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Q64433

- CH10_MOUSE

UniProt

Q64433 - CH10_MOUSE

Protein

10 kDa heat shock protein, mitochondrial

Gene

Hspe1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Eukaryotic CPN10 homolog which is essential for mitochondrial protein biogenesis, together with CPN60. Binds to CPN60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.

    GO - Molecular functioni

    1. ATP binding Source: InterPro
    2. chaperone binding Source: UniProtKB

    GO - Biological processi

    1. protein folding Source: InterPro
    2. response to stress Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Stress response

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    10 kDa heat shock protein, mitochondrial
    Short name:
    Hsp10
    Alternative name(s):
    10 kDa chaperonin
    Chaperonin 10
    Short name:
    CPN10
    Gene namesi
    Name:Hspe1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:104680. Hspe1.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 10210110 kDa heat shock protein, mitochondrialPRO_0000174918Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei8 – 81N6-acetyllysine1 Publication
    Modified residuei28 – 281N6-succinyllysine1 Publication
    Modified residuei40 – 401N6-acetyllysine; alternate1 Publication
    Modified residuei40 – 401N6-malonyllysine; alternateBy similarity
    Modified residuei40 – 401N6-succinyllysine; alternate1 Publication
    Modified residuei54 – 541N6-malonyllysine; alternateBy similarity
    Modified residuei54 – 541N6-succinyllysine; alternate1 Publication
    Modified residuei56 – 561N6-acetyllysine; alternate2 Publications
    Modified residuei56 – 561N6-malonyllysine; alternateBy similarity
    Modified residuei56 – 561N6-succinyllysine; alternate1 Publication
    Modified residuei66 – 661N6-acetyllysine; alternate1 Publication
    Modified residuei66 – 661N6-succinyllysine; alternate1 Publication
    Modified residuei70 – 701N6-acetyllysine; alternate1 Publication
    Modified residuei70 – 701N6-succinyllysine; alternate1 Publication
    Modified residuei79 – 791PhosphothreonineBy similarity
    Modified residuei80 – 801N6-acetyllysine; alternate1 Publication
    Modified residuei80 – 801N6-succinyllysine; alternate1 Publication
    Modified residuei86 – 861N6-acetyllysine; alternate1 Publication
    Modified residuei86 – 861N6-succinyllysine; alternate1 Publication
    Modified residuei99 – 991N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ64433.
    PaxDbiQ64433.
    PRIDEiQ64433.

    2D gel databases

    REPRODUCTION-2DPAGEQ64433.

    PTM databases

    PhosphoSiteiQ64433.

    Expressioni

    Inductioni

    By stress.

    Gene expression databases

    ArrayExpressiQ64433.
    BgeeiQ64433.
    CleanExiMM_HSPE1.
    GenevestigatoriQ64433.

    Interactioni

    Subunit structurei

    Homohexamer.By similarity

    Protein-protein interaction databases

    IntActiQ64433. 1 interaction.
    MINTiMINT-1839191.

    Structurei

    3D structure databases

    ProteinModelPortaliQ64433.
    SMRiQ64433. Positions 11-98.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GroES chaperonin family.Curated

    Phylogenomic databases

    eggNOGiCOG0234.
    GeneTreeiENSGT00390000006350.
    HOGENOMiHOG000133897.
    HOVERGENiHBG000385.
    InParanoidiQ64433.
    KOiK04078.
    OMAiQDRIIVK.
    OrthoDBiEOG71CFPD.
    PhylomeDBiQ64433.
    TreeFamiTF313814.

    Family and domain databases

    Gene3Di2.30.33.40. 1 hit.
    HAMAPiMF_00580. CH10.
    InterProiIPR020818. Chaperonin_Cpn10.
    IPR018369. Chaprnonin_Cpn10_CS.
    IPR011032. GroES-like.
    [Graphical view]
    PANTHERiPTHR10772. PTHR10772. 1 hit.
    PfamiPF00166. Cpn10. 1 hit.
    [Graphical view]
    PRINTSiPR00297. CHAPERONIN10.
    SMARTiSM00883. Cpn10. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 1 hit.
    PROSITEiPS00681. CHAPERONINS_CPN10. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q64433-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGQAFRKFL PLFDRVLVER SAAETVTKGG IMLPEKSQGK VLQATVVAVG    50
    SGGKGKSGEI EPVSVKVGDK VLLPEYGGTK VVLDDKDYFL FRDSDILGKY 100
    VD 102
    Length:102
    Mass (Da):10,963
    Last modified:January 23, 2007 - v2
    Checksum:i08BEB5566DBE8A3D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09659 mRNA. Translation: AAA62229.1.
    AF251024 Genomic DNA. Translation: AAF67345.1.
    AK088121 mRNA. Translation: BAC40159.1.
    BC024385 mRNA. Translation: AAH24385.1.
    CCDSiCCDS35570.1.
    PIRiA55075.
    RefSeqiNP_032329.1. NM_008303.4.
    UniGeneiMm.215667.

    Genome annotation databases

    EnsembliENSMUST00000075242; ENSMUSP00000074724; ENSMUSG00000073676.
    GeneIDi15528.
    KEGGimmu:15528.
    UCSCiuc007bac.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09659 mRNA. Translation: AAA62229.1 .
    AF251024 Genomic DNA. Translation: AAF67345.1 .
    AK088121 mRNA. Translation: BAC40159.1 .
    BC024385 mRNA. Translation: AAH24385.1 .
    CCDSi CCDS35570.1.
    PIRi A55075.
    RefSeqi NP_032329.1. NM_008303.4.
    UniGenei Mm.215667.

    3D structure databases

    ProteinModelPortali Q64433.
    SMRi Q64433. Positions 11-98.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q64433. 1 interaction.
    MINTi MINT-1839191.

    PTM databases

    PhosphoSitei Q64433.

    2D gel databases

    REPRODUCTION-2DPAGE Q64433.

    Proteomic databases

    MaxQBi Q64433.
    PaxDbi Q64433.
    PRIDEi Q64433.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000075242 ; ENSMUSP00000074724 ; ENSMUSG00000073676 .
    GeneIDi 15528.
    KEGGi mmu:15528.
    UCSCi uc007bac.2. mouse.

    Organism-specific databases

    CTDi 3336.
    MGIi MGI:104680. Hspe1.

    Phylogenomic databases

    eggNOGi COG0234.
    GeneTreei ENSGT00390000006350.
    HOGENOMi HOG000133897.
    HOVERGENi HBG000385.
    InParanoidi Q64433.
    KOi K04078.
    OMAi QDRIIVK.
    OrthoDBi EOG71CFPD.
    PhylomeDBi Q64433.
    TreeFami TF313814.

    Miscellaneous databases

    NextBioi 288450.
    PROi Q64433.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q64433.
    Bgeei Q64433.
    CleanExi MM_HSPE1.
    Genevestigatori Q64433.

    Family and domain databases

    Gene3Di 2.30.33.40. 1 hit.
    HAMAPi MF_00580. CH10.
    InterProi IPR020818. Chaperonin_Cpn10.
    IPR018369. Chaprnonin_Cpn10_CS.
    IPR011032. GroES-like.
    [Graphical view ]
    PANTHERi PTHR10772. PTHR10772. 1 hit.
    Pfami PF00166. Cpn10. 1 hit.
    [Graphical view ]
    PRINTSi PR00297. CHAPERONIN10.
    SMARTi SM00883. Cpn10. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50129. SSF50129. 1 hit.
    PROSITEi PS00681. CHAPERONINS_CPN10. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, expression, and purification of a functional nonacetylated mammalian mitochondrial chaperonin 10."
      Dickson R., Larsen B., Viitanen P.V., Tormey M.B., Geske J., Strange R., Bemis L.T.
      J. Biol. Chem. 269:26858-26864(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The murine chaperonin 10 gene family contains an intronless, putative gene for early pregnancy factor, Cpn10-rs1."
      Fletcher B.H., Cassady A.I., Summers K.M., Cavanagh A.C.
      Mamm. Genome 12:133-140(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/Sv.
    3. "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: NOD.
      Tissue: Thymus.
    4. "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-3.
      Tissue: Mammary gland.
    5. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 8-15; 29-36; 41-54 AND 71-92, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.
    6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-56, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-28; LYS-40; LYS-54; LYS-56; LYS-66; LYS-70; LYS-80 AND LYS-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast and Liver.
    7. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8; LYS-40; LYS-56; LYS-66; LYS-70; LYS-80; LYS-86 AND LYS-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiCH10_MOUSE
    AccessioniPrimary (citable) accession number: Q64433
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 118 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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