CLPB

ClpB homolog, mitochondrial AAA ATPase chaperonin
Identifiers
Symbols	CLPB ; ANKCLB; HSP78; MEGCANN; MGCA7; SKD3
External IDs	OMIM: 616254 MGI: 1100517 HomoloGene: 32067 GeneCards: CLPB Gene
EC number	3.6.1.3
Gene ontology Molecular function • molecular_function • protein binding • ATP binding • ATPase activity Cellular component • cellular_component • mitochondrion Biological process • metabolic process • cellular response to heat Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	81570	20480
Ensembl	ENSG00000162129	ENSMUSG00000001829
UniProt	Q9H078	Q60649
RefSeq (mRNA)	NM_001258392	NM_009191
RefSeq (protein)	NP_001245321	NP_033217
Location (UCSC)	Chr 11: 72.29 – 72.43 Mb	Chr 7: 101.66 – 101.79 Mb
PubMed search

Caseinolytic peptidase B protein homolog, also known as mitochondrial AAA ATPase chaperonin, is an enzyme that in humans is encoded by the CLPB gene.,^[1][2][3] which encodes an ATP-dependent protease and chaperone; it is a chaperone involved in disaggregating proteins and also has a role in de novo protein synthesis under mild stress conditions.

Structure

Gene

The gene CLPB encodes protein Caseinolytic peptidase B protein homolog in human. The human CLPB gene has 19 exons and locates at chromosome band 11q13.4.^[3]{

Protein

The human protein Caseinolytic peptidase B protein homolog has five isoforms due to alternative splicing. Isoform 1 is considered as one having the 'canonical' sequence. The pretein is 78.7 kDa in size and composed of 707 amino acids. It contains a N-terminal mitochondrial targeting sequence (1-36 amino acids). After processing, the matured mitochondrial protein has a theoretical pI of this protein isoform is 8.53.^[4]

References

1. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A (Mar 2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Res 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
2. Perier F, Radeke CM, Raab-Graham KF, Vandenberg CA (Mar 1995). "Expression of a putative ATPase suppresses the growth defect of a yeast potassium transport mutant: identification of a mammalian member of the Clp/HSP104 family". Gene 152 (2): 157–63. doi:10.1016/0378-1119(94)00697-Q. PMID 7835694.
3. "Entrez Gene: CLPB ClpB caseinolytic peptidase B homolog (E. coli)".
4. "Q9H078 - CLPB_HUMAN". Uniprot.

Further reading

• Rual JF, Venkatesan K, Hao T; et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Colland F, Jacq X, Trouplin V; et al. (2004). "Functional proteomics mapping of a human signaling pathway.". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
• Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Leonard D, Ajuh P, Lamond AI, Legerski RJ (2003). "hLodestar/HuF2 interacts with CDC5L and is involved in pre-mRNA splicing.". Biochem. Biophys. Res. Commun. 308 (4): 793–801. doi:10.1016/S0006-291X(03)01486-4. PMID 12927788.
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.