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P63038

- CH60_MOUSE

UniProt

P63038 - CH60_MOUSE

Protein

60 kDa heat shock protein, mitochondrial

Gene

Hspd1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (31 Aug 2004)
      Previous versions | rss
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    Functioni

    Implicated in mitochondrial protein import and macromolecular assembly. May facilitate the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix.

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. double-stranded RNA binding Source: MGI
    3. lipopolysaccharide binding Source: BHF-UCL

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
    2. B cell cytokine production Source: Ensembl
    3. B cell proliferation Source: Ensembl
    4. isotype switching to IgG isotypes Source: Ensembl
    5. MyD88-dependent toll-like receptor signaling pathway Source: Ensembl
    6. negative regulation of apoptotic process Source: Ensembl
    7. positive regulation of apoptotic process Source: Ensembl
    8. positive regulation of interferon-alpha production Source: MGI
    9. positive regulation of interferon-gamma production Source: BHF-UCL
    10. positive regulation of interleukin-10 production Source: Ensembl
    11. positive regulation of interleukin-12 production Source: Ensembl
    12. positive regulation of interleukin-6 production Source: Ensembl
    13. positive regulation of macrophage activation Source: Ensembl
    14. positive regulation of T cell activation Source: BHF-UCL
    15. positive regulation of T cell mediated immune response to tumor cell Source: Ensembl
    16. protein refolding Source: Ensembl
    17. response to unfolded protein Source: Ensembl
    18. T cell activation Source: MGI

    Keywords - Molecular functioni

    Chaperone

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_199101. Mitochondrial protein import.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    60 kDa heat shock protein, mitochondrial
    Alternative name(s):
    60 kDa chaperonin
    Chaperonin 60
    Short name:
    CPN60
    HSP-65
    Heat shock protein 60
    Short name:
    HSP-60
    Short name:
    Hsp60
    Mitochondrial matrix protein P1
    Gene namesi
    Name:Hspd1
    Synonyms:Hsp60
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:96242. Hspd1.

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. cell surface Source: Ensembl
    2. coated pit Source: Ensembl
    3. coated vesicle Source: Ensembl
    4. cyclin-dependent protein kinase activating kinase holoenzyme complex Source: Ensembl
    5. cytoplasm Source: MGI
    6. cytosol Source: Ensembl
    7. early endosome Source: Ensembl
    8. extracellular space Source: Ensembl
    9. intracellular membrane-bounded organelle Source: MGI
    10. lipopolysaccharide receptor complex Source: Ensembl
    11. mitochondrial inner membrane Source: MGI
    12. mitochondrial matrix Source: UniProtKB-SubCell
    13. mitochondrion Source: MGI
    14. plasma membrane Source: MGI
    15. protein complex Source: UniProtKB
    16. secretory granule Source: MGI

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2626Mitochondrion1 PublicationAdd
    BLAST
    Chaini27 – 57354760 kDa heat shock protein, mitochondrialPRO_0000005027Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei31 – 311N6-succinyllysine1 Publication
    Modified residuei70 – 701Phosphoserine1 Publication
    Modified residuei75 – 751N6-acetyllysine1 Publication
    Modified residuei82 – 821N6-acetyllysine; alternateBy similarity
    Modified residuei82 – 821N6-succinyllysine; alternate1 Publication
    Modified residuei87 – 871N6-acetyllysine1 Publication
    Modified residuei91 – 911N6-acetyllysine1 Publication
    Modified residuei125 – 1251N6-acetyllysine; alternate1 Publication
    Modified residuei125 – 1251N6-succinyllysine; alternate1 Publication
    Modified residuei130 – 1301N6-acetyllysine1 Publication
    Modified residuei133 – 1331N6-acetyllysine; alternate1 Publication
    Modified residuei133 – 1331N6-malonyllysine; alternateBy similarity
    Modified residuei133 – 1331N6-succinyllysine; alternate1 Publication
    Modified residuei156 – 1561N6-acetyllysine1 Publication
    Modified residuei191 – 1911N6-acetyllysine; alternate1 Publication
    Modified residuei191 – 1911N6-succinyllysine; alternate1 Publication
    Modified residuei202 – 2021N6-acetyllysine; alternate1 Publication
    Modified residuei202 – 2021N6-succinyllysine; alternate1 Publication
    Modified residuei205 – 2051N6-acetyllysine; alternate1 Publication
    Modified residuei205 – 2051N6-succinyllysine; alternate1 Publication
    Modified residuei218 – 2181N6-acetyllysine; alternate1 Publication
    Modified residuei218 – 2181N6-succinyllysine; alternate1 Publication
    Modified residuei236 – 2361N6-acetyllysine; alternate1 Publication
    Modified residuei236 – 2361N6-succinyllysine; alternate1 Publication
    Modified residuei249 – 2491N6-acetyllysine1 Publication
    Modified residuei250 – 2501N6-acetyllysine; alternate1 Publication
    Modified residuei250 – 2501N6-succinyllysine; alternate1 Publication
    Modified residuei269 – 2691N6-acetyllysine1 Publication
    Modified residuei292 – 2921N6-acetyllysine1 Publication
    Modified residuei301 – 3011N6-succinyllysine1 Publication
    Modified residuei314 – 3141N6-acetyllysine1 Publication
    Modified residuei352 – 3521N6-acetyllysine; alternate1 Publication
    Modified residuei352 – 3521N6-succinyllysine; alternate1 Publication
    Modified residuei359 – 3591N6-acetyllysine1 Publication
    Modified residuei389 – 3891N6-acetyllysine1 Publication
    Modified residuei396 – 3961N6-acetyllysine; alternateBy similarity
    Modified residuei396 – 3961N6-succinyllysine; alternate1 Publication
    Modified residuei410 – 4101Phosphoserine1 Publication
    Modified residuei455 – 4551N6-acetyllysine; alternate1 Publication
    Modified residuei455 – 4551N6-succinyllysine; alternate1 Publication
    Modified residuei469 – 4691N6-acetyllysine1 Publication
    Modified residuei481 – 4811N6-acetyllysine; alternate1 Publication
    Modified residuei481 – 4811N6-succinyllysine; alternate1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP63038.
    PaxDbiP63038.
    PRIDEiP63038.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00308885.
    P63038.
    SWISS-2DPAGEP63038.
    UCD-2DPAGEP19227.
    P63038.

    Miscellaneous databases

    PMAP-CutDBP63038.

    Expressioni

    Gene expression databases

    ArrayExpressiP63038.
    BgeeiP63038.
    CleanExiMM_HSPD1.
    GenevestigatoriP63038.

    Interactioni

    Subunit structurei

    Interacts with ATAD3A By similarity. Interacts with METTL20 and METTL21B By similarity. Interacts with HRAS.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi200451. 12 interactions.
    DIPiDIP-31396N.
    IntActiP63038. 20 interactions.
    MINTiMINT-1860238.

    Structurei

    3D structure databases

    ProteinModelPortaliP63038.
    SMRiP63038. Positions 27-551.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the chaperonin (HSP60) family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0459.
    GeneTreeiENSGT00390000005727.
    HOVERGENiHBG001982.
    InParanoidiP63038.
    KOiK04077.
    OMAiEYGDMIG.
    OrthoDBiEOG7HTHGJ.
    PhylomeDBiP63038.
    TreeFamiTF300475.

    Family and domain databases

    Gene3Di1.10.560.10. 2 hits.
    3.50.7.10. 1 hit.
    HAMAPiMF_00600. CH60.
    InterProiIPR018370. Chaperonin_Cpn60_CS.
    IPR001844. Chaprnin_Cpn60.
    IPR002423. Cpn60/TCP-1.
    IPR027409. GroEL-like_apical_dom.
    IPR027413. GROEL-like_equatorial.
    [Graphical view]
    PANTHERiPTHR11353. PTHR11353. 1 hit.
    PfamiPF00118. Cpn60_TCP1. 1 hit.
    [Graphical view]
    PRINTSiPR00298. CHAPERONIN60.
    SUPFAMiSSF48592. SSF48592. 2 hits.
    SSF52029. SSF52029. 1 hit.
    TIGRFAMsiTIGR02348. GroEL. 1 hit.
    PROSITEiPS00296. CHAPERONINS_CPN60. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P63038-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MLRLPTVLRQ MRPVSRALAP HLTRAYAKDV KFGADARALM LQGVDLLADA    50
    VAVTMGPKGR TVIIEQSWGS PKVTKDGVTV AKSIDLKDKY KNIGAKLVQD 100
    VANNTNEEAG DGTTTATVLA RSIAKEGFEK ISKGANPVEI RRGVMLAVDA 150
    VIAELKKQSK PVTTPEEIAQ VATISANGDK DIGNIISDAM KKVGRKGVIT 200
    VKDGKTLNDE LEIIEGMKFD RGYISPYFIN TSKGQKCEFQ DAYVLLSEKK 250
    ISSVQSIVPA LEIANAHRKP LVIIAEDVDG EALSTLVLNR LKVGLQVVAV 300
    KAPGFGDNRK NQLKDMAIAT GGAVFGEEGL NLNLEDVQAH DLGKVGEVIV 350
    TKDDAMLLKG KGDKAHIEKR IQEITEQLDI TTSEYEKEKL NERLAKLSDG 400
    VAVLKVGGTS DVEVNEKKDR VTDALNATRA AVEEGIVLGG GCALLRCIPA 450
    LDSLKPANED QKIGIEIIKR ALKIPAMTIA KNAGVEGSLI VEKILQSSSE 500
    VGYDAMLGDF VNMVEKGIID PTKVVRTALL DAAGVASLLT TAEAVVTEIP 550
    KEEKDPGMGA MGGMGGGMGG GMF 573
    Length:573
    Mass (Da):60,955
    Last modified:August 31, 2004 - v1
    Checksum:i0014B58B77D0127B
    GO
    Isoform 2 (identifier: P63038-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-315: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:258
    Mass (Da):27,015
    Checksum:iDD79DC2838C3771B
    GO

    Sequence cautioni

    The sequence AAI06113.1 differs from that shown. Reason: . Potential poly-A sequence.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4 – 41L → H AA sequence (PubMed:1347942)Curated
    Sequence conflicti139 – 1391E → K AA sequence (PubMed:1347942)Curated
    Sequence conflicti251 – 2511I → F in CAA37653. (PubMed:1979012)Curated
    Sequence conflicti364 – 3641K → E in BAC40607. (PubMed:16141072)Curated
    Sequence conflicti518 – 5181I → V in CAA38762. (PubMed:2263486)Curated
    Sequence conflicti527 – 5271T → Q AA sequence (PubMed:1347942)Curated
    Sequence conflicti547 – 5471T → V AA sequence (PubMed:1347942)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 315315Missing in isoform 2. 1 PublicationVSP_025020Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55023 mRNA. Translation: CAA38762.1.
    AK088844 mRNA. Translation: BAC40607.1.
    AK143882 mRNA. Translation: BAE25581.1.
    AK146831 mRNA. Translation: BAE27466.1.
    BC016400 mRNA. Translation: AAH16400.1.
    BC018545 mRNA. Translation: AAH18545.1.
    BC106112 mRNA. Translation: AAI06113.1. Sequence problems.
    X53584 mRNA. Translation: CAA37653.1.
    CCDSiCCDS35569.1. [P63038-1]
    PIRiS13084. HHMS60.
    RefSeqiNP_034607.3. NM_010477.4. [P63038-1]
    XP_006495769.1. XM_006495706.1. [P63038-1]
    UniGeneiMm.1777.

    Genome annotation databases

    EnsembliENSMUST00000027123; ENSMUSP00000027123; ENSMUSG00000025980. [P63038-1]
    GeneIDi15510.
    KEGGimmu:15510.
    UCSCiuc007bab.2. mouse. [P63038-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55023 mRNA. Translation: CAA38762.1 .
    AK088844 mRNA. Translation: BAC40607.1 .
    AK143882 mRNA. Translation: BAE25581.1 .
    AK146831 mRNA. Translation: BAE27466.1 .
    BC016400 mRNA. Translation: AAH16400.1 .
    BC018545 mRNA. Translation: AAH18545.1 .
    BC106112 mRNA. Translation: AAI06113.1 . Sequence problems.
    X53584 mRNA. Translation: CAA37653.1 .
    CCDSi CCDS35569.1. [P63038-1 ]
    PIRi S13084. HHMS60.
    RefSeqi NP_034607.3. NM_010477.4. [P63038-1 ]
    XP_006495769.1. XM_006495706.1. [P63038-1 ]
    UniGenei Mm.1777.

    3D structure databases

    ProteinModelPortali P63038.
    SMRi P63038. Positions 27-551.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200451. 12 interactions.
    DIPi DIP-31396N.
    IntActi P63038. 20 interactions.
    MINTi MINT-1860238.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00308885.
    P63038.
    SWISS-2DPAGE P63038.
    UCD-2DPAGE P19227.
    P63038.

    Proteomic databases

    MaxQBi P63038.
    PaxDbi P63038.
    PRIDEi P63038.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000027123 ; ENSMUSP00000027123 ; ENSMUSG00000025980 . [P63038-1 ]
    GeneIDi 15510.
    KEGGi mmu:15510.
    UCSCi uc007bab.2. mouse. [P63038-1 ]

    Organism-specific databases

    CTDi 3329.
    MGIi MGI:96242. Hspd1.

    Phylogenomic databases

    eggNOGi COG0459.
    GeneTreei ENSGT00390000005727.
    HOVERGENi HBG001982.
    InParanoidi P63038.
    KOi K04077.
    OMAi EYGDMIG.
    OrthoDBi EOG7HTHGJ.
    PhylomeDBi P63038.
    TreeFami TF300475.

    Enzyme and pathway databases

    Reactomei REACT_199101. Mitochondrial protein import.

    Miscellaneous databases

    ChiTaRSi HSPD1. mouse.
    NextBioi 288418.
    PMAP-CutDB P63038.
    PROi P63038.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P63038.
    Bgeei P63038.
    CleanExi MM_HSPD1.
    Genevestigatori P63038.

    Family and domain databases

    Gene3Di 1.10.560.10. 2 hits.
    3.50.7.10. 1 hit.
    HAMAPi MF_00600. CH60.
    InterProi IPR018370. Chaperonin_Cpn60_CS.
    IPR001844. Chaprnin_Cpn60.
    IPR002423. Cpn60/TCP-1.
    IPR027409. GroEL-like_apical_dom.
    IPR027413. GROEL-like_equatorial.
    [Graphical view ]
    PANTHERi PTHR11353. PTHR11353. 1 hit.
    Pfami PF00118. Cpn60_TCP1. 1 hit.
    [Graphical view ]
    PRINTSi PR00298. CHAPERONIN60.
    SUPFAMi SSF48592. SSF48592. 2 hits.
    SSF52029. SSF52029. 1 hit.
    TIGRFAMsi TIGR02348. GroEL. 1 hit.
    PROSITEi PS00296. CHAPERONINS_CPN60. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide and deduced amino acid sequence of a murine cDNA clone encoding one member of the hsp65 multigene family."
      Loetscher E., Allison J.P.
      Nucleic Acids Res. 18:7153-7153(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: C57BL/6.
      Tissue: Thymus.
    2. "An interaction between p21ras and heat shock protein hsp60, a chaperonin."
      Ikawa S., Weinberg R.A.
      Proc. Natl. Acad. Sci. U.S.A. 89:2012-2016(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 527-548, INTERACTION WITH HRAS.
    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] (ISOFORM 1).
      Strain: C57BL/6J and NOD.
      Tissue: Heart, Kidney and 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] (ISOFORMS 1 AND 2).
      Strain: 129 and FVB/N.
      Tissue: Mammary tumor.
    5. "Nucleotide sequence of mouse HSP60 (chaperonin, GroEL homolog) cDNA."
      Venner T.J., Gupta R.S.
      Biochim. Biophys. Acta 1087:336-338(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-573 (ISOFORM 1).
      Strain: BALB/c.
      Tissue: Fibroblast.
    6. "Separation and sequencing of familiar and novel murine proteins using preparative two-dimensional gel electrophoresis."
      Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.
      Electrophoresis 15:735-745(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-47.
      Tissue: Fibroblast.
    7. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    9. "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: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-31; LYS-82; LYS-125; LYS-133; LYS-191; LYS-202; LYS-205; LYS-218; LYS-236; LYS-250; LYS-301; LYS-352; LYS-396; LYS-455 AND LYS-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast and Liver.
    10. "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-75; LYS-87; LYS-91; LYS-125; LYS-130; LYS-133; LYS-156; LYS-191; LYS-202; LYS-205; LYS-218; LYS-236; LYS-249; LYS-250; LYS-269; LYS-292; LYS-314; LYS-352; LYS-359; LYS-389; LYS-455; LYS-469 AND LYS-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiCH60_MOUSE
    AccessioniPrimary (citable) accession number: P63038
    Secondary accession number(s): P19226
    , P19227, P97602, Q3KQP2, Q3UIP0, Q8C2C7, Q8VEF4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 31, 2004
    Last sequence update: August 31, 2004
    Last modified: October 1, 2014
    This is version 106 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, 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

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