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Protein

10 kDa heat shock protein, mitochondrial

Gene

HSPE1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp60, 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 (PubMed:7912672, PubMed:1346131, PubMed:11422376). 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 (Probable).1 Publication3 Publications

GO - Molecular functioni

  • ATP binding Source: InterPro
  • chaperone binding Source: UniProtKB
  • metal ion binding Source: GO_Central
  • RNA binding Source: UniProtKB
  • unfolded protein binding Source: GO_Central

GO - Biological processi

  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • chaperone cofactor-dependent protein refolding Source: GO_Central
  • osteoblast differentiation Source: UniProtKB
  • protein folding Source: ProtInc
  • response to unfolded protein Source: ProtInc

Keywordsi

Molecular functionChaperone
Biological processStress response

Names & Taxonomyi

Protein namesi
Recommended name:
10 kDa heat shock protein, mitochondrial
Short name:
Hsp10
Alternative name(s):
10 kDa chaperonin
Chaperonin 10
Short name:
CPN10
Early-pregnancy factor
Short name:
EPF
Gene namesi
Name:HSPE1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiHostDB:ENSG00000115541.10
HGNCiHGNC:5269 HSPE1
MIMi600141 gene
neXtProtiNX_P61604

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; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

DisGeNETi3336
OpenTargetsiENSG00000115541
PharmGKBiPA29535

Polymorphism and mutation databases

BioMutaiHSPE1
DMDMi47606335

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001749172 – 10210 kDa heat shock protein, mitochondrialAdd BLAST101

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei8N6-acetyllysineBy similarity1
Modified residuei28N6-succinyllysineBy similarity1
Modified residuei40N6-acetyllysine; alternateBy similarity1
Modified residuei40N6-malonyllysine; alternate1 Publication1
Modified residuei40N6-succinyllysine; alternateBy similarity1
Modified residuei54N6-malonyllysine; alternate1 Publication1
Modified residuei54N6-succinyllysine; alternateBy similarity1
Modified residuei56N6-acetyllysine; alternateCombined sources1
Modified residuei56N6-malonyllysine; alternate1 Publication1
Modified residuei56N6-succinyllysine; alternateBy similarity1
Modified residuei66N6-acetyllysine; alternateBy similarity1
Modified residuei66N6-succinyllysine; alternateBy similarity1
Modified residuei70N6-acetyllysine; alternateBy similarity1
Modified residuei70N6-succinyllysine; alternateBy similarity1
Modified residuei79PhosphothreonineCombined sources1
Modified residuei80N6-acetyllysine; alternateBy similarity1
Modified residuei80N6-succinyllysine; alternateBy similarity1
Modified residuei86N6-acetyllysine; alternateCombined sources1
Modified residuei86N6-succinyllysine; alternateBy similarity1
Modified residuei99N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP61604
MaxQBiP61604
PaxDbiP61604
PeptideAtlasiP61604
PRIDEiP61604
TopDownProteomicsiP61604

2D gel databases

UCD-2DPAGEiP61604

PTM databases

iPTMnetiP61604
PhosphoSitePlusiP61604

Expressioni

Inductioni

By stress.

Gene expression databases

BgeeiENSG00000115541
CleanExiHS_HSPE1
ExpressionAtlasiP61604 baseline and differential
GenevisibleiP61604 HS

Organism-specific databases

HPAiCAB017366
HPA038755
HPA048272

Interactioni

Subunit structurei

Homoheptamer arranged in a ring structure (PubMed:25918392). 2 heptameric Hsp10 rings interact with a Hsp60 tetradecamer in the structure of a back-to-back double heptameric ring to form the symmetrical football complex (PubMed:25918392).1 Publication

GO - Molecular functioni

  • chaperone binding Source: UniProtKB
  • unfolded protein binding Source: GO_Central

Protein-protein interaction databases

BioGridi109568, 124 interactors
IntActiP61604, 33 interactors
STRINGi9606.ENSP00000233893

Structurei

Secondary structure

1102
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 11Combined sources6
Beta strandi15 – 20Combined sources6
Beta strandi28 – 30Combined sources3
Beta strandi42 – 49Combined sources8
Beta strandi56 – 59Combined sources4
Beta strandi70 – 72Combined sources3
Beta strandi79 – 83Combined sources5
Beta strandi86 – 92Combined sources7
Turni93 – 95Combined sources3
Beta strandi98 – 100Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4PJ1X-ray3.151/2/O/P/Q/R/S/T/U/V/W/X/Y/Z1-102[»]
ProteinModelPortaliP61604
SMRiP61604
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GroES chaperonin family.Curated

Phylogenomic databases

eggNOGiKOG1641 Eukaryota
COG0234 LUCA
GeneTreeiENSGT00390000006350
HOGENOMiHOG000133897
HOVERGENiHBG000385
InParanoidiP61604
KOiK04078
OMAiPGRIDDN
OrthoDBiEOG091G0ZIY
PhylomeDBiP61604
TreeFamiTF313814

Family and domain databases

CDDicd00320 cpn10, 1 hit
Gene3Di2.30.33.40, 1 hit
HAMAPiMF_00580 CH10, 1 hit
InterProiView protein in InterPro
IPR020818 Chaperonin_GroES
IPR037124 Chaperonin_GroES_sf
IPR018369 Chaprnonin_Cpn10_CS
IPR011032 GroES-like_sf
PANTHERiPTHR10772 PTHR10772, 1 hit
PfamiView protein in Pfam
PF00166 Cpn10, 1 hit
PRINTSiPR00297 CHAPERONIN10
SMARTiView protein in SMART
SM00883 Cpn10, 1 hit
SUPFAMiSSF50129 SSF50129, 1 hit
PROSITEiView protein in PROSITE
PS00681 CHAPERONINS_CPN10, 1 hit

Sequencei

Sequence statusi: Complete.

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

P61604-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGQAFRKFL PLFDRVLVER SAAETVTKGG IMLPEKSQGK VLQATVVAVG
60 70 80 90 100
SGSKGKGGEI QPVSVKVGDK VLLPEYGGTK VVLDDKDYFL FRDGDILGKY

VD
Length:102
Mass (Da):10,932
Last modified:January 23, 2007 - v2
Checksum:i1F3192C81F6EDB78
GO

Mass spectrometryi

Molecular mass is 10843.5±0.2 Da from positions 2 - 102. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75821 mRNA Translation: CAA53455.1
U07550 mRNA Translation: AAA50953.1
AJ250915 Genomic DNA Translation: CAB75425.1
AK312104 mRNA Translation: BAG35040.1
CR407688 mRNA Translation: CAG28616.1
AC020550 Genomic DNA Translation: AAX93146.1
CH471063 Genomic DNA Translation: EAW70163.1
BC023518 mRNA Translation: AAH23518.1
AH007060 Genomic DNA Translation: AAC95387.1
CCDSiCCDS2320.1
PIRiS47532
RefSeqiNP_002148.1, NM_002157.2
UniGeneiHs.1197

Genome annotation databases

EnsembliENST00000233893; ENSP00000233893; ENSG00000115541
GeneIDi3336
KEGGihsa:3336
UCSCiuc002uul.4 human

Similar proteinsi

Entry informationi

Entry nameiCH10_HUMAN
AccessioniPrimary (citable) accession number: P61604
Secondary accession number(s): O95421
, Q04984, Q53X54, Q9UDH0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 137 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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