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Charged multivesicular body protein 4b (Chromatin-modifying protein 4b) (CHMP4b)

 CHM4B_MOUSE             Reviewed;         224 AA.
Q9D8B3; A2AVM1; Q3TXM7; Q91VM7; Q922P1;
01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-2002, sequence version 2.
12-SEP-2018, entry version 141.
RecName: Full=Charged multivesicular body protein 4b;
AltName: Full=Chromatin-modifying protein 4b;
Short=CHMP4b;
Name=Chmp4b;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Small intestine, and Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[5]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND LYS-6, CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Probable core component of the endosomal sorting
required for transport complex III (ESCRT-III) which is involved
in multivesicular bodies (MVBs) formation and sorting of endosomal
cargo proteins into MVBs. MVBs contain intraluminal vesicles
(ILVs) that are generated by invagination and scission from the
limiting membrane of the endosome and mostly are delivered to
lysosomes enabling degradation of membrane proteins, such as
stimulated growth factor receptors, lysosomal enzymes and lipids.
The MVB pathway appears to require the sequential function of
ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly
dissociate from the invaginating membrane before the ILV is
released. The ESCRT machinery also functions in topologically
equivalent membrane fission events, such as the terminal stages of
cytokinesis. Together with SPAST, the ESCRT-III complex promotes
nuclear envelope sealing and mitotic spindle disassembly during
late anaphase. Plays a role in the endosomal sorting pathway.
ESCRT-III proteins are believed to mediate the necessary vesicle
extrusion and/or membrane fission activities, possibly in
conjunction with the AAA ATPase VPS4. When overexpressed,
membrane-assembled circular arrays of CHMP4B filaments can promote
or stabilize negative curvature and outward budding. CHMP4A/B/C
are required for the exosomal release of SDCBP, CD63 and syndecan.
{ECO:0000250|UniProtKB:Q9H444}.
-!- SUBUNIT: Probable core component of the endosomal sorting required
for transport complex III (ESCRT-III). ESCRT-III components are
thought to multimerize to form a flat lattice on the perimeter
membrane of the endosome. Several assembly forms of ESCRT-III may
exist that interact and act sequentially. Interacts with CHMP6 and
CHMP4C. Interacts with PDCD6IP; the interaction is direct.
Interacts with VPS4A; the interaction is direct. Interacts with
VPS4B; the interaction is direct. Interacts with CHMP7. Interacts
with CFTR; the interaction requires misfolded CFTR. Interacts with
PTPN23 (By similarity). {ECO:0000250|UniProtKB:Q9H444}.
-!- INTERACTION:
Q8WUM4:PDCD6IP (xeno); NbExp=2; IntAct=EBI-8322817, EBI-310624;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:Q9H444}. Late endosome membrane
{ECO:0000250|UniProtKB:Q9H444}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q9H444}. Midbody
{ECO:0000250|UniProtKB:Q9H444}. Nucleus envelope
{ECO:0000250|UniProtKB:Q9H444}. Note=Recruited to the nuclear
envelope by CHMP7 during late anaphase. Localizes transiently to
the midbody arms immediately before abscission.
{ECO:0000250|UniProtKB:Q9H444}.
-!- DOMAIN: The acidic C-terminus and the basic N-termminus are
thought to render the protein in a closed, soluble and inactive
conformation through an autoinhibitory intramolecular interaction.
The open and active conformation, which enables membrane binding
and oligomerization, is achieved by interaction with other
cellular binding partners, probably including other ESCRT
components (By similarity). {ECO:0000250}.
-!- PTM: ISGylated. Isgylation weakens its interaction with VPS4A (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH06905.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AK008205; Type=Erroneous termination; Positions=56; Note=Translated as Lys.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AK008205; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK156473; BAE33724.1; -; mRNA.
EMBL; AK159193; BAE34888.1; -; mRNA.
EMBL; AL929557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC006905; AAH06905.1; ALT_INIT; mRNA.
EMBL; BC011429; AAH11429.1; -; mRNA.
EMBL; BC059279; AAH59279.1; -; mRNA.
CCDS; CCDS16938.1; -.
RefSeq; NP_083638.1; NM_029362.3.
UniGene; Mm.262480; -.
ProteinModelPortal; Q9D8B3; -.
SMR; Q9D8B3; -.
BioGrid; 217613; 85.
ComplexPortal; CPX-332; ESCRT-III complex, variant Chmp1b1.
ComplexPortal; CPX-333; ESCRT-III complex, variant Chmp1b2.
DIP; DIP-61322N; -.
IntAct; Q9D8B3; 88.
MINT; Q9D8B3; -.
STRING; 10090.ENSMUSP00000036206; -.
iPTMnet; Q9D8B3; -.
PhosphoSitePlus; Q9D8B3; -.
EPD; Q9D8B3; -.
MaxQB; Q9D8B3; -.
PaxDb; Q9D8B3; -.
PeptideAtlas; Q9D8B3; -.
PRIDE; Q9D8B3; -.
Ensembl; ENSMUST00000044277; ENSMUSP00000036206; ENSMUSG00000038467.
GeneID; 75608; -.
KEGG; mmu:75608; -.
UCSC; uc008njp.1; mouse.
CTD; 128866; -.
MGI; MGI:1922858; Chmp4b.
eggNOG; KOG1656; Eukaryota.
eggNOG; ENOG410YE9I; LUCA.
GeneTree; ENSGT00390000005006; -.
HOGENOM; HOG000209960; -.
HOVERGEN; HBG050928; -.
InParanoid; Q9D8B3; -.
KO; K12194; -.
OMA; MQVNTLE; -.
OrthoDB; EOG091G0V7X; -.
PhylomeDB; Q9D8B3; -.
TreeFam; TF314269; -.
Reactome; R-MMU-1632852; Macroautophagy.
Reactome; R-MMU-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
ChiTaRS; Chmp4b; mouse.
PRO; PR:Q9D8B3; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000038467; Expressed in 294 organ(s), highest expression level in dentate gyrus of hippocampal formation.
CleanEx; MM_CHMP4B; -.
Genevisible; Q9D8B3; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL.
GO; GO:0005768; C:endosome; ISO:MGI.
GO; GO:0000815; C:ESCRT III complex; ISS:UniProtKB.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0030117; C:membrane coat; ISO:MGI.
GO; GO:0030496; C:midbody; ISO:MGI.
GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
GO; GO:0031982; C:vesicle; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0006914; P:autophagy; ISO:MGI.
GO; GO:0000920; P:cell separation after cytokinesis; ISO:MGI.
GO; GO:0010458; P:exit from mitosis; ISS:UniProtKB.
GO; GO:0036438; P:maintenance of lens transparency; ISO:MGI.
GO; GO:0090148; P:membrane fission; ISS:UniProtKB.
GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
GO; GO:0007080; P:mitotic metaphase plate congression; ISO:MGI.
GO; GO:1902902; P:negative regulation of autophagosome assembly; ISO:MGI.
GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
GO; GO:0031468; P:nuclear envelope reassembly; ISS:UniProtKB.
GO; GO:0006997; P:nucleus organization; ISO:MGI.
GO; GO:1902188; P:positive regulation of viral release from host cell; ISO:MGI.
GO; GO:0006620; P:posttranslational protein targeting to endoplasmic reticulum membrane; ISO:MGI.
GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
GO; GO:0010506; P:regulation of autophagy; IMP:ParkinsonsUK-UCL.
GO; GO:0010824; P:regulation of centrosome duplication; ISO:MGI.
GO; GO:1901673; P:regulation of mitotic spindle assembly; ISO:MGI.
GO; GO:0050792; P:regulation of viral process; ISO:MGI.
GO; GO:0090611; P:ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway; ISO:MGI.
GO; GO:0007034; P:vacuolar transport; IEA:InterPro.
GO; GO:0046755; P:viral budding; ISO:MGI.
GO; GO:0039702; P:viral budding via host ESCRT complex; ISO:MGI.
InterPro; IPR005024; Snf7_fam.
Pfam; PF03357; Snf7; 1.
1: Evidence at protein level;
Acetylation; Coiled coil; Complete proteome; Cytoplasm; Endosome;
Membrane; Nucleus; Phosphoprotein; Protein transport;
Reference proteome; Transport; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:23806337}.
CHAIN 2 224 Charged multivesicular body protein 4b.
/FTId=PRO_0000211490.
REGION 2 153 Intramolecular interaction with C-
terminus. {ECO:0000250}.
REGION 154 224 Intramolecular interaction with N-
terminus. {ECO:0000250}.
COILED 23 183 {ECO:0000255}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 6 6 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 114 114 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9H444}.
MOD_RES 184 184 Phosphoserine.
{ECO:0000250|UniProtKB:Q9H444}.
MOD_RES 223 223 Phosphoserine.
{ECO:0000250|UniProtKB:Q9H444}.
CONFLICT 167 167 E -> K (in Ref. 1; AK008205).
{ECO:0000305}.
SEQUENCE 224 AA; 24936 MW; DB1D79C3C9ECCB2F CRC64;
MSVFGKLFGA GGGKAGKGGP TPQEAIQRLR DTEEMLSKKQ EFLEKKIEQE LTAAKKHGTK
NKRAALQALK RKKRYEKQLA QIDGTLSTIE FQREALENAN TNTEVLKNMG YAAKAMKAAH
DNMDIDKVDE LMQDIADQQE LAEEISTAIS KPVGFGEEFD EDELMAELEE LEQEELDKNL
LEISGPETVP LPNVPSVALP SKPAKKKEEE DDDMKELENW AGSM


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