P10809 (CH60_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	HSPD1
Synonyms:	HSP60

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	573 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Subunit structure	Interacts with HRAS By similarity. Interacts with HBV protein X and HTLV-1 protein p40tax. Interacts with ATAD3A. Ref.9 Ref.19 Ref.29
Subcellular location	Mitochondrion matrix.
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. 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 occurrs within the first two decades of life. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.31
Sequence similarities	Belongs to the chaperonin (HSP60) family.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Mitochondrion
Disease	Disease mutation Hereditary spastic paraplegia Leukodystrophy Neurodegeneration
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' protein folding Inferred from sequence or structural similarity. 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 virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cell 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 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 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 plasma membrane part Inferred from electronic annotation. Source: Compara secretory granule Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular_function	ATP 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 cell surface binding Inferred from direct assay PubMed 11807771. Source: BHF-UCL lipopolysaccharide binding Inferred from direct assay PubMed 17164250. Source: BHF-UCL 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

With	Entry	#Exp.	IntAct	Notes
BRCA1	P38398	2	EBI-352528,EBI-349905
FHIT	P49789	5	EBI-352528,EBI-741760

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 26	26	Mitochondrion Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
	Chain	27 – 573	547	60 kDa heat shock protein, mitochondrial		PRO_0000005026
Amino acid modifications
	Modified residue	70	1	Phosphoserine Ref.21 Ref.22 Ref.25 Ref.28
	Modified residue	82	1	N6-acetyllysine Ref.24
	Modified residue	125	1	N6-acetyllysine Ref.24
	Modified residue	130	1	N6-acetyllysine Ref.24
	Modified residue	133	1	N6-malonyllysine Ref.27
	Modified residue	202	1	N6-acetyllysine Ref.24
	Modified residue	218	1	N6-acetyllysine Ref.24
	Modified residue	223	1	Phosphotyrosine By similarity
	Modified residue	269	1	N6-acetyllysine Ref.24
	Modified residue	352	1	N6-acetyllysine Ref.24
	Modified residue	359	1	N6-acetyllysine Ref.24
	Modified residue	396	1	N6-acetyllysine Ref.24
	Modified residue	469	1	N6-acetyllysine Ref.24
Natural variations
	Natural variant	29	1	D → G in HLD4; transfection with the mutant protein impairs cell growth that worsens with increasing temperature. Ref.31		VAR_054785
	Natural variant	98	1	V → I in SPG13. Ref.30		VAR_026748
Experimental info
	Sequence conflict	67	1	S → G in AAA36022. Ref.2
	Sequence conflict	111	1	D → N in BAG35173. Ref.5
	Sequence conflict	177	1	N → S in BAG35173. Ref.5
	Sequence conflict	202	1	K → KAS in ABB01006. Ref.4
	Sequence conflict	260	1	A → T in BAG35173. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P10809 [UniParc]. Last modified August 1, 1990. Version 2. Checksum: E51E1BAD9615899C	FASTA	573	61,055
	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

References

	« Hide 'large scale' referencesShow '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. , 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, 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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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]	"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.
[31]	"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.

Web resources

GeneReviews

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.
IPI	IPI00784154.
PIR	A32800.
RefSeq	NP_002147.2. NM_002156.4. NP_955472.1. NM_199440.1.
UniGene	Hs.595053. Hs.727543.
3D structure databases
ProteinModelPortal	P10809.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-58N.
IntAct	P10809. 43 interactions.
MINT	MINT-1162735.
STRING	9606.ENSP00000340019.
PTM databases
PhosphoSite	P10809.
Polymorphism databases
DMDM	129379.
2D gel databases
DOSAC-COBS-2DPAGE	P10809.
OGP	P10809.
REPRODUCTION-2DPAGE	IPI00784154. P10809.
SWISS-2DPAGE	P10809.
UCD-2DPAGE	P10809.
Proteomic databases
PaxDb	P10809.
PRIDE	P10809.
Protocols and materials databases
DNASU	3329.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000345042; ENSP00000340019; ENSG00000144381. ENST00000388968; ENSP00000373620; ENSG00000144381.
GeneID	3329.
KEGG	hsa:3329.
UCSC	uc002uui.3. human.
Organism-specific databases
CTD	3329.
GeneCards	GC02M198315.
HGNC	HGNC:5261. HSPD1.
HPA	CAB002775. HPA001523.
MIM	118190. gene. 605280. phenotype. 612233. phenotype.
neXtProt	NX_P10809.
Orphanet	100994. Autosomal dominant spastic paraplegia type 13. 280288. Pelizaeus-Merzbacher-like due to HSPD1 mutation.
PharmGKB	PA29527.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0459.
HOGENOM	HOG000076290.
HOVERGEN	HBG001982.
InParanoid	P10809.
KO	K04077.
OMA	CATRAAV.
OrthoDB	EOG4PK27J.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
Gene expression databases
ArrayExpress	P10809.
Bgee	P10809.
CleanEx	HS_HSPD1.
Genevestigator	P10809.
GermOnline	ENSG00000144381. Homo sapiens.
Family and domain databases
Gene3D	1.10.560.10. 2 hits. 3.50.7.10. 1 hit.
InterPro	IPR018370. Chaperonin_Cpn60_CS. IPR001844. Chaprnin_Cpn60. IPR002423. Cpn60/TCP-1. IPR027409. GroEL-like_apical_dom. IPR027413. GROEL-like_equatorial. [Graphical view]
PANTHER	PTHR11353. PTHR11353. 1 hit.
Pfam	PF00118. Cpn60_TCP1. 1 hit. [Graphical view]
PRINTS	PR00298. CHAPERONIN60.
SUPFAM	SSF48592. GroEL-ATPase. 1 hit. SSF52029. SSF52029. 1 hit.
TIGRFAMs	TIGR02348. GroEL. 1 hit.
PROSITE	PS00296. CHAPERONINS_CPN60. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL4721.
ChiTaRS	HSPD1. human.
GenomeRNAi	3329.
NextBio	13188.
SOURCE	Search...

Entry information

Entry name

CH60_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 166 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.