CHM1A_HUMAN
ID CHM1A_HUMAN Reviewed; 196 AA.
AC Q9HD42; A2RU09; Q14468; Q15779; Q96G31;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Charged multivesicular body protein 1a;
DE AltName: Full=Chromatin-modifying protein 1a;
DE Short=CHMP1a;
DE AltName: Full=Vacuolar protein sorting-associated protein 46-1;
DE Short=Vps46-1;
DE Short=hVps46-1;
GN Name=CHMP1A;
GN Synonyms=CHMP1 {ECO:0000303|PubMed:11559748},
GN KIAA0047 {ECO:0000303|PubMed:15489334}, PCOLN3,
GN PRSM1 {ECO:0000303|PubMed:11559747};
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] {ECO:0000312|EMBL:AAC50775.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PRELIMINARY FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Fibroblast, and Placenta;
RX PubMed=8863740; DOI=10.1016/0378-1119(96)00510-0;
RA Scott I.C., Halila R., Jenkins J.M., Mehan S., Apostolou S., Winqvist R.,
RA Callen D.F., Prockop D.J., Peltonen L., Kadler K.E.;
RT "Molecular cloning, expression and chromosomal localization of a human gene
RT encoding a 33 kDa putative metallopeptidase (PRSM1).";
RL Gene 174:135-143(1996).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAG01448.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP INDUCTION.
RC TISSUE=Placenta {ECO:0000269|PubMed:11559747};
RX PubMed=11559747; DOI=10.1242/jcs.114.13.2383;
RA Stauffer D.R., Howard T.L., Nyun T., Hollenberg S.M.;
RT "CHMP1 is a novel nuclear matrix protein affecting chromatin structure and
RT cell-cycle progression.";
RL J. Cell Sci. 114:2383-2393(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N.,
RA Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II. The
RT coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAP35487.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain {ECO:0000312|EMBL:AAH10000.2}, and
RC Kidney {ECO:0000269|PubMed:15489334};
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 [7] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH VPS4A.
RX PubMed=11559748; DOI=10.1242/jcs.114.13.2395;
RA Howard T.L., Stauffer D.R., Degnin C.R., Hollenberg S.M.;
RT "CHMP1 functions as a member of a newly defined family of vesicle
RT trafficking proteins.";
RL J. Cell Sci. 114:2395-2404(2001).
RN [8] {ECO:0000305}
RP INTERACTION WITH CHMP1B; 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 [9] {ECO:0000305}
RP SELF-ASSOCIATION, AND INTERACTION WITH CHMP1B AND VPS4A.
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 [10]
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [12]
RP INTERACTION WITH IST1.
RX PubMed=19129480; DOI=10.1091/mbc.e08-05-0474;
RA Agromayor M., Carlton J.G., Phelan J.P., Matthews D.R., Carlin L.M.,
RA Ameer-Beg S., Bowers K., Martin-Serrano J.;
RT "Essential role of hIST1 in cytokinesis.";
RL Mol. Biol. Cell 20:1374-1387(2009).
RN [13]
RP FUNCTION, INTERACTION WITH IST1, AND MUTAGENESIS OF LEU-191 AND LEU-194.
RX PubMed=19129479; DOI=10.1091/mbc.e08-05-0475;
RA Bajorek M., Morita E., Skalicky J.J., Morham S.G., Babst M.,
RA Sundquist W.I.;
RT "Biochemical analyses of human IST1 and its function in cytokinesis.";
RL Mol. Biol. Cell 20:1360-1373(2009).
RN [14]
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 [15]
RP INVOLVEMENT IN PCH8.
RX PubMed=23023333; DOI=10.1038/ng.2425;
RA Mochida G.H., Ganesh V.S., de Michelena M.I., Dias H., Atabay K.D.,
RA Kathrein K.L., Huang H.T., Hill R.S., Felie J.M., Rakiec D., Gleason D.,
RA Hill A.D., Malik A.N., Barry B.J., Partlow J.N., Tan W.H., Glader L.J.,
RA Barkovich A.J., Dobyns W.B., Zon L.I., Walsh C.A.;
RT "CHMP1A encodes an essential regulator of BMI1-INK4A in cerebellar
RT development.";
RL Nat. Genet. 44:1260-1264(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND IDENTIFICATION BY
RP 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 [18]
RP STRUCTURE BY NMR OF 180-196 IN COMPLEX WITH 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 [19]
RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 184-196 IN COMPLEX WITH MITD1,
RP FUNCTION, AND INTERACTION WITH MITD1.
RX PubMed=23045692; DOI=10.1073/pnas.1206839109;
RA Hadders M.A., Agromayor M., Obita T., Perisic O., Caballe A., Kloc M.,
RA Lamers M.H., Williams R.L., Martin-Serrano J.;
RT "ESCRT-III binding protein MITD1 is involved in cytokinesis and has an
RT unanticipated PLD fold that binds membranes.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:17424-17429(2012).
CC -!- FUNCTION: Probable peripherally associated component of the endosomal
CC sorting required for transport complex III (ESCRT-III) which is
CC involved in multivesicular bodies (MVBs) formation and sorting of
CC endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles
CC (ILVs) that are generated by invagination and scission from the
CC limiting membrane of the endosome and mostly are delivered to lysosomes
CC enabling degradation of membrane proteins, such as stimulated growth
CC factor receptors, lysosomal enzymes and lipids. The MVB pathway appears
CC to require the sequential function of ESCRT-O, -I,-II and -III
CC complexes. ESCRT-III proteins mostly dissociate from the invaginating
CC membrane before the ILV is released. The ESCRT machinery also functions
CC in topologically equivalent membrane fission events, such as the
CC terminal stages of cytokinesis and the budding of enveloped viruses
CC (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to
CC mediate the necessary vesicle extrusion and/or membrane fission
CC activities, possibly in conjunction with the AAA ATPase VPS4. Involved
CC in cytokinesis. Involved in recruiting VPS4A and/or VPS4B to the
CC midbody of dividing cells. May also be involved in chromosome
CC condensation. Targets the Polycomb group (PcG) protein BMI1/PCGF4 to
CC regions of condensed chromatin. May play a role in stable cell cycle
CC progression and in PcG gene silencing. {ECO:0000269|PubMed:11559747,
CC ECO:0000269|PubMed:11559748, ECO:0000269|PubMed:19129479,
CC ECO:0000269|PubMed:23045692}.
CC -!- SUBUNIT: Probable peripherally associated component of the endosomal
CC sorting required for transport complex III (ESCRT-III). ESCRT-III
CC components are thought to multimerize to form a flat lattice on the
CC perimeter membrane of the endosome. Several assembly forms of ESCRT-III
CC may exist that interact and act sequentially. Self-associates.
CC Interacts with CHMP1B. Interacts with VPS4A. Interacts with VPS4B.
CC Interacts with PHF1. Interacts with IST1. Interacts with MITD1.
CC {ECO:0000269|PubMed:11559748, ECO:0000269|PubMed:14505570,
CC ECO:0000269|PubMed:14519844, ECO:0000269|PubMed:17928862,
CC ECO:0000269|PubMed:19129479, ECO:0000269|PubMed:19129480,
CC ECO:0000269|PubMed:23045692}.
CC -!- INTERACTION:
CC Q9HD42; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-1057156, EBI-725606;
CC Q9HD42; Q9HD42: CHMP1A; NbExp=6; IntAct=EBI-1057156, EBI-1057156;
CC Q9HD42; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-1057156, EBI-742054;
CC Q9HD42; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-1057156, EBI-739467;
CC Q9HD42; P42858: HTT; NbExp=12; IntAct=EBI-1057156, EBI-466029;
CC Q9HD42; P53990-3: IST1; NbExp=3; IntAct=EBI-1057156, EBI-12188567;
CC Q9HD42; Q8WV92: MITD1; NbExp=3; IntAct=EBI-1057156, EBI-2691489;
CC Q9HD42; D3DTS7: PMP22; NbExp=3; IntAct=EBI-1057156, EBI-25882629;
CC Q9HD42; P25786: PSMA1; NbExp=3; IntAct=EBI-1057156, EBI-359352;
CC Q9HD42; O00560: SDCBP; NbExp=3; IntAct=EBI-1057156, EBI-727004;
CC Q9HD42; P37840: SNCA; NbExp=3; IntAct=EBI-1057156, EBI-985879;
CC Q9HD42; O95630: STAMBP; NbExp=7; IntAct=EBI-1057156, EBI-396676;
CC Q9HD42; Q99757: TXN2; NbExp=3; IntAct=EBI-1057156, EBI-2932492;
CC Q9HD42; P40818: USP8; NbExp=3; IntAct=EBI-1057156, EBI-1050865;
CC Q9HD42; Q9UN37: VPS4A; NbExp=6; IntAct=EBI-1057156, EBI-1171942;
CC Q9HD42; O75351: VPS4B; NbExp=3; IntAct=EBI-1057156, EBI-2514459;
CC Q9HD42; Q9NP79: VTA1; NbExp=3; IntAct=EBI-1057156, EBI-740160;
CC Q9HD42; P07947: YES1; NbExp=3; IntAct=EBI-1057156, EBI-515331;
CC Q9HD42-1; Q9UN37: VPS4A; NbExp=2; IntAct=EBI-15663713, EBI-1171942;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome membrane; Peripheral membrane
CC protein. Nucleus matrix. Note=The cytoplasmic form is partially
CC membrane-associated and localizes to early endosomes. The nuclear form
CC remains associated with the chromosome scaffold during mitosis. On
CC overexpression, it localizes to nuclear bodies characterized by
CC nuclease-resistant condensed chromatin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:11559747};
CC IsoId=Q9HD42-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=Q9HD42-2; Sequence=VSP_051716;
CC -!- TISSUE SPECIFICITY: Expressed in placenta, cultured skin fibroblasts
CC and in osteoblast cell line MG-63. {ECO:0000269|PubMed:8863740}.
CC -!- INDUCTION: By muristerone. {ECO:0000269|PubMed:11559747}.
CC -!- DISEASE: Pontocerebellar hypoplasia 8 (PCH8) [MIM:614961]: An autosomal
CC recessive neurodevelopmental disorder characterized by severe
CC psychomotor retardation, abnormal movements, hypotonia, spasticity, and
CC variable visual defects. Brain MRI shows pontocerebellar hypoplasia,
CC decreased cerebral white matter, and a thin corpus callosum.
CC {ECO:0000269|PubMed:23023333}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000255}.
CC -!- CAUTION: Was originally (PubMed:8863740) thought to be a
CC metalloprotease (PRSM1). This was based on a wrong translation of the
CC ORF which gave rise to a putative protein of 318 AA containing a
CC pattern reminiscent of zinc metalloproteases.
CC {ECO:0000305|PubMed:8863740}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50775.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=BAA07557.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR EMBL; U58048; AAC50775.1; ALT_SEQ; mRNA.
DR EMBL; AF281063; AAG01448.1; -; mRNA.
DR EMBL; D38554; BAA07557.1; ALT_SEQ; mRNA.
DR EMBL; BT006841; AAP35487.1; -; mRNA.
DR EMBL; AC010538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007527; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC010000; AAH10000.2; -; mRNA.
DR EMBL; BC132711; AAI32712.1; -; mRNA.
DR EMBL; BC132713; AAI32714.1; -; mRNA.
DR CCDS; CCDS45552.1; -. [Q9HD42-1]
DR PIR; JC4963; JC4963.
DR RefSeq; NP_002759.2; NM_002768.4. [Q9HD42-1]
DR PDB; 2JQ9; NMR; -; B=180-196.
DR PDB; 2YMB; X-ray; 3.40 A; F/H=184-196.
DR PDB; 4A5X; X-ray; 1.91 A; C/D=184-196.
DR PDBsum; 2JQ9; -.
DR PDBsum; 2YMB; -.
DR PDBsum; 4A5X; -.
DR AlphaFoldDB; Q9HD42; -.
DR SMR; Q9HD42; -.
DR BioGRID; 111148; 134.
DR ComplexPortal; CPX-329; ESCRT-III complex.
DR CORUM; Q9HD42; -.
DR DIP; DIP-50647N; -.
DR IntAct; Q9HD42; 53.
DR MINT; Q9HD42; -.
DR STRING; 9606.ENSP00000380998; -.
DR MoonDB; Q9HD42; Curated.
DR iPTMnet; Q9HD42; -.
DR MetOSite; Q9HD42; -.
DR PhosphoSitePlus; Q9HD42; -.
DR BioMuta; CHMP1A; -.
DR DMDM; 62510514; -.
DR EPD; Q9HD42; -.
DR jPOST; Q9HD42; -.
DR MassIVE; Q9HD42; -.
DR MaxQB; Q9HD42; -.
DR PaxDb; Q9HD42; -.
DR PeptideAtlas; Q9HD42; -.
DR PRIDE; Q9HD42; -.
DR ProteomicsDB; 81828; -. [Q9HD42-1]
DR ProteomicsDB; 81829; -. [Q9HD42-2]
DR Antibodypedia; 1706; 238 antibodies from 26 providers.
DR DNASU; 5119; -.
DR Ensembl; ENST00000397901.8; ENSP00000380998.3; ENSG00000131165.16. [Q9HD42-1]
DR GeneID; 5119; -.
DR KEGG; hsa:5119; -.
DR MANE-Select; ENST00000397901.8; ENSP00000380998.3; NM_002768.5; NP_002759.2.
DR UCSC; uc002fnu.5; human. [Q9HD42-1]
DR CTD; 5119; -.
DR DisGeNET; 5119; -.
DR GeneCards; CHMP1A; -.
DR HGNC; HGNC:8740; CHMP1A.
DR HPA; ENSG00000131165; Low tissue specificity.
DR MalaCards; CHMP1A; -.
DR MIM; 164010; gene.
DR MIM; 614961; phenotype.
DR neXtProt; NX_Q9HD42; -.
DR OpenTargets; ENSG00000131165; -.
DR Orphanet; 324569; Pontocerebellar hypoplasia type 8.
DR PharmGKB; PA33085; -.
DR VEuPathDB; HostDB:ENSG00000131165; -.
DR eggNOG; KOG3232; Eukaryota.
DR GeneTree; ENSGT00950000182832; -.
DR HOGENOM; CLU_080826_1_0_1; -.
DR InParanoid; Q9HD42; -.
DR OMA; KFASKQM; -.
DR PhylomeDB; Q9HD42; -.
DR TreeFam; TF300076; -.
DR PathwayCommons; Q9HD42; -.
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR SignaLink; Q9HD42; -.
DR SIGNOR; Q9HD42; -.
DR BioGRID-ORCS; 5119; 330 hits in 1084 CRISPR screens.
DR ChiTaRS; CHMP1A; human.
DR EvolutionaryTrace; Q9HD42; -.
DR GeneWiki; CHMP1A; -.
DR GenomeRNAi; 5119; -.
DR Pharos; Q9HD42; Tbio.
DR PRO; PR:Q9HD42; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9HD42; protein.
DR Bgee; ENSG00000131165; Expressed in endometrium epithelium and 211 other tissues.
DR ExpressionAtlas; Q9HD42; baseline and differential.
DR Genevisible; Q9HD42; HS.
DR GO; GO:1904930; C:amphisome membrane; IDA:ComplexPortal.
DR GO; GO:0000421; C:autophagosome membrane; IDA:ComplexPortal.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; IDA:UniProtKB.
DR GO; GO:0000815; C:ESCRT III complex; IBA:GO_Central.
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:0005815; C:microtubule organizing center; IDA: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:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; IDA:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008237; F:metallopeptidase activity; TAS:ProtInc.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR GO; GO:0097352; P:autophagosome maturation; IMP:ComplexPortal.
DR GO; GO:0006914; P:autophagy; IMP:ComplexPortal.
DR GO; GO:0051301; P:cell division; 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:0090148; P:membrane fission; IC:ComplexPortal.
DR GO; GO:0061952; P:midbody abscission; IMP:UniProtKB.
DR GO; GO:0007076; P:mitotic chromosome condensation; IDA: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:0010629; P:negative regulation of gene expression; IDA: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:0016192; P:vesicle-mediated transport; IDA:UniProtKB.
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 IDEAL; IID00253; -.
DR InterPro; IPR029888; CHMP1A.
DR InterPro; IPR005024; Snf7_fam.
DR PANTHER; PTHR10476; PTHR10476; 1.
DR PANTHER; PTHR10476:SF17; PTHR10476:SF17; 1.
DR Pfam; PF03357; Snf7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Coiled coil; Cytoplasm; Endosome; Membrane; Neurodegeneration; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Transport.
FT CHAIN 1..196
FT /note="Charged multivesicular body protein 1a"
FT /id="PRO_0000211448"
FT REGION 173..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 5..47
FT /evidence="ECO:0000255"
FT COILED 102..124
FT /evidence="ECO:0000255"
FT MOTIF 185..195
FT /note="MIT-interacting motif"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..128
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_051716"
FT MUTAGEN 191
FT /note="L->A: No effect on interaction with IST1; when
FT associated with L-194."
FT /evidence="ECO:0000269|PubMed:19129479"
FT MUTAGEN 194
FT /note="L->A: No effect on interaction with IST1; when
FT associated with L-194."
FT /evidence="ECO:0000269|PubMed:19129479"
FT CONFLICT 77
FT /note="Q -> D (in Ref. 1; AAC50775)"
FT /evidence="ECO:0000305"
FT HELIX 184..195
FT /evidence="ECO:0007829|PDB:4A5X"
SQ SEQUENCE 196 AA; 21703 MW; 85D0ED7D10828D60 CRC64;
MDDTLFQLKF TAKQLEKLAK KAEKDSKAEQ AKVKKALLQK NVECARVYAE NAIRKKNEGV
NWLRMASRVD AVASKVQTAV TMKGVTKNMA QVTKALDKAL STMDLQKVSS VMDRFEQQVQ
NLDVHTSVME DSMSSATTLT TPQEQVDSLI MQIAEENGLE VLDQLSQLPE GASAVGESSV
RSQEDQLSRR LAALRN
