P63038 (CH60_MOUSE) 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
HSP-65
Heat shock protein 60
Short name=HSP-60
Short name=Hsp60
Mitochondrial matrix protein P1

Gene names

Name:	Hspd1
Synonyms:	Hsp60

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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 ATAD3A By similarity. Interacts with HRAS. Ref.2
Subcellular location	Mitochondrion matrix By similarity.
Sequence similarities	Belongs to the chaperonin (HSP60) family.
Sequence caution	The sequence AAI06113.1 differs from that shown. Reason: . Potential poly-A sequence.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing
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	B cell cytokine production Inferred from electronic annotation. Source: Compara B cell proliferation Inferred from electronic annotation. Source: Compara MyD88-dependent toll-like receptor signaling pathway Inferred from electronic annotation. Source: Compara 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 electronic annotation. Source: Compara isotype switching to IgG isotypes Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of T cell activation Inferred from direct assay PubMed 17164250. Source: BHF-UCL positive regulation of T cell mediated immune response to tumor cell Inferred from electronic annotation. Source: Compara positive regulation of apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of interferon-alpha production Inferred from direct assay PubMed 17164250. Source: MGI positive regulation of interferon-gamma production Inferred from direct assay PubMed 17164250. Source: BHF-UCL positive regulation of interleukin-10 production Inferred from electronic annotation. Source: Compara positive regulation of interleukin-12 production Inferred from electronic annotation. Source: Compara positive regulation of interleukin-6 production Inferred from electronic annotation. Source: Compara positive regulation of macrophage activation Inferred from electronic annotation. Source: Compara protein refolding Inferred from electronic annotation. Source: Compara response to unfolded protein Inferred from electronic annotation. Source: Compara
Cellular_component	cell surface Inferred from electronic annotation. Source: Compara coated pit Inferred from electronic annotation. Source: Compara coated vesicle Inferred from electronic annotation. Source: Compara cyclin-dependent protein kinase activating kinase holoenzyme complex Inferred from electronic annotation. Source: Compara cytosol Inferred from electronic annotation. Source: Compara early endosome Inferred from electronic annotation. Source: Compara extracellular space Inferred from electronic annotation. Source: Compara lipopolysaccharide receptor complex Inferred from electronic annotation. Source: Compara mitochondrial inner membrane Inferred from direct assay PubMed 12865426. Source: MGI mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay PubMed 15252132. Source: MGI secretory granule Inferred from direct assay PubMed 1516759PubMed 8824711. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cell surface binding Inferred from electronic annotation. Source: Compara lipopolysaccharide binding Inferred from direct assay PubMed 17164250. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P63038-1)

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.

Isoform 2 (identifier: P63038-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 26	26	Mitochondrion Ref.6
	Chain	27 – 573	547	60 kDa heat shock protein, mitochondrial		PRO_0000005027
Amino acid modifications
	Modified residue	70	1	Phosphoserine By similarity
	Modified residue	82	1	N6-acetyllysine By similarity
	Modified residue	125	1	N6-acetyllysine By similarity
	Modified residue	130	1	N6-acetyllysine By similarity
	Modified residue	133	1	N6-malonyllysine By similarity
	Modified residue	202	1	N6-acetyllysine By similarity
	Modified residue	218	1	N6-acetyllysine By similarity
	Modified residue	223	1	Phosphotyrosine Ref.8
	Modified residue	269	1	N6-acetyllysine By similarity
	Modified residue	352	1	N6-acetyllysine By similarity
	Modified residue	359	1	N6-acetyllysine By similarity
	Modified residue	396	1	N6-acetyllysine By similarity
	Modified residue	469	1	N6-acetyllysine By similarity
Natural variations
	Alternative sequence	1 – 315	315	Missing in isoform 2.		VSP_025020
Experimental info
	Sequence conflict	4	1	L → H AA sequence Ref.2
	Sequence conflict	139	1	E → K AA sequence Ref.2
	Sequence conflict	251	1	I → F in CAA37653. Ref.5
	Sequence conflict	364	1	K → E in BAC40607. Ref.3
	Sequence conflict	518	1	I → V in CAA38762. Ref.1
	Sequence conflict	527	1	T → Q AA sequence Ref.2
	Sequence conflict	547	1	T → V AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 31, 2004. Version 1. Checksum: 0014B58B77D0127B	FASTA	573	60,955
	10 20 30 40 50 60 MLRLPTVLRQ MRPVSRALAP 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 DIGNIISDAM KKVGRKGVIT VKDGKTLNDE LEIIEGMKFD RGYISPYFIN TSKGQKCEFQ 250 260 270 280 290 300 DAYVLLSEKK ISSVQSIVPA LEIANAHRKP LVIIAEDVDG EALSTLVLNR LKVGLQVVAV 310 320 330 340 350 360 KAPGFGDNRK NQLKDMAIAT GGAVFGEEGL NLNLEDVQAH DLGKVGEVIV TKDDAMLLKG 370 380 390 400 410 420 KGDKAHIEKR IQEITEQLDI TTSEYEKEKL NERLAKLSDG VAVLKVGGTS DVEVNEKKDR 430 440 450 460 470 480 VTDALNATRA AVEEGIVLGG GCALLRCIPA LDSLKPANED QKIGIEIIKR ALKIPAMTIA 490 500 510 520 530 540 KNAGVEGSLI VEKILQSSSE VGYDAMLGDF VNMVEKGIID PTKVVRTALL DAAGVASLLT 550 560 570 TAEAVVTEIP KEEKDPGMGA MGGMGGGMGG GMF
	Isoform 2 [UniParc]. Checksum: DD79DC2838C3771B	FASTA	258	27,015
	10 20 30 40 50 60 MAIATGGAVF GEEGLNLNLE DVQAHDLGKV GEVIVTKDDA MLLKGKGDKA HIEKRIQEIT 70 80 90 100 110 120 EQLDITTSEY EKEKLNERLA KLSDGVAVLK VGGTSDVEVN EKKDRVTDAL NATRAAVEEG 130 140 150 160 170 180 IVLGGGCALL RCIPALDSLK PANEDQKIGI EIIKRALKIP AMTIAKNAGV EGSLIVEKIL 190 200 210 220 230 240 QSSSEVGYDA MLGDFVNMVE KGIIDPTKVV RTALLDAAGV ASLLTTAEAV VTEIPKEEKD 250 PGMGAMGGMG GGMGGGMF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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 Cited for: PROTEIN SEQUENCE OF 38-58; 61-72; 97-121; 134-141; 143-191; 196-202; 206-233; 237-290; 293-309; 345-359; 371-387; 397-417; 421-469; 474-516 AND 527-554. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
[8]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-223, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00308885. IPI00845678.
PIR	HHMS60. S13084.
RefSeq	NP_034607.3. NM_010477.4.
UniGene	Mm.1777.
3D structure databases
ProteinModelPortal	P63038.
SMR	P63038. Positions 27-551.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-31396N.
IntAct	P63038. 8 interactions.
MINT	MINT-1860238.
2D gel databases
REPRODUCTION-2DPAGE	IPI00308885. P63038.
SWISS-2DPAGE	P63038.
UCD-2DPAGE	P19227. P63038.
Proteomic databases
PaxDb	P63038.
PRIDE	P63038.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000027123; ENSMUSP00000027123; ENSMUSG00000025980.
GeneID	15510.
KEGG	mmu:15510.
UCSC	uc007bab.2. mouse.
Organism-specific databases
CTD	3329.
MGI	MGI:96242. Hspd1.
Phylogenomic databases
eggNOG	COG0459.
GeneTree	ENSGT00390000005727.
HOVERGEN	HBG001982.
InParanoid	P63038.
KO	K04077.
OMA	CATRAAV.
OrthoDB	EOG4PK27J.
Gene expression databases
ArrayExpress	P63038.
Bgee	P63038.
CleanEx	MM_HSPD1.
Genevestigator	P63038.
GermOnline	ENSMUSG00000025980. Mus musculus.
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
ChiTaRS	HSPD1. mouse.
NextBio	288418.
PMAP-CutDB	P63038.
SOURCE	Search...

Entry information

Entry name

CH60_MOUSE

Accession

Primary (citable) accession number: P63038
Secondary accession number(s): P19226 , P19227, P97602, Q3KQP2, Q3UIP0, Q8C2C7, Q8VEF4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	August 31, 2004
Last modified:	May 29, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program