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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

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.

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • insulin binding Source: RGD
  • lipopolysaccharide binding Source: Ensembl
  • misfolded protein binding Source: RGD
  • protease binding Source: RGD
  • protein complex binding Source: RGD
  • protein heterodimerization activity Source: RGD

GO - Biological processi

  • 'de novo' protein folding Source: RGD
  • apoptotic mitochondrial changes Source: RGD
  • chaperone mediated protein folding requiring cofactor Source: RGD
  • detection of misfolded protein Source: RGD
  • 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-6 secretion Source: RGD
  • positive regulation of T cell activation Source: Ensembl
  • positive regulation of tumor necrosis factor secretion Source: RGD
  • protein refolding Source: InterPro
  • 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
  • T cell activation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
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 namesi
Name:Hspd1
Synonyms:Hsp60
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 9

Organism-specific databases

RGDi621314. Hspd1.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: RGD
  • cytoplasm Source: RGD
  • cytosol Source: RGD
  • extracellular space Source: RGD
  • Golgi apparatus Source: RGD
  • 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
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2626MitochondrionBy similarityAdd
BLAST
Chaini27 – 57354760 kDa heat shock protein, mitochondrialPRO_0000005029Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei31 – 311N6-succinyllysineBy similarity
Modified residuei67 – 671PhosphoserineBy similarity
Modified residuei70 – 701PhosphoserineCombined sources
Modified residuei75 – 751N6-acetyllysineBy similarity
Modified residuei82 – 821N6-acetyllysine; alternateBy similarity
Modified residuei82 – 821N6-succinyllysine; alternateBy similarity
Modified residuei87 – 871N6-acetyllysineBy similarity
Modified residuei90 – 901PhosphotyrosineBy similarity
Modified residuei91 – 911N6-acetyllysineBy similarity
Modified residuei125 – 1251N6-acetyllysine; alternateBy similarity
Modified residuei125 – 1251N6-succinyllysine; alternateBy similarity
Modified residuei130 – 1301N6-acetyllysineBy similarity
Modified residuei133 – 1331N6-acetyllysine; alternateBy similarity
Modified residuei133 – 1331N6-malonyllysine; alternateBy similarity
Modified residuei133 – 1331N6-succinyllysine; alternateBy similarity
Modified residuei156 – 1561N6-acetyllysineBy similarity
Modified residuei191 – 1911N6-acetyllysine; alternateBy similarity
Modified residuei191 – 1911N6-succinyllysine; alternateBy similarity
Modified residuei202 – 2021N6-acetyllysine; alternateBy similarity
Modified residuei202 – 2021N6-succinyllysine; alternateBy similarity
Modified residuei205 – 2051N6-acetyllysine; alternateBy similarity
Modified residuei205 – 2051N6-succinyllysine; alternateBy similarity
Modified residuei218 – 2181N6-acetyllysine; alternateBy similarity
Modified residuei218 – 2181N6-succinyllysine; alternateBy similarity
Modified residuei236 – 2361N6-acetyllysine; alternateBy similarity
Modified residuei236 – 2361N6-succinyllysine; alternateBy similarity
Modified residuei249 – 2491N6-acetyllysineBy similarity
Modified residuei250 – 2501N6-acetyllysine; alternateBy similarity
Modified residuei250 – 2501N6-succinyllysine; alternateBy similarity
Modified residuei269 – 2691N6-acetyllysineBy similarity
Modified residuei292 – 2921N6-acetyllysineBy similarity
Modified residuei301 – 3011N6-succinyllysineBy similarity
Modified residuei314 – 3141N6-acetyllysineBy similarity
Modified residuei352 – 3521N6-acetyllysine; alternateBy similarity
Modified residuei352 – 3521N6-succinyllysine; alternateBy similarity
Modified residuei359 – 3591N6-acetyllysineBy similarity
Modified residuei389 – 3891N6-acetyllysineBy similarity
Modified residuei396 – 3961N6-acetyllysine; alternateBy similarity
Modified residuei396 – 3961N6-succinyllysine; alternateBy similarity
Modified residuei410 – 4101PhosphoserineBy similarity
Modified residuei455 – 4551N6-acetyllysine; alternateBy similarity
Modified residuei455 – 4551N6-succinyllysine; alternateBy similarity
Modified residuei469 – 4691N6-acetyllysineBy similarity
Modified residuei481 – 4811N6-acetyllysine; alternateBy similarity
Modified residuei481 – 4811N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP63039.
PRIDEiP63039.

2D gel databases

World-2DPAGE0004:P63039.

PTM databases

iPTMnetiP63039.
PhosphoSiteiP63039.

Expressioni

Gene expression databases

GenevisibleiP63039. RN.

Interactioni

Subunit structurei

Interacts with HRAS. Interacts with ATAD3A (By similarity). Interacts with ETFBKMT and METTL21B (By similarity).By similarity

Binary interactionsi

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

GO - Molecular functioni

  • insulin binding Source: RGD
  • misfolded protein binding Source: RGD
  • protease binding Source: RGD
  • protein complex binding Source: RGD
  • protein heterodimerization activity Source: RGD

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliP63039.
SMRiP63039. Positions 27-550.
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.
OMAiSNAMKKV.
OrthoDBiEOG7HTHGJ.
PhylomeDBiP63039.
TreeFamiTF300475.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.50.7.10. 1 hit.
HAMAPiMF_00600. CH60.
InterProiIPR018370. Chaperonin_Cpn60_CS.
IPR001844. Chaprnin_Cpn60.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00298. CHAPERONIN60.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02348. GroEL. 1 hit.
PROSITEiPS00296. CHAPERONINS_CPN60. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti121 – 1211R → P in AAC53362 (Ref. 2) Curated
Sequence conflicti537 – 5371S → P in CAA38564 (PubMed:1979858).Curated

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP63039.
SMRiP63039. Positions 27-550.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP63039.
PhosphoSiteiP63039.

2D gel databases

World-2DPAGE0004:P63039.

Proteomic databases

PaxDbiP63039.
PRIDEiP63039.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3329.
RGDi621314. Hspd1.

Phylogenomic databases

eggNOGiKOG0356. Eukaryota.
COG0459. LUCA.
GeneTreeiENSGT00390000005727.
HOGENOMiHOG000076290.
HOVERGENiHBG001982.
InParanoidiP63039.
KOiK04077.
OMAiSNAMKKV.
OrthoDBiEOG7HTHGJ.
PhylomeDBiP63039.
TreeFamiTF300475.

Miscellaneous databases

NextBioi612488.
PROiP63039.

Gene expression databases

GenevisibleiP63039. RN.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.50.7.10. 1 hit.
HAMAPiMF_00600. CH60.
InterProiIPR018370. Chaperonin_Cpn60_CS.
IPR001844. Chaprnin_Cpn60.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00298. CHAPERONIN60.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02348. GroEL. 1 hit.
PROSITEiPS00296. CHAPERONINS_CPN60. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA and deduced amino acid sequence of rat liver prehsp60 (chaperonin-60)."
    Peralta D., Hartman D.J., McIntosh A.M., Hoogenraad N.J., Hoej P.B.
    Nucleic Acids Res. 18:7162-7162(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Liver.
  2. Ryan M.T., Herd S.M., Sberna G., Samuel M.M., Hoogenraad N.J., Hoej P.B.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Sprague-Dawley and Wistar.
  3. "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: Heart.
  4. "Nucleotide sequence of rat hsp60 (chaperonin, GroEL homolog) cDNA."
    Venner T.J., Gupta R.S.
    Nucleic Acids Res. 18:5309-5309(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-573.
    Tissue: Kidney.
  5. Lubec G., Afjehi-Sadat L., Diao W., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 38-58; 61-72; 143-157; 222-233; 237-309; 345-352; 371-387; 397-405; 421-446; 463-469 AND 482-493, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain, Hippocampus and Spinal cord.
  6. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCH60_RAT
AccessioniPrimary (citable) accession number: P63039
Secondary accession number(s): P19226, P19227, P97602
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: May 11, 2016
This is version 112 of the entry and version 1 of the sequence. [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

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.