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Q9CQ10

- CHMP3_MOUSE

UniProt

Q9CQ10 - CHMP3_MOUSE

Protein

Charged multivesicular body protein 3

Gene

Chmp3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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. Selectively binds to phosphatidylinositol 3,5-bisphosphate PtdIns(3,5)P2 and PtdIns(3,4)P2 in preference to other phosphoinositides tested. Involved in late stages of cytokinesis. Plays a role in endosomal sorting/trafficking of EGF receptor By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei48 – 481Important for autoinhibitory functionBy similarity
    Binding sitei218 – 2181STAMBPBy similarity

    GO - Molecular functioni

    1. phosphatidylinositol-4,5-bisphosphate binding Source: Ensembl

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell division Source: UniProtKB-KW
    3. endosome to lysosome transport Source: Ensembl
    4. protein transport Source: UniProtKB-KW
    5. regulation of endosome size Source: Ensembl

    Keywords - Biological processi

    Cell cycle, Cell division, 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 3
    Alternative name(s):
    Chromatin-modifying protein 3
    Vacuolar protein sorting-associated protein 24
    Gene namesi
    Name:Chmp3
    Synonyms:Vps24
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:1913950. Chmp3.

    Subcellular locationi

    Cytoplasmcytosol By similarity. Membrane By similarity; Lipid-anchor By similarity. Endosome By similarity. Late endosome membrane By similarity
    Note: Localizes to the midbody of dividing cells.By similarity

    GO - Cellular componenti

    1. cytosol Source: UniProtKB-SubCell
    2. early endosome Source: Ensembl
    3. late endosome membrane Source: UniProtKB-SubCell
    4. midbody Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Endosome, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedSequence Analysis
    Chaini2 – 224223Charged multivesicular body protein 3PRO_0000211481Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineSequence Analysis
    Cross-linki179 – 179Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei200 – 2001Phosphoserine1 Publication

    Keywords - PTMi

    Isopeptide bond, Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9CQ10.
    PaxDbiQ9CQ10.
    PRIDEiQ9CQ10.

    PTM databases

    PhosphoSiteiQ9CQ10.

    Expressioni

    Tissue specificityi

    Expressed in lung, testis, heart, spleen, skeletal muscle, kidney, liver and brain.1 Publication

    Gene expression databases

    BgeeiQ9CQ10.
    CleanExiMM_VPS24.
    GenevestigatoriQ9CQ10.

    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. Forms a metastable monomer in solution; its core structure (without part of the putative autoinhibitory C-terminal acidic region) oligomerizes into a flat lattice via two different dimerization interfaces. In vitro, heteromerizes with CHMP2A (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. May interact with IGFBP7; the relevance of such interaction however remains unclear. Interacts with CHMP2A. Interacts with CHMP4A; the interaction requires the release of CHMP4A autoinhibition. Interacts with VPS4A. Interacts with STAMBP; the interaction appears to relieve the autoinhibition of CHMP3 By similarity. Interacts with VTA1 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi211654. 3 interactions.
    IntActiQ9CQ10. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9CQ10.
    SMRiQ9CQ10. Positions 5-181.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 113112Intramolecular interaction with C-terminusBy similarityAdd
    BLAST
    Regioni59 – 646Important for autoinhibitory functionBy similarity
    Regioni151 – 22474Interaction with VPS4ABy similarityAdd
    BLAST
    Regioni151 – 22272Intramolecular interaction with N-terminusBy similarityAdd
    BLAST
    Regioni168 – 1692Important for autoinhibitory functionBy similarity
    Regioni196 – 22429Interaction with STAMBPBy similarityAdd
    BLAST
    Regioni205 – 2095Interaction with STAMBPBy similarity
    Regioni223 – 2242Interaction with STAMBPBy similarity

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili22 – 5433Sequence AnalysisAdd
    BLAST
    Coiled coili149 – 22476Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi201 – 21313MIT-interacting motifBy similarityAdd
    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.
    GeneTreeiENSGT00550000074896.
    HOGENOMiHOG000177219.
    HOVERGENiHBG107031.
    InParanoidiQ9CQ10.
    KOiK12193.
    OMAiMLDETMD.
    OrthoDBiEOG7D59Q2.
    PhylomeDBiQ9CQ10.
    TreeFamiTF105848.

    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.

    Q9CQ10-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGLFGKTQEK PPKELVNEWS LKIRKEMRVV DRQIRDIQRE EEKVKRSVKD    50
    AAKKGQKEVC VVLAKEMIRS RKAVSKLYAS KAHMNSVLMG MKNQLAVLRV 100
    AGSLQKSTEV MKAMQSLVKI PEIQATMREL SKEMMKAGII EEMLEDTFES 150
    MDDQEEMEEA AEMEIDRILF EITAGALGKA PSKVTDALPE PEPAGAMAAS 200
    EEGEEEEDEE DLEAMQSRLA TLRS 224
    Length:224
    Mass (Da):25,219
    Last modified:January 23, 2007 - v3
    Checksum:iDC1A566E86D82A07
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 71T → S in BAB26273. (PubMed:16141072)Curated
    Sequence conflicti161 – 1611A → V in BAB31306. (PubMed:16141072)Curated
    Sequence conflicti170 – 1701F → L in BAB31306. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK009414 mRNA. Translation: BAB26273.1.
    AK014818 mRNA. Translation: BAB29566.1.
    AK016677 mRNA. Translation: BAB30375.1.
    AK018611 mRNA. Translation: BAB31306.1.
    AK083562 mRNA. Translation: BAC38951.1.
    BC049964 mRNA. Translation: AAH49964.1.
    CCDSiCCDS20232.1.
    RefSeqiNP_080059.2. NM_025783.3.
    UniGeneiMm.181278.

    Genome annotation databases

    EnsembliENSMUST00000059462; ENSMUSP00000109815; ENSMUSG00000053119.
    ENSMUST00000065364; ENSMUSP00000068410; ENSMUSG00000053119.
    GeneIDi66700.
    KEGGimmu:66700.
    UCSCiuc009cgw.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK009414 mRNA. Translation: BAB26273.1 .
    AK014818 mRNA. Translation: BAB29566.1 .
    AK016677 mRNA. Translation: BAB30375.1 .
    AK018611 mRNA. Translation: BAB31306.1 .
    AK083562 mRNA. Translation: BAC38951.1 .
    BC049964 mRNA. Translation: AAH49964.1 .
    CCDSi CCDS20232.1.
    RefSeqi NP_080059.2. NM_025783.3.
    UniGenei Mm.181278.

    3D structure databases

    ProteinModelPortali Q9CQ10.
    SMRi Q9CQ10. Positions 5-181.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 211654. 3 interactions.
    IntActi Q9CQ10. 2 interactions.

    PTM databases

    PhosphoSitei Q9CQ10.

    Proteomic databases

    MaxQBi Q9CQ10.
    PaxDbi Q9CQ10.
    PRIDEi Q9CQ10.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000059462 ; ENSMUSP00000109815 ; ENSMUSG00000053119 .
    ENSMUST00000065364 ; ENSMUSP00000068410 ; ENSMUSG00000053119 .
    GeneIDi 66700.
    KEGGi mmu:66700.
    UCSCi uc009cgw.1. mouse.

    Organism-specific databases

    CTDi 51652.
    MGIi MGI:1913950. Chmp3.

    Phylogenomic databases

    eggNOGi COG5491.
    GeneTreei ENSGT00550000074896.
    HOGENOMi HOG000177219.
    HOVERGENi HBG107031.
    InParanoidi Q9CQ10.
    KOi K12193.
    OMAi MLDETMD.
    OrthoDBi EOG7D59Q2.
    PhylomeDBi Q9CQ10.
    TreeFami TF105848.

    Enzyme and pathway databases

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

    Miscellaneous databases

    NextBioi 322405.
    PROi Q9CQ10.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9CQ10.
    CleanExi MM_VPS24.
    Genevestigatori Q9CQ10.

    Family and domain databases

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

    Publicationsi

    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: Cecum, Testis and Tongue.
    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: 129.
      Tissue: Mammary tumor.
    3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    4. "Characterization of a novel alternatively spliced human transcript encoding an N-terminally truncated Vps24 protein that suppresses the effects of Bax in an ESCRT independent manner in yeast."
      Khoury C.M., Yang Z., Ismail S., Greenwood M.T.
      Gene 391:233-241(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiCHMP3_MOUSE
    AccessioniPrimary (citable) accession number: Q9CQ10
    Secondary accession number(s): Q9D2Z2, Q9D7A5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 90 of the entry and version 3 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