Full text data of CHMP1B
CHMP1B
(C18orf2)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Charged multivesicular body protein 1b (CHMP1.5; Chromatin-modifying protein 1b; CHMP1b; Vacuolar protein sorting-associated protein 46-2; Vps46-2; hVps46-2)
Charged multivesicular body protein 1b (CHMP1.5; Chromatin-modifying protein 1b; CHMP1b; Vacuolar protein sorting-associated protein 46-2; Vps46-2; hVps46-2)
UniProt
Q7LBR1
ID CHM1B_HUMAN Reviewed; 199 AA.
AC Q7LBR1; Q96E89; Q9HD41;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 1.
DT 22-JAN-2014, entry version 79.
DE RecName: Full=Charged multivesicular body protein 1b;
DE AltName: Full=CHMP1.5;
DE AltName: Full=Chromatin-modifying protein 1b;
DE Short=CHMP1b;
DE AltName: Full=Vacuolar protein sorting-associated protein 46-2;
DE Short=Vps46-2;
DE Short=hVps46-2;
GN Name=CHMP1B; Synonyms=C18orf2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=11474171;
RA Vuoristo J.T., Berrettini W.H., Ala-Kokko L.;
RT "C18orf2, a novel, highly conserved intronless gene within intron 5 of
RT the GNAL gene on chromosome 18p11.";
RL Cytogenet. Cell Genet. 93:19-22(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11559747;
RA Stauffer D.R., Howard T.L., Nyun T., Hollenberg S.M.;
RT "CHMP1 is a novel nuclear matrix protein affecting chromatin structure
RT and cell-cycle progression.";
RL J. Cell Sci. 114:2383-2393(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Melanoma, 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH CHMP1A; 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 [5]
RP FUNCTION IN HIV-1 BUDDING, AND INTERACTION WITH CHMP1A; CHMP2A AND
RP 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
RT sorting factors by using alternative adaptor proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003).
RN [6]
RP ERRATUM.
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 [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SPAST.
RX PubMed=15537668; DOI=10.1093/hmg/ddi003;
RA Reid E., Connell J.W., Edwards T.L., Duley S., Brown S.E.,
RA Sanderson C.M.;
RT "The hereditary spastic paraplegia protein spastin interacts with the
RT ESCRT-III complex-associated endosomal protein CHMP1B.";
RL Hum. Mol. Genet. 14:19-38(2005).
RN [8]
RP INTERACTION WITH VPS4A.
RX PubMed=16174732; DOI=10.1073/pnas.0502165102;
RA Scott A., Gaspar J., Stuchell-Brereton M.D., Alam S.L., Skalicky J.J.,
RA Sundquist W.I.;
RT "Structure and ESCRT-III protein interactions of the MIT domain of
RT human VPS4A.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13813-13818(2005).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH STAMBP.
RX PubMed=16730941; DOI=10.1016/j.ygeno.2006.04.003;
RA Tsang H.T.H., Connell J.W., Brown S.E., Thompson A., Reid E.,
RA Sanderson C.M.;
RT "A systematic analysis of human CHMP protein interactions: additional
RT MIT domain-containing proteins bind to multiple components of the
RT human ESCRT III complex.";
RL Genomics 88:333-346(2006).
RN [10]
RP INTERACTION WITH VPS4A AND VPS4B, AND MUTAGENESIS OF LEU-192 AND
RP LEU-195.
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 [11]
RP INTERACTION WITH VTA1 AND VPS4B, AND MUTAGENESIS OF 158-ASP-GLU-159.
RX PubMed=18385515; DOI=10.1091/mbc.E07-12-1263;
RA Shim S., Merrill S.A., Hanson P.I.;
RT "Novel interactions of ESCRT-III with LIP5 and VPS4 and their
RT implications for ESCRT-III disassembly.";
RL Mol. Biol. Cell 19:2661-2672(2008).
RN [12]
RP INTERACTION WITH IST1; VTA1; VPS4A; MITD1 AND STAMBP.
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, AND INTERACTION WITH IST1.
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.,
RA Buerckstuemmer T., 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 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
RT interferon-induced gene ISG15.";
RL J. Virol. 85:7153-7161(2011).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 145-194 IN COMPLEX WITH
RP SPAST, SUBCELLULAR LOCATION, INTERACTION WITH VPS4A, AND MUTAGENESIS
RP OF THR-178; ALA-181; GLU-184; LEU-188 AND LEU-192.
RX PubMed=18997780; DOI=10.1038/nsmb.1512;
RA Yang D., Rismanchi N., Renvoise B., Lippincott-Schwartz J.,
RA Blackstone C., Hurley J.H.;
RT "Structural basis for midbody targeting of spastin by the ESCRT-III
RT protein CHMP1B.";
RL Nat. Struct. Mol. Biol. 15:1278-1286(2008).
CC -!- FUNCTION: Probable peripherally associated component of the
CC endosomal sorting required for transport complex III (ESCRT-III)
CC which is involved in multivesicular bodies (MVBs) formation and
CC sorting of endosomal cargo proteins into MVBs. MVBs contain
CC intraluminal vesicles (ILVs) that are generated by invagination
CC and scission from the limiting membrane of the endosome and mostly
CC are delivered to lysosomes enabling degradation of membrane
CC proteins, such as stimulated growth factor receptors, lysosomal
CC enzymes and lipids. The MVB pathway appears to require the
CC sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-
CC III proteins mostly dissociate from the invaginating membrane
CC before the ILV is released. The ESCRT machinery also functions in
CC topologically equivalent membrane fission events, such as the
CC terminal stages of cytokinesis and the budding of enveloped
CC viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are
CC believed to mediate the necessary vesicle extrusion and/or
CC membrane fission activities, possibly in conjunction with the AAA
CC ATPase VPS4. Involved in cytokinesis. Involved in recruiting VPS4A
CC and/or VPS4B and SPAST to the midbody of dividing cells. Involved
CC in HIV-1 p6- and p9-dependent virus release.
CC -!- SUBUNIT: Probable peripherally associated component of the
CC endosomal sorting required for transport complex III (ESCRT-III).
CC ESCRT-III components are thought to multimerize to form a flat
CC lattice on the perimeter membrane of the endosome. Several
CC assembly forms of ESCRT-III may exist that interact and act
CC sequentally. Interacts with CHMP1A. Interacts with VTA1; the
CC interaction probably involves the open conformation of CHMP1B.
CC Interacts with CHMP2A. Interacts with VPS4A; the interaction is
CC direct. Interacts with VPS4B; the interaction is direct. Interacts
CC with SPAST (via MIT domain); the interaction is direct. Interacts
CC with IST1. Interacts with MITD1. Interacts with STAMBP.
CC -!- INTERACTION:
CC O95630:STAMBP; NbExp=5; IntAct=EBI-2118090, EBI-396676;
CC P40818:USP8; NbExp=5; IntAct=EBI-2118090, EBI-1050865;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Endosome. Late endosome
CC membrane; Peripheral membrane protein (Probable). Note=Localizes
CC to the midbody of dividing cells, colocalizing with CEP55 and
CC CHMP5. Localized at the periphery of the Fleming body.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in pancreas,
CC kidney, skeletal muscle, liver, lung, placenta and brain.
CC -!- SIMILARITY: Belongs to the SNF7 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG01449.1; Type=Erroneous initiation;
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DR EMBL; AF306520; AAL48200.1; -; Genomic_DNA.
DR EMBL; AF281064; AAG01449.1; ALT_INIT; mRNA.
DR EMBL; BC065933; AAH65933.1; -; mRNA.
DR EMBL; BC012733; AAH12733.3; -; mRNA.
DR RefSeq; NP_065145.2; NM_020412.4.
DR UniGene; Hs.656244; -.
DR PDB; 3EAB; X-ray; 2.50 A; G/H/I/J/K/L=148-197.
DR PDBsum; 3EAB; -.
DR ProteinModelPortal; Q7LBR1; -.
DR SMR; Q7LBR1; 148-197.
DR DIP; DIP-48534N; -.
DR IntAct; Q7LBR1; 9.
DR MINT; MINT-6946813; -.
DR PhosphoSite; Q7LBR1; -.
DR DMDM; 73917735; -.
DR PeptideAtlas; Q7LBR1; -.
DR PRIDE; Q7LBR1; -.
DR DNASU; 57132; -.
DR Ensembl; ENST00000526991; ENSP00000432279; ENSG00000255112.
DR GeneID; 57132; -.
DR KEGG; hsa:57132; -.
DR UCSC; uc002kqe.3; human.
DR CTD; 57132; -.
DR GeneCards; GC18P011851; -.
DR HGNC; HGNC:24287; CHMP1B.
DR MIM; 606486; gene.
DR neXtProt; NX_Q7LBR1; -.
DR PharmGKB; PA142672110; -.
DR HOVERGEN; HBG080200; -.
DR KO; K12197; -.
DR OMA; RSAKKCD; -.
DR OrthoDB; EOG7BP843; -.
DR EvolutionaryTrace; Q7LBR1; -.
DR GeneWiki; CHMP1B; -.
DR GenomeRNAi; 57132; -.
DR NextBio; 63047; -.
DR PRO; PR:Q7LBR1; -.
DR ArrayExpress; Q7LBR1; -.
DR Bgee; Q7LBR1; -.
DR CleanEx; HS_C18orf2; -.
DR CleanEx; HS_CHMP1B; -.
DR Genevestigator; Q7LBR1; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000910; P:cytokinesis; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR005024; Snf7.
DR Pfam; PF03357; Snf7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Coiled coil;
KW Complete proteome; Cytoplasm; Endosome; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1 199 Charged multivesicular body protein 1b.
FT /FTId=PRO_0000211454.
FT REGION 132 156 Interaction with IST1.
FT REGION 174 199 Interaction with SPAST.
FT REGION 180 199 Interaction with VTA1.
FT REGION 180 196 Interaction with VPS4A, MITD1 and STAMBP.
FT REGION 183 199 Interaction with VPS4B.
FT COILED 26 48 Potential.
FT COILED 178 199 Potential.
FT MOTIF 186 196 MIT-interacting motif.
FT MUTAGEN 158 159 DE->AA: Diminishes interaction with
FT VPS4B.
FT MUTAGEN 178 178 T->R: Abolishes interaction with SPAST
FT and no effect on interaction with VPS4A;
FT when associated with R-181 and R-184.
FT MUTAGEN 181 181 A->R: Abolishes interaction with SPAScT
FT and no effect on interaction with VPS4A;
FT when associated with R-178 and R-184.
FT MUTAGEN 184 184 E->A: Decreases interaction with SPAST.
FT MUTAGEN 184 184 E->R: Abolishes interaction with SPAST
FT and no effect on interaction with VPS4A;
FT when associated with R-178 and R-181.
FT MUTAGEN 188 188 L->A: Abolishes interaction with SPAST
FT and VPS4A; when associated with A-192.
FT MUTAGEN 192 192 L->A: Abolishes interaction with SPAST
FT and VPS4A; when associated with A-188.
FT MUTAGEN 192 192 L->A: Abolishes interaction with VPS4B.
FT MUTAGEN 195 195 L->A: Abolishes interaction with VPS4B.
FT HELIX 151 159
FT HELIX 174 193
SQ SEQUENCE 199 AA; 22109 MW; 8071E94D20D85AB5 CRC64;
MSNMEKHLFN LKFAAKELSR SAKKCDKEEK AEKAKIKKAI QKGNMEVARI HAENAIRQKN
QAVNFLRMSA RVDAVAARVQ TAVTMGKVTK SMAGVVKSMD ATLKTMNLEK ISALMDKFEH
QFETLDVQTQ QMEDTMSSTT TLTTPQNQVD MLLQEMADEA GLDLNMELPQ GQTGSVGTSV
ASAEQDELSQ RLARLRDQV
//
ID CHM1B_HUMAN Reviewed; 199 AA.
AC Q7LBR1; Q96E89; Q9HD41;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 1.
DT 22-JAN-2014, entry version 79.
DE RecName: Full=Charged multivesicular body protein 1b;
DE AltName: Full=CHMP1.5;
DE AltName: Full=Chromatin-modifying protein 1b;
DE Short=CHMP1b;
DE AltName: Full=Vacuolar protein sorting-associated protein 46-2;
DE Short=Vps46-2;
DE Short=hVps46-2;
GN Name=CHMP1B; Synonyms=C18orf2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=11474171;
RA Vuoristo J.T., Berrettini W.H., Ala-Kokko L.;
RT "C18orf2, a novel, highly conserved intronless gene within intron 5 of
RT the GNAL gene on chromosome 18p11.";
RL Cytogenet. Cell Genet. 93:19-22(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11559747;
RA Stauffer D.R., Howard T.L., Nyun T., Hollenberg S.M.;
RT "CHMP1 is a novel nuclear matrix protein affecting chromatin structure
RT and cell-cycle progression.";
RL J. Cell Sci. 114:2383-2393(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Melanoma, 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH CHMP1A; 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 [5]
RP FUNCTION IN HIV-1 BUDDING, AND INTERACTION WITH CHMP1A; CHMP2A AND
RP 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
RT sorting factors by using alternative adaptor proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003).
RN [6]
RP ERRATUM.
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 [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SPAST.
RX PubMed=15537668; DOI=10.1093/hmg/ddi003;
RA Reid E., Connell J.W., Edwards T.L., Duley S., Brown S.E.,
RA Sanderson C.M.;
RT "The hereditary spastic paraplegia protein spastin interacts with the
RT ESCRT-III complex-associated endosomal protein CHMP1B.";
RL Hum. Mol. Genet. 14:19-38(2005).
RN [8]
RP INTERACTION WITH VPS4A.
RX PubMed=16174732; DOI=10.1073/pnas.0502165102;
RA Scott A., Gaspar J., Stuchell-Brereton M.D., Alam S.L., Skalicky J.J.,
RA Sundquist W.I.;
RT "Structure and ESCRT-III protein interactions of the MIT domain of
RT human VPS4A.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13813-13818(2005).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH STAMBP.
RX PubMed=16730941; DOI=10.1016/j.ygeno.2006.04.003;
RA Tsang H.T.H., Connell J.W., Brown S.E., Thompson A., Reid E.,
RA Sanderson C.M.;
RT "A systematic analysis of human CHMP protein interactions: additional
RT MIT domain-containing proteins bind to multiple components of the
RT human ESCRT III complex.";
RL Genomics 88:333-346(2006).
RN [10]
RP INTERACTION WITH VPS4A AND VPS4B, AND MUTAGENESIS OF LEU-192 AND
RP LEU-195.
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 [11]
RP INTERACTION WITH VTA1 AND VPS4B, AND MUTAGENESIS OF 158-ASP-GLU-159.
RX PubMed=18385515; DOI=10.1091/mbc.E07-12-1263;
RA Shim S., Merrill S.A., Hanson P.I.;
RT "Novel interactions of ESCRT-III with LIP5 and VPS4 and their
RT implications for ESCRT-III disassembly.";
RL Mol. Biol. Cell 19:2661-2672(2008).
RN [12]
RP INTERACTION WITH IST1; VTA1; VPS4A; MITD1 AND STAMBP.
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, AND INTERACTION WITH IST1.
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.,
RA Buerckstuemmer T., 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 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
RT interferon-induced gene ISG15.";
RL J. Virol. 85:7153-7161(2011).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 145-194 IN COMPLEX WITH
RP SPAST, SUBCELLULAR LOCATION, INTERACTION WITH VPS4A, AND MUTAGENESIS
RP OF THR-178; ALA-181; GLU-184; LEU-188 AND LEU-192.
RX PubMed=18997780; DOI=10.1038/nsmb.1512;
RA Yang D., Rismanchi N., Renvoise B., Lippincott-Schwartz J.,
RA Blackstone C., Hurley J.H.;
RT "Structural basis for midbody targeting of spastin by the ESCRT-III
RT protein CHMP1B.";
RL Nat. Struct. Mol. Biol. 15:1278-1286(2008).
CC -!- FUNCTION: Probable peripherally associated component of the
CC endosomal sorting required for transport complex III (ESCRT-III)
CC which is involved in multivesicular bodies (MVBs) formation and
CC sorting of endosomal cargo proteins into MVBs. MVBs contain
CC intraluminal vesicles (ILVs) that are generated by invagination
CC and scission from the limiting membrane of the endosome and mostly
CC are delivered to lysosomes enabling degradation of membrane
CC proteins, such as stimulated growth factor receptors, lysosomal
CC enzymes and lipids. The MVB pathway appears to require the
CC sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-
CC III proteins mostly dissociate from the invaginating membrane
CC before the ILV is released. The ESCRT machinery also functions in
CC topologically equivalent membrane fission events, such as the
CC terminal stages of cytokinesis and the budding of enveloped
CC viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are
CC believed to mediate the necessary vesicle extrusion and/or
CC membrane fission activities, possibly in conjunction with the AAA
CC ATPase VPS4. Involved in cytokinesis. Involved in recruiting VPS4A
CC and/or VPS4B and SPAST to the midbody of dividing cells. Involved
CC in HIV-1 p6- and p9-dependent virus release.
CC -!- SUBUNIT: Probable peripherally associated component of the
CC endosomal sorting required for transport complex III (ESCRT-III).
CC ESCRT-III components are thought to multimerize to form a flat
CC lattice on the perimeter membrane of the endosome. Several
CC assembly forms of ESCRT-III may exist that interact and act
CC sequentally. Interacts with CHMP1A. Interacts with VTA1; the
CC interaction probably involves the open conformation of CHMP1B.
CC Interacts with CHMP2A. Interacts with VPS4A; the interaction is
CC direct. Interacts with VPS4B; the interaction is direct. Interacts
CC with SPAST (via MIT domain); the interaction is direct. Interacts
CC with IST1. Interacts with MITD1. Interacts with STAMBP.
CC -!- INTERACTION:
CC O95630:STAMBP; NbExp=5; IntAct=EBI-2118090, EBI-396676;
CC P40818:USP8; NbExp=5; IntAct=EBI-2118090, EBI-1050865;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Endosome. Late endosome
CC membrane; Peripheral membrane protein (Probable). Note=Localizes
CC to the midbody of dividing cells, colocalizing with CEP55 and
CC CHMP5. Localized at the periphery of the Fleming body.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in pancreas,
CC kidney, skeletal muscle, liver, lung, placenta and brain.
CC -!- SIMILARITY: Belongs to the SNF7 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG01449.1; Type=Erroneous initiation;
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DR EMBL; AF306520; AAL48200.1; -; Genomic_DNA.
DR EMBL; AF281064; AAG01449.1; ALT_INIT; mRNA.
DR EMBL; BC065933; AAH65933.1; -; mRNA.
DR EMBL; BC012733; AAH12733.3; -; mRNA.
DR RefSeq; NP_065145.2; NM_020412.4.
DR UniGene; Hs.656244; -.
DR PDB; 3EAB; X-ray; 2.50 A; G/H/I/J/K/L=148-197.
DR PDBsum; 3EAB; -.
DR ProteinModelPortal; Q7LBR1; -.
DR SMR; Q7LBR1; 148-197.
DR DIP; DIP-48534N; -.
DR IntAct; Q7LBR1; 9.
DR MINT; MINT-6946813; -.
DR PhosphoSite; Q7LBR1; -.
DR DMDM; 73917735; -.
DR PeptideAtlas; Q7LBR1; -.
DR PRIDE; Q7LBR1; -.
DR DNASU; 57132; -.
DR Ensembl; ENST00000526991; ENSP00000432279; ENSG00000255112.
DR GeneID; 57132; -.
DR KEGG; hsa:57132; -.
DR UCSC; uc002kqe.3; human.
DR CTD; 57132; -.
DR GeneCards; GC18P011851; -.
DR HGNC; HGNC:24287; CHMP1B.
DR MIM; 606486; gene.
DR neXtProt; NX_Q7LBR1; -.
DR PharmGKB; PA142672110; -.
DR HOVERGEN; HBG080200; -.
DR KO; K12197; -.
DR OMA; RSAKKCD; -.
DR OrthoDB; EOG7BP843; -.
DR EvolutionaryTrace; Q7LBR1; -.
DR GeneWiki; CHMP1B; -.
DR GenomeRNAi; 57132; -.
DR NextBio; 63047; -.
DR PRO; PR:Q7LBR1; -.
DR ArrayExpress; Q7LBR1; -.
DR Bgee; Q7LBR1; -.
DR CleanEx; HS_C18orf2; -.
DR CleanEx; HS_CHMP1B; -.
DR Genevestigator; Q7LBR1; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000910; P:cytokinesis; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR005024; Snf7.
DR Pfam; PF03357; Snf7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Coiled coil;
KW Complete proteome; Cytoplasm; Endosome; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1 199 Charged multivesicular body protein 1b.
FT /FTId=PRO_0000211454.
FT REGION 132 156 Interaction with IST1.
FT REGION 174 199 Interaction with SPAST.
FT REGION 180 199 Interaction with VTA1.
FT REGION 180 196 Interaction with VPS4A, MITD1 and STAMBP.
FT REGION 183 199 Interaction with VPS4B.
FT COILED 26 48 Potential.
FT COILED 178 199 Potential.
FT MOTIF 186 196 MIT-interacting motif.
FT MUTAGEN 158 159 DE->AA: Diminishes interaction with
FT VPS4B.
FT MUTAGEN 178 178 T->R: Abolishes interaction with SPAST
FT and no effect on interaction with VPS4A;
FT when associated with R-181 and R-184.
FT MUTAGEN 181 181 A->R: Abolishes interaction with SPAScT
FT and no effect on interaction with VPS4A;
FT when associated with R-178 and R-184.
FT MUTAGEN 184 184 E->A: Decreases interaction with SPAST.
FT MUTAGEN 184 184 E->R: Abolishes interaction with SPAST
FT and no effect on interaction with VPS4A;
FT when associated with R-178 and R-181.
FT MUTAGEN 188 188 L->A: Abolishes interaction with SPAST
FT and VPS4A; when associated with A-192.
FT MUTAGEN 192 192 L->A: Abolishes interaction with SPAST
FT and VPS4A; when associated with A-188.
FT MUTAGEN 192 192 L->A: Abolishes interaction with VPS4B.
FT MUTAGEN 195 195 L->A: Abolishes interaction with VPS4B.
FT HELIX 151 159
FT HELIX 174 193
SQ SEQUENCE 199 AA; 22109 MW; 8071E94D20D85AB5 CRC64;
MSNMEKHLFN LKFAAKELSR SAKKCDKEEK AEKAKIKKAI QKGNMEVARI HAENAIRQKN
QAVNFLRMSA RVDAVAARVQ TAVTMGKVTK SMAGVVKSMD ATLKTMNLEK ISALMDKFEH
QFETLDVQTQ QMEDTMSSTT TLTTPQNQVD MLLQEMADEA GLDLNMELPQ GQTGSVGTSV
ASAEQDELSQ RLARLRDQV
//
MIM
606486
*RECORD*
*FIELD* NO
606486
*FIELD* TI
*606486 CHMP FAMILY, MEMBER 1B; CHMP1B
;;CHROMATIN-MODIFYING PROTEIN 1B;;
CHARGED MULTIVESICULAR BODY PROTEIN 1B;;
read moreCHROMOSOME 18 OPEN READING FRAME 2; C18ORF2
*FIELD* TX
DESCRIPTION
CHMP1B belongs to the chromatin-modifying protein/charged multivesicular
body protein (CHMP) family. These proteins are components of ESCRT-III
(endosomal sorting complex required for transport III), a complex
involved in degradation of surface receptor proteins and formation of
endocytic multivesicular bodies (MVBs). Some CHMPs have both nuclear and
cytoplasmic/vesicular distributions, and one such CHMP, CHMP1A (164010),
is required for both MVB formation and regulation of cell cycle
progression (Tsang et al., 2006).
CLONING
By in silico gene trapping, Vuoristo et al. (2001) identified a novel
gene, designated C18ORF2, embedded in exon 5 of the GNAL gene (139312)
on chromosome 18p11. The C18ORF2 gene encodes a deduced 199-amino acid
protein with a predicted molecular mass of 22.1 kD. The protein is
highly conserved across several species and shares 55% sequence identity
with the PRSM1 gene (CHMP1A). RT-PCR analysis detected moderate
expression of C18ORF2 in all tissues tested.
GENE FUNCTION
Scott et al. (2005) found that the C-terminal half of the endosomal
sorting complex protein CHMP1B bound the microtubule-interacting and
transport (MIT) domain of VPS4A (609982).
Using a yeast 2-hybrid approach, Reid et al. (2005) identified CHMP1B as
a binding partner of spastin (SPAST; 604277), mutations in which are the
most common cause of hereditary spastic paraplegia, which results in
degeneration of long axons. CHMP1B and spastin proteins showed clear
cytoplasmic colocalization in transfected cells; CHMP1B and spastin
proteins interacted specifically in vitro and in vivo in complementation
assays, and spastin coimmunoprecipitated with CHMP1B. The interaction
was mediated by a region of spastin lying between residues 80 and 196
and containing an MIT domain. Expression of epitope-tagged CHMP1B in
mammalian cells prevented the development of the abnormal microtubule
phenotype associated with expression of ATPase-defective spastin. The
authors suggested a role for spastin in intracellular membrane traffic
events, and proposed that defects in intracellular membrane traffic may
be a significant cause of motor neuron pathology.
Tsang et al. (2006) performed a systematic yeast 2-hybrid analysis of
human ESCRT-III components, including CHMP1B. The novel CHMP1B-binding
partners included SSRP1 (604328), which may be involved in chromatin
remodeling, TRAF4AF1, which may be involved in signal transduction, and
AMSH (606247). Coimmunoprecipitation assays confirmed the interaction
between CHMP1B and AMSH, and the 2 proteins partially colocalized with
M6PR (154540) on late endosomal membranes.
GENE STRUCTURE
Vuoristo et al. (2001) determined that the C18ORF2 gene is intronless.
MAPPING
By genomic sequence analysis, Vuoristo et al. (2001) identified the
C18ORF2 gene within intron 5 of the GNAL gene (139312) on chromosome
18p11.
*FIELD* RF
1. Reid, E.; Connell, J.; Edwards, T. L.; Duley, S.; Brown, S. E.;
Sanderson, C. M.: The hereditary spastic paraplegia protein spastin
interacts with the ESCRT-III complex-associated endosomal protein
CHMP1B. Hum. Molec. Genet. 14: 19-38, 2005.
2. Scott, A.; Gaspar, J.; Stuchell-Brereton, M. D.; Alam, S. L.; Skalicky,
J. J.; Sundquist, W. I.: Structure and ESCRT-III protein interactions
of the MIT domain of human VPS4A. Proc. Nat. Acad. Sci. 102: 13813-13818,
2005.
3. Tsang, H. T. H.; Connell, J. W.; Brown, S. E.; Thompson, A.; Reid,
E.; Sanderson, C. M.: A systematic analysis of human CHMP protein
interactions: additional MIT domain-containing proteins bind to multiple
components of the human ESCRT III complex. Genomics 88: 333-346,
2006.
4. Vuoristo, J. T.; Berrettini, W. H.; Ala-Kokko, L.: C18orf2, a
novel, highly conserved intronless gene within intron 5 of the GNAL
gene on chromosome 18p11. Cytogenet. Cell Genet. 93: 19-22, 2001.
*FIELD* CN
George E. Tiller - updated: 10/31/2007
Patricia A. Hartz - updated: 3/27/2007
Patricia A. Hartz - updated: 3/20/2006
*FIELD* CD
Carol A. Bocchini: 11/25/2001
*FIELD* ED
terry: 03/10/2011
wwang: 3/2/2011
mgross: 9/4/2009
alopez: 11/2/2007
terry: 10/31/2007
mgross: 4/2/2007
mgross: 3/28/2007
mgross: 3/27/2007
mgross: 4/13/2006
mgross: 3/20/2006
cwells: 11/26/2001
carol: 11/25/2001
*RECORD*
*FIELD* NO
606486
*FIELD* TI
*606486 CHMP FAMILY, MEMBER 1B; CHMP1B
;;CHROMATIN-MODIFYING PROTEIN 1B;;
CHARGED MULTIVESICULAR BODY PROTEIN 1B;;
read moreCHROMOSOME 18 OPEN READING FRAME 2; C18ORF2
*FIELD* TX
DESCRIPTION
CHMP1B belongs to the chromatin-modifying protein/charged multivesicular
body protein (CHMP) family. These proteins are components of ESCRT-III
(endosomal sorting complex required for transport III), a complex
involved in degradation of surface receptor proteins and formation of
endocytic multivesicular bodies (MVBs). Some CHMPs have both nuclear and
cytoplasmic/vesicular distributions, and one such CHMP, CHMP1A (164010),
is required for both MVB formation and regulation of cell cycle
progression (Tsang et al., 2006).
CLONING
By in silico gene trapping, Vuoristo et al. (2001) identified a novel
gene, designated C18ORF2, embedded in exon 5 of the GNAL gene (139312)
on chromosome 18p11. The C18ORF2 gene encodes a deduced 199-amino acid
protein with a predicted molecular mass of 22.1 kD. The protein is
highly conserved across several species and shares 55% sequence identity
with the PRSM1 gene (CHMP1A). RT-PCR analysis detected moderate
expression of C18ORF2 in all tissues tested.
GENE FUNCTION
Scott et al. (2005) found that the C-terminal half of the endosomal
sorting complex protein CHMP1B bound the microtubule-interacting and
transport (MIT) domain of VPS4A (609982).
Using a yeast 2-hybrid approach, Reid et al. (2005) identified CHMP1B as
a binding partner of spastin (SPAST; 604277), mutations in which are the
most common cause of hereditary spastic paraplegia, which results in
degeneration of long axons. CHMP1B and spastin proteins showed clear
cytoplasmic colocalization in transfected cells; CHMP1B and spastin
proteins interacted specifically in vitro and in vivo in complementation
assays, and spastin coimmunoprecipitated with CHMP1B. The interaction
was mediated by a region of spastin lying between residues 80 and 196
and containing an MIT domain. Expression of epitope-tagged CHMP1B in
mammalian cells prevented the development of the abnormal microtubule
phenotype associated with expression of ATPase-defective spastin. The
authors suggested a role for spastin in intracellular membrane traffic
events, and proposed that defects in intracellular membrane traffic may
be a significant cause of motor neuron pathology.
Tsang et al. (2006) performed a systematic yeast 2-hybrid analysis of
human ESCRT-III components, including CHMP1B. The novel CHMP1B-binding
partners included SSRP1 (604328), which may be involved in chromatin
remodeling, TRAF4AF1, which may be involved in signal transduction, and
AMSH (606247). Coimmunoprecipitation assays confirmed the interaction
between CHMP1B and AMSH, and the 2 proteins partially colocalized with
M6PR (154540) on late endosomal membranes.
GENE STRUCTURE
Vuoristo et al. (2001) determined that the C18ORF2 gene is intronless.
MAPPING
By genomic sequence analysis, Vuoristo et al. (2001) identified the
C18ORF2 gene within intron 5 of the GNAL gene (139312) on chromosome
18p11.
*FIELD* RF
1. Reid, E.; Connell, J.; Edwards, T. L.; Duley, S.; Brown, S. E.;
Sanderson, C. M.: The hereditary spastic paraplegia protein spastin
interacts with the ESCRT-III complex-associated endosomal protein
CHMP1B. Hum. Molec. Genet. 14: 19-38, 2005.
2. Scott, A.; Gaspar, J.; Stuchell-Brereton, M. D.; Alam, S. L.; Skalicky,
J. J.; Sundquist, W. I.: Structure and ESCRT-III protein interactions
of the MIT domain of human VPS4A. Proc. Nat. Acad. Sci. 102: 13813-13818,
2005.
3. Tsang, H. T. H.; Connell, J. W.; Brown, S. E.; Thompson, A.; Reid,
E.; Sanderson, C. M.: A systematic analysis of human CHMP protein
interactions: additional MIT domain-containing proteins bind to multiple
components of the human ESCRT III complex. Genomics 88: 333-346,
2006.
4. Vuoristo, J. T.; Berrettini, W. H.; Ala-Kokko, L.: C18orf2, a
novel, highly conserved intronless gene within intron 5 of the GNAL
gene on chromosome 18p11. Cytogenet. Cell Genet. 93: 19-22, 2001.
*FIELD* CN
George E. Tiller - updated: 10/31/2007
Patricia A. Hartz - updated: 3/27/2007
Patricia A. Hartz - updated: 3/20/2006
*FIELD* CD
Carol A. Bocchini: 11/25/2001
*FIELD* ED
terry: 03/10/2011
wwang: 3/2/2011
mgross: 9/4/2009
alopez: 11/2/2007
terry: 10/31/2007
mgross: 4/2/2007
mgross: 3/28/2007
mgross: 3/27/2007
mgross: 4/13/2006
mgross: 3/20/2006
cwells: 11/26/2001
carol: 11/25/2001