Q8BJF9 (CHM2B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Charged multivesicular body protein 2b

Alternative name(s):
Chromatin-modifying protein 2b
Short name=CHMP2b

Gene names

Name:

Chmp2b

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	213 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

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. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4 By similarity.
Subunit structure	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 sequentally. Interacts with CHMP2A. Interacts with VPS4A. Interacts with VPS4B; the interaction is direct By similarity.
Subcellular location	Cytoplasm › cytosol By similarity. Late endosome membrane; Peripheral membrane protein By similarity.
Tissue specificity	In brain, it is expressed in all neuronal populations with a relatively enhanced expression in the hippocampus, frontal and temporal lobes and in both granule and Purkinje cells of the cerebellum. Not expressed in astrocytes or oligodendrocytes. Ref.3
Sequence similarities	Belongs to the SNF7 family.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cytoplasm Endosome Membrane
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell late endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 213	213	Charged multivesicular body protein 2b		PRO_0000211470
Regions
	Coiled coil	25 – 55	31	Potential
	Motif	201 – 211	11	MIT-interacting motif
Amino acid modifications
	Modified residue	199	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	131	1	E → D in BAB23339. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8BJF9 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: AC5B40ED59E4489B	FASTA	213	23,935
	10 20 30 40 50 60 MASLFKKKTV DDVIKEQNRE LRGTQRAIIR DRAALEKQEK QLELEIKKMA KIGNKEACRV 70 80 90 100 110 120 LAKQLVHLRK QKTRTFAVSS KVTSMSTQTK VMNSQMKMAG AMSTTAKTMQ AVNKKMDPQK 130 140 150 160 170 180 TLQTMQNFQK ENMKMEMTEE MINDTLDDIF DGSDDEEESQ DIVNQVLDEI GIEISGKMAK 190 200 210 APSAARSLPS ASTSKATISD EEIERQLKAL GVD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Spinal ganglion.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6 and Czech II. Tissue: Brain and Mammary tumor.
[3]	"Mutations in the endosomal ESCRTIII-complex subunit CHMP2B in frontotemporal dementia." Skibinski G., Parkinson N.J., Brown J.M., Chakrabarti L., Lloyd S.L., Hummerich H., Nielsen J.E., Hodges J.R., Spillantini M.G., Thusgaard T., Brandner S., Brun A., Rossor M.N., Gade A., Johannsen P., Soerensen S.A., Gydesen S., Fisher E.M.C., Collinge J. Nat. Genet. 37:806-808(2005) [PubMed: 16041373] [Abstract] Cited for: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK004506 mRNA. Translation: BAB23339.1. AK084111 mRNA. Translation: BAC39118.1. BC042626 mRNA. Translation: AAH42626.1. BC055809 mRNA. Translation: AAH55809.1.
IPI	IPI00222386.
RefSeq	NP_081155.1. NM_026879.2.
UniGene	Mm.432944.
3D structure databases
ProteinModelPortal	Q8BJF9.
SMR	Q8BJF9. Positions 4-182.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8BJF9.
PTM databases
PhosphoSite	Q8BJF9.
Proteomic databases
PRIDE	Q8BJF9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000004965; ENSMUSP00000004965; ENSMUSG00000004843.
GeneID	68942.
KEGG	mmu:68942.
UCSC	uc007zqj.1. mouse.
Organism-specific databases
CTD	25978.
MGI	MGI:1916192. Chmp2b.
Phylogenomic databases
eggNOG	roNOG12224.
GeneTree	ENSGT00550000074737.
HOGENOM	HBG464741.
HOVERGEN	HBG102628.
InParanoid	Q8BJF9.
OMA	GNKEACK.
OrthoDB	EOG469QW1.
PhylomeDB	Q8BJF9.
Gene expression databases
ArrayExpress	Q8BJF9.
Bgee	Q8BJF9.
CleanEx	MM_CHMP2B.
Genevestigator	Q8BJF9.
GermOnline	ENSMUSG00000004843. Mus musculus.
Family and domain databases
InterPro	IPR005024. Snf7. [Graphical view]
KO	K12192.
Pfam	PF03357. Snf7. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	328237.
SOURCE	Search...

Entry information

Entry name

CHM2B_MOUSE

Accession

Primary (citable) accession number: Q8BJF9
Secondary accession number(s): Q80UZ4, Q9CT65

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	March 1, 2003
Last modified:	November 16, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program