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Protein

60 kDa heat shock protein, mitochondrial

Gene

Hspd1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates 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. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein.By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei75ATPBy similarity1
Binding sitei440ATP; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei520ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi111 – 115ATPBy similarity5

GO - Molecular functioni

  • apolipoprotein A-I binding Source: Ensembl
  • ATP binding Source: UniProtKB-KW
  • chaperone binding Source: Ensembl
  • double-stranded RNA binding Source: Ensembl
  • high-density lipoprotein particle binding Source: Ensembl
  • hydrolase activity Source: UniProtKB-KW
  • insulin binding Source: RGD
  • lipopolysaccharide binding Source: Ensembl
  • misfolded protein binding Source: RGD
  • p53 binding Source: Ensembl
  • protease binding Source: RGD
  • protein binding involved in protein folding Source: GO_Central
  • protein complex binding Source: RGD
  • protein heterodimerization activity Source: RGD
  • ubiquitin protein ligase binding Source: Ensembl
  • unfolded protein binding Source: GO_Central

GO - Biological processi

  • 'de novo' protein folding Source: RGD
  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  • apoptotic mitochondrial changes Source: RGD
  • B cell cytokine production Source: Ensembl
  • B cell proliferation Source: Ensembl
  • chaperone mediated protein folding requiring cofactor Source: RGD
  • detection of misfolded protein Source: RGD
  • interaction with symbiont Source: Ensembl
  • isotype switching to IgG isotypes Source: Ensembl
  • MyD88-dependent toll-like receptor signaling pathway Source: Ensembl
  • negative regulation of apoptotic process Source: RGD
  • negative regulation of apoptotic process in bone marrow Source: RGD
  • negative regulation of neuron apoptotic process Source: RGD
  • negative regulation of reactive oxygen species biosynthetic process Source: RGD
  • positive regulation of inflammatory response Source: RGD
  • positive regulation of interferon-alpha production Source: Ensembl
  • positive regulation of interferon-gamma production Source: Ensembl
  • positive regulation of interleukin-10 production Source: Ensembl
  • positive regulation of interleukin-12 production Source: Ensembl
  • positive regulation of interleukin-6 secretion Source: RGD
  • positive regulation of macrophage activation Source: Ensembl
  • positive regulation of T cell activation Source: Ensembl
  • positive regulation of T cell mediated immune response to tumor cell Source: Ensembl
  • positive regulation of tumor necrosis factor secretion Source: RGD
  • protein import into mitochondrial intermembrane space Source: GO_Central
  • protein refolding Source: Ensembl
  • protein stabilization Source: Ensembl
  • response to activity Source: RGD
  • response to ATP Source: RGD
  • response to cocaine Source: RGD
  • response to cold Source: AgBase
  • response to drug Source: RGD
  • response to estrogen Source: RGD
  • response to glucocorticoid Source: RGD
  • response to heat Source: RGD
  • response to hydrogen peroxide Source: RGD
  • response to hypoxia Source: RGD
  • response to ischemia Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to organic substance Source: RGD
  • response to unfolded protein Source: Ensembl
  • T cell activation Source: GO_Central

Keywordsi

Molecular functionChaperone, Hydrolase
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
60 kDa heat shock protein, mitochondrial (EC:3.6.4.9)
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 namesi
Name:Hspd1
Synonyms:Hsp60
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 9

Organism-specific databases

RGDi621314. Hspd1.

Subcellular locationi

  • Mitochondrion matrix By similarity

GO - Cellular componenti

  • cell surface Source: RGD
  • clathrin-coated pit Source: Ensembl
  • coated vesicle Source: Ensembl
  • cyclin-dependent protein kinase activating kinase holoenzyme complex Source: Ensembl
  • cytoplasm Source: RGD
  • cytosol Source: RGD
  • early endosome Source: Ensembl
  • extracellular exosome Source: Ensembl
  • extracellular matrix Source: Ensembl
  • extracellular space Source: RGD
  • Golgi apparatus Source: RGD
  • lipopolysaccharide receptor complex Source: Ensembl
  • membrane raft Source: RGD
  • mitochondrial crista Source: RGD
  • mitochondrial inner membrane Source: RGD
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: RGD
  • myelin sheath Source: Ensembl
  • peroxisomal matrix Source: RGD
  • plasma membrane Source: Ensembl
  • protein complex Source: UniProtKB
  • rough endoplasmic reticulum Source: RGD
  • secretory granule Source: RGD
  • zymogen granule Source: RGD

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 26MitochondrionBy similarityAdd BLAST26
ChainiPRO_000000502927 – 57360 kDa heat shock protein, mitochondrialAdd BLAST547

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei31N6-succinyllysineBy similarity1
Modified residuei67PhosphoserineBy similarity1
Modified residuei70PhosphoserineCombined sources1
Modified residuei75N6-acetyllysineBy similarity1
Modified residuei82N6-acetyllysine; alternateBy similarity1
Modified residuei82N6-succinyllysine; alternateBy similarity1
Modified residuei87N6-acetyllysineBy similarity1
Modified residuei90PhosphotyrosineBy similarity1
Modified residuei91N6-acetyllysineBy similarity1
Modified residuei125N6-acetyllysine; alternateBy similarity1
Modified residuei125N6-succinyllysine; alternateBy similarity1
Modified residuei130N6-acetyllysineBy similarity1
Modified residuei133N6-acetyllysine; alternateBy similarity1
Modified residuei133N6-malonyllysine; alternateBy similarity1
Modified residuei133N6-succinyllysine; alternateBy similarity1
Modified residuei156N6-acetyllysineBy similarity1
Modified residuei191N6-acetyllysine; alternateBy similarity1
Modified residuei191N6-succinyllysine; alternateBy similarity1
Modified residuei202N6-acetyllysine; alternateBy similarity1
Modified residuei202N6-succinyllysine; alternateBy similarity1
Modified residuei205N6-acetyllysine; alternateBy similarity1
Modified residuei205N6-succinyllysine; alternateBy similarity1
Modified residuei218N6-acetyllysine; alternateBy similarity1
Modified residuei218N6-succinyllysine; alternateBy similarity1
Modified residuei236N6-acetyllysine; alternateBy similarity1
Modified residuei236N6-succinyllysine; alternateBy similarity1
Modified residuei249N6-acetyllysineBy similarity1
Modified residuei250N6-acetyllysine; alternateBy similarity1
Modified residuei250N6-succinyllysine; alternateBy similarity1
Modified residuei269N6-acetyllysineBy similarity1
Modified residuei292N6-acetyllysineBy similarity1
Modified residuei301N6-succinyllysineBy similarity1
Modified residuei314N6-acetyllysineBy similarity1
Modified residuei352N6-acetyllysine; alternateBy similarity1
Modified residuei352N6-succinyllysine; alternateBy similarity1
Modified residuei359N6-acetyllysineBy similarity1
Modified residuei389N6-acetyllysineBy similarity1
Modified residuei396N6-acetyllysine; alternateBy similarity1
Modified residuei396N6-succinyllysine; alternateBy similarity1
Modified residuei410PhosphoserineBy similarity1
Modified residuei455N6-acetyllysine; alternateBy similarity1
Modified residuei455N6-succinyllysine; alternateBy similarity1
Modified residuei469N6-acetyllysineBy similarity1
Modified residuei481N6-acetyllysine; alternateBy similarity1
Modified residuei481N6-succinyllysine; alternateBy similarity1
Modified residuei488PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP63039.
PRIDEiP63039.

2D gel databases

World-2DPAGEi0004:P63039.

PTM databases

iPTMnetiP63039.
PhosphoSitePlusiP63039.

Expressioni

Gene expression databases

BgeeiENSRNOG00000014525.
GenevisibleiP63039. RN.

Interactioni

Subunit structurei

Homoheptamer arranged in a ring structure. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. Interacts with 2 heptameric Hsp10 rings to form the symmetrical football complex (By similarity). Interacts with HRAS (By similarity). Interacts with ATAD3A. Interacts with ETFBKMT and METTL21B (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
BaxQ636902EBI-432091,EBI-822405

GO - Molecular functioni

  • apolipoprotein A-I binding Source: Ensembl
  • chaperone binding Source: Ensembl
  • insulin binding Source: RGD
  • misfolded protein binding Source: RGD
  • p53 binding Source: Ensembl
  • protease binding Source: RGD
  • protein binding involved in protein folding Source: GO_Central
  • protein complex binding Source: RGD
  • protein heterodimerization activity Source: RGD
  • ubiquitin protein ligase binding Source: Ensembl
  • unfolded protein binding Source: GO_Central

Protein-protein interaction databases

BioGridi248912. 5 interactors.
IntActiP63039. 5 interactors.
MINTiMINT-1860257.
STRINGi10116.ENSRNOP00000063666.

Structurei

3D structure databases

ProteinModelPortaliP63039.
SMRiP63039.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the chaperonin (HSP60) family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0356. Eukaryota.
COG0459. LUCA.
GeneTreeiENSGT00390000005727.
HOGENOMiHOG000076290.
HOVERGENiHBG001982.
InParanoidiP63039.
KOiK04077.
OMAiTDTDKME.
OrthoDBiEOG091G04JM.
PhylomeDBiP63039.
TreeFamiTF300475.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.50.7.10. 1 hit.
HAMAPiMF_00600. CH60. 1 hit.
InterProiView protein in InterPro
IPR018370. Chaperonin_Cpn60_CS.
IPR001844. Chaprnin_Cpn60.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
PfamiView protein in Pfam
PF00118. Cpn60_TCP1. 1 hit.
PRINTSiPR00298. CHAPERONIN60.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02348. GroEL. 1 hit.
PROSITEiView protein in PROSITE
PS00296. CHAPERONINS_CPN60. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P63039-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRLPTVLRQ MRPVSRALAP HLTRAYAKDV KFGADARALM LQGVDLLADA
60 70 80 90 100
VAVTMGPKGR TVIIEQSWGS PKVTKDGVTV AKSIDLKDKY KNIGAKLVQD
110 120 130 140 150
VANNTNEEAG DGTTTATVLA RSIAKEGFEK ISKGANPVEI RRGVMLAVDA
160 170 180 190 200
VIAELKKQSK PVTTPEEIAQ VATISANGDK DIGNIISDAM KKVGRKGVIT
210 220 230 240 250
VKDGKTLNDE LEIIEGMKFD RGYISPYFIN TSKGQKCEFQ DAYVLLSEKK
260 270 280 290 300
ISSVQSIVPA LEIANAHRKP LVIIAEDVDG EALSTLVLNR LKVGLQVVAV
310 320 330 340 350
KAPGFGDNRK NQLKDMAIAT GGAVFGEEGL NLNLEDVQAH DLGKVGEVIV
360 370 380 390 400
TKDDAMLLKG KGDKAHIEKR IQEITEQLDI TTSEYEKEKL NERLAKLSDG
410 420 430 440 450
VAVLKVGGTS DVEVNEKKDR VTDALNATRA AVEEGIVLGG GCALLRCIPA
460 470 480 490 500
LDSLKPANED QKIGIEIIKR ALKIPAMTIA KNAGVEGSLI VEKILQSSSE
510 520 530 540 550
VGYDAMLGDF VNMVEKGIID PTKVVRTALL DAAGVASLLT TAEAVVTEIP
560 570
KEEKDPGMGA MGGMGGGMGG GMF
Length:573
Mass (Da):60,955
Last modified:August 31, 2004 - v1
Checksum:i0014B58B77D0127B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti121R → P in AAC53362 (Ref. 2) Curated1
Sequence conflicti537S → P in CAA38564 (PubMed:1979858).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54793 mRNA. Translation: CAA38564.1.
U68562 Genomic DNA. Translation: AAC53362.1.
BC086507 mRNA. Translation: AAH86507.1.
X53585 mRNA. Translation: CAA37654.1.
PIRiS13089. HHRT60.
RefSeqiNP_071565.2. NM_022229.2.
XP_006244994.1. XM_006244932.2.
UniGeneiRn.102058.
Rn.129767.

Genome annotation databases

EnsembliENSRNOT00000066589; ENSRNOP00000063666; ENSRNOG00000014525.
GeneIDi63868.
KEGGirno:63868.
UCSCiRGD:621314. rat.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiCH60_RAT
AccessioniPrimary (citable) accession number: P63039
Secondary accession number(s): P19226, P19227, P97602
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: June 7, 2017
This is version 123 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families