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Q64433 (CH10_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
10 kDa heat shock protein, mitochondrial

Short name=Hsp10
Alternative name(s):
10 kDa chaperonin
Chaperonin 10
Short name=CPN10
Gene names
Name:Hspe1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length102 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Homohexamer By similarity.

Subcellular location

Mitochondrion matrix.

Induction

By stress.

Sequence similarities

Belongs to the GroES chaperonin family.

Ontologies

Keywords
   Biological processStress response
   Cellular componentMitochondrion
   Molecular functionChaperone
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from electronic annotation. Source: InterPro

response to stress

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: InterPro

chaperone binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 10210110 kDa heat shock protein, mitochondrial
PRO_0000174918

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue401N6-malonyllysine By similarity
Modified residue541N6-malonyllysine By similarity
Modified residue561N6-acetyllysine; alternate By similarity
Modified residue561N6-malonyllysine; alternate By similarity
Modified residue791Phosphothreonine By similarity
Modified residue861N6-acetyllysine By similarity
Modified residue991N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q64433 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 08BEB5566DBE8A3D

FASTA10210,963
        10         20         30         40         50         60 
MAGQAFRKFL PLFDRVLVER SAAETVTKGG IMLPEKSQGK VLQATVVAVG SGGKGKSGEI 

        70         80         90        100 
EPVSVKVGDK VLLPEYGGTK VVLDDKDYFL FRDSDILGKY VD 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, expression, and purification of a functional nonacetylated mammalian mitochondrial chaperonin 10."
Dickson R., Larsen B., Viitanen P.V., Tormey M.B., Geske J., Strange R., Bemis L.T.
J. Biol. Chem. 269:26858-26864(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The murine chaperonin 10 gene family contains an intronless, putative gene for early pregnancy factor, Cpn10-rs1."
Fletcher B.H., Cassady A.I., Summers K.M., Cavanagh A.C.
Mamm. Genome 12:133-140(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/Sv.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: NOD.
Tissue: Thymus.
[4]"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].
Strain: FVB/N-3.
Tissue: Mammary gland.
[5]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 8-15; 29-36; 41-54 AND 71-92, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U09659 mRNA. Translation: AAA62229.1.
AF251024 Genomic DNA. Translation: AAF67345.1.
AK088121 mRNA. Translation: BAC40159.1.
BC024385 mRNA. Translation: AAH24385.1.
IPIIPI00263863.
PIRA55075.
RefSeqNP_032329.1. NM_008303.4.
UniGeneMm.215667.

3D structure databases

ProteinModelPortalQ64433.
SMRQ64433. Positions 11-98.
ModBaseSearch...

PTM databases

PhosphoSiteQ64433.

2D gel databases

REPRODUCTION-2DPAGEQ64433.

Proteomic databases

PaxDbQ64433.
PRIDEQ64433.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000075242; ENSMUSP00000074724; ENSMUSG00000073676.
GeneID15528.
KEGGmmu:15528.

Organism-specific databases

CTD3336.
MGIMGI:104680. Hspe1.

Phylogenomic databases

eggNOGCOG0234.
GeneTreeENSGT00390000006350.
HOGENOMHOG000133897.
HOVERGENHBG000385.
InParanoidQ64433.
KOK04078.
OMAYFLFRDA.
OrthoDBEOG45DWR5.

Gene expression databases

ArrayExpressQ64433.
BgeeQ64433.
CleanExMM_HSPE1.
GenevestigatorQ64433.
GermOnlineENSMUSG00000073676. Mus musculus.

Family and domain databases

Gene3D2.30.33.40. 1 hit.
InterProIPR020818. Chaperonin_Cpn10.
IPR018369. Chaprnonin_Cpn10_CS.
IPR011032. GroES-like.
[Graphical view]
PANTHERPTHR10772. PTHR10772. 1 hit.
PfamPF00166. Cpn10. 1 hit.
[Graphical view]
PRINTSPR00297. CHAPERONIN10.
SMARTSM00883. Cpn10. 1 hit.
[Graphical view]
SUPFAMSSF50129. GroES_like. 1 hit.
PROSITEPS00681. CHAPERONINS_CPN10. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio288450.
SOURCESearch...

Entry information

Entry nameCH10_MOUSE
AccessionPrimary (citable) accession number: Q64433
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families