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Charged multivesicular body protein 6 (Chromatin-modifying protein 6) (Vacuolar protein sorting-associated protein 20) (Vps20) (hVps20)

 CHMP6_HUMAN             Reviewed;         201 AA.
Q96FZ7; A8K7U0; Q53FU4; Q9HAE8;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 139.
RecName: Full=Charged multivesicular body protein 6;
AltName: Full=Chromatin-modifying protein 6;
AltName: Full=Vacuolar protein sorting-associated protein 20;
Short=Vps20;
Short=hVps20;
Name=CHMP6; Synonyms=VPS20;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
PubMed=14583093; DOI=10.1042/BJ20031347;
Peck J.W., Bowden E.T., Burbelo P.D.;
"Structure and function of human Vps20 and Snf7 proteins.";
Biochem. J. 377:693-700(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Embryo, and Synovial cell;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney proximal tubule;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INTERACTION WITH VPS25; CHMP4B; VPS4A AND VPS4B.
PubMed=14505570; DOI=10.1016/S0092-8674(03)00714-1;
von Schwedler U.K., Stuchell M., Mueller B., Ward D.M., Chung H.-Y.,
Morita E., Wang H.E., Davis T., He G.P., Cimbora D.M., Scott A.,
Kraeusslich H.-G., Kaplan J., Morham S.G., Sundquist W.I.;
"The protein network of HIV budding.";
Cell 114:701-713(2003).
[7]
INTERACTION WITH CHMP4A; CHMP4B; CHMP4C; VPS25; SNF8 AND VPS36.
PubMed=14519844; DOI=10.1073/pnas.2133846100;
Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.;
"Divergent retroviral late-budding domains recruit vacuolar protein
sorting factors by using alternative adaptor proteins.";
Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003).
[8]
ERRATUM.
Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.;
Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003).
[9]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MYRISTOYLATION AT GLY-2,
INTERACTION WITH CHMP4B AND VPS25, AND MUTAGENESIS OF GLY-2 AND
ARG-49.
PubMed=15511219; DOI=10.1042/BJ20041227;
Yorikawa C., Shibata H., Waguri S., Hatta K., Horii M., Katoh K.,
Kobayashi T., Uchiyama Y., Maki M.;
"Human CHMP6, a myristoylated ESCRT-III protein, interacts directly
with an ESCRT-II component EAP20 and regulates endosomal cargo
sorting.";
Biochem. J. 387:17-26(2005).
[10]
AUTOINHIBITORY MECHANISM, INTERACTION, AND MUTAGENESIS OF
168-ILE--SER-201.
PubMed=17547705; DOI=10.1111/j.1600-0854.2007.00584.x;
Shim S., Kimpler L.A., Hanson P.I.;
"Structure/function analysis of four core ESCRT-III proteins reveals
common regulatory role for extreme C-terminal domain.";
Traffic 8:1068-1079(2007).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
ISGYLATION, AND INTERACTION WITH VPS4A.
PubMed=21543490; DOI=10.1128/JVI.02610-10;
Kuang Z., Seo E.J., Leis J.;
"Mechanism of inhibition of retrovirus release from cells by
interferon-induced gene ISG15.";
J. Virol. 85:7153-7161(2011).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-130, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25255805; DOI=10.1038/ncomms5919;
Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U.,
Wright M.H., Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
"Global profiling of co- and post-translationally N-myristoylated
proteomes in human cells.";
Nat. Commun. 5:4919-4919(2014).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[17]
STRUCTURE BY NMR OF 168-179 IN COMPLEX WITH VPS4A, AND MUTAGENESIS OF
LEU-170; VAL-173 AND LEU-178.
PubMed=18606141; DOI=10.1016/j.devcel.2008.05.014;
Kieffer C., Skalicky J.J., Morita E., De Domenico I., Ward D.M.,
Kaplan J., Sundquist W.I.;
"Two distinct modes of ESCRT-III recognition are required for VPS4
functions in lysosomal protein targeting and HIV-1 budding.";
Dev. Cell 15:62-73(2008).
-!- FUNCTION: Probable core component of the endosomal sorting
required for transport complex III (ESCRT-III) which is involved
in multivesicular bodies (MVBs) formation and sorting of endosomal
cargo proteins into MVBs. MVBs contain intraluminal vesicles
(ILVs) that are generated by invagination and scission from the
limiting membrane of the endosome and mostly are delivered to
lysosomes enabling degradation of membrane proteins, such as
stimulated growth factor receptors, lysosomal enzymes and lipids.
The MVB pathway appears to require the sequential function of
ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly
dissociate from the invaginating membrane before the ILV is
released. The ESCRT machinery also functions in topologically
equivalent membrane fission events, such as the terminal stages of
cytokinesis and the budding of enveloped viruses (HIV-1 and other
lentiviruses). ESCRT-III proteins are believed to mediate the
necessary vesicle extrusion and/or membrane fission activities,
possibly in conjunction with the AAA ATPase VPS4. In the ESCRT-III
complex, it probably serves as an acceptor for the ESCRT-II
complex on endosomal membranes.
-!- SUBUNIT: Probable core component of the endosomal sorting required
for transport complex III (ESCRT-III). ESCRT-III components are
thought to multimerize to form a flat lattice on the perimeter
membrane of the endosome. Several assembly forms of ESCRT-III may
exist that interact and act sequentally. Interacts with VPS4A; the
interaction is direct. Interacts with VPS4B; the interaction is
direct. Interacts with CHMP4A, CHMP4B and CHMP4C. Interacts with
SNF8, VPS25 and VPS36. {ECO:0000269|PubMed:14505570,
ECO:0000269|PubMed:14519844, ECO:0000269|PubMed:15511219,
ECO:0000269|PubMed:17547705, ECO:0000269|PubMed:18606141,
ECO:0000269|PubMed:21543490}.
-!- INTERACTION:
Q9BRG1:VPS25; NbExp=6; IntAct=EBI-1049648, EBI-741945;
-!- SUBCELLULAR LOCATION: Endomembrane system. Endosome membrane;
Lipid-anchor. Late endosome membrane {ECO:0000305}. Membrane
{ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Localizes to
endosomal membranes.
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:15511219}.
-!- DOMAIN: The acidic C-terminus and the basic N-termminus are
thought to render the protein in a closed, soluble and inactive
conformation through an autoinhibitory intramolecular interaction.
The open and active conformation, which enables membrane binding
and oligomerization, is achieved by interaction with other
cellular binding partners, probably including other ESCRT
components.
-!- PTM: ISGylated in a CHMP5-dependent manner. Isgylation weakens its
interaction with VPS4A. {ECO:0000269|PubMed:21543490}.
-!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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EMBL; AY329087; AAQ91196.1; -; mRNA.
EMBL; AK021811; BAB13901.1; -; mRNA.
EMBL; CR457284; CAG33565.1; -; mRNA.
EMBL; AK223187; BAD96907.1; -; mRNA.
EMBL; AK292105; BAF84794.1; -; mRNA.
EMBL; BC010108; AAH10108.1; -; mRNA.
CCDS; CCDS11774.1; -.
RefSeq; NP_078867.2; NM_024591.4.
UniGene; Hs.514560; -.
PDB; 2K3W; NMR; -; B=166-181.
PDB; 3HTU; X-ray; 2.00 A; B/D/F/H=11-48.
PDBsum; 2K3W; -.
PDBsum; 3HTU; -.
ProteinModelPortal; Q96FZ7; -.
SMR; Q96FZ7; -.
BioGrid; 122771; 14.
CORUM; Q96FZ7; -.
IntAct; Q96FZ7; 12.
MINT; MINT-5003442; -.
STRING; 9606.ENSP00000317468; -.
iPTMnet; Q96FZ7; -.
PhosphoSitePlus; Q96FZ7; -.
BioMuta; CHMP6; -.
DMDM; 73917777; -.
EPD; Q96FZ7; -.
MaxQB; Q96FZ7; -.
PaxDb; Q96FZ7; -.
PeptideAtlas; Q96FZ7; -.
PRIDE; Q96FZ7; -.
DNASU; 79643; -.
Ensembl; ENST00000325167; ENSP00000317468; ENSG00000176108.
GeneID; 79643; -.
KEGG; hsa:79643; -.
UCSC; uc002jyw.4; human.
CTD; 79643; -.
EuPathDB; HostDB:ENSG00000176108.9; -.
GeneCards; CHMP6; -.
HGNC; HGNC:25675; CHMP6.
HPA; HPA023001; -.
HPA; HPA024460; -.
MIM; 610901; gene.
neXtProt; NX_Q96FZ7; -.
OpenTargets; ENSG00000176108; -.
PharmGKB; PA142672114; -.
eggNOG; KOG2910; Eukaryota.
eggNOG; ENOG4111HN3; LUCA.
GeneTree; ENSGT00720000108863; -.
HOGENOM; HOG000208642; -.
HOVERGEN; HBG080510; -.
InParanoid; Q96FZ7; -.
KO; K12195; -.
OMA; YQKRITQ; -.
PhylomeDB; Q96FZ7; -.
TreeFam; TF105929; -.
Reactome; R-HSA-162588; Budding and maturation of HIV virion.
Reactome; R-HSA-1632852; Macroautophagy.
Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
EvolutionaryTrace; Q96FZ7; -.
GeneWiki; CHMP6; -.
GenomeRNAi; 79643; -.
PRO; PR:Q96FZ7; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000176108; -.
CleanEx; HS_CHMP6; -.
ExpressionAtlas; Q96FZ7; baseline and differential.
Genevisible; Q96FZ7; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
GO; GO:0000815; C:ESCRT III complex; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0032403; F:protein complex binding; IDA:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0000920; P:cell separation after cytokinesis; IMP:UniProtKB.
GO; GO:0016197; P:endosomal transport; TAS:Reactome.
GO; GO:1904902; P:ESCRT III complex assembly; NAS:ParkinsonsUK-UCL.
GO; GO:0016236; P:macroautophagy; TAS:ParkinsonsUK-UCL.
GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
GO; GO:0036258; P:multivesicular body assembly; TAS:ParkinsonsUK-UCL.
GO; GO:0007175; P:negative regulation of epidermal growth factor-activated receptor activity; IMP:UniProtKB.
GO; GO:0006997; P:nucleus organization; IMP:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0007034; P:vacuolar transport; IEA:InterPro.
GO; GO:0039702; P:viral budding via host ESCRT complex; IDA:UniProtKB.
GO; GO:0019058; P:viral life cycle; TAS:Reactome.
InterPro; IPR005024; Snf7_fam.
Pfam; PF03357; Snf7; 1.
1: Evidence at protein level;
3D-structure; Coiled coil; Complete proteome; Endosome; Lipoprotein;
Membrane; Myristate; Phosphoprotein; Polymorphism; Protein transport;
Reference proteome; Transport; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:25255805}.
CHAIN 2 201 Charged multivesicular body protein 6.
/FTId=PRO_0000211508.
REGION 170 181 Interaction with VPS4A.
COILED 10 145 {ECO:0000255}.
MOTIF 168 179 Type-2 MIT-interacting motif.
MOD_RES 119 119 Phosphoserine.
{ECO:0000250|UniProtKB:P0C0A3}.
MOD_RES 130 130 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:25255805,
ECO:0000305|PubMed:15511219}.
VARIANT 55 55 G -> S (in dbSNP:rs61037507).
/FTId=VAR_061807.
MUTAGEN 2 2 G->A: Abolishes myristoylation.
{ECO:0000269|PubMed:15511219}.
MUTAGEN 49 49 R->E: Does not affect the subcellular
location. {ECO:0000269|PubMed:15511219}.
MUTAGEN 168 201 Missing: Membrane association; releases
autoinhibition.
{ECO:0000269|PubMed:17547705}.
MUTAGEN 170 170 L->D: Abolishes interaction with VPS4A.
{ECO:0000269|PubMed:18606141}.
MUTAGEN 173 173 V->D: Abolishes interaction with VPS4A.
{ECO:0000269|PubMed:18606141}.
MUTAGEN 178 178 L->D: Reduces interaction with VPS4A.
{ECO:0000269|PubMed:18606141}.
CONFLICT 17 17 D -> G (in Ref. 4; BAD96907).
{ECO:0000305}.
CONFLICT 106 106 F -> L (in Ref. 2; BAB13901).
{ECO:0000305}.
HELIX 15 43 {ECO:0000244|PDB:3HTU}.
SEQUENCE 201 AA; 23485 MW; 0D490C4DE047DC02 CRC64;
MGNLFGRKKQ SRVTEQDKAI LQLKQQRDKL RQYQKRIAQQ LERERALARQ LLRDGRKERA
KLLLKKKRYQ EQLLDRTENQ ISSLEAMVQS IEFTQIEMKV MEGLQFGNEC LNKMHQVMSI
EEVERILDET QEAVEYQRQI DELLAGSFTQ EDEDAILEEL SAITQEQIEL PEVPSEPLPE
KIPENVPVKA RPRQAELVAA S


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