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P10809

- CH60_HUMAN

UniProt

P10809 - CH60_HUMAN

Protein

60 kDa heat shock protein, mitochondrial

Gene

HSPD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 181 (01 Oct 2014)
      Sequence version 2 (01 Aug 1990)
      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. ATPase activity Source: BHF-UCL
    2. ATP binding Source: UniProtKB-KW
    3. chaperone binding Source: UniProtKB
    4. DNA replication origin binding Source: BHF-UCL
    5. double-stranded RNA binding Source: MGI
    6. lipopolysaccharide binding Source: BHF-UCL
    7. p53 binding Source: UniProtKB
    8. poly(A) RNA binding Source: UniProtKB
    9. protein binding Source: UniProtKB
    10. single-stranded DNA binding Source: BHF-UCL
    11. unfolded protein binding Source: UniProtKB

    GO - Biological processi

    1. 'de novo' protein folding Source: BHF-UCL
    2. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: BHF-UCL
    3. ATP catabolic process Source: GOC
    4. B cell activation Source: BHF-UCL
    5. B cell cytokine production Source: BHF-UCL
    6. B cell proliferation Source: BHF-UCL
    7. chaperone-mediated protein complex assembly Source: BHF-UCL
    8. isotype switching to IgG isotypes Source: BHF-UCL
    9. MyD88-dependent toll-like receptor signaling pathway Source: BHF-UCL
    10. negative regulation of apoptotic process Source: UniProtKB
    11. positive regulation of apoptotic process Source: BHF-UCL
    12. positive regulation of interferon-alpha production Source: BHF-UCL
    13. positive regulation of interferon-gamma production Source: BHF-UCL
    14. positive regulation of interleukin-10 production Source: BHF-UCL
    15. positive regulation of interleukin-12 production Source: BHF-UCL
    16. positive regulation of interleukin-6 production Source: BHF-UCL
    17. positive regulation of macrophage activation Source: BHF-UCL
    18. positive regulation of T cell activation Source: BHF-UCL
    19. positive regulation of T cell mediated immune response to tumor cell Source: BHF-UCL
    20. protein maturation Source: BHF-UCL
    21. protein refolding Source: UniProtKB
    22. protein stabilization Source: UniProtKB
    23. response to unfolded protein Source: BHF-UCL
    24. T cell activation Source: MGI
    25. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Host-virus interaction

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_118595. 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
    Heat shock protein 60
    Short name:
    HSP-60
    Short name:
    Hsp60
    HuCHA60
    Mitochondrial matrix protein P1
    P60 lymphocyte protein
    Gene namesi
    Name:HSPD1
    Synonyms:HSP60
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:5261. HSPD1.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: UniProtKB
    2. coated pit Source: BHF-UCL
    3. coated vesicle Source: BHF-UCL
    4. cytoplasm Source: UniProtKB
    5. cytosol Source: UniProtKB
    6. early endosome Source: BHF-UCL
    7. extracellular space Source: BHF-UCL
    8. extracellular vesicular exosome Source: UniProtKB
    9. lipopolysaccharide receptor complex Source: BHF-UCL
    10. membrane Source: UniProtKB
    11. mitochondrial inner membrane Source: BHF-UCL
    12. mitochondrial matrix Source: BHF-UCL
    13. mitochondrion Source: UniProtKB
    14. plasma membrane Source: Ensembl
    15. protein complex Source: UniProtKB
    16. secretory granule Source: BHF-UCL

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Spastic paraplegia 13, autosomal dominant (SPG13) [MIM:605280]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti98 – 981V → I in SPG13. 1 Publication
    VAR_026748
    Leukodystrophy, hypomyelinating, 4 (HLD4) [MIM:612233]: A severe autosomal recessive hypomyelinating leukodystrophy. Clinically characterized by infantile-onset rotary nystagmus, progressive spastic paraplegia, neurologic regression, motor impairment, profound mental retardation. Death usually occurs within the first two decades of life.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti29 – 291D → G in HLD4; transfection with the mutant protein impairs cell growth that worsens with increasing temperature. 1 Publication
    VAR_054785

    Keywords - Diseasei

    Disease mutation, Hereditary spastic paraplegia, Leukodystrophy, Neurodegeneration

    Organism-specific databases

    MIMi605280. phenotype.
    612233. phenotype.
    Orphaneti100994. Autosomal dominant spastic paraplegia type 13.
    280288. Pelizaeus-Merzbacher-like due to HSPD1 mutation.
    PharmGKBiPA29527.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2626Mitochondrion7 PublicationsAdd
    BLAST
    Chaini27 – 57354760 kDa heat shock protein, mitochondrialPRO_0000005026Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei31 – 311N6-succinyllysineBy similarity
    Modified residuei70 – 701Phosphoserine4 Publications
    Modified residuei75 – 751N6-acetyllysineBy similarity
    Modified residuei82 – 821N6-acetyllysine; alternate1 Publication
    Modified residuei82 – 821N6-succinyllysine; alternateBy similarity
    Modified residuei87 – 871N6-acetyllysineBy similarity
    Modified residuei91 – 911N6-acetyllysineBy similarity
    Modified residuei125 – 1251N6-acetyllysine; alternate1 Publication
    Modified residuei125 – 1251N6-succinyllysine; alternateBy similarity
    Modified residuei130 – 1301N6-acetyllysine1 Publication
    Modified residuei133 – 1331N6-acetyllysine; alternateBy similarity
    Modified residuei133 – 1331N6-malonyllysine; alternate1 Publication
    Modified residuei133 – 1331N6-succinyllysine; alternateBy similarity
    Modified residuei156 – 1561N6-acetyllysineBy similarity
    Modified residuei191 – 1911N6-acetyllysine; alternateBy similarity
    Modified residuei191 – 1911N6-succinyllysine; alternateBy similarity
    Modified residuei202 – 2021N6-acetyllysine; alternate1 Publication
    Modified residuei202 – 2021N6-succinyllysine; alternateBy similarity
    Modified residuei205 – 2051N6-acetyllysine; alternateBy similarity
    Modified residuei205 – 2051N6-succinyllysine; alternateBy similarity
    Modified residuei218 – 2181N6-acetyllysine; alternate1 Publication
    Modified residuei218 – 2181N6-succinyllysine; alternateBy similarity
    Modified residuei236 – 2361N6-acetyllysine; alternateBy similarity
    Modified residuei236 – 2361N6-succinyllysine; alternateBy similarity
    Modified residuei249 – 2491N6-acetyllysineBy similarity
    Modified residuei250 – 2501N6-acetyllysine; alternateBy similarity
    Modified residuei250 – 2501N6-succinyllysine; alternateBy similarity
    Modified residuei269 – 2691N6-acetyllysine1 Publication
    Modified residuei292 – 2921N6-acetyllysineBy similarity
    Modified residuei301 – 3011N6-succinyllysineBy similarity
    Modified residuei314 – 3141N6-acetyllysineBy similarity
    Modified residuei352 – 3521N6-acetyllysine; alternate1 Publication
    Modified residuei352 – 3521N6-succinyllysine; alternateBy similarity
    Modified residuei359 – 3591N6-acetyllysine1 Publication
    Modified residuei389 – 3891N6-acetyllysineBy similarity
    Modified residuei396 – 3961N6-acetyllysine; alternate1 Publication
    Modified residuei396 – 3961N6-succinyllysine; alternateBy similarity
    Modified residuei410 – 4101PhosphoserineBy similarity
    Modified residuei469 – 4691N6-acetyllysine1 Publication
    Modified residuei481 – 4811N6-acetyllysine; alternateBy similarity
    Modified residuei481 – 4811N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP10809.
    PaxDbiP10809.
    PRIDEiP10809.

    2D gel databases

    DOSAC-COBS-2DPAGEP10809.
    OGPiP10809.
    REPRODUCTION-2DPAGEIPI00784154.
    P10809.
    SWISS-2DPAGEP10809.
    UCD-2DPAGEP10809.

    PTM databases

    PhosphoSiteiP10809.

    Expressioni

    Gene expression databases

    ArrayExpressiP10809.
    BgeeiP10809.
    CleanExiHS_HSPD1.
    GenevestigatoriP10809.

    Organism-specific databases

    HPAiCAB002775.
    HPA001523.
    HPA050025.

    Interactioni

    Subunit structurei

    Interacts with HRAS By similarity. Interacts with HBV protein X and HTLV-1 protein p40tax. Interacts with ATAD3A. Interacts with METTL20 and METTL21B.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BRCA1P383982EBI-352528,EBI-349905
    FHITP497895EBI-352528,EBI-741760
    MFHAS1Q9Y4C43EBI-352528,EBI-2864441

    Protein-protein interaction databases

    BioGridi109561. 127 interactions.
    DIPiDIP-58N.
    IntActiP10809. 67 interactions.
    MINTiMINT-1162735.
    STRINGi9606.ENSP00000340019.

    Structurei

    3D structure databases

    ProteinModelPortaliP10809.
    SMRiP10809. Positions 27-551.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the chaperonin (HSP60) family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0459.
    HOGENOMiHOG000076290.
    HOVERGENiHBG001982.
    InParanoidiP10809.
    KOiK04077.
    OMAiNYKAANE.
    OrthoDBiEOG7HTHGJ.
    PhylomeDBiP10809.
    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: P10809-1) [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

    MLRLPTVFRQ MRPVSRVLAP HLTRAYAKDV KFGADARALM LQGVDLLADA    50
    VAVTMGPKGR TVIIEQSWGS PKVTKDGVTV AKSIDLKDKY KNIGAKLVQD 100
    VANNTNEEAG DGTTTATVLA RSIAKEGFEK ISKGANPVEI RRGVMLAVDA 150
    VIAELKKQSK PVTTPEEIAQ VATISANGDK EIGNIISDAM KKVGRKGVIT 200
    VKDGKTLNDE LEIIEGMKFD RGYISPYFIN TSKGQKCEFQ DAYVLLSEKK 250
    ISSIQSIVPA LEIANAHRKP LVIIAEDVDG EALSTLVLNR LKVGLQVVAV 300
    KAPGFGDNRK NQLKDMAIAT GGAVFGEEGL TLNLEDVQPH DLGKVGEVIV 350
    TKDDAMLLKG KGDKAQIEKR IQEIIEQLDV TTSEYEKEKL NERLAKLSDG 400
    VAVLKVGGTS DVEVNEKKDR VTDALNATRA AVEEGIVLGG GCALLRCIPA 450
    LDSLTPANED QKIGIEIIKR TLKIPAMTIA KNAGVEGSLI VEKIMQSSSE 500
    VGYDAMAGDF VNMVEKGIID PTKVVRTALL DAAGVASLLT TAEVVVTEIP 550
    KEEKDPGMGA MGGMGGGMGG GMF 573
    Length:573
    Mass (Da):61,055
    Last modified:August 1, 1990 - v2
    Checksum:iE51E1BAD9615899C
    GO
    Isoform 2 (identifier: P10809-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         144-158: VMLAVDAVIAELKKQ → RNVCCHHSVLNFSVL
         159-573: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:158
    Mass (Da):17,100
    Checksum:i9FC1907D8E2C1ECE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti67 – 671S → G in AAA36022. (PubMed:1980192)Curated
    Sequence conflicti111 – 1111D → N in BAG35173. (PubMed:14702039)Curated
    Sequence conflicti177 – 1771N → S in BAG35173. (PubMed:14702039)Curated
    Sequence conflicti202 – 2021K → KAS in ABB01006. 1 PublicationCurated
    Sequence conflicti260 – 2601A → T in BAG35173. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti29 – 291D → G in HLD4; transfection with the mutant protein impairs cell growth that worsens with increasing temperature. 1 Publication
    VAR_054785
    Natural varianti98 – 981V → I in SPG13. 1 Publication
    VAR_026748

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei144 – 15815VMLAV…ELKKQ → RNVCCHHSVLNFSVL in isoform 2. 1 PublicationVSP_056144Add
    BLAST
    Alternative sequencei159 – 573415Missing in isoform 2. 1 PublicationVSP_056145Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22382 mRNA. Translation: AAA60127.1.
    M34664 mRNA. Translation: AAA36022.1.
    AJ250915 Genomic DNA. Translation: CAB75426.1.
    DQ217936 Genomic DNA. Translation: ABB01006.1.
    AK301276 mRNA. Translation: BAH13448.1.
    AK312240 mRNA. Translation: BAG35173.1.
    AC010746 Genomic DNA. No translation available.
    AC020550 Genomic DNA. No translation available.
    AC114809 Genomic DNA. No translation available.
    BC002676 mRNA. Translation: AAH02676.1.
    BC003030 mRNA. Translation: AAH03030.1.
    BC067082 mRNA. Translation: AAH67082.1.
    BC073746 mRNA. Translation: AAH73746.1.
    CCDSiCCDS33357.1.
    PIRiA32800.
    RefSeqiNP_002147.2. NM_002156.4.
    NP_955472.1. NM_199440.1.
    XP_005246575.1. XM_005246518.1.
    UniGeneiHs.595053.
    Hs.727543.

    Genome annotation databases

    EnsembliENST00000345042; ENSP00000340019; ENSG00000144381.
    ENST00000388968; ENSP00000373620; ENSG00000144381.
    ENST00000544407; ENSP00000441296; ENSG00000144381.
    GeneIDi3329.
    KEGGihsa:3329.
    UCSCiuc002uui.3. human.

    Polymorphism databases

    DMDMi129379.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22382 mRNA. Translation: AAA60127.1 .
    M34664 mRNA. Translation: AAA36022.1 .
    AJ250915 Genomic DNA. Translation: CAB75426.1 .
    DQ217936 Genomic DNA. Translation: ABB01006.1 .
    AK301276 mRNA. Translation: BAH13448.1 .
    AK312240 mRNA. Translation: BAG35173.1 .
    AC010746 Genomic DNA. No translation available.
    AC020550 Genomic DNA. No translation available.
    AC114809 Genomic DNA. No translation available.
    BC002676 mRNA. Translation: AAH02676.1 .
    BC003030 mRNA. Translation: AAH03030.1 .
    BC067082 mRNA. Translation: AAH67082.1 .
    BC073746 mRNA. Translation: AAH73746.1 .
    CCDSi CCDS33357.1.
    PIRi A32800.
    RefSeqi NP_002147.2. NM_002156.4.
    NP_955472.1. NM_199440.1.
    XP_005246575.1. XM_005246518.1.
    UniGenei Hs.595053.
    Hs.727543.

    3D structure databases

    ProteinModelPortali P10809.
    SMRi P10809. Positions 27-551.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109561. 127 interactions.
    DIPi DIP-58N.
    IntActi P10809. 67 interactions.
    MINTi MINT-1162735.
    STRINGi 9606.ENSP00000340019.

    Chemistry

    ChEMBLi CHEMBL4721.

    PTM databases

    PhosphoSitei P10809.

    Polymorphism databases

    DMDMi 129379.

    2D gel databases

    DOSAC-COBS-2DPAGE P10809.
    OGPi P10809.
    REPRODUCTION-2DPAGE IPI00784154.
    P10809.
    SWISS-2DPAGE P10809.
    UCD-2DPAGE P10809.

    Proteomic databases

    MaxQBi P10809.
    PaxDbi P10809.
    PRIDEi P10809.

    Protocols and materials databases

    DNASUi 3329.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000345042 ; ENSP00000340019 ; ENSG00000144381 .
    ENST00000388968 ; ENSP00000373620 ; ENSG00000144381 .
    ENST00000544407 ; ENSP00000441296 ; ENSG00000144381 .
    GeneIDi 3329.
    KEGGi hsa:3329.
    UCSCi uc002uui.3. human.

    Organism-specific databases

    CTDi 3329.
    GeneCardsi GC02M198315.
    HGNCi HGNC:5261. HSPD1.
    HPAi CAB002775.
    HPA001523.
    HPA050025.
    MIMi 118190. gene.
    605280. phenotype.
    612233. phenotype.
    neXtProti NX_P10809.
    Orphaneti 100994. Autosomal dominant spastic paraplegia type 13.
    280288. Pelizaeus-Merzbacher-like due to HSPD1 mutation.
    PharmGKBi PA29527.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0459.
    HOGENOMi HOG000076290.
    HOVERGENi HBG001982.
    InParanoidi P10809.
    KOi K04077.
    OMAi NYKAANE.
    OrthoDBi EOG7HTHGJ.
    PhylomeDBi P10809.
    TreeFami TF300475.

    Enzyme and pathway databases

    Reactomei REACT_118595. Mitochondrial protein import.

    Miscellaneous databases

    ChiTaRSi HSPD1. human.
    GeneWikii GroEL.
    GenomeRNAii 3329.
    NextBioi 13188.
    PROi P10809.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P10809.
    Bgeei P10809.
    CleanExi HS_HSPD1.
    Genevestigatori P10809.

    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. "Primary structure of a human mitochondrial protein homologous to the bacterial and plant chaperonins and to the 65-kilodalton mycobacterial antigen."
      Jindal S., Dudani A.K., Singh B., Harley C.B., Gupta R.S.
      Mol. Cell. Biol. 9:2279-2283(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Nucleotide sequences and novel structural features of human and Chinese hamster hsp60 (chaperonin) gene families."
      Venner T.J., Singh B., Gupta R.S.
      DNA Cell Biol. 9:545-552(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Genomic structure of the human mitochondrial chaperonin genes: HSP60 and HSP10 are localised head to head on chromosome 2 separated by a bidirectional promoter."
      Hansen J.J., Bross P., Westergaard M., Nielsen M.N., Eiberg H., Boerglum A.D., Mogensen J., Kristiansen K., Bolund L., Gregersen N.
      Hum. Genet. 112:71-77(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Genetic variation in immune response genes."
      Tan J., Ong R., Hibberd M.L., Seielstad M.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "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] (ISOFORMS 1 AND 2).
      Tissue: Adrenal gland and Spleen.
    6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1).
      Tissue: Lung, Skin and Uterus.
    8. "Amino-acid sequence homology of a polymorphic cellular protein from human lymphocytes and the chaperonins from Escherichia coli (groEL) and chloroplasts (Rubisco-binding protein)."
      Waldinger D., Eckerskorn C., Lottspeich F., Cleve H.
      Biol. Chem. Hoppe-Seyler 369:1185-1189(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-573.
    9. "Development of a database of amino acid sequences for human colon carcinoma proteins separated by two-dimensional polyacrylamide gel electrophoresis."
      Ward L.D., Hong J., Whitehead R.H., Simpson R.J.
      Electrophoresis 11:883-891(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-55.
      Tissue: Colon carcinoma.
    10. "Complex formation of human T-cell leukemia virus type I p40tax transactivator with cellular polypeptides."
      Nagata K., Ide Y., Takagi T., Ohtani K., Aoshima M., Tozawa H., Nakamura M., Sugamura K.
      J. Virol. 66:1040-1049(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-55, INTERACTION WITH HTLV-1 P40TAX.
    11. "Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2."
      Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E., Simpson R.J., Dorow D.S.
      Electrophoresis 18:588-598(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-50.
      Tissue: Mammary carcinoma.
    12. "The human myocardial two-dimensional gel protein database: update 1994."
      Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.
      Electrophoresis 15:1459-1465(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-46.
      Tissue: Heart.
    13. "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 27-37.
      Tissue: Platelet.
    14. "Human liver protein map: a reference database established by microsequencing and gel comparison."
      Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
      Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-35.
      Tissue: Liver.
    15. Bienvenut W.V.
      Submitted (OCT-2004) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 61-72, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    16. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 61-72; 206-218; 237-249; 251-290; 430-446 AND 463-469, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    17. "Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes."
      Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.
      Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 97-121; 251-268 AND 430-446.
      Tissue: Adipocyte.
    18. "A two-dimensional gel database of human colon carcinoma proteins."
      Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.
      Electrophoresis 18:605-613(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
      Tissue: Colon carcinoma.
    19. Cited for: MITOCHONDRIAL IMPORT.
    20. "Interaction of the hepatitis B virus X protein (HBx) with heat shock protein 60 enhances HBx-mediated apoptosis."
      Tanaka Y., Kanai F., Kawakami T., Tateishi K., Ijichi H., Kawabe T., Arakawa Y., Kawakami T., Nishimura T., Shirakata Y., Koike K., Omata M.
      Biochem. Biophys. Res. Commun. 318:461-469(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HBV PROTEIN X.
    21. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    25. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-82; LYS-125; LYS-130; LYS-202; LYS-218; LYS-269; LYS-352; LYS-359; LYS-396 AND LYS-469, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. Cited for: MALONYLATION AT LYS-133.
    29. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "ATAD3B is a human embryonic stem cell specific mitochondrial protein, re-expressed in cancer cells, that functions as dominant negative for the ubiquitous ATAD3A."
      Merle N., Feraud O., Gilquin B., Hubstenberger A., Kieffer-Jacquinot S., Assard N., Bennaceur-Griscelli A., Honnorat J., Baudier J.
      Mitochondrion 12:441-448(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATAD3A.
    31. "A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity."
      Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.
      PLoS Genet. 9:E1003210-E1003210(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH METTL20 AND METTL21B.
    32. "Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60."
      Hansen J.J., Durr A., Cournu-Rebeix I., Georgopoulos C., Ang D., Nielsen M.N., Davoine C.-S., Brice A., Fontaine B., Gregersen N., Bross P.
      Am. J. Hum. Genet. 70:1328-1332(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SPG13 ILE-98.
    33. "Mitochondrial Hsp60 chaperonopathy causes an autosomal-recessive neurodegenerative disorder linked to brain hypomyelination and leukodystrophy."
      Magen D., Georgopoulos C., Bross P., Ang D., Segev Y., Goldsher D., Nemirovski A., Shahar E., Ravid S., Luder A., Heno B., Gershoni-Baruch R., Skorecki K., Mandel H.
      Am. J. Hum. Genet. 83:30-42(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HLD4 GLY-29, CHARACTERIZATION OF VARIANT HLD4 GLY-29.

    Entry informationi

    Entry nameiCH60_HUMAN
    AccessioniPrimary (citable) accession number: P10809
    Secondary accession number(s): B2R5M6
    , B7Z712, Q38L19, Q9UCR6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: August 1, 1990
    Last modified: October 1, 2014
    This is version 181 of the entry and version 2 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

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3