CH1B1_MOUSE
ID CH1B1_MOUSE Reviewed; 199 AA.
AC Q99LU0; Q3UB77; Q9CXR5;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Charged multivesicular body protein 1b-1;
DE AltName: Full=Chromatin-modifying protein 1b-1;
DE Short=CHMP1b-1;
GN Name=Chmp1b1; Synonyms=Chmp1b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP PROTEIN SEQUENCE OF 105-110, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
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. 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 and SPAST to
CC the midbody of dividing cells (By similarity). {ECO:0000250}.
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. Interacts with CHMP1A.
CC Interacts with VTA1; the interaction probably involves the open
CC conformation of CHMP1B. Interacts with CHMP2A. Interacts with VPS4A;
CC the interaction is direct. Interacts with VPS4B; the interaction is
CC direct. Interacts with SPAST (via MIT domain); the interaction is
CC direct. Interacts with IST1. Interacts with MITD1. Interacts with
CC STAMBP (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Endosome
CC {ECO:0000250}. Late endosome membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Note=Localizes to the midbody of
CC dividing cells, colocalizing with CEP55 and CHMP5. Localized at the
CC periphery of the Fleming body (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR EMBL; AK014091; BAB29150.2; -; mRNA.
DR EMBL; AK151071; BAE30087.1; -; mRNA.
DR EMBL; CT010307; CAJ18515.1; -; mRNA.
DR EMBL; BC002229; AAH02229.1; -; mRNA.
DR CCDS; CCDS84391.1; -.
DR RefSeq; NP_077152.1; NM_024190.2.
DR AlphaFoldDB; Q99LU0; -.
DR SMR; Q99LU0; -.
DR BioGRID; 211913; 2.
DR ComplexPortal; CPX-332; ESCRT-III complex, variant Chmp1b1.
DR IntAct; Q99LU0; 1.
DR iPTMnet; Q99LU0; -.
DR PhosphoSitePlus; Q99LU0; -.
DR EPD; Q99LU0; -.
DR MaxQB; Q99LU0; -.
DR PRIDE; Q99LU0; -.
DR ProteomicsDB; 281600; -.
DR Antibodypedia; 54046; 117 antibodies from 23 providers.
DR DNASU; 67064; -.
DR Ensembl; ENSMUST00000210564; ENSMUSP00000147285; ENSMUSG00000109901.
DR GeneID; 67064; -.
DR KEGG; mmu:67064; -.
DR UCSC; uc008flu.2; mouse.
DR CTD; 57132; -.
DR MGI; MGI:1914314; Chmp1b.
DR VEuPathDB; HostDB:ENSMUSG00000109901; -.
DR GeneTree; ENSGT00950000182832; -.
DR InParanoid; Q99LU0; -.
DR OMA; MMGEQTS; -.
DR OrthoDB; 1441797at2759; -.
DR PhylomeDB; Q99LU0; -.
DR BioGRID-ORCS; 67064; 0 hits in 20 CRISPR screens.
DR PRO; PR:Q99LU0; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q99LU0; protein.
DR Bgee; ENSMUSG00000109901; Expressed in urinary bladder urothelium and 244 other tissues.
DR GO; GO:1904930; C:amphisome membrane; ISO:MGI.
DR GO; GO:0000421; C:autophagosome membrane; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; ISO:MGI.
DR GO; GO:0000815; C:ESCRT III complex; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0005828; C:kinetochore microtubule; ISO:MGI.
DR GO; GO:0005765; C:lysosomal membrane; ISO:MGI.
DR GO; GO:0030117; C:membrane coat; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR GO; GO:0032585; C:multivesicular body membrane; ISO:MGI.
DR GO; GO:0005643; C:nuclear pore; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0090541; F:MIT domain binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0097352; P:autophagosome maturation; ISO:MGI.
DR GO; GO:0006914; P:autophagy; ISO:MGI.
DR GO; GO:0051301; P:cell division; ISO:MGI.
DR GO; GO:0032509; P:endosome transport via multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:0045184; P:establishment of protein localization; ISO:MGI.
DR GO; GO:1902774; P:late endosome to lysosome transport; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISO:MGI.
DR GO; GO:0036258; P:multivesicular body assembly; IC:ComplexPortal.
DR GO; GO:0071985; P:multivesicular body sorting pathway; ISO:MGI.
DR GO; GO:0061763; P:multivesicular body-lysosome fusion; IC:ComplexPortal.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0031468; P:nuclear membrane reassembly; ISO:MGI.
DR GO; GO:0006997; P:nucleus organization; ISO:MGI.
DR GO; GO:0001778; P:plasma membrane repair; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR GO; GO:0010824; P:regulation of centrosome duplication; ISO:MGI.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; ISO:MGI.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; ISO:MGI.
DR GO; GO:0051469; P:vesicle fusion with vacuole; IC:ComplexPortal.
DR GO; GO:0046761; P:viral budding from plasma membrane; ISO:MGI.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; ISO:MGI.
DR InterPro; IPR005024; Snf7_fam.
DR PANTHER; PTHR10476; PTHR10476; 1.
DR Pfam; PF03357; Snf7; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Endosome; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..199
FT /note="Charged multivesicular body protein 1b-1"
FT /id="PRO_0000211455"
FT REGION 132..156
FT /note="Interaction with IST1"
FT /evidence="ECO:0000250"
FT REGION 167..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..199
FT /note="Interaction with SPAST"
FT /evidence="ECO:0000250"
FT REGION 180..199
FT /note="Interaction with VTA1"
FT /evidence="ECO:0000250"
FT REGION 180..196
FT /note="Interaction with VPS4A, MITD1 and STAMBP"
FT /evidence="ECO:0000250"
FT REGION 183..199
FT /note="Interaction with VPS4B"
FT /evidence="ECO:0000250"
FT COILED 10..48
FT /evidence="ECO:0000255"
FT COILED 178..199
FT /evidence="ECO:0000255"
FT MOTIF 186..196
FT /note="MIT-interacting motif"
FT COMPBIAS 168..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 185
FT /note="Q -> A (in Ref. 1; BAB29150)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 199 AA; 22124 MW; 51E3096E0FBC90D8 CRC64;
MSNMEKHLFN LKFAAKELNR SSKKCDKEEK AEKAKIKKAI QKGNMEVARI HAENAIRQKN
QGVNFLRMSA RVDAVAARVQ TAVTMGKVTK SMAGVVKSMD ATLKSMNLEK ISALMDKFEH
QFETLDVQTQ QMEDTMSSTT TLTTPQNQVD MLLQEMADEA GLDLNMELPQ GQTGSVGTSV
ASAEQDELSQ RLARLRDQV
