CHMP7_HUMAN
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 03-AUG-2022, entry version 158.
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:28242692, PubMed:26040712). 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; D3DTS7: PMP22; NbExp=3; IntAct=EBI-749253, EBI-25882629;
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_152272.4. [Q8WUX9-1]
DR AlphaFoldDB; Q8WUX9; -.
DR SMR; Q8WUX9; -.
DR BioGRID; 124879; 79.
DR ComplexPortal; CPX-329; ESCRT-III complex.
DR IntAct; Q8WUX9; 28.
DR MINT; Q8WUX9; -.
DR STRING; 9606.ENSP00000380794; -.
DR iPTMnet; Q8WUX9; -.
DR MetOSite; Q8WUX9; -.
DR PhosphoSitePlus; Q8WUX9; -.
DR BioMuta; CHMP7; -.
DR DMDM; 73917782; -.
DR EPD; Q8WUX9; -.
DR jPOST; Q8WUX9; -.
DR MassIVE; Q8WUX9; -.
DR MaxQB; Q8WUX9; -.
DR PaxDb; Q8WUX9; -.
DR PeptideAtlas; Q8WUX9; -.
DR PRIDE; Q8WUX9; -.
DR ProteomicsDB; 4465; -.
DR ProteomicsDB; 74719; -. [Q8WUX9-1]
DR Antibodypedia; 22730; 83 antibodies from 19 providers.
DR DNASU; 91782; -.
DR Ensembl; ENST00000313219.8; ENSP00000324491.7; ENSG00000147457.14. [Q8WUX9-1]
DR Ensembl; ENST00000397677.6; ENSP00000380794.1; ENSG00000147457.14. [Q8WUX9-1]
DR Ensembl; ENST00000519503.5; ENSP00000427948.1; ENSG00000147457.14. [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 CTD; 91782; -.
DR GeneCards; CHMP7; -.
DR HGNC; HGNC:28439; CHMP7.
DR HPA; ENSG00000147457; Tissue enhanced (lymphoid).
DR MIM; 611130; gene.
DR neXtProt; NX_Q8WUX9; -.
DR OpenTargets; ENSG00000147457; -.
DR PharmGKB; PA142672115; -.
DR VEuPathDB; HostDB:ENSG00000147457; -.
DR eggNOG; KOG2911; Eukaryota.
DR GeneTree; ENSGT00720000108860; -.
DR HOGENOM; CLU_044768_0_0_1; -.
DR InParanoid; Q8WUX9; -.
DR OMA; NFMFSDF; -.
DR OrthoDB; 832779at2759; -.
DR PhylomeDB; Q8WUX9; -.
DR TreeFam; TF312851; -.
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 BioGRID-ORCS; 91782; 544 hits in 1089 CRISPR screens.
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 203 other tissues.
DR ExpressionAtlas; Q8WUX9; baseline and differential.
DR Genevisible; Q8WUX9; 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: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; 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: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; IC: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 InterPro; IPR005024; Snf7_fam.
DR PANTHER; PTHR22761; PTHR22761; 1.
DR Pfam; PF03357; Snf7; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; 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 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
