CHM2B_HUMAN
ID CHM2B_HUMAN Reviewed; 213 AA.
AC Q9UQN3; B4DJG8; Q53HC7; Q9Y4U6;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Charged multivesicular body protein 2b;
DE AltName: Full=CHMP2.5;
DE AltName: Full=Chromatin-modifying protein 2b;
DE Short=CHMP2b;
DE AltName: Full=Vacuolar protein sorting-associated protein 2-2;
DE Short=Vps2-2;
DE Short=hVps2-2;
GN Name=CHMP2B; ORFNames=CGI-84;
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=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus;
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 MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix;
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 [8]
RP 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, TISSUE SPECIFICITY, AND VARIANT FTDALS7 TYR-148.
RX PubMed=16041373; DOI=10.1038/ng1609;
RA Skibinski G., Parkinson N.J., Brown J.M., Chakrabarti L., Lloyd S.L.,
RA Hummerich H., Nielsen J.E., Hodges J.R., Spillantini M.G., Thusgaard T.,
RA Brandner S., Brun A., Rossor M.N., Gade A., Johannsen P., Soerensen S.A.,
RA Gydesen S., Fisher E.M.C., Collinge J.;
RT "Mutations in the endosomal ESCRTIII-complex subunit CHMP2B in
RT frontotemporal dementia.";
RL Nat. Genet. 37:806-808(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, AND IDENTIFICATION BY
RP 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, 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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [19]
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 [20]
RP STRUCTURE BY NMR OF 195-213 IN COMPLEX WITH VPS4B, AND INTERACTION WITH
RP VPS4A.
RX PubMed=17928862; DOI=10.1038/nature06172;
RA Stuchell-Brereton M.D., Skalicky J.J., Kieffer C., Karren M.A.,
RA Ghaffarian S., Sundquist W.I.;
RT "ESCRT-III recognition by VPS4 ATPases.";
RL Nature 449:740-744(2007).
RN [21]
RP VARIANT FTDALS7 HIS-206, AND VARIANT VAL-29.
RX PubMed=16807408; DOI=10.1212/01.wnl.0000231510.89311.8b;
RA Parkinson N., Ince P.G., Smith M.O., Highley R., Skibinski G.,
RA Andersen P.M., Morrison K.E., Pall H.S., Hardiman O., Collinge J.,
RA Shaw P.J., Fisher E.M.;
RT "ALS phenotypes with mutations in CHMP2B (charged multivesicular body
RT protein 2B).";
RL Neurology 67:1074-1077(2006).
RN [22]
RP VARIANTS FTDALS7 VAL-29; ASN-104 AND HIS-206, AND CHARACTERIZATION OF
RP VARIANTS FTDALS7 VAL-29; ASN-104 AND HIS-206.
RX PubMed=20352044; DOI=10.1371/journal.pone.0009872;
RA Cox L.E., Ferraiuolo L., Goodall E.F., Heath P.R., Higginbottom A.,
RA Mortiboys H., Hollinger H.C., Hartley J.A., Brockington A., Burness C.E.,
RA Morrison K.E., Wharton S.B., Grierson A.J., Ince P.G., Kirby J., Shaw P.J.;
RT "Mutations in CHMP2B in lower motor neuron predominant amyotrophic lateral
RT sclerosis (ALS).";
RL PLoS ONE 5:E9872-E9872(2010).
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.
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 CHMP2A. Interacts with VPS4A.
CC Interacts with VPS4B; the interaction is direct.
CC {ECO:0000269|PubMed:14519844, ECO:0000269|PubMed:17928862}.
CC -!- INTERACTION:
CC Q9UQN3; Q9Y3E7: CHMP3; NbExp=2; IntAct=EBI-718324, EBI-2118119;
CC Q9UQN3; Q9H444: CHMP4B; NbExp=2; IntAct=EBI-718324, EBI-749627;
CC Q9UQN3; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-718324, EBI-750109;
CC Q9UQN3; PRO_0000037309 [P0C6X7]: rep; Xeno; NbExp=2; IntAct=EBI-718324, EBI-25475797;
CC Q9UQN3; PRO_0000037316 [P0C6X7]: rep; Xeno; NbExp=2; IntAct=EBI-718324, EBI-25475825;
CC Q9UQN3-1; O75351: VPS4B; NbExp=2; IntAct=EBI-15663586, EBI-2514459;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16041373}.
CC Late endosome membrane {ECO:0000305|PubMed:16041373}; Peripheral
CC membrane protein {ECO:0000305|PubMed:16041373}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UQN3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UQN3-2; Sequence=VSP_045142;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in brain, heart,
CC skeletal muscle, spleen, kidney, liver, small intestine, pancreas,
CC lung, placenta and leukocytes. In brain, it is expressed in cerebellum,
CC cerebral cortex, medulla, spinal chord, occipital lobe, frontal lobe,
CC temporal lobe and putamen. {ECO:0000269|PubMed:16041373}.
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 (By similarity).
CC {ECO:0000250}.
CC -!- DISEASE: Frontotemporal dementia and/or amyotrophic lateral sclerosis 7
CC (FTDALS7) [MIM:600795]: A neurodegenerative disorder characterized by
CC frontotemporal dementia and/or amyotrophic lateral sclerosis in
CC affected individuals. There is high intrafamilial variation.
CC Frontotemporal dementia (FTD) is characterized by frontal and temporal
CC lobe atrophy associated with neuronal loss, gliosis, and dementia.
CC Patients exhibit progressive changes in social, behavioral, and/or
CC language function. Amyotrophic lateral sclerosis (ALS) is characterized
CC by the death of motor neurons in the brain, brainstem, and spinal cord,
CC resulting in fatal paralysis. FTDALS7 is an autosomal dominant form
CC characterized by onset of ALS or FTD in adulthood. A few patients may
CC have both phenotypes. {ECO:0000269|PubMed:16041373,
CC ECO:0000269|PubMed:16807408, ECO:0000269|PubMed:20352044}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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; AF151842; AAD34079.1; -; mRNA.
DR EMBL; AL080122; CAB45721.1; -; mRNA.
DR EMBL; AK296072; BAG58830.1; -; mRNA.
DR EMBL; CR533456; CAG38487.1; -; mRNA.
DR EMBL; AK222654; BAD96374.1; -; mRNA.
DR EMBL; AC123511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC130885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001553; AAH01553.1; -; mRNA.
DR CCDS; CCDS2918.1; -. [Q9UQN3-1]
DR CCDS; CCDS58840.1; -. [Q9UQN3-2]
DR PIR; T12468; T12468.
DR RefSeq; NP_001231573.1; NM_001244644.1. [Q9UQN3-2]
DR RefSeq; NP_054762.2; NM_014043.3. [Q9UQN3-1]
DR PDB; 2JQK; NMR; -; B=195-213.
DR PDBsum; 2JQK; -.
DR AlphaFoldDB; Q9UQN3; -.
DR SMR; Q9UQN3; -.
DR BioGRID; 117462; 98.
DR ComplexPortal; CPX-329; ESCRT-III complex.
DR CORUM; Q9UQN3; -.
DR DIP; DIP-50766N; -.
DR IntAct; Q9UQN3; 52.
DR MINT; Q9UQN3; -.
DR STRING; 9606.ENSP00000263780; -.
DR iPTMnet; Q9UQN3; -.
DR MetOSite; Q9UQN3; -.
DR PhosphoSitePlus; Q9UQN3; -.
DR BioMuta; CHMP2B; -.
DR DMDM; 73917746; -.
DR EPD; Q9UQN3; -.
DR jPOST; Q9UQN3; -.
DR MassIVE; Q9UQN3; -.
DR MaxQB; Q9UQN3; -.
DR PaxDb; Q9UQN3; -.
DR PeptideAtlas; Q9UQN3; -.
DR PRIDE; Q9UQN3; -.
DR ProteomicsDB; 4379; -.
DR ProteomicsDB; 85561; -. [Q9UQN3-1]
DR Antibodypedia; 32034; 282 antibodies from 34 providers.
DR DNASU; 25978; -.
DR Ensembl; ENST00000263780.9; ENSP00000263780.4; ENSG00000083937.10. [Q9UQN3-1]
DR Ensembl; ENST00000471660.5; ENSP00000419998.1; ENSG00000083937.10. [Q9UQN3-2]
DR GeneID; 25978; -.
DR KEGG; hsa:25978; -.
DR MANE-Select; ENST00000263780.9; ENSP00000263780.4; NM_014043.4; NP_054762.2.
DR UCSC; uc003dqp.5; human. [Q9UQN3-1]
DR CTD; 25978; -.
DR DisGeNET; 25978; -.
DR GeneCards; CHMP2B; -.
DR GeneReviews; CHMP2B; -.
DR HGNC; HGNC:24537; CHMP2B.
DR HPA; ENSG00000083937; Low tissue specificity.
DR MalaCards; CHMP2B; -.
DR MIM; 600795; phenotype.
DR MIM; 609512; gene.
DR neXtProt; NX_Q9UQN3; -.
DR OpenTargets; ENSG00000083937; -.
DR Orphanet; 803; Amyotrophic lateral sclerosis.
DR Orphanet; 275864; Behavioral variant of frontotemporal dementia.
DR Orphanet; 100070; Progressive non-fluent aphasia.
DR Orphanet; 100069; Semantic dementia.
DR PharmGKB; PA142672112; -.
DR VEuPathDB; HostDB:ENSG00000083937; -.
DR eggNOG; KOG3231; Eukaryota.
DR GeneTree; ENSGT00950000182832; -.
DR HOGENOM; CLU_069208_1_2_1; -.
DR InParanoid; Q9UQN3; -.
DR OMA; NMREFQM; -.
DR OrthoDB; 1480977at2759; -.
DR PhylomeDB; Q9UQN3; -.
DR TreeFam; TF314163; -.
DR PathwayCommons; Q9UQN3; -.
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; Q9UQN3; -.
DR SIGNOR; Q9UQN3; -.
DR BioGRID-ORCS; 25978; 11 hits in 1077 CRISPR screens.
DR ChiTaRS; CHMP2B; human.
DR EvolutionaryTrace; Q9UQN3; -.
DR GeneWiki; CHMP2B; -.
DR GenomeRNAi; 25978; -.
DR Pharos; Q9UQN3; Tbio.
DR PRO; PR:Q9UQN3; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9UQN3; protein.
DR Bgee; ENSG00000083937; Expressed in medial globus pallidus and 217 other tissues.
DR ExpressionAtlas; Q9UQN3; baseline and differential.
DR Genevisible; Q9UQN3; HS.
DR GO; GO:1904930; C:amphisome membrane; IDA:ComplexPortal.
DR GO; GO:0000421; C:autophagosome membrane; IDA:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; 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: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:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0097352; P:autophagosome maturation; IMP:ComplexPortal.
DR GO; GO:0006914; P:autophagy; IMP:ComplexPortal.
DR GO; GO:0050890; P:cognition; IMP:UniProtKB.
DR GO; GO:0007032; P:endosome organization; IMP:UniProtKB.
DR GO; GO:0032509; P:endosome transport via multivesicular body sorting pathway; IBA:GO_Central.
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:0045324; P:late endosome to vacuole transport; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; TAS:ParkinsonsUK-UCL.
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; TAS:ParkinsonsUK-UCL.
DR GO; GO:0071985; P:multivesicular body sorting pathway; IDA:ComplexPortal.
DR GO; GO:0061763; P:multivesicular body-lysosome fusion; TAS:ParkinsonsUK-UCL.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:ComplexPortal.
DR GO; GO:0070050; P:neuron cellular homeostasis; 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; IBA:GO_Central.
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:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IDA:ComplexPortal.
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:UniProtKB.
DR GO; GO:0019076; P:viral release from host cell; IMP:UniProtKB.
DR InterPro; IPR005024; Snf7_fam.
DR PANTHER; PTHR10476; PTHR10476; 1.
DR Pfam; PF03357; Snf7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing;
KW Amyotrophic lateral sclerosis; Coiled coil; Cytoplasm; Disease variant;
KW Endosome; Membrane; Neurodegeneration; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..213
FT /note="Charged multivesicular body protein 2b"
FT /id="PRO_0000211469"
FT REGION 179..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 25..55
FT /evidence="ECO:0000255"
FT MOTIF 201..211
FT /note="MIT-interacting motif"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..42
FT /note="MASLFKKKTVDDVIKEQNRELRGTQRAIIRDRAALEKQEKQL -> M (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_045142"
FT VARIANT 29
FT /note="I -> V (in FTDALS7; cells expressing the mutant
FT protein have large cytoplasmic vacuoles with an
FT accumulation of the mutant protein on the outer membrane
FT termed halos; cells with the mutant protein also have
FT aberrant localization of CD63 and an increase in MAP1LC3A1
FT overall indicating a defect in the autophagic pathway;
FT dbSNP:rs63750818)"
FT /evidence="ECO:0000269|PubMed:16807408,
FT ECO:0000269|PubMed:20352044"
FT /id="VAR_038373"
FT VARIANT 104
FT /note="T -> N (in FTDALS7; cells expressing the mutant
FT protein have large cytoplasmic vacuoles with an
FT accumulation of the mutant protein on the outer membrane
FT termed halos; cells with the mutant protein also have
FT aberrant localization of CD63 and an increase in MAP1LC3A
FT overall indicating a defect in the autophagic pathway;
FT dbSNP:rs281864934)"
FT /evidence="ECO:0000269|PubMed:20352044"
FT /id="VAR_068689"
FT VARIANT 148
FT /note="D -> Y (in FTDALS7; dbSNP:rs63750653)"
FT /evidence="ECO:0000269|PubMed:16041373"
FT /id="VAR_023383"
FT VARIANT 206
FT /note="Q -> H (in FTDALS7; cells expressing the mutant
FT protein have large cytoplasmic vacuoles with an
FT accumulation of the mutant protein on the outer membrane
FT termed halos; cells with the mutant protein also have
FT aberrant localization of CD63 and an increase in MAP1LC3A
FT overall indicating a defect in the autophagic pathway;
FT dbSNP:rs63751126)"
FT /evidence="ECO:0000269|PubMed:16807408,
FT ECO:0000269|PubMed:20352044"
FT /id="VAR_038374"
FT CONFLICT 8
FT /note="K -> R (in Ref. 2; CAB45721 and 3; CAG38487)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="N -> S (in Ref. 5; BAD96374)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="E -> V (in Ref. 2; CAB45721 and 3; CAG38487)"
FT /evidence="ECO:0000305"
FT HELIX 201..210
FT /evidence="ECO:0007829|PDB:2JQK"
SQ SEQUENCE 213 AA; 23907 MW; BA192A0EAC45C19B CRC64;
MASLFKKKTV DDVIKEQNRE LRGTQRAIIR DRAALEKQEK QLELEIKKMA KIGNKEACKV
LAKQLVHLRK QKTRTFAVSS KVTSMSTQTK VMNSQMKMAG AMSTTAKTMQ AVNKKMDPQK
TLQTMQNFQK ENMKMEMTEE MINDTLDDIF DGSDDEEESQ DIVNQVLDEI GIEISGKMAK
APSAARSLPS ASTSKATISD EEIERQLKAL GVD
