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P63038 (CH60_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·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
HSP-65
Heat shock protein 60
Short name=HSP-60
Short name=Hsp60
Mitochondrial matrix protein P1
Gene names
Name:Hspd1
Synonyms:Hsp60
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 ATAD3A By similarity. Interacts with METTL20 and METTL21B By similarity. Interacts with HRAS. Ref.2

Subcellular location

Mitochondrion matrix By similarity HAMAP-Rule MF_00600.

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 componentMitochondrion
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processB cell cytokine production

Inferred from electronic annotation. Source: Ensembl

B cell proliferation

Inferred from electronic annotation. Source: Ensembl

MyD88-dependent toll-like receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

isotype switching to IgG isotypes

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

positive regulation of interleukin-12 production

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-6 production

Inferred from electronic annotation. Source: Ensembl

positive regulation of macrophage activation

Inferred from electronic annotation. Source: Ensembl

protein refolding

Inferred from electronic annotation. Source: Ensembl

response to unfolded protein

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell surface

Inferred from electronic annotation. Source: Ensembl

coated pit

Inferred from electronic annotation. Source: Ensembl

coated vesicle

Inferred from electronic annotation. Source: Ensembl

cyclin-dependent protein kinase activating kinase holoenzyme complex

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 21874024. Source: MGI

cytosol

Inferred from electronic annotation. Source: Ensembl

early endosome

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from electronic annotation. Source: Ensembl

intracellular membrane-bounded organelle

Inferred from direct assay PubMed 15136728PubMed 16708399. Source: MGI

lipopolysaccharide receptor complex

Inferred from electronic annotation. Source: Ensembl

mitochondrial inner membrane

Inferred from direct assay PubMed 12865426. Source: MGI

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 12931191PubMed 14651853PubMed 1516759PubMed 16959573PubMed 18614015PubMed 23976951PubMed 8824711PubMed 9867803. Source: MGI

plasma membrane

Inferred from direct assay PubMed 15252132. Source: MGI

protein complex

Inferred from sequence or structural similarity. Source: UniProtKB

secretory granule

Inferred from direct assay PubMed 1516759PubMed 8824711. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

double-stranded RNA binding

Inferred from sequence orthology PubMed 21266579. Source: MGI

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2626Mitochondrion Ref.6
Chain27 – 57354760 kDa heat shock protein, mitochondrial HAMAP-Rule MF_00600
PRO_0000005027

Amino acid modifications

Modified residue311N6-succinyllysine Ref.9
Modified residue701Phosphoserine Ref.8
Modified residue751N6-acetyllysine Ref.10
Modified residue821N6-acetyllysine; alternate By similarity
Modified residue821N6-succinyllysine; alternate Ref.9
Modified residue871N6-acetyllysine Ref.10
Modified residue911N6-acetyllysine Ref.10
Modified residue1251N6-acetyllysine; alternate Ref.10
Modified residue1251N6-succinyllysine; alternate Ref.9
Modified residue1301N6-acetyllysine Ref.10
Modified residue1331N6-acetyllysine; alternate Ref.10
Modified residue1331N6-malonyllysine; alternate By similarity
Modified residue1331N6-succinyllysine; alternate Ref.9
Modified residue1561N6-acetyllysine Ref.10
Modified residue1911N6-acetyllysine; alternate Ref.10
Modified residue1911N6-succinyllysine; alternate Ref.9
Modified residue2021N6-acetyllysine; alternate Ref.10
Modified residue2021N6-succinyllysine; alternate Ref.9
Modified residue2051N6-acetyllysine; alternate Ref.10
Modified residue2051N6-succinyllysine; alternate Ref.9
Modified residue2181N6-acetyllysine; alternate Ref.10
Modified residue2181N6-succinyllysine; alternate Ref.9
Modified residue2361N6-acetyllysine; alternate Ref.10
Modified residue2361N6-succinyllysine; alternate Ref.9
Modified residue2491N6-acetyllysine Ref.10
Modified residue2501N6-acetyllysine; alternate Ref.10
Modified residue2501N6-succinyllysine; alternate Ref.9
Modified residue2691N6-acetyllysine Ref.10
Modified residue2921N6-acetyllysine Ref.10
Modified residue3011N6-succinyllysine Ref.9
Modified residue3141N6-acetyllysine Ref.10
Modified residue3521N6-acetyllysine; alternate Ref.10
Modified residue3521N6-succinyllysine; alternate Ref.9
Modified residue3591N6-acetyllysine Ref.10
Modified residue3891N6-acetyllysine Ref.10
Modified residue3961N6-acetyllysine; alternate By similarity
Modified residue3961N6-succinyllysine; alternate Ref.9
Modified residue4101Phosphoserine Ref.8
Modified residue4551N6-acetyllysine; alternate Ref.10
Modified residue4551N6-succinyllysine; alternate Ref.9
Modified residue4691N6-acetyllysine Ref.10
Modified residue4811N6-acetyllysine; alternate Ref.10
Modified residue4811N6-succinyllysine; alternate Ref.9

Natural variations

Alternative sequence1 – 315315Missing in isoform 2.
VSP_025020

Experimental info

Sequence conflict41L → H AA sequence Ref.2
Sequence conflict1391E → K AA sequence Ref.2
Sequence conflict2511I → F in CAA37653. Ref.5
Sequence conflict3641K → E in BAC40607. Ref.3
Sequence conflict5181I → V in CAA38762. Ref.1
Sequence conflict5271T → Q AA sequence Ref.2
Sequence conflict5471T → V AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 31, 2004. Version 1.
Checksum: 0014B58B77D0127B

FASTA57360,955
        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 

« Hide

Isoform 2 [UniParc].

Checksum: DD79DC2838C3771B
Show »

FASTA25827,015

References

« Hide '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. expand/collapse author list , 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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[9]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-31; LYS-82; LYS-125; LYS-133; LYS-191; LYS-202; LYS-205; LYS-218; LYS-236; LYS-250; LYS-301; LYS-352; LYS-396; LYS-455 AND LYS-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast and Liver.
[10]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-75; LYS-87; LYS-91; LYS-125; LYS-130; LYS-133; LYS-156; LYS-191; LYS-202; LYS-205; LYS-218; LYS-236; LYS-249; LYS-250; LYS-269; LYS-292; LYS-314; LYS-352; LYS-359; LYS-389; LYS-455; LYS-469 AND LYS-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+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.
CCDSCCDS35569.1. [P63038-1]
PIRHHMS60. S13084.
RefSeqNP_034607.3. NM_010477.4. [P63038-1]
XP_006495769.1. XM_006495706.1. [P63038-1]
UniGeneMm.1777.

3D structure databases

ProteinModelPortalP63038.
SMRP63038. Positions 27-551.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200451. 12 interactions.
DIPDIP-31396N.
IntActP63038. 20 interactions.
MINTMINT-1860238.

2D gel databases

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

Proteomic databases

MaxQBP63038.
PaxDbP63038.
PRIDEP63038.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027123; ENSMUSP00000027123; ENSMUSG00000025980. [P63038-1]
GeneID15510.
KEGGmmu:15510.
UCSCuc007bab.2. mouse. [P63038-1]

Organism-specific databases

CTD3329.
MGIMGI:96242. Hspd1.

Phylogenomic databases

eggNOGCOG0459.
GeneTreeENSGT00390000005727.
HOVERGENHBG001982.
InParanoidP63038.
KOK04077.
OMAEYGDMIG.
OrthoDBEOG7HTHGJ.
PhylomeDBP63038.
TreeFamTF300475.

Gene expression databases

ArrayExpressP63038.
BgeeP63038.
CleanExMM_HSPD1.
GenevestigatorP63038.

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. mouse.
NextBio288418.
PMAP-CutDBP63038.
PROP63038.
SOURCESearch...

Entry information

Entry nameCH60_MOUSE
AccessionPrimary (citable) accession number: P63038
Secondary accession number(s): P19226 expand/collapse secondary AC list , P19227, P97602, Q3KQP2, Q3UIP0, Q8C2C7, Q8VEF4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: July 9, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot