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Q9DB34

- CHM2A_MOUSE

UniProt

Q9DB34 - CHM2A_MOUSE

Protein

Charged multivesicular body protein 2a

Gene

Chmp2a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    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

    1. protein binding Source: MGI

    GO - Biological processi

    1. protein transport Source: UniProtKB-KW

    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 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: Chromosome 7

    Organism-specific databases

    MGIiMGI:1916203. Chmp2a.

    Subcellular locationi

    Late endosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cytoplasm 1 Publication
    Note: Localizes to the midbody of dividing cells. Localized in two distinct rings on either side of the Fleming body.

    GO - Cellular componenti

    1. cytosol Source: MGI
    2. late endosome membrane Source: UniProtKB-SubCell

    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

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

    Sequencei

    Sequence statusi: Complete.

    Q9DB34-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDLLFGRRKT PEELLRQNQR ALNRAMRELD RERQKLETQE KKIIADIKKM    50
    AKQGQMDAVR IMAKDLVRTR RYVRKFVLMR ANIQAVSLKI QTLKSNNSMA 100
    QAMKGVTKAM GTMNRQLKLP QIQKIMMEFE RQAEIMDMKE EMMNDAIDDA 150
    MGDEEDEEES DAVVSQVLDE LGLSLTDELS NLPSTGGSLS VAAGGKKAEA 200
    TASALADADA DLEERLKNLR RD 222
    Length:222
    Mass (Da):25,134
    Last modified:June 1, 2001 - v1
    Checksum:iF2B86C623832E29E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK005267 mRNA. Translation: BAB23919.1.
    BC012230 mRNA. Translation: AAH12230.1.
    CCDSiCCDS20824.1.
    RefSeqiNP_081161.1. NM_026885.3.
    XP_006540408.1. XM_006540345.1.
    UniGeneiMm.295670.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK005267 mRNA. Translation: BAB23919.1 .
    BC012230 mRNA. Translation: AAH12230.1 .
    CCDSi CCDS20824.1.
    RefSeqi NP_081161.1. NM_026885.3.
    XP_006540408.1. XM_006540345.1.
    UniGenei Mm.295670.

    3D structure databases

    ProteinModelPortali Q9DB34.
    SMRi Q9DB34. Positions 9-132.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 213137. 2 interactions.
    IntActi Q9DB34. 1 interaction.
    MINTi MINT-4616048.
    STRINGi 10090.ENSMUSP00000005711.

    Proteomic databases

    MaxQBi Q9DB34.
    PaxDbi Q9DB34.
    PRIDEi Q9DB34.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000005711 ; ENSMUSP00000005711 ; ENSMUSG00000033916 .
    GeneIDi 68953.
    KEGGi mmu:68953.
    UCSCi uc009ffc.2. mouse.

    Organism-specific databases

    CTDi 27243.
    MGIi MGI:1916203. Chmp2a.

    Phylogenomic databases

    eggNOGi COG5491.
    GeneTreei ENSGT00550000074737.
    HOGENOMi HOG000177218.
    HOVERGENi HBG107298.
    InParanoidi Q9DB34.
    KOi K12191.
    OMAi KNGQMGA.
    OrthoDBi EOG7992S8.
    PhylomeDBi Q9DB34.
    TreeFami TF300118.

    Enzyme and pathway databases

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

    Miscellaneous databases

    NextBioi 328271.
    PROi Q9DB34.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9DB34.
    CleanExi MM_CHMP2A.
    Genevestigatori Q9DB34.

    Family and domain databases

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

    Publicationsi

    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: October 1, 2014
    This is version 97 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