ID CHMP7_HUMAN Reviewed; 453 AA. AC Q8WUX9; B2RDT3; B4DKJ6; D3DSS1; Q8NDM1; Q9BT50; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 28-JAN-2026, entry version 175. DE RecName: Full=Charged multivesicular body protein 7; DE AltName: Full=Chromatin-modifying protein 7; GN Name=CHMP7; 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] (ISOFORMS 1 AND 2). RC TISSUE=Testis; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., RA Platzer M., Shimizu N., Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lymph, and Ovary; 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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CHMP4B. RX PubMed=16856878; DOI=10.1042/bj20060897; RA Horii M., Shibata H., Kobayashi R., Katoh K., Yorikawa C., Yasuda J., RA Maki M.; RT "CHMP7, a novel ESCRT-III-related protein, associates with CHMP4b and RT functions in the endosomal sorting pathway."; RL Biochem. J. 400:23-32(2006). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [8] 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417, 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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-408; SER-410; SER-417; RP SER-431 AND SER-441, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; 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 FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=26040712; DOI=10.1038/nature14408; RA Vietri M., Schink K.O., Campsteijn C., Wegner C.S., Schultz S.W., RA Christ L., Thoresen S.B., Brech A., Raiborg C., Stenmark H.; RT "Spastin and ESCRT-III coordinate mitotic spindle disassembly and nuclear RT envelope sealing."; RL Nature 522:231-235(2015). RN [15] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH LEMD2. RX PubMed=28242692; DOI=10.1073/pnas.1613916114; RA Gu M., LaJoie D., Chen O.S., von Appen A., Ladinsky M.S., Redd M.J., RA Nikolova L., Bjorkman P.J., Sundquist W.I., Ullman K.S., Frost A.; RT "LEM2 recruits CHMP7 for ESCRT-mediated nuclear envelope closure in fission RT yeast and human cells."; RL Proc. Natl. Acad. Sci. U.S.A. 114:E2166-E2175(2017). CC -!- FUNCTION: ESCRT-III-like protein required to recruit the ESCRT-III CC complex to the nuclear envelope (NE) during late anaphase CC (PubMed:26040712). Together with SPAST, the ESCRT-III complex promotes CC NE sealing and mitotic spindle disassembly during late anaphase CC (PubMed:26040712, PubMed:28242692). Recruited to the reforming NE CC during anaphase by LEMD2 (PubMed:28242692). Plays a role in the CC endosomal sorting pathway (PubMed:16856878). CC {ECO:0000269|PubMed:16856878, ECO:0000269|PubMed:26040712, CC ECO:0000269|PubMed:28242692}. CC -!- SUBUNIT: Interacts with CHMP4B, but not with VPS25 (PubMed:16856878). CC Interacts with LEMD2 (via C-terminus) (PubMed:28242692). CC {ECO:0000269|PubMed:16856878, ECO:0000269|PubMed:28242692}. CC -!- INTERACTION: CC Q8WUX9; P55212: CASP6; NbExp=3; IntAct=EBI-749253, EBI-718729; CC Q8WUX9; P06307: CCK; NbExp=3; IntAct=EBI-749253, EBI-6624398; CC Q8WUX9; P28329-3: CHAT; NbExp=3; IntAct=EBI-749253, EBI-25837549; CC Q8WUX9; Q9H444: CHMP4B; NbExp=3; IntAct=EBI-749253, EBI-749627; CC Q8WUX9; G5E9A7: DMWD; NbExp=3; IntAct=EBI-749253, EBI-10976677; CC Q8WUX9; O14645: DNALI1; NbExp=3; IntAct=EBI-749253, EBI-395638; CC Q8WUX9; P22607: FGFR3; NbExp=3; IntAct=EBI-749253, EBI-348399; CC Q8WUX9; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-749253, EBI-10226858; CC Q8WUX9; Q14957: GRIN2C; NbExp=3; IntAct=EBI-749253, EBI-8285963; CC Q8WUX9; P06396: GSN; NbExp=3; IntAct=EBI-749253, EBI-351506; CC Q8WUX9; P01112: HRAS; NbExp=4; IntAct=EBI-749253, EBI-350145; CC Q8WUX9; P54652: HSPA2; NbExp=3; IntAct=EBI-749253, EBI-356991; CC Q8WUX9; O14901: KLF11; NbExp=3; IntAct=EBI-749253, EBI-948266; CC Q8WUX9; P13473-2: LAMP2; NbExp=3; IntAct=EBI-749253, EBI-21591415; CC Q8WUX9; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-749253, EBI-2811583; CC Q8WUX9; A0A6Q8PF08: PMP22; NbExp=3; IntAct=EBI-749253, EBI-50433196; CC Q8WUX9; P62826: RAN; NbExp=3; IntAct=EBI-749253, EBI-286642; CC Q8WUX9; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-749253, EBI-5235340; CC Q8WUX9; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-749253, EBI-741480; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16856878}. Nucleus CC envelope {ECO:0000269|PubMed:26040712}. Nucleus envelope CC {ECO:0000269|PubMed:28242692}. Note=Diffused localization, with some CC punctate distribution, especially in the perinuclear area CC (PubMed:16856878). Localizes to the reforming nuclear envelope on CC chromatin disks during late anaphase (PubMed:26040712, CC PubMed:28242692). {ECO:0000269|PubMed:16856878, CC ECO:0000269|PubMed:26040712, ECO:0000269|PubMed:28242692}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8WUX9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8WUX9-2; Sequence=VSP_056945, VSP_056946; CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK296592; BAG59208.1; -; mRNA. DR EMBL; AK315664; BAG38030.1; -; mRNA. DR EMBL; AL833843; CAD38703.2; -; mRNA. DR EMBL; AC100861; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471080; EAW63632.1; -; Genomic_DNA. DR EMBL; CH471080; EAW63634.1; -; Genomic_DNA. DR EMBL; BC004344; AAH04344.1; -; mRNA. DR EMBL; BC019110; AAH19110.1; -; mRNA. DR EMBL; BC042050; AAH42050.1; -; mRNA. DR CCDS; CCDS6040.1; -. [Q8WUX9-1] DR RefSeq; NP_689485.1; NM_152272.5. [Q8WUX9-1] DR AlphaFoldDB; Q8WUX9; -. DR SMR; Q8WUX9; -. DR BioGRID; 124879; 90. DR ComplexPortal; CPX-329; ESCRT-III complex. DR FunCoup; Q8WUX9; 2592. DR IntAct; Q8WUX9; 32. DR MINT; Q8WUX9; -. DR STRING; 9606.ENSP00000380794; -. DR GlyGen; Q8WUX9; 1 site, 1 N-linked glycan (1 site). DR iPTMnet; Q8WUX9; -. DR MetOSite; Q8WUX9; -. DR PhosphoSitePlus; Q8WUX9; -. DR BioMuta; CHMP7; -. DR DMDM; 73917782; -. DR jPOST; Q8WUX9; -. DR MassIVE; Q8WUX9; -. DR PaxDb; 9606-ENSP00000380794; -. DR PeptideAtlas; Q8WUX9; -. DR ProteomicsDB; 4465; -. DR ProteomicsDB; 74719; -. [Q8WUX9-1] DR Pumba; Q8WUX9; -. DR Antibodypedia; 22730; 75 antibodies from 18 providers. DR DNASU; 91782; -. DR Ensembl; ENST00000313219.8; ENSP00000324491.7; ENSG00000147457.15. [Q8WUX9-1] DR Ensembl; ENST00000397677.6; ENSP00000380794.1; ENSG00000147457.15. [Q8WUX9-1] DR Ensembl; ENST00000519503.5; ENSP00000427948.1; ENSG00000147457.15. [Q8WUX9-2] DR GeneID; 91782; -. DR KEGG; hsa:91782; -. DR MANE-Select; ENST00000397677.6; ENSP00000380794.1; NM_152272.5; NP_689485.1. DR UCSC; uc003xdc.3; human. [Q8WUX9-1] DR AGR; HGNC:28439; -. DR ClinPGx; PA142672115; -. DR CTD; 91782; -. DR DisGeNET; 91782; -. DR GeneCards; CHMP7; -. DR HGNC; HGNC:28439; CHMP7. DR HPA; ENSG00000147457; Tissue enhanced (lymphoid). DR MIM; 611130; gene. DR OpenTargets; ENSG00000147457; -. DR VEuPathDB; HostDB:ENSG00000147457; -. DR eggNOG; KOG2911; Eukaryota. DR GeneTree; ENSGT00720000108860; -. DR HOGENOM; CLU_044768_0_0_1; -. DR InParanoid; Q8WUX9; -. DR OMA; LQLQFMR; -. DR OrthoDB; 10250120at2759; -. DR PAN-GO; Q8WUX9; 3 GO annotations based on evolutionary models. DR PhylomeDB; Q8WUX9; -. DR PathwayCommons; Q8WUX9; -. 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; Q8WUX9; -. DR SIGNOR; Q8WUX9; -. DR Agora; ENSG00000147457; -. DR BioGRID-ORCS; 91782; 560 hits in 1169 CRISPR screens. DR CD-CODE; 38BEFE36; Synthetic Condensate 000277. DR ChiTaRS; CHMP7; human. DR GenomeRNAi; 91782; -. DR Pharos; Q8WUX9; Tbio. DR PRO; PR:Q8WUX9; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q8WUX9; protein. DR Bgee; ENSG00000147457; Expressed in lymph node and 205 other cell types or tissues. DR ExpressionAtlas; Q8WUX9; baseline and differential. DR GO; GO:1904930; C:amphisome membrane; IDA:ComplexPortal. DR GO; GO:0000421; C:autophagosome membrane; IDA:ComplexPortal. DR GO; GO:0000785; C:chromatin; IDA:ARUK-UCL. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0000815; C:ESCRT III complex; IDA: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:0005635; C:nuclear envelope; IDA:UniProtKB. DR GO; GO:0005643; C:nuclear pore; IDA:ComplexPortal. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal. DR GO; GO:0097352; P:autophagosome maturation; IMP:ComplexPortal. DR GO; GO:0006914; P:autophagy; IMP:ComplexPortal. DR GO; GO:1904903; P:ESCRT III complex disassembly; NAS:ParkinsonsUK-UCL. DR GO; GO:0010458; P:exit from mitosis; IMP:UniProtKB. DR GO; GO:1902774; P:late endosome to lysosome transport; IMP:ComplexPortal. DR GO; GO:0045324; P:late endosome to vacuole transport; IMP:UniProtKB. 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; 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; NAS: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:0031468; P:nuclear membrane reassembly; IMP:UniProtKB. DR GO; GO:0006997; P:nucleus organization; IMP:UniProtKB. DR GO; GO:0001778; P:plasma membrane repair; IDA:ComplexPortal. DR GO; GO:0071168; P:protein localization to chromatin; IMP:ARUK-UCL. 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: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:ComplexPortal. DR FunFam; 1.10.287.1060:FF:000007; Charged multivesicular body protein 7; 1. DR Gene3D; 6.10.250.1710; -; 1. DR Gene3D; 1.10.287.1060; ESAT-6-like; 1. DR InterPro; IPR057471; CHMP7_WHD. DR InterPro; IPR005024; Snf7_fam. DR PANTHER; PTHR22761; CHARGED MULTIVESICULAR BODY PROTEIN; 1. DR PANTHER; PTHR22761:SF21; CHARGED MULTIVESICULAR BODY PROTEIN 7; 1. DR Pfam; PF03357; Snf7; 1. DR Pfam; PF25239; WHD_CHMP7; 1. DR Pfam; PF25880; WHD_CHMP7_1st; 1. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Cytoplasm; Nucleus; Phosphoprotein; KW Protein transport; Proteomics identification; Reference proteome; KW Transport. FT CHAIN 1..453 FT /note="Charged multivesicular body protein 7" FT /id="PRO_0000211516" FT REGION 1..22 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 392..417 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 431..453 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 243..312 FT /evidence="ECO:0000255" FT COMPBIAS 10..22 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 392..403 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 232 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8R1T1" FT MOD_RES 408 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 410 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 417 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 431 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 441 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 101..162 FT /note="RGELQRESDFMASVDSSWISWGVGVFLLKPLKWTLSNMLGDNKVPAEEVLVA FT VELLKEKAEE -> KRLRRCIVCIRTRPSPPTPWWPCQSSAPSVLTPAQMRGPSTWCCC FT SCRRRRGSQSSSRTGRR (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056945" FT VAR_SEQ 163..452 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056946" FT CONFLICT 433..434 FT /note="GG -> E (in Ref. 2; CAD38703)" FT /evidence="ECO:0000305" FT CONFLICT 440..442 FT /note="KSP -> NLQ (in Ref. 2; CAD38703)" FT /evidence="ECO:0000305" SQ SEQUENCE 453 AA; 50911 MW; CF91D562B918AEA1 CRC64; MWSPEREAEA PAGGDPAGLL PPEWEEDEER MSFLFSAFKR SREVNSTDWD SKMGFWAPLV LSHSRRQGVV RLRLRDLQEA FQRKGSVPLG LATVLQDLLR RGELQRESDF MASVDSSWIS WGVGVFLLKP LKWTLSNMLG DNKVPAEEVL VAVELLKEKA EEVYRLYQNS PLSSHPVVAL SELSTLCANS CPDERTFYLV LLQLQKEKRV TVLEQNGEKI VKFARGPRAK VSPVNDVDVG VYQLMQSEQL LSRKVESLSQ EAERCKEEAR RACRAGKKQL ALRSLKAKQR TEKRIEALHA KLDTVQGILD RIYASQTDQM VFNAYQAGVG ALKLSMKDVT VEKAESLVDQ IQELCDTQDE VSQTLAGGVT NGLDFDSEEL EKELDILLQD TTKEPLDLPD NPRNRHFTNS VPNPRISDAE LEAELEKLSL SEGGLVPSSK SPKRQLEPTL KPL //