CHMP5_HUMAN
ID CHMP5_HUMAN Reviewed; 219 AA.
AC Q9NZZ3; B2RD95; B4DIR6; Q5VXW2; Q96AV2; Q9HB68; Q9NYS4; Q9Y323;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 175.
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 {ECO:0000303|PubMed:10810093}, HSPC177, PNAS-114, PNAS-2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., 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., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., 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., Rogers J.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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., Yan W.,
RA 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 sorting
RT factors by using alternative adaptor proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003).
RN [9]
RP ERRATUM OF PUBMED:14519844.
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., Hill J.,
RA 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., Rodesch C.K.,
RA Sundquist W.I.;
RT "Human ESCRT and ALIX proteins interact with proteins of the midbody and
RT function in cytokinesis.";
RL EMBO J. 26:4215-4227(2007).
RN [12]
RP INTERACTION WITH VTA1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17261583; DOI=10.1074/jbc.m611635200;
RA Ma Y.M., Boucrot E., Villen J., Affar el B., Gygi S.P., Goettlinger H.G.,
RA Kirchhausen T.;
RT "Targeting of AMSH to endosomes is required for epidermal growth factor
RT 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 IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT 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., Buerckstuemmer T.,
RA 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 interferon-
RT induced gene ISG15.";
RL J. Virol. 85:7153-7161(2011).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP INTERACTION WITH NOD2, AND INDUCTION.
RX PubMed=27812135; DOI=10.1371/journal.pone.0165420;
RA Thiebaut R., Esmiol S., Lecine P., Mahfouz B., Hermant A., Nicoletti C.,
RA Parnis S., Perroy J., Borg J.P., Pascoe L., Hugot J.P., Ollendorff V.;
RT "Characterization and Genetic Analyses of New Genes Coding for NOD2
RT Interacting Proteins.";
RL PLoS ONE 11:E0165420-E0165420(2016).
RN [19]
RP STEAROYLATION AT LYS-7 (MICROBIAL INFECTION), AND MUTAGENESIS OF
RP 7-LYS--LYS-11 AND LYS-7.
RX PubMed=30061757; DOI=10.1038/s41564-018-0215-6;
RA Liu W., Zhou Y., Peng T., Zhou P., Ding X., Li Z., Zhong H., Xu Y.,
RA Chen S., Hang H.C., Shao F.;
RT "Nepsilon-fatty acylation of multiple membrane-associated proteins by
RT Shigella IcsB effector to modulate host function.";
RL Nat. Microbiol. 3:996-1009(2018).
CC -!- FUNCTION: Probable peripherally associated component of the endosomal
CC sorting required for transport complex III (ESCRT-III) which is
CC involved in multivesicular bodies (MVBs) formation and sorting of
CC endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles
CC (ILVs) that are generated by invagination and scission from the
CC limiting membrane of the endosome and mostly are delivered to lysosomes
CC enabling degradation of membrane proteins, such as stimulated growth
CC factor receptors, lysosomal enzymes and lipids. The MVB pathway appears
CC to require the sequential function of ESCRT-O, -I,-II and -III
CC complexes. ESCRT-III proteins mostly dissociate from the invaginating
CC membrane before the ILV is released. The ESCRT machinery also functions
CC in topologically equivalent membrane fission events, such as the
CC terminal stages of cytokinesis and the budding of enveloped viruses
CC (HIV-1 and other lentiviruses) (PubMed:14519844). ESCRT-III proteins
CC are believed to mediate the necessary vesicle extrusion and/or membrane
CC fission activities, possibly in conjunction with the AAA ATPase VPS4.
CC Involved in HIV-1 p6- and p9-dependent virus release (PubMed:14519844).
CC {ECO:0000269|PubMed:14519844}.
CC -!- SUBUNIT: Probable peripherally associated component of the endosomal
CC sorting required for transport complex III (ESCRT-III). ESCRT-III
CC components are thought to multimerize to form a flat lattice on the
CC perimeter membrane of the endosome. Several assembly forms of ESCRT-III
CC may exist that interact and act sequentially. Interacts with VTA1; the
CC interaction involves soluble CHMP5 (PubMed:15644320, PubMed:17261583,
CC PubMed:21543490). Interacts with CHMP2A (PubMed:14519844). Interacts
CC with NOD2 (PubMed:27812135). {ECO:0000269|PubMed:14519844,
CC ECO:0000269|PubMed:15644320, ECO:0000269|PubMed:17261583,
CC ECO:0000269|PubMed:21543490, ECO:0000269|PubMed:27812135}.
CC -!- INTERACTION:
CC Q9NZZ3; Q9H444: CHMP4B; NbExp=4; IntAct=EBI-751303, EBI-749627;
CC Q9NZZ3; Q8WV92: MITD1; NbExp=3; IntAct=EBI-751303, EBI-2691489;
CC Q9NZZ3; O95630: STAMBP; NbExp=2; IntAct=EBI-751303, EBI-396676;
CC Q9NZZ3; O75351: VPS4B; NbExp=6; IntAct=EBI-751303, EBI-2514459;
CC Q9NZZ3; Q9NP79: VTA1; NbExp=3; IntAct=EBI-751303, EBI-740160;
CC Q9NZZ3-1; Q5VW32: BROX; NbExp=6; IntAct=EBI-15979532, EBI-6286053;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15644320}.
CC Endosome membrane {ECO:0000305}; Peripheral membrane protein
CC {ECO:0000305}. Midbody {ECO:0000269|PubMed:17853893}. Note=Localizes to
CC the midbody of dividing cells (PubMed:17853893). Localized in two
CC distinct rings on either side of the Flemming body (PubMed:17853893).
CC {ECO:0000269|PubMed:17853893}.
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 -!- INDUCTION: Up-regulated by muramyl-dipeptide and lipopolysaccharide.
CC {ECO:0000269|PubMed:27812135}.
CC -!- PTM: (Microbial infection) Stearoylated By S.flexneri N-epsilon-fatty
CC acyltransferase IcsB, promoting S.flexneri evasion of autophagy.
CC {ECO:0000269|PubMed:30061757}.
CC -!- PTM: ISGylated. Isgylation inhibits its interaction with VTA1.
CC {ECO:0000269|PubMed:21543490}.
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG23821.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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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; -; NOT_ANNOTATED_CDS; 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 CCDS; CCDS56569.1; -. [Q9NZZ3-2]
DR CCDS; CCDS6537.1; -. [Q9NZZ3-1]
DR RefSeq; NP_001182465.1; NM_001195536.1. [Q9NZZ3-2]
DR RefSeq; NP_057494.3; NM_016410.5. [Q9NZZ3-1]
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 PDB; 4TXR; X-ray; 1.00 A; C=139-195.
DR PDBsum; 2LXM; -.
DR PDBsum; 3ULY; -.
DR PDBsum; 3UM0; -.
DR PDBsum; 3UM1; -.
DR PDBsum; 3UM2; -.
DR PDBsum; 4TXR; -.
DR AlphaFoldDB; Q9NZZ3; -.
DR BMRB; Q9NZZ3; -.
DR SMR; Q9NZZ3; -.
DR BioGRID; 119579; 64.
DR ComplexPortal; CPX-329; ESCRT-III complex.
DR CORUM; Q9NZZ3; -.
DR DIP; DIP-50420N; -.
DR IntAct; Q9NZZ3; 50.
DR MINT; Q9NZZ3; -.
DR STRING; 9606.ENSP00000223500; -.
DR GlyGen; Q9NZZ3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NZZ3; -.
DR MetOSite; Q9NZZ3; -.
DR PhosphoSitePlus; Q9NZZ3; -.
DR BioMuta; CHMP5; -.
DR DMDM; 51702157; -.
DR EPD; Q9NZZ3; -.
DR jPOST; Q9NZZ3; -.
DR MassIVE; Q9NZZ3; -.
DR MaxQB; Q9NZZ3; -.
DR PaxDb; Q9NZZ3; -.
DR PeptideAtlas; Q9NZZ3; -.
DR PRIDE; Q9NZZ3; -.
DR ProteomicsDB; 83526; -. [Q9NZZ3-1]
DR ProteomicsDB; 83527; -. [Q9NZZ3-2]
DR TopDownProteomics; Q9NZZ3-1; -. [Q9NZZ3-1]
DR Antibodypedia; 25186; 242 antibodies from 29 providers.
DR DNASU; 51510; -.
DR Ensembl; ENST00000223500.9; ENSP00000223500.7; ENSG00000086065.14. [Q9NZZ3-1]
DR Ensembl; ENST00000419016.6; ENSP00000442725.1; ENSG00000086065.14. [Q9NZZ3-2]
DR GeneID; 51510; -.
DR KEGG; hsa:51510; -.
DR MANE-Select; ENST00000223500.9; ENSP00000223500.7; NM_016410.6; NP_057494.3.
DR UCSC; uc003zsm.5; human. [Q9NZZ3-1]
DR CTD; 51510; -.
DR DisGeNET; 51510; -.
DR GeneCards; CHMP5; -.
DR HGNC; HGNC:26942; CHMP5.
DR HPA; ENSG00000086065; Low tissue specificity.
DR MIM; 610900; gene.
DR neXtProt; NX_Q9NZZ3; -.
DR OpenTargets; ENSG00000086065; -.
DR PharmGKB; PA134903143; -.
DR VEuPathDB; HostDB:ENSG00000086065; -.
DR eggNOG; KOG1655; Eukaryota.
DR GeneTree; ENSGT00550000074817; -.
DR HOGENOM; CLU_079409_0_0_1; -.
DR InParanoid; Q9NZZ3; -.
DR OMA; MEQAQTM; -.
DR OrthoDB; 1301560at2759; -.
DR PhylomeDB; Q9NZZ3; -.
DR TreeFam; TF300122; -.
DR PathwayCommons; Q9NZZ3; -.
DR Reactome; R-HSA-162588; Budding and maturation of HIV virion.
DR Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR SignaLink; Q9NZZ3; -.
DR SIGNOR; Q9NZZ3; -.
DR BioGRID-ORCS; 51510; 456 hits in 1050 CRISPR screens.
DR ChiTaRS; CHMP5; human.
DR GeneWiki; CHMP5; -.
DR GenomeRNAi; 51510; -.
DR Pharos; Q9NZZ3; Tbio.
DR PRO; PR:Q9NZZ3; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9NZZ3; protein.
DR Bgee; ENSG00000086065; Expressed in germinal epithelium of ovary and 208 other tissues.
DR Genevisible; Q9NZZ3; HS.
DR GO; GO:1904930; C:amphisome membrane; IDA:ComplexPortal.
DR GO; GO:0000421; C:autophagosome membrane; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IDA:ComplexPortal.
DR GO; GO:0005828; C:kinetochore microtubule; IDA:ComplexPortal.
DR GO; GO:0005765; C:lysosomal membrane; IDA:ComplexPortal.
DR GO; GO:0030496; C:midbody; IDA:ComplexPortal.
DR GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR GO; GO:0032585; C:multivesicular body membrane; IDA:ComplexPortal.
DR GO; GO:0005643; C:nuclear pore; IDA:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0097352; P:autophagosome maturation; IMP:ComplexPortal.
DR GO; GO:0006914; P:autophagy; IMP:ComplexPortal.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:UniProtKB.
DR GO; GO:0071225; P:cellular response to muramyl dipeptide; IMP:UniProtKB.
DR GO; GO:1904903; P:ESCRT III complex disassembly; NAS:ParkinsonsUK-UCL.
DR GO; GO:1902774; P:late endosome to lysosome transport; IMP:ComplexPortal.
DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:0090148; P:membrane fission; IC:ComplexPortal.
DR GO; GO:0061952; P:midbody abscission; IMP:UniProtKB.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
DR GO; GO:0036258; P:multivesicular body assembly; NAS:ParkinsonsUK-UCL.
DR GO; GO:0071985; P:multivesicular body sorting pathway; IDA:ComplexPortal.
DR GO; GO:0061763; P:multivesicular body-lysosome fusion; IC:ComplexPortal.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:ComplexPortal.
DR GO; GO:0031468; P:nuclear membrane reassembly; IMP:ComplexPortal.
DR GO; GO:0006997; P:nucleus organization; IMP:UniProtKB.
DR GO; GO:0001778; P:plasma membrane repair; IDA:ComplexPortal.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0010824; P:regulation of centrosome duplication; IMP:UniProtKB.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IMP:UniProtKB.
DR GO; GO:0001919; P:regulation of receptor recycling; IEA:Ensembl.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IDA:ComplexPortal.
DR GO; GO:0006900; P:vesicle budding from membrane; IBA:GO_Central.
DR GO; GO:0051469; P:vesicle fusion with vacuole; IC:ComplexPortal.
DR GO; GO:0046755; P:viral budding; IMP:UniProtKB.
DR GO; GO:0046761; P:viral budding from plasma membrane; IDA:ComplexPortal.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IDA:ComplexPortal.
DR InterPro; IPR005024; Snf7_fam.
DR PANTHER; PTHR22761; PTHR22761; 1.
DR Pfam; PF03357; Snf7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Endosome;
KW Lipoprotein; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..219
FT /note="Charged multivesicular body protein 5"
FT /id="PRO_0000211500"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..158
FT /note="Interaction with VTA1"
FT REGION 188..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 26..179
FT /evidence="ECO:0000255"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT LIPID 7
FT /note="(Microbial infection) N6-stearoyl lysine"
FT /evidence="ECO:0000269|PubMed:30061757"
FT VAR_SEQ 166..219
FT /note="ELDALGDELLADEDSSYLDEAASAPAIPEGVPTDTKNKDGVLVDEFGLPQIP
FT AS -> GWSSGG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042556"
FT MUTAGEN 7..11
FT /note="KAKPK->RARPR: Decreased stearoylation in response to
FT S.flexneri infection."
FT /evidence="ECO:0000269|PubMed:30061757"
FT MUTAGEN 7
FT /note="K->R: Decreased stearoylation in response to
FT S.flexneri infection."
FT /evidence="ECO:0000269|PubMed:30061757"
FT CONFLICT 14
FT /note="P -> R (in Ref. 1; AAD27743)"
FT /evidence="ECO:0000305"
FT CONFLICT 19
FT /note="D -> G (in Ref. 6; AAH16698)"
FT /evidence="ECO:0000305"
FT CONFLICT 84..93
FT /note="QQSFNMEQAN -> NSHSTWTGH (in Ref. 1; AAD27743)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="Q -> P (in Ref. 1; AAD27743)"
FT /evidence="ECO:0000305"
FT HELIX 160..175
FT /evidence="ECO:0007829|PDB:4TXR"
FT HELIX 182..188
FT /evidence="ECO:0007829|PDB:4TXR"
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
