ID   CHMP6_HUMAN             Reviewed;         201 AA.
AC   Q96FZ7; A8K7U0; Q53FU4; Q9HAE8;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 176.
DE   RecName: Full=Charged multivesicular body protein 6;
DE   AltName: Full=Chromatin-modifying protein 6;
DE   AltName: Full=Vacuolar protein sorting-associated protein 20;
DE            Short=Vps20;
DE            Short=hVps20;
GN   Name=CHMP6; Synonyms=VPS20;
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 [MRNA], AND SUBCELLULAR LOCATION.
RX   PubMed=14583093; DOI=10.1042/bj20031347;
RA   Peck J.W., Bowden E.T., Burbelo P.D.;
RT   "Structure and function of human Vps20 and Snf7 proteins.";
RL   Biochem. J. 377:693-700(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo, and Synovial cell;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney proximal tubule;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Uterus;
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   [6]
RP   INTERACTION WITH VPS25; CHMP4B; VPS4A AND VPS4B.
RX   PubMed=14505570; DOI=10.1016/s0092-8674(03)00714-1;
RA   von Schwedler U.K., Stuchell M., Mueller B., Ward D.M., Chung H.-Y.,
RA   Morita E., Wang H.E., Davis T., He G.P., Cimbora D.M., Scott A.,
RA   Kraeusslich H.-G., Kaplan J., Morham S.G., Sundquist W.I.;
RT   "The protein network of HIV budding.";
RL   Cell 114:701-713(2003).
RN   [7]
RP   INTERACTION WITH CHMP4A; CHMP4B; CHMP4C; VPS25; SNF8 AND VPS36.
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   [8]
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   [9]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MYRISTOYLATION AT GLY-2,
RP   INTERACTION WITH CHMP4B AND VPS25, AND MUTAGENESIS OF GLY-2 AND ARG-49.
RX   PubMed=15511219; DOI=10.1042/bj20041227;
RA   Yorikawa C., Shibata H., Waguri S., Hatta K., Horii M., Katoh K.,
RA   Kobayashi T., Uchiyama Y., Maki M.;
RT   "Human CHMP6, a myristoylated ESCRT-III protein, interacts directly with an
RT   ESCRT-II component EAP20 and regulates endosomal cargo sorting.";
RL   Biochem. J. 387:17-26(2005).
RN   [10]
RP   AUTOINHIBITORY MECHANISM, INTERACTION, AND MUTAGENESIS OF 168-ILE--SER-201.
RX   PubMed=17547705; DOI=10.1111/j.1600-0854.2007.00584.x;
RA   Shim S., Kimpler L.A., Hanson P.I.;
RT   "Structure/function analysis of four core ESCRT-III proteins reveals common
RT   regulatory role for extreme C-terminal domain.";
RL   Traffic 8:1068-1079(2007).
RN   [11]
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   [12]
RP   ISGYLATION, AND INTERACTION WITH VPS4A.
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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-130, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [14]
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   [15]
RP   MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=25255805; DOI=10.1038/ncomms5919;
RA   Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA   Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT   "Global profiling of co- and post-translationally N-myristoylated proteomes
RT   in human cells.";
RL   Nat. Commun. 5:4919-4919(2014).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [17]
RP   STRUCTURE BY NMR OF 168-179 IN COMPLEX WITH VPS4A, AND MUTAGENESIS OF
RP   LEU-170; VAL-173 AND LEU-178.
RX   PubMed=18606141; DOI=10.1016/j.devcel.2008.05.014;
RA   Kieffer C., Skalicky J.J., Morita E., De Domenico I., Ward D.M., Kaplan J.,
RA   Sundquist W.I.;
RT   "Two distinct modes of ESCRT-III recognition are required for VPS4
RT   functions in lysosomal protein targeting and HIV-1 budding.";
RL   Dev. Cell 15:62-73(2008).
CC   -!- FUNCTION: Probable core component of the endosomal sorting required for
CC       transport complex III (ESCRT-III) which is involved in multivesicular
CC       bodies (MVBs) formation and sorting of endosomal cargo proteins into
CC       MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by
CC       invagination and scission from the limiting membrane of the endosome
CC       and mostly are delivered to lysosomes enabling degradation of membrane
CC       proteins, such as stimulated growth factor receptors, lysosomal enzymes
CC       and lipids. The MVB pathway appears to require the sequential function
CC       of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly
CC       dissociate from the invaginating membrane before the ILV is released.
CC       The ESCRT machinery also functions in topologically equivalent membrane
CC       fission events, such as the terminal stages of cytokinesis and the
CC       budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III
CC       proteins are believed to mediate the necessary vesicle extrusion and/or
CC       membrane fission activities, possibly in conjunction with the AAA
CC       ATPase VPS4. In the ESCRT-III complex, it probably serves as an
CC       acceptor for the ESCRT-II complex on endosomal membranes.
CC   -!- SUBUNIT: Probable core component of the endosomal sorting required for
CC       transport complex III (ESCRT-III). ESCRT-III components are thought to
CC       multimerize to form a flat lattice on the perimeter membrane of the
CC       endosome. Several assembly forms of ESCRT-III may exist that interact
CC       and act sequentially. Interacts with VPS4A; the interaction is direct.
CC       Interacts with VPS4B; the interaction is direct. Interacts with CHMP4A,
CC       CHMP4B and CHMP4C. Interacts with SNF8, VPS25 and VPS36.
CC       {ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:14519844,
CC       ECO:0000269|PubMed:15511219, ECO:0000269|PubMed:17547705,
CC       ECO:0000269|PubMed:18606141, ECO:0000269|PubMed:21543490}.
CC   -!- INTERACTION:
CC       Q96FZ7; P50570-2: DNM2; NbExp=3; IntAct=EBI-1049648, EBI-10968534;
CC       Q96FZ7; Q16637: SMN2; NbExp=3; IntAct=EBI-1049648, EBI-395421;
CC       Q96FZ7; O14656-2: TOR1A; NbExp=3; IntAct=EBI-1049648, EBI-25847109;
CC       Q96FZ7; Q9BRG1: VPS25; NbExp=7; IntAct=EBI-1049648, EBI-741945;
CC   -!- SUBCELLULAR LOCATION: Endomembrane system. Endosome membrane; Lipid-
CC       anchor. Late endosome membrane {ECO:0000305}. Membrane {ECO:0000305};
CC       Lipid-anchor {ECO:0000305}. Note=Localizes to endosomal membranes.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC       {ECO:0000269|PubMed:15511219}.
CC   -!- DOMAIN: The acidic C-terminus and the basic N-termminus are thought to
CC       render the protein in a closed, soluble and inactive conformation
CC       through an autoinhibitory intramolecular interaction. The open and
CC       active conformation, which enables membrane binding and
CC       oligomerization, is achieved by interaction with other cellular binding
CC       partners, probably including other ESCRT components.
CC   -!- PTM: ISGylated in a CHMP5-dependent manner. Isgylation weakens its
CC       interaction with VPS4A. {ECO:0000269|PubMed:21543490}.
CC   -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR   EMBL; AY329087; AAQ91196.1; -; mRNA.
DR   EMBL; AK021811; BAB13901.1; -; mRNA.
DR   EMBL; CR457284; CAG33565.1; -; mRNA.
DR   EMBL; AK223187; BAD96907.1; -; mRNA.
DR   EMBL; AK292105; BAF84794.1; -; mRNA.
DR   EMBL; BC010108; AAH10108.1; -; mRNA.
DR   CCDS; CCDS11774.1; -.
DR   RefSeq; NP_078867.2; NM_024591.4.
DR   PDB; 2K3W; NMR; -; B=166-181.
DR   PDB; 3HTU; X-ray; 2.00 A; B/D/F/H=11-48.
DR   PDBsum; 2K3W; -.
DR   PDBsum; 3HTU; -.
DR   AlphaFoldDB; Q96FZ7; -.
DR   SMR; Q96FZ7; -.
DR   BioGRID; 122771; 60.
DR   ComplexPortal; CPX-329; ESCRT-III complex.
DR   CORUM; Q96FZ7; -.
DR   IntAct; Q96FZ7; 24.
DR   MINT; Q96FZ7; -.
DR   STRING; 9606.ENSP00000317468; -.
DR   iPTMnet; Q96FZ7; -.
DR   MetOSite; Q96FZ7; -.
DR   PhosphoSitePlus; Q96FZ7; -.
DR   BioMuta; CHMP6; -.
DR   DMDM; 73917777; -.
DR   EPD; Q96FZ7; -.
DR   jPOST; Q96FZ7; -.
DR   MassIVE; Q96FZ7; -.
DR   MaxQB; Q96FZ7; -.
DR   PaxDb; 9606-ENSP00000317468; -.
DR   PeptideAtlas; Q96FZ7; -.
DR   ProteomicsDB; 76576; -.
DR   Pumba; Q96FZ7; -.
DR   Antibodypedia; 19789; 184 antibodies from 24 providers.
DR   DNASU; 79643; -.
DR   Ensembl; ENST00000325167.9; ENSP00000317468.5; ENSG00000176108.9.
DR   GeneID; 79643; -.
DR   KEGG; hsa:79643; -.
DR   MANE-Select; ENST00000325167.9; ENSP00000317468.5; NM_024591.5; NP_078867.2.
DR   UCSC; uc002jyw.4; human.
DR   AGR; HGNC:25675; -.
DR   CTD; 79643; -.
DR   DisGeNET; 79643; -.
DR   GeneCards; CHMP6; -.
DR   HGNC; HGNC:25675; CHMP6.
DR   HPA; ENSG00000176108; Low tissue specificity.
DR   MIM; 610901; gene.
DR   neXtProt; NX_Q96FZ7; -.
DR   OpenTargets; ENSG00000176108; -.
DR   PharmGKB; PA142672114; -.
DR   VEuPathDB; HostDB:ENSG00000176108; -.
DR   eggNOG; KOG2910; Eukaryota.
DR   GeneTree; ENSGT00720000108863; -.
DR   HOGENOM; CLU_086201_3_0_1; -.
DR   InParanoid; Q96FZ7; -.
DR   OMA; QMLAGHL; -.
DR   OrthoDB; 5398551at2759; -.
DR   PhylomeDB; Q96FZ7; -.
DR   TreeFam; TF105929; -.
DR   PathwayCommons; Q96FZ7; -.
DR   Reactome; R-HSA-162588; Budding and maturation of HIV virion.
DR   Reactome; R-HSA-1632852; Macroautophagy.
DR   Reactome; R-HSA-5620971; Pyroptosis.
DR   Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR   Reactome; R-HSA-9610379; HCMV Late Events.
DR   Reactome; R-HSA-9615710; Late endosomal microautophagy.
DR   Reactome; R-HSA-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR   Reactome; R-HSA-9679504; Translation of Replicase and Assembly of the Replication Transcription Complex.
DR   Reactome; R-HSA-9694676; Translation of Replicase and Assembly of the Replication Transcription Complex.
DR   SignaLink; Q96FZ7; -.
DR   SIGNOR; Q96FZ7; -.
DR   BioGRID-ORCS; 79643; 803 hits in 1169 CRISPR screens.
DR   EvolutionaryTrace; Q96FZ7; -.
DR   GeneWiki; CHMP6; -.
DR   GenomeRNAi; 79643; -.
DR   Pharos; Q96FZ7; Tbio.
DR   PRO; PR:Q96FZ7; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q96FZ7; Protein.
DR   Bgee; ENSG00000176108; Expressed in apex of heart and 176 other cell types or tissues.
DR   ExpressionAtlas; Q96FZ7; baseline and differential.
DR   GO; GO:1904930; C:amphisome membrane; IDA:ComplexPortal.
DR   GO; GO:0000421; C:autophagosome membrane; IDA:ComplexPortal.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR   GO; GO:0000815; C:ESCRT III complex; 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:0016020; C:membrane; HDA:UniProtKB.
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:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR   GO; GO:0097352; P:autophagosome maturation; IMP:ComplexPortal.
DR   GO; GO:0006914; P:autophagy; IMP:ComplexPortal.
DR   GO; GO:1904902; P:ESCRT III complex assembly; 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:0016236; P:macroautophagy; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0090148; P:membrane fission; NAS:ComplexPortal.
DR   GO; GO:0061952; P:midbody abscission; IMP:UniProtKB.
DR   GO; GO:0007080; P:mitotic metaphase chromosome alignment; IMP:UniProtKB.
DR   GO; GO:0036258; P:multivesicular body assembly; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0071985; P:multivesicular body sorting pathway; IDA:ComplexPortal.
DR   GO; GO:0061763; P:multivesicular body-lysosome fusion; NAS:ComplexPortal.
DR   GO; GO:0007175; P:negative regulation of epidermal growth factor-activated receptor activity; IMP:UniProtKB.
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:1901673; P:regulation of mitotic spindle assembly; IMP:ComplexPortal.
DR   GO; GO:0042176; P:regulation of protein catabolic process; IMP:UniProtKB.
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; NAS:ComplexPortal.
DR   GO; GO:0046761; P:viral budding from plasma membrane; IDA:ComplexPortal.
DR   GO; GO:0039702; P:viral budding via host ESCRT complex; IDA:UniProtKB.
DR   Gene3D; 1.10.287.1060; ESAT-6-like; 1.
DR   InterPro; IPR005024; Snf7_fam.
DR   PANTHER; PTHR22761; CHARGED MULTIVESICULAR BODY PROTEIN; 1.
DR   PANTHER; PTHR22761:SF5; CHARGED MULTIVESICULAR BODY PROTEIN 6; 1.
DR   Pfam; PF03357; Snf7; 1.
DR   Genevisible; Q96FZ7; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Endosome; Lipoprotein; Membrane; Myristate;
KW   Phosphoprotein; Protein transport; Reference proteome; Transport;
KW   Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:25255805"
FT   CHAIN           2..201
FT                   /note="Charged multivesicular body protein 6"
FT                   /id="PRO_0000211508"
FT   REGION          170..181
FT                   /note="Interaction with VPS4A"
FT   COILED          10..145
FT                   /evidence="ECO:0000255"
FT   MOTIF           168..179
FT                   /note="Type-2 MIT-interacting motif"
FT   MOD_RES         119
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0A3"
FT   MOD_RES         130
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000269|PubMed:25255805,
FT                   ECO:0000305|PubMed:15511219"
FT   VARIANT         55
FT                   /note="G -> S (in dbSNP:rs61037507)"
FT                   /id="VAR_061807"
FT   MUTAGEN         2
FT                   /note="G->A: Abolishes myristoylation."
FT                   /evidence="ECO:0000269|PubMed:15511219"
FT   MUTAGEN         49
FT                   /note="R->E: Does not affect the subcellular location."
FT                   /evidence="ECO:0000269|PubMed:15511219"
FT   MUTAGEN         168..201
FT                   /note="Missing: Membrane association; releases
FT                   autoinhibition."
FT                   /evidence="ECO:0000269|PubMed:17547705"
FT   MUTAGEN         170
FT                   /note="L->D: Abolishes interaction with VPS4A."
FT                   /evidence="ECO:0000269|PubMed:18606141"
FT   MUTAGEN         173
FT                   /note="V->D: Abolishes interaction with VPS4A."
FT                   /evidence="ECO:0000269|PubMed:18606141"
FT   MUTAGEN         178
FT                   /note="L->D: Reduces interaction with VPS4A."
FT                   /evidence="ECO:0000269|PubMed:18606141"
FT   CONFLICT        17
FT                   /note="D -> G (in Ref. 4; BAD96907)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        106
FT                   /note="F -> L (in Ref. 2; BAB13901)"
FT                   /evidence="ECO:0000305"
FT   HELIX           15..43
FT                   /evidence="ECO:0007829|PDB:3HTU"
SQ   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
//