Chmp5 was primarily a cytosolic protein.
Fluorescence-tagged human CHMP5 localized to vesicles near the nucleus
in transfected COS-7 cells.
GENE FUNCTION
Using affinity purification experiments, Ward et al. (2005) showed that
LIP5 (610902) specifically interacted with CHMP5. Depletion of CHMP5 by
small-interfering RNA did not alter the distribution of early or late
endocytic markers in HeLa and 293T cells, but it altered EGFR (131550)
trafficking and reduced EGFR degradation in lysosomes. Depletion of
CHMP5 in 293T cells infected with human immunodeficiency virus (HIV)-1
increased release of infectious particles.
Tsang et al. (2006) performed a systematic yeast 2-hybrid analysis of
human ESCRT-III components, including CHMP5. CHMP5 interacted with
SMARCA4 (603254), which may be involved in chromatin remodeling. In
addition, CHMP5 interacted with the SUMO (see SUMO1; 601912)-conjugating
enzyme UBE2I (601661) and appeared to be part of a network connecting
CHMP1A, CHMP4B (610897), and CHMP5 with UBE2I, SUMO1, PIAS2 (603567),
and HIPK2 (606868), all of which are involved in nuclear sumoylation
processes.
MAPPING
Hartz (2007) mapped the CHMP5 gene to chromosome 9p13.3 based on an
alignment of the CHMP5 sequence (GenBank GENBANK AF132968) with the
genomic sequence (build 36.1).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 3/29/2007.
2. Tsang, H. T. H.; Connell, J. W.; Brown, S. E.; Thompson, A.; Reid,
E.; Sanderson, C. M.: A systematic analysis of human CHMP protein
interactions: additional MIT domain-containing proteins bind to multiple
components of the human ESCRT III complex. Genomics 88: 333-346,
2006.
3. Ward, D. M.; Vaughn, M. B.; Shiflett, S. L.; White, P. L.; Pollock,
A. L.; Hill, J.; Schnegelberger, R.; Sundquist, W. I.; Kaplan, J.
: The role of LIP5 and CHMP5 in multivesicular body formation and
HIV-1 budding in mammalian cells. J. Biol. Chem. 280: 10548-10555,
2005.
*FIELD* CD
Patricia A. Hartz: 3/29/2007
*FIELD* ED
mgross: 03/30/2007
mgross: 3/29/2007
*RECORD*
*FIELD* NO
610900
*FIELD* TI
*610900 CHMP FAMILY, MEMBER 5; CHMP5
;;CHROMATIN-MODIFYING PROTEIN 5;;
CHARGED MULTIVESICULAR BODY PROTEIN 5;;
read moreHSPC177
*FIELD* TX
DESCRIPTION
CHMP5 belongs to the chromatin-modifying protein/charged multivesicular
body protein (CHMP) family. These proteins are components of ESCRT-III
(endosomal sorting complex required for transport III), a complex
involved in degradation of surface receptor proteins and formation of
endocytic multivesicular bodies (MVBs). Some CHMPs have both nuclear and
cytoplasmic/vesicular distributions, and one such CHMP, CHMP1A (164010),
is required for both MVB formation and regulation of cell cycle
progression (Tsang et al., 2006).
CLONING
Ward et al. (2005) stated that CHMP5 is a small coiled-coil protein.
Cell fractionation of COS-7 cells followed by Western blot analysis
showed that endogenous Chmp5 was primarily a cytosolic protein.
Fluorescence-tagged human CHMP5 localized to vesicles near the nucleus
in transfected COS-7 cells.
GENE FUNCTION
Using affinity purification experiments, Ward et al. (2005) showed that
LIP5 (610902) specifically interacted with CHMP5. Depletion of CHMP5 by
small-interfering RNA did not alter the distribution of early or late
endocytic markers in HeLa and 293T cells, but it altered EGFR (131550)
trafficking and reduced EGFR degradation in lysosomes. Depletion of
CHMP5 in 293T cells infected with human immunodeficiency virus (HIV)-1
increased release of infectious particles.
Tsang et al. (2006) performed a systematic yeast 2-hybrid analysis of
human ESCRT-III components, including CHMP5. CHMP5 interacted with
SMARCA4 (603254), which may be involved in chromatin remodeling. In
addition, CHMP5 interacted with the SUMO (see SUMO1; 601912)-conjugating
enzyme UBE2I (601661) and appeared to be part of a network connecting
CHMP1A, CHMP4B (610897), and CHMP5 with UBE2I, SUMO1, PIAS2 (603567),
and HIPK2 (606868), all of which are involved in nuclear sumoylation
processes.
MAPPING
Hartz (2007) mapped the CHMP5 gene to chromosome 9p13.3 based on an
alignment of the CHMP5 sequence (GenBank GENBANK AF132968) with the
genomic sequence (build 36.1).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 3/29/2007.
2. Tsang, H. T. H.; Connell, J. W.; Brown, S. E.; Thompson, A.; Reid,
E.; Sanderson, C. M.: A systematic analysis of human CHMP protein
interactions: additional MIT domain-containing proteins bind to multiple
components of the human ESCRT III complex. Genomics 88: 333-346,
2006.
3. Ward, D. M.; Vaughn, M. B.; Shiflett, S. L.; White, P. L.; Pollock,
A. L.; Hill, J.; Schnegelberger, R.; Sundquist, W. I.; Kaplan, J.
: The role of LIP5 and CHMP5 in multivesicular body formation and
HIV-1 budding in mammalian cells. J. Biol. Chem. 280: 10548-10555,
2005.
*FIELD* CD
Patricia A. Hartz: 3/29/2007
*FIELD* ED
mgross: 03/30/2007
mgross: 3/29/2007