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Entry version 148 (07 Oct 2020)
Sequence version 1 (31 Aug 2004)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • ATP + H(2)O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.By similarity EC:5.6.1.7

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei75ATPBy similarity1
Binding sitei440ATP; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei520ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi111 – 115ATPBy similarity5

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionChaperone, Isomerase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-1268020, Mitochondrial protein import

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
60 kDa heat shock protein, mitochondrial (EC:5.6.1.7By similarity)
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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Hspd1
Synonyms:Hsp60
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 9

Organism-specific databases

Rat genome database

More...
RGDi
621314, Hspd1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 26MitochondrionBy similarityAdd BLAST26
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000502927 – 57360 kDa heat shock protein, mitochondrialAdd BLAST547

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki551Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P63039

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P63039

PRoteomics IDEntifications database

More...
PRIDEi
P63039

2D gel databases

The World-2DPAGE database

More...
World-2DPAGEi
0004:P63039

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
P63039

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P63039

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P63039

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P63039

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000014525, Expressed in female gonad and 21 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P63039, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P63039, RN

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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).

Interacts with MFHAS1 (By similarity).

By similarity

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
248912, 8 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P63039

Protein interaction database and analysis system

More...
IntActi
P63039, 9 interactors

Molecular INTeraction database

More...
MINTi
P63039

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000063666

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P63039

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the chaperonin (HSP60) family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0356, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000005727

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_016503_3_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P63039

KEGG Orthology (KO)

More...
KOi
K04077

Identification of Orthologs from Complete Genome Data

More...
OMAi
TDTDKME

Database of Orthologous Groups

More...
OrthoDBi
415781at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P63039

TreeFam database of animal gene trees

More...
TreeFami
TF300475

Family and domain databases

Conserved Domains Database

More...
CDDi
cd03344, GroEL, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.560.10, 1 hit
3.30.260.10, 1 hit
3.50.7.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00600, CH60, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR018370, Chaperonin_Cpn60_CS
IPR001844, Chaprnin_Cpn60
IPR002423, Cpn60/TCP-1
IPR027409, GroEL-like_apical_dom_sf
IPR027413, GROEL-like_equatorial_sf
IPR027410, TCP-1-like_intermed_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00118, Cpn60_TCP1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00298, CHAPERONIN60

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48592, SSF48592, 1 hit
SSF52029, SSF52029, 1 hit
SSF54849, SSF54849, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02348, GroEL, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00296, CHAPERONINS_CPN60, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i0014B58B77D0127B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti121R → P in AAC53362 (Ref. 2) Curated1
Sequence conflicti537S → P in CAA38564 (PubMed:1979858).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X54793 mRNA Translation: CAA38564.1
U68562 Genomic DNA Translation: AAC53362.1
BC086507 mRNA Translation: AAH86507.1
X53585 mRNA Translation: CAA37654.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S13089, HHRT60

NCBI Reference Sequences

More...
RefSeqi
NP_071565.2, NM_022229.2
XP_006244994.1, XM_006244932.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000066589; ENSRNOP00000063666; ENSRNOG00000014525

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
63868

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:63868

UCSC genome browser

More...
UCSCi
RGD:621314, rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

3D structure databases

SMRiP63039
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi248912, 8 interactors
CORUMiP63039
IntActiP63039, 9 interactors
MINTiP63039
STRINGi10116.ENSRNOP00000063666

PTM databases

CarbonylDBiP63039
iPTMnetiP63039
PhosphoSitePlusiP63039
SwissPalmiP63039

2D gel databases

World-2DPAGEi0004:P63039

Proteomic databases

jPOSTiP63039
PaxDbiP63039
PRIDEiP63039

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3329
RGDi621314, Hspd1

Phylogenomic databases

eggNOGiKOG0356, Eukaryota
GeneTreeiENSGT00390000005727
HOGENOMiCLU_016503_3_0_1
InParanoidiP63039
KOiK04077
OMAiTDTDKME
OrthoDBi415781at2759
PhylomeDBiP63039
TreeFamiTF300475

Enzyme and pathway databases

ReactomeiR-RNO-1268020, Mitochondrial protein import

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P63039

Gene expression databases

BgeeiENSRNOG00000014525, Expressed in female gonad and 21 other tissues
ExpressionAtlasiP63039, baseline and differential
GenevisibleiP63039, RN

Family and domain databases

CDDicd03344, GroEL, 1 hit
Gene3Di1.10.560.10, 1 hit
3.30.260.10, 1 hit
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_sf
IPR027413, GROEL-like_equatorial_sf
IPR027410, TCP-1-like_intermed_sf
PfamiView protein in Pfam
PF00118, Cpn60_TCP1, 1 hit
PRINTSiPR00298, CHAPERONIN60
SUPFAMiSSF48592, SSF48592, 1 hit
SSF52029, SSF52029, 1 hit
SSF54849, SSF54849, 1 hit
TIGRFAMsiTIGR02348, GroEL, 1 hit
PROSITEiView protein in PROSITE
PS00296, CHAPERONINS_CPN60, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCH60_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P63039
Secondary accession number(s): P19226, P19227, P97602
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: October 7, 2020
This is version 148 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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