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Protein

10 kDa heat shock protein, mitochondrial

Gene

HSPE1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Eukaryotic CPN10 homolog which is essential for mitochondrial protein biogenesis, together with CPN60. Binds to CPN60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.

GO - Molecular functioni

  • ATP binding Source: InterPro
  • chaperone binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • unfolded protein binding Source: UniProtKB

GO - Biological processi

  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • osteoblast differentiation Source: UniProtKB
  • protein folding Source: ProtInc
  • response to unfolded protein Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress 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
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:5269. HSPE1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29535.

Polymorphism and mutation databases

BioMutaiHSPE1.
DMDMi47606335.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 10210110 kDa heat shock protein, mitochondrialPRO_0000174917Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei8 – 81N6-acetyllysineBy similarity
Modified residuei28 – 281N6-succinyllysineBy similarity
Modified residuei40 – 401N6-acetyllysine; alternateBy similarity
Modified residuei40 – 401N6-malonyllysine; alternate1 Publication
Modified residuei40 – 401N6-succinyllysine; alternateBy similarity
Modified residuei54 – 541N6-malonyllysine; alternate1 Publication
Modified residuei54 – 541N6-succinyllysine; alternateBy similarity
Modified residuei56 – 561N6-acetyllysine; alternate1 Publication
Modified residuei56 – 561N6-malonyllysine; alternate1 Publication
Modified residuei56 – 561N6-succinyllysine; alternateBy similarity
Modified residuei66 – 661N6-acetyllysine; alternateBy similarity
Modified residuei66 – 661N6-succinyllysine; alternateBy similarity
Modified residuei70 – 701N6-acetyllysine; alternateBy similarity
Modified residuei70 – 701N6-succinyllysine; alternateBy similarity
Modified residuei79 – 791Phosphothreonine1 Publication
Modified residuei80 – 801N6-acetyllysine; alternateBy similarity
Modified residuei80 – 801N6-succinyllysine; alternateBy similarity
Modified residuei86 – 861N6-acetyllysine; alternate1 Publication
Modified residuei86 – 861N6-succinyllysine; alternateBy similarity
Modified residuei99 – 991N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP61604.
PaxDbiP61604.
PeptideAtlasiP61604.
PRIDEiP61604.

2D gel databases

UCD-2DPAGEP61604.

PTM databases

PhosphoSiteiP61604.

Expressioni

Inductioni

By stress.

Gene expression databases

BgeeiP61604.
CleanExiHS_HSPE1.
ExpressionAtlasiP61604. baseline and differential.
GenevestigatoriP61604.

Organism-specific databases

HPAiCAB017366.
HPA038755.
HPA048272.

Interactioni

Subunit structurei

Homohexamer.

Binary interactionsi

WithEntry#Exp.IntActNotes
FHITP497894EBI-711483,EBI-741760

Protein-protein interaction databases

BioGridi109568. 36 interactions.
IntActiP61604. 26 interactions.
MINTiMINT-1373857.
STRINGi9606.ENSP00000233893.

Structurei

3D structure databases

ProteinModelPortaliP61604.
SMRiP61604. Positions 11-98.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GroES chaperonin family.Curated

Phylogenomic databases

eggNOGiCOG0234.
GeneTreeiENSGT00390000006350.
HOGENOMiHOG000133897.
HOVERGENiHBG000385.
InParanoidiP61604.
KOiK04078.
OMAiAIKPIEN.
OrthoDBiEOG71CFPD.
PhylomeDBiP61604.
TreeFamiTF313814.

Family and domain databases

Gene3Di2.30.33.40. 1 hit.
HAMAPiMF_00580. CH10.
InterProiIPR020818. Chaperonin_Cpn10.
IPR018369. Chaprnonin_Cpn10_CS.
IPR011032. GroES-like.
[Graphical view]
PANTHERiPTHR10772. PTHR10772. 1 hit.
PfamiPF00166. Cpn10. 1 hit.
[Graphical view]
PRINTSiPR00297. CHAPERONIN10.
SMARTiSM00883. Cpn10. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
PROSITEiPS00681. CHAPERONINS_CPN10. 1 hit.
[Graphical view]

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.3. human.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP61604.
SMRiP61604. Positions 11-98.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109568. 36 interactions.
IntActiP61604. 26 interactions.
MINTiMINT-1373857.
STRINGi9606.ENSP00000233893.

PTM databases

PhosphoSiteiP61604.

Polymorphism and mutation databases

BioMutaiHSPE1.
DMDMi47606335.

2D gel databases

UCD-2DPAGEP61604.

Proteomic databases

MaxQBiP61604.
PaxDbiP61604.
PeptideAtlasiP61604.
PRIDEiP61604.

Protocols and materials databases

DNASUi3336.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000233893; ENSP00000233893; ENSG00000115541.
GeneIDi3336.
KEGGihsa:3336.
UCSCiuc002uul.3. human.

Organism-specific databases

CTDi3336.
GeneCardsiGC02P198328.
HGNCiHGNC:5269. HSPE1.
HPAiCAB017366.
HPA038755.
HPA048272.
MIMi600141. gene.
neXtProtiNX_P61604.
PharmGKBiPA29535.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0234.
GeneTreeiENSGT00390000006350.
HOGENOMiHOG000133897.
HOVERGENiHBG000385.
InParanoidiP61604.
KOiK04078.
OMAiAIKPIEN.
OrthoDBiEOG71CFPD.
PhylomeDBiP61604.
TreeFamiTF313814.

Miscellaneous databases

ChiTaRSiHSPE1. human.
GeneWikiiGroES.
GenomeRNAii3336.
NextBioi13204.
PROiP61604.
SOURCEiSearch...

Gene expression databases

BgeeiP61604.
CleanExiHS_HSPE1.
ExpressionAtlasiP61604. baseline and differential.
GenevestigatoriP61604.

Family and domain databases

Gene3Di2.30.33.40. 1 hit.
HAMAPiMF_00580. CH10.
InterProiIPR020818. Chaperonin_Cpn10.
IPR018369. Chaprnonin_Cpn10_CS.
IPR011032. GroES-like.
[Graphical view]
PANTHERiPTHR10772. PTHR10772. 1 hit.
PfamiPF00166. Cpn10. 1 hit.
[Graphical view]
PRINTSiPR00297. CHAPERONIN10.
SMARTiSM00883. Cpn10. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
PROSITEiPS00681. CHAPERONINS_CPN10. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and cloning of human chaperonin 10 homologue."
    Monzini N., Legname G., Marcucci F., Gromo G., Modena D.
    Biochim. Biophys. Acta 1218:478-480(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Isolation, sequence analysis and characterization of a cDNA encoding human chaperonin 10."
    Chen J.J., McNealy D.J., Dalal S., Androphy E.J.
    Biochim. Biophys. Acta 1219:189-190(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Genomic structure of the human mitochondrial chaperonin genes: HSP60 and HSP10 are localised head to head on chromosome 2 separated by a bidirectional promoter."
    Hansen J.J., Bross P., Westergaard M., Nielsen M.N., Eiberg H., Boerglum A.D., Mogensen J., Kristiansen K., Bolund L., Gregersen N.
    Hum. Genet. 112:71-77(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: Uterus.
  9. "Mapping and characterization of the eukaryotic early pregnancy factor/chaperonin 10 gene family."
    Summers K.M., Fletcher B.H., Macaranas D.D., Somodevilla-Torres M.J., Murphy R.M., Osborne M.J., Spurr N.K., Cassady A.I., Cavanagh A.C.
    Somat. Cell Mol. Genet. 24:315-326(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100.
  10. Bienvenut W.V.
    Submitted (MAR-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-15; 41-54; 57-66 AND 81-92, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  11. "The purification of early-pregnancy factor to homogeneity from human platelets and identification as chaperonin 10."
    Cavanagh A.C., Morton H.
    Eur. J. Biochem. 222:551-560(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 8-19; 28-54 AND 70-102, MASS SPECTROMETRY.
    Tissue: Platelet.
  12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-56; LYS-86 AND LYS-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: MALONYLATION AT LYS-40; LYS-54 AND LYS-56.
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCH10_HUMAN
AccessioniPrimary (citable) accession number: P61604
Secondary accession number(s): O95421
, Q04984, Q53X54, Q9UDH0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: January 23, 2007
Last modified: May 27, 2015
This is version 110 of the entry and version 2 of the sequence. [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

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.