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Protein

Charged multivesicular body protein 2a

Gene

Chmp2a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 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).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_303468. Lysosome Vesicle Biogenesis.
REACT_334712. Endosomal Sorting Complex Required For Transport (ESCRT).

Names & Taxonomyi

Protein namesi
Recommended name:
Charged multivesicular body protein 2a
Alternative name(s):
Chromatin-modifying protein 2a
Short name:
CHMP2a
Vacuolar protein sorting-associated protein 2
Short name:
mVps2
Gene namesi
Name:Chmp2a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1916203. Chmp2a.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: MGI
  • extracellular exosome Source: MGI
  • late endosome membrane Source: UniProtKB-SubCell
  • membrane Source: MGI
  • membrane coat Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 222222Charged multivesicular body protein 2aPRO_0000211463Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei184 – 1841PhosphoserineBy similarity
Modified residuei185 – 1851PhosphothreonineBy similarity
Modified residuei188 – 1881PhosphoserineBy similarity
Modified residuei190 – 1901PhosphoserineBy similarity
Modified residuei203 – 2031PhosphoserineBy similarity

Post-translational modificationi

ISGylated in a CHMP5-dependent manner. Isgylation weakens and inhibits its interactions with VPS4A and VTA1 respectively (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9DB34.
PaxDbiQ9DB34.
PRIDEiQ9DB34.

Expressioni

Tissue specificityi

Widely expressed. Highly expressed in brain, heart, liver and kidney.1 Publication

Gene expression databases

BgeeiQ9DB34.
CleanExiMM_CHMP2A.
GenevestigatoriQ9DB34.

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. In vitro, heteromerizes with CHMP3 (but not CHMP4) to form helical tubular structures that expose membrane-interacting sites on the outside whereas VPS4B can associate on the inside of the tubule. Interacts with CHMP1B, CHMP2B, CHMP3, CHMP4A, CHMP4B, CHMP4C and CHMP5. Interacts with VPS4A; the interaction is direct. Interacts with VPS4B; the interaction is direct. Interacts with MITD1. Interacts with VTA1; the interaction probably involves the open conformation of CHMP2A (By similarity).By similarity

Protein-protein interaction databases

BioGridi213137. 2 interactions.
IntActiQ9DB34. 1 interaction.
MINTiMINT-4616048.
STRINGi10090.ENSMUSP00000005711.

Structurei

3D structure databases

ProteinModelPortaliQ9DB34.
SMRiQ9DB34. Positions 9-132.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni56 – 222167Interaction with VPS4BBy similarityAdd
BLAST
Regioni217 – 2226Interaction with VTA1By similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili12 – 5342Sequence AnalysisAdd
BLAST
Coiled coili195 – 22228Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi210 – 22011MIT-interacting motifAdd
BLAST

Domaini

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.

Sequence similaritiesi

Belongs to the SNF7 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5491.
GeneTreeiENSGT00550000074737.
HOGENOMiHOG000177218.
HOVERGENiHBG107298.
InParanoidiQ9DB34.
KOiK12191.
OMAiKNGQMGA.
OrthoDBiEOG7992S8.
PhylomeDBiQ9DB34.
TreeFamiTF300118.

Family and domain databases

InterProiIPR005024. Snf7_fam.
[Graphical view]
PfamiPF03357. Snf7. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9DB34-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLLFGRRKT PEELLRQNQR ALNRAMRELD RERQKLETQE KKIIADIKKM
60 70 80 90 100
AKQGQMDAVR IMAKDLVRTR RYVRKFVLMR ANIQAVSLKI QTLKSNNSMA
110 120 130 140 150
QAMKGVTKAM GTMNRQLKLP QIQKIMMEFE RQAEIMDMKE EMMNDAIDDA
160 170 180 190 200
MGDEEDEEES DAVVSQVLDE LGLSLTDELS NLPSTGGSLS VAAGGKKAEA
210 220
TASALADADA DLEERLKNLR RD
Length:222
Mass (Da):25,134
Last modified:June 1, 2001 - v1
Checksum:iF2B86C623832E29E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005267 mRNA. Translation: BAB23919.1.
BC012230 mRNA. Translation: AAH12230.1.
CCDSiCCDS20824.1.
RefSeqiNP_081161.1. NM_026885.3.
XP_006540408.1. XM_006540345.2.
UniGeneiMm.295670.

Genome annotation databases

EnsembliENSMUST00000005711; ENSMUSP00000005711; ENSMUSG00000033916.
GeneIDi68953.
KEGGimmu:68953.
UCSCiuc009ffc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005267 mRNA. Translation: BAB23919.1.
BC012230 mRNA. Translation: AAH12230.1.
CCDSiCCDS20824.1.
RefSeqiNP_081161.1. NM_026885.3.
XP_006540408.1. XM_006540345.2.
UniGeneiMm.295670.

3D structure databases

ProteinModelPortaliQ9DB34.
SMRiQ9DB34. Positions 9-132.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi213137. 2 interactions.
IntActiQ9DB34. 1 interaction.
MINTiMINT-4616048.
STRINGi10090.ENSMUSP00000005711.

Proteomic databases

MaxQBiQ9DB34.
PaxDbiQ9DB34.
PRIDEiQ9DB34.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000005711; ENSMUSP00000005711; ENSMUSG00000033916.
GeneIDi68953.
KEGGimmu:68953.
UCSCiuc009ffc.2. mouse.

Organism-specific databases

CTDi27243.
MGIiMGI:1916203. Chmp2a.

Phylogenomic databases

eggNOGiCOG5491.
GeneTreeiENSGT00550000074737.
HOGENOMiHOG000177218.
HOVERGENiHBG107298.
InParanoidiQ9DB34.
KOiK12191.
OMAiKNGQMGA.
OrthoDBiEOG7992S8.
PhylomeDBiQ9DB34.
TreeFamiTF300118.

Enzyme and pathway databases

ReactomeiREACT_303468. Lysosome Vesicle Biogenesis.
REACT_334712. Endosomal Sorting Complex Required For Transport (ESCRT).

Miscellaneous databases

NextBioi328271.
PROiQ9DB34.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DB34.
CleanExiMM_CHMP2A.
GenevestigatoriQ9DB34.

Family and domain databases

InterProiIPR005024. Snf7_fam.
[Graphical view]
PfamiPF03357. Snf7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mammalian class E Vps proteins, SBP1 and mVps2/CHMP2A, interact with and regulate the function of an AAA-ATPase SKD1/Vps4B."
    Fujita H., Umezuki Y., Imamura K., Ishikawa D., Uchimura S., Nara A., Yoshimori T., Hayashizaki Y., Kawai J., Ishidoh K., Tanaka Y., Himeno M.
    J. Cell Sci. 117:2997-3009(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH VPS4B.
  2. "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: Cerebellum.
  3. "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: FVB/N.
    Tissue: Mammary tumor.
  4. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiCHM2A_MOUSE
AccessioniPrimary (citable) accession number: Q9DB34
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: June 1, 2001
Last modified: May 27, 2015
This is version 104 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.