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O43633

- CHM2A_HUMAN

UniProt

O43633 - CHM2A_HUMAN

Protein

Charged multivesicular body protein 2a

Gene

CHMP2A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
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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 and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in HIV-1 p6- and p9-dependent virus release.2 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein domain specific binding Source: UniProtKB

    GO - Biological processi

    1. endosomal transport Source: Reactome
    2. establishment of protein localization Source: UniProt
    3. membrane organization Source: Reactome
    4. positive regulation of viral release from host cell Source: UniProt
    5. protein transport Source: UniProtKB-KW
    6. regulation of viral process Source: UniProt
    7. viral life cycle Source: Reactome
    8. viral process Source: Reactome

    Keywords - Biological processi

    Protein transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_27258. Endosomal Sorting Complex Required For Transport (ESCRT).
    REACT_6359. Budding and maturation of HIV virion.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Charged multivesicular body protein 2a
    Alternative name(s):
    Chromatin-modifying protein 2a
    Short name:
    CHMP2a
    Putative breast adenocarcinoma marker BC-2
    Vacuolar protein sorting-associated protein 2-1
    Short name:
    Vps2-1
    Short name:
    hVps2-1
    Gene namesi
    Name:CHMP2A
    Synonyms:BC2, CHMP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:30216. CHMP2A.

    Subcellular locationi

    Late endosome membrane 2 Publications; Peripheral membrane protein 2 Publications; Cytoplasmic side 2 Publications
    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: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. late endosome membrane Source: UniProtKB-SubCell
    4. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi169 – 1702DE → AA: Diminishes interaction with VPS4B. 1 Publication
    Mutagenesisi181 – 22242Missing: Membrane association; releases autoinhibition. 1 PublicationAdd
    BLAST
    Mutagenesisi216 – 2161L → A: Diminishes interaction with VTA1. 2 Publications
    Mutagenesisi217 – 2226Missing: Abolishes interaction with VTA1. 1 Publication

    Organism-specific databases

    PharmGKBiPA142672111.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 222222Charged multivesicular body protein 2aPRO_0000211462Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Post-translational modificationi

    ISGylated in a CHMP5-dependent manner. Isgylation weakens and inhibits its interactions with VPS4A and VTA1 respectively.1 Publication

    Keywords - PTMi

    Acetylation, Ubl conjugation

    Proteomic databases

    MaxQBiO43633.
    PaxDbiO43633.
    PeptideAtlasiO43633.
    PRIDEiO43633.

    2D gel databases

    OGPiO43633.

    PTM databases

    PhosphoSiteiO43633.

    Expressioni

    Gene expression databases

    ArrayExpressiO43633.
    BgeeiO43633.
    CleanExiHS_CHMP2A.
    GenevestigatoriO43633.

    Organism-specific databases

    HPAiHPA041153.
    HPA042031.

    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.7 Publications

    Protein-protein interaction databases

    BioGridi118091. 20 interactions.
    DIPiDIP-48533N.
    IntActiO43633. 6 interactions.
    MINTiMINT-5005843.
    STRINGi9606.ENSP00000310440.

    Structurei

    3D structure databases

    ProteinModelPortaliO43633.
    SMRiO43633. Positions 9-132.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni56 – 222167Interaction with VPS4BAdd
    BLAST
    Regioni217 – 2226Interaction with VTA1

    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.
    HOGENOMiHOG000177218.
    HOVERGENiHBG107298.
    InParanoidiO43633.
    KOiK12191.
    OMAiKNGQMGA.
    PhylomeDBiO43633.
    TreeFamiTF300118.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    O43633-1 [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
    AASALADADA DLEERLKNLR RD 222
    Length:222
    Mass (Da):25,104
    Last modified:June 1, 1998 - v1
    Checksum:iF2B86C623829E32E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF042384 mRNA. Translation: AAC00005.1.
    AJ277113 Genomic DNA. Translation: CAC14310.1.
    AY364248 mRNA. Translation: AAQ76807.1.
    BT007298 mRNA. Translation: AAP35962.1.
    CR457002 mRNA. Translation: CAG33283.1.
    AK311974 mRNA. Translation: BAG34913.1.
    CH471135 Genomic DNA. Translation: EAW72609.1.
    BC002502 mRNA. Translation: AAH02502.1.
    CCDSiCCDS12986.1.
    RefSeqiNP_055268.1. NM_014453.3.
    NP_940818.1. NM_198426.2.
    UniGeneiHs.12107.

    Genome annotation databases

    EnsembliENST00000312547; ENSP00000310440; ENSG00000130724.
    ENST00000600118; ENSP00000469240; ENSG00000130724.
    ENST00000601220; ENSP00000472680; ENSG00000130724.
    GeneIDi27243.
    KEGGihsa:27243.
    UCSCiuc002qti.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF042384 mRNA. Translation: AAC00005.1 .
    AJ277113 Genomic DNA. Translation: CAC14310.1 .
    AY364248 mRNA. Translation: AAQ76807.1 .
    BT007298 mRNA. Translation: AAP35962.1 .
    CR457002 mRNA. Translation: CAG33283.1 .
    AK311974 mRNA. Translation: BAG34913.1 .
    CH471135 Genomic DNA. Translation: EAW72609.1 .
    BC002502 mRNA. Translation: AAH02502.1 .
    CCDSi CCDS12986.1.
    RefSeqi NP_055268.1. NM_014453.3.
    NP_940818.1. NM_198426.2.
    UniGenei Hs.12107.

    3D structure databases

    ProteinModelPortali O43633.
    SMRi O43633. Positions 9-132.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118091. 20 interactions.
    DIPi DIP-48533N.
    IntActi O43633. 6 interactions.
    MINTi MINT-5005843.
    STRINGi 9606.ENSP00000310440.

    PTM databases

    PhosphoSitei O43633.

    2D gel databases

    OGPi O43633.

    Proteomic databases

    MaxQBi O43633.
    PaxDbi O43633.
    PeptideAtlasi O43633.
    PRIDEi O43633.

    Protocols and materials databases

    DNASUi 27243.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000312547 ; ENSP00000310440 ; ENSG00000130724 .
    ENST00000600118 ; ENSP00000469240 ; ENSG00000130724 .
    ENST00000601220 ; ENSP00000472680 ; ENSG00000130724 .
    GeneIDi 27243.
    KEGGi hsa:27243.
    UCSCi uc002qti.3. human.

    Organism-specific databases

    CTDi 27243.
    GeneCardsi GC19M059062.
    HGNCi HGNC:30216. CHMP2A.
    HPAi HPA041153.
    HPA042031.
    MIMi 610893. gene.
    neXtProti NX_O43633.
    PharmGKBi PA142672111.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5491.
    HOGENOMi HOG000177218.
    HOVERGENi HBG107298.
    InParanoidi O43633.
    KOi K12191.
    OMAi KNGQMGA.
    PhylomeDBi O43633.
    TreeFami TF300118.

    Enzyme and pathway databases

    Reactomei REACT_27258. Endosomal Sorting Complex Required For Transport (ESCRT).
    REACT_6359. Budding and maturation of HIV virion.

    Miscellaneous databases

    ChiTaRSi CHMP2A. human.
    GeneWikii CHMP2A.
    GenomeRNAii 27243.
    NextBioi 50143.
    PROi O43633.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43633.
    Bgeei O43633.
    CleanExi HS_CHMP2A.
    Genevestigatori O43633.

    Family and domain databases

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

    Publicationsi

    1. Slater C., Thill G., Obar R.
      Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Role of the BC-2 gene in breast cancer."
      Koczan D., Reimer T., Rump A., Merck-Rousseau M.F., Rosenthal A., Friese K., Thiesen H.J.
      Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "NovelFam3000 -- uncharacterized human protein domains conserved across model organisms."
      Kemmer D., Podowski R.M., Arenillas D., Lim J., Hodges E., Roth P., Sonnhammer E.L.L., Hoeoeg C., Wasserman W.W.
      BMC Genomics 7:48-48(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Skeletal muscle.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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].
      Tissue: Skin.
    9. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-7, ACETYLATION AT MET-1.
      Tissue: Platelet.
    10. "Materials and methods for detection of breast cancer."
      Keesee S.K., Obar R., Wu Y.-J.
      Patent number US5914238, 05-JUN-1996
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 72-222, PROTEIN SEQUENCE OF 75-89 AND 197-205.
    11. "CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins."
      Howard T.L., Stauffer D.R., Degnin C.R., Hollenberg S.M.
      J. Cell Sci. 114:2395-2404(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VPS4B.
    12. Cited for: FUNCTION IN HIV-1 BUDDING, INTERACTION WITH VPS4A AND VPS4B.
    13. "Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins."
      Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.
      Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HIV-1 BUDDING, INTERACTION WITH CHMP1B; CHMP2B; CHMP3; CHMP4A; CHMP4B; CHMP4C; CHMP5 AND VPS4A.
    14. Erratum
      Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.
      Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003)
    15. "A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex."
      Tsang H.T.H., Connell J.W., Brown S.E., Thompson A., Reid E., Sanderson C.M.
      Genomics 88:333-346(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MITD1.
    16. "Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis."
      Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P., Rodesch C.K., Sundquist W.I.
      EMBO J. 26:4215-4227(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    17. "Structure/function analysis of four core ESCRT-III proteins reveals common regulatory role for extreme C-terminal domain."
      Shim S., Kimpler L.A., Hanson P.I.
      Traffic 8:1068-1079(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: AUTOINHIBITORY MECHANISM, INTERACTION WITH VPS4B, MUTAGENESIS OF 181-ASN--ASP-222.
    18. "Novel interactions of ESCRT-III with LIP5 and VPS4 and their implications for ESCRT-III disassembly."
      Shim S., Merrill S.A., Hanson P.I.
      Mol. Biol. Cell 19:2661-2672(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VTA1, MUTAGENESIS OF 169-ASP-GLU-170; LEU-216 AND 217-LYS--ASP-222.
    19. Cited for: POLYMERIZATION WITH CHMP3, ELECTRON MICROSCOPY.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Mechanism of inhibition of retrovirus release from cells by interferon-induced gene ISG15."
      Kuang Z., Seo E.J., Leis J.
      J. Virol. 85:7153-7161(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ISGYLATION, INTERACTION WITH VTA1 AND VPS4A.

    Entry informationi

    Entry nameiCHM2A_HUMAN
    AccessioniPrimary (citable) accession number: O43633
    Secondary accession number(s): B2R4W6, Q3ZTT0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 121 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Its overexpression strongly inhibits HIV-1 release.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3