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Q8BJF9

- CHM2B_MOUSE

UniProt

Q8BJF9 - CHM2B_MOUSE

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Protein

Charged multivesicular body protein 2b

Gene
Chmp2b
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

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.

GO - Biological processi

  1. protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_198518. Endosomal Sorting Complex Required For Transport (ESCRT).

Names & Taxonomyi

Protein namesi
Recommended name:
Charged multivesicular body protein 2b
Alternative name(s):
Chromatin-modifying protein 2b
Short name:
CHMP2b
Gene namesi
Name:Chmp2b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 16

Organism-specific databases

MGIiMGI:1916192. Chmp2b.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB-SubCell
  2. late endosome membrane Source: UniProtKB-SubCell
  3. mitochondrion Source: Ensembl
  4. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 213212Charged multivesicular body protein 2bPRO_0000211470Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei199 – 1991Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8BJF9.
PaxDbiQ8BJF9.
PRIDEiQ8BJF9.

PTM databases

PhosphoSiteiQ8BJF9.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiQ8BJF9.
CleanExiMM_CHMP2B.
GenevestigatoriQ8BJF9.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

IntActiQ8BJF9. 1 interaction.
STRINGi10090.ENSMUSP00000004965.

Structurei

3D structure databases

ProteinModelPortaliQ8BJF9.
SMRiQ8BJF9. Positions 7-141.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili25 – 5531 Reviewed predictionAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi201 – 21111MIT-interacting motifAdd
BLAST

Sequence similaritiesi

Belongs to the SNF7 family.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG268821.
GeneTreeiENSGT00550000074737.
HOGENOMiHOG000177218.
HOVERGENiHBG102628.
InParanoidiQ8BJF9.
KOiK12192.
OMAiKTMQDFQ.
OrthoDBiEOG79GT8Q.
PhylomeDBiQ8BJF9.
TreeFamiTF314163.

Family and domain databases

InterProiIPR005024. Snf7.
[Graphical view]
PfamiPF03357. Snf7. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8BJF9-1 [UniParc]FASTAAdd to Basket

« Hide

MASLFKKKTV DDVIKEQNRE LRGTQRAIIR DRAALEKQEK QLELEIKKMA    50
KIGNKEACRV LAKQLVHLRK QKTRTFAVSS KVTSMSTQTK VMNSQMKMAG 100
AMSTTAKTMQ AVNKKMDPQK TLQTMQNFQK ENMKMEMTEE MINDTLDDIF 150
DGSDDEEESQ DIVNQVLDEI GIEISGKMAK APSAARSLPS ASTSKATISD 200
EEIERQLKAL GVD 213
Length:213
Mass (Da):23,935
Last modified:March 1, 2003 - v1
Checksum:iAC5B40ED59E4489B
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti131 – 1311E → D in BAB23339. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK004506 mRNA. Translation: BAB23339.1.
AK084111 mRNA. Translation: BAC39118.1.
BC042626 mRNA. Translation: AAH42626.1.
BC055809 mRNA. Translation: AAH55809.1.
CCDSiCCDS28269.1.
RefSeqiNP_081155.1. NM_026879.2.
UniGeneiMm.432944.

Genome annotation databases

EnsembliENSMUST00000004965; ENSMUSP00000004965; ENSMUSG00000004843.
GeneIDi68942.
KEGGimmu:68942.
UCSCiuc007zqj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK004506 mRNA. Translation: BAB23339.1 .
AK084111 mRNA. Translation: BAC39118.1 .
BC042626 mRNA. Translation: AAH42626.1 .
BC055809 mRNA. Translation: AAH55809.1 .
CCDSi CCDS28269.1.
RefSeqi NP_081155.1. NM_026879.2.
UniGenei Mm.432944.

3D structure databases

ProteinModelPortali Q8BJF9.
SMRi Q8BJF9. Positions 7-141.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8BJF9. 1 interaction.
STRINGi 10090.ENSMUSP00000004965.

PTM databases

PhosphoSitei Q8BJF9.

Proteomic databases

MaxQBi Q8BJF9.
PaxDbi Q8BJF9.
PRIDEi Q8BJF9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000004965 ; ENSMUSP00000004965 ; ENSMUSG00000004843 .
GeneIDi 68942.
KEGGi mmu:68942.
UCSCi uc007zqj.1. mouse.

Organism-specific databases

CTDi 25978.
MGIi MGI:1916192. Chmp2b.

Phylogenomic databases

eggNOGi NOG268821.
GeneTreei ENSGT00550000074737.
HOGENOMi HOG000177218.
HOVERGENi HBG102628.
InParanoidi Q8BJF9.
KOi K12192.
OMAi KTMQDFQ.
OrthoDBi EOG79GT8Q.
PhylomeDBi Q8BJF9.
TreeFami TF314163.

Enzyme and pathway databases

Reactomei REACT_198518. Endosomal Sorting Complex Required For Transport (ESCRT).

Miscellaneous databases

ChiTaRSi CHMP2B. mouse.
NextBioi 328237.
PROi Q8BJF9.
SOURCEi Search...

Gene expression databases

Bgeei Q8BJF9.
CleanExi MM_CHMP2B.
Genevestigatori Q8BJF9.

Family and domain databases

InterProi IPR005024. Snf7.
[Graphical view ]
Pfami PF03357. Snf7. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6 and Czech II.
    Tissue: Brain and Mammary tumor.
  3. Cited for: TISSUE SPECIFICITY.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCHM2B_MOUSE
AccessioniPrimary (citable) accession number: Q8BJF9
Secondary accession number(s): Q80UZ4, Q9CT65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: March 1, 2003
Last modified: September 3, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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