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P10809 (CH60_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 179. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:HSPD1
Synonyms:HSP60
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length573 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_00600

Subunit structure

Interacts with HRAS By similarity. Interacts with HBV protein X and HTLV-1 protein p40tax. Interacts with ATAD3A. Interacts with METTL20 and METTL21B. Ref.9 Ref.19 Ref.29 Ref.30

Subcellular location

Mitochondrion matrix HAMAP-Rule MF_00600.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.31

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.32

Sequence similarities

Belongs to the chaperonin (HSP60) family.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentMitochondrion
   DiseaseDisease mutation
Hereditary spastic paraplegia
Leukodystrophy
Neurodegeneration
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' protein folding

Inferred from sequence or structural similarity. Source: BHF-UCL

ATP catabolic process

Inferred from sequence or structural similarity. Source: GOC

B cell activation

Inferred from direct assay PubMed 16148103. Source: BHF-UCL

B cell cytokine production

Inferred from direct assay PubMed 16148103. Source: BHF-UCL

B cell proliferation

Inferred from direct assay PubMed 16148103. Source: BHF-UCL

MyD88-dependent toll-like receptor signaling pathway

Inferred from direct assay PubMed 16148103. Source: BHF-UCL

T cell activation

Inferred from direct assay PubMed 15371451PubMed 17164250PubMed 18256040. Source: MGI

activation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay PubMed 17823127. Source: BHF-UCL

chaperone-mediated protein complex assembly

Inferred from sequence or structural similarity. Source: BHF-UCL

isotype switching to IgG isotypes

Inferred from direct assay PubMed 16148103. Source: BHF-UCL

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 18086682. Source: UniProtKB

positive regulation of T cell activation

Inferred from direct assay PubMed 16148103PubMed 17164250. Source: BHF-UCL

positive regulation of T cell mediated immune response to tumor cell

Inferred from direct assay PubMed 10663613. Source: BHF-UCL

positive regulation of apoptotic process

Inferred from mutant phenotype PubMed 17823127. Source: BHF-UCL

positive regulation of interferon-alpha production

Inferred from direct assay PubMed 17164250. Source: BHF-UCL

positive regulation of interferon-gamma production

Inferred from direct assay PubMed 17164250. Source: BHF-UCL

positive regulation of interleukin-10 production

Inferred from direct assay PubMed 16148103. Source: BHF-UCL

positive regulation of interleukin-12 production

Inferred from direct assay PubMed 17164250. Source: BHF-UCL

positive regulation of interleukin-6 production

Inferred from direct assay PubMed 16148103. Source: BHF-UCL

positive regulation of macrophage activation

Inferred from direct assay PubMed 17164250. Source: BHF-UCL

protein maturation

Inferred from sequence or structural similarity. Source: BHF-UCL

protein refolding

Inferred from direct assay PubMed 11050098. Source: UniProtKB

protein stabilization

Inferred from mutant phenotype PubMed 18086682. Source: UniProtKB

response to unfolded protein

Inferred from direct assay PubMed 11050098. Source: BHF-UCL

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell surface

Inferred from direct assay PubMed 9243807. Source: UniProtKB

coated pit

Inferred from direct assay PubMed 11807771. Source: BHF-UCL

coated vesicle

Inferred from direct assay PubMed 11807771. Source: BHF-UCL

cytoplasm

Inferred from direct assay PubMed 21328542. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 18086682. Source: UniProtKB

early endosome

Inferred from direct assay PubMed 11807771. Source: BHF-UCL

extracellular space

Inferred from direct assay PubMed 18229457. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337. Source: UniProt

lipopolysaccharide receptor complex

Inferred from direct assay PubMed 17164250. Source: BHF-UCL

mitochondrial inner membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

mitochondrial matrix

Traceable author statement PubMed 17823127. Source: BHF-UCL

mitochondrion

Inferred from direct assay PubMed 18086682. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from direct assay PubMed 21328542. Source: UniProtKB

secretory granule

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Inferred from sequence or structural similarity. Source: BHF-UCL

DNA replication origin binding

Inferred from sequence or structural similarity. Source: BHF-UCL

chaperone binding

Inferred from physical interaction PubMed 10205158. Source: UniProtKB

double-stranded RNA binding

Inferred from direct assay PubMed 21266579. Source: MGI

lipopolysaccharide binding

Inferred from direct assay PubMed 17164250. Source: BHF-UCL

p53 binding

Inferred from physical interaction PubMed 18086682. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 18086682. Source: UniProtKB

single-stranded DNA binding

Inferred from sequence or structural similarity. Source: BHF-UCL

unfolded protein binding

Inferred by curator PubMed 11050098. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2626Mitochondrion Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
Chain27 – 57354760 kDa heat shock protein, mitochondrial HAMAP-Rule MF_00600
PRO_0000005026

Amino acid modifications

Modified residue311N6-succinyllysine By similarity
Modified residue701Phosphoserine Ref.21 Ref.22 Ref.25 Ref.28
Modified residue751N6-acetyllysine By similarity
Modified residue821N6-acetyllysine; alternate Ref.24
Modified residue821N6-succinyllysine; alternate By similarity
Modified residue871N6-acetyllysine By similarity
Modified residue911N6-acetyllysine By similarity
Modified residue1251N6-acetyllysine; alternate Ref.24
Modified residue1251N6-succinyllysine; alternate By similarity
Modified residue1301N6-acetyllysine Ref.24
Modified residue1331N6-acetyllysine; alternate By similarity
Modified residue1331N6-malonyllysine; alternate Ref.27
Modified residue1331N6-succinyllysine; alternate By similarity
Modified residue1561N6-acetyllysine By similarity
Modified residue1911N6-acetyllysine; alternate By similarity
Modified residue1911N6-succinyllysine; alternate By similarity
Modified residue2021N6-acetyllysine; alternate Ref.24
Modified residue2021N6-succinyllysine; alternate By similarity
Modified residue2051N6-acetyllysine; alternate By similarity
Modified residue2051N6-succinyllysine; alternate By similarity
Modified residue2181N6-acetyllysine; alternate Ref.24
Modified residue2181N6-succinyllysine; alternate By similarity
Modified residue2361N6-acetyllysine; alternate By similarity
Modified residue2361N6-succinyllysine; alternate By similarity
Modified residue2491N6-acetyllysine By similarity
Modified residue2501N6-acetyllysine; alternate By similarity
Modified residue2501N6-succinyllysine; alternate By similarity
Modified residue2691N6-acetyllysine Ref.24
Modified residue2921N6-acetyllysine By similarity
Modified residue3011N6-succinyllysine By similarity
Modified residue3141N6-acetyllysine By similarity
Modified residue3521N6-acetyllysine; alternate Ref.24
Modified residue3521N6-succinyllysine; alternate By similarity
Modified residue3591N6-acetyllysine Ref.24
Modified residue3891N6-acetyllysine By similarity
Modified residue3961N6-acetyllysine; alternate Ref.24
Modified residue3961N6-succinyllysine; alternate By similarity
Modified residue4101Phosphoserine By similarity
Modified residue4691N6-acetyllysine Ref.24
Modified residue4811N6-acetyllysine; alternate By similarity
Modified residue4811N6-succinyllysine; alternate By similarity

Natural variations

Natural variant291D → G in HLD4; transfection with the mutant protein impairs cell growth that worsens with increasing temperature. Ref.32
VAR_054785
Natural variant981V → I in SPG13. Ref.31
VAR_026748

Experimental info

Sequence conflict671S → G in AAA36022. Ref.2
Sequence conflict1111D → N in BAG35173. Ref.5
Sequence conflict1771N → S in BAG35173. Ref.5
Sequence conflict2021K → KAS in ABB01006. Ref.4
Sequence conflict2601A → T in BAG35173. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P10809 [UniParc].

Last modified August 1, 1990. Version 2.
Checksum: E51E1BAD9615899C

FASTA57361,055
        10         20         30         40         50         60 
MLRLPTVFRQ MRPVSRVLAP HLTRAYAKDV KFGADARALM LQGVDLLADA VAVTMGPKGR 

        70         80         90        100        110        120 
TVIIEQSWGS PKVTKDGVTV AKSIDLKDKY KNIGAKLVQD VANNTNEEAG DGTTTATVLA 

       130        140        150        160        170        180 
RSIAKEGFEK ISKGANPVEI RRGVMLAVDA VIAELKKQSK PVTTPEEIAQ VATISANGDK 

       190        200        210        220        230        240 
EIGNIISDAM KKVGRKGVIT VKDGKTLNDE LEIIEGMKFD RGYISPYFIN TSKGQKCEFQ 

       250        260        270        280        290        300 
DAYVLLSEKK ISSIQSIVPA LEIANAHRKP LVIIAEDVDG EALSTLVLNR LKVGLQVVAV 

       310        320        330        340        350        360 
KAPGFGDNRK NQLKDMAIAT GGAVFGEEGL TLNLEDVQPH DLGKVGEVIV TKDDAMLLKG 

       370        380        390        400        410        420 
KGDKAQIEKR IQEIIEQLDV TTSEYEKEKL NERLAKLSDG VAVLKVGGTS DVEVNEKKDR 

       430        440        450        460        470        480 
VTDALNATRA AVEEGIVLGG GCALLRCIPA LDSLTPANED QKIGIEIIKR TLKIPAMTIA 

       490        500        510        520        530        540 
KNAGVEGSLI VEKIMQSSSE VGYDAMAGDF VNMVEKGIID PTKVVRTALL DAAGVASLLT 

       550        560        570 
TAEVVVTEIP KEEKDPGMGA MGGMGGGMGG GMF 

« Hide

References

« Hide 'large scale' references
[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].
[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].
[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. expand/collapse author list , 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: Adrenal gland.
[6]"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: Lung, Skin and Uterus.
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]Bienvenut W.V.
Submitted (OCT-2004) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 61-72, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[15]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.
[16]"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.
[17]"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.
[18]"Mitochondrial import of the human chaperonin (HSP60) protein."
Singh B., Patel H.V., Ridley R.G., Freeman K.B., Gupta R.S.
Biochem. Biophys. Res. Commun. 169:391-396(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: MITOCHONDRIAL IMPORT.
[19]"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.
[20]"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].
[21]"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.
[22]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"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.
[24]"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].
[25]"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.
[26]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"The first identification of lysine malonylation substrates and its regulatory enzyme."
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J., Verdin E., Ye Y., Zhao Y.
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: MALONYLATION AT LYS-133.
[28]"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].
[29]"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.
[30]"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.
[31]"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.
[32]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M22382 mRNA. Translation: AAA60127.1.
M34664 mRNA. Translation: AAA36022.1.
AJ250915 Genomic DNA. Translation: CAB75426.1.
DQ217936 Genomic DNA. Translation: ABB01006.1.
AK312240 mRNA. Translation: BAG35173.1.
BC002676 mRNA. Translation: AAH02676.1.
BC003030 mRNA. Translation: AAH03030.1.
BC067082 mRNA. Translation: AAH67082.1.
BC073746 mRNA. Translation: AAH73746.1.
CCDSCCDS33357.1.
PIRA32800.
RefSeqNP_002147.2. NM_002156.4.
NP_955472.1. NM_199440.1.
XP_005246575.1. XM_005246518.1.
UniGeneHs.595053.
Hs.727543.

3D structure databases

ProteinModelPortalP10809.
SMRP10809. Positions 27-551.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109561. 139 interactions.
DIPDIP-58N.
IntActP10809. 66 interactions.
MINTMINT-1162735.
STRING9606.ENSP00000340019.

Chemistry

ChEMBLCHEMBL4721.

PTM databases

PhosphoSiteP10809.

Polymorphism databases

DMDM129379.

2D gel databases

DOSAC-COBS-2DPAGEP10809.
OGPP10809.
REPRODUCTION-2DPAGEIPI00784154.
P10809.
SWISS-2DPAGEP10809.
UCD-2DPAGEP10809.

Proteomic databases

MaxQBP10809.
PaxDbP10809.
PRIDEP10809.

Protocols and materials databases

DNASU3329.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000345042; ENSP00000340019; ENSG00000144381.
ENST00000388968; ENSP00000373620; ENSG00000144381.
GeneID3329.
KEGGhsa:3329.
UCSCuc002uui.3. human.

Organism-specific databases

CTD3329.
GeneCardsGC02M198315.
HGNCHGNC:5261. HSPD1.
HPACAB002775.
HPA001523.
HPA050025.
MIM118190. gene.
605280. phenotype.
612233. phenotype.
neXtProtNX_P10809.
Orphanet100994. Autosomal dominant spastic paraplegia type 13.
280288. Pelizaeus-Merzbacher-like due to HSPD1 mutation.
PharmGKBPA29527.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0459.
HOGENOMHOG000076290.
HOVERGENHBG001982.
InParanoidP10809.
KOK04077.
OMANYKAANE.
OrthoDBEOG7HTHGJ.
PhylomeDBP10809.
TreeFamTF300475.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressP10809.
BgeeP10809.
CleanExHS_HSPD1.
GenevestigatorP10809.

Family and domain databases

Gene3D1.10.560.10. 2 hits.
3.50.7.10. 1 hit.
HAMAPMF_00600. CH60.
InterProIPR018370. Chaperonin_Cpn60_CS.
IPR001844. Chaprnin_Cpn60.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
[Graphical view]
PANTHERPTHR11353. PTHR11353. 1 hit.
PfamPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSPR00298. CHAPERONIN60.
SUPFAMSSF48592. SSF48592. 2 hits.
SSF52029. SSF52029. 1 hit.
TIGRFAMsTIGR02348. GroEL. 1 hit.
PROSITEPS00296. CHAPERONINS_CPN60. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHSPD1. human.
GeneWikiGroEL.
GenomeRNAi3329.
NextBio13188.
PROP10809.
SOURCESearch...

Entry information

Entry nameCH60_HUMAN
AccessionPrimary (citable) accession number: P10809
Secondary accession number(s): B2R5M6, Q38L19, Q9UCR6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: August 1, 1990
Last modified: July 9, 2014
This is version 179 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM