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CALML5

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2B1U

Identifiers

Aliases

CALML5, CLSP, calmodulin like 5

External IDs

OMIM: 605183 MGI: 1931464 HomoloGene: 49485 GeneCards: CALML5

Gene location (Human)

Chr.	Chromosome 10 (human)^[1]

Band	10p15.1	Start	5,498,697 bp^[1]
Band	10p15.1	End	5,499,570 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 13 (mouse)^[2]

Band	13\|13 A1	Start	3,887,757 bp^[2]
Band	13\|13 A1	End	3,888,673 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

skin of abdomen

vulva

human penis

nipple

minor salivary gland

parotid gland

gums

cavity of mouth

vagina

thymus

Top expressed in

esophagus

belly cord

skin of abdomen

superior surface of tongue

skin of back

condyle

fossa

molar

ankle joint

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	metal ion binding calcium ion binding enzyme regulator activity
Cellular component	extracellular region ficolin-1-rich granule lumen nucleus
Biological process	signal transduction epidermis development neutrophil degranulation calcium-mediated signaling regulation of catalytic activity spindle pole body organization
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


51806


80796

Ensembl


ENSG00000178372


ENSMUSG00000033765

UniProt


Q9NZT1


Q9JM83

RefSeq (mRNA)


NM_017422


NM_020036

RefSeq (protein)


NP_059118


NP_064420

Location (UCSC)

Chr 10: 5.5 – 5.5 Mb

Chr 13: 3.89 – 3.89 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Calmodulin-like protein 5 is a protein that in humans is encoded by the CALML5 gene.^[5]^[6]

This gene encodes a novel calcium binding protein expressed in the epidermis and related to the calmodulin family of calcium binding proteins. Functional studies with recombinant protein demonstrate it does bind calcium and undergoes a conformational change when it does so. Abundant expression is detected only in reconstructed epidermis and is restricted to differentiating keratinocytes. In addition, it can associate with transglutaminase 3, shown to be a key enzyme in the terminal differentiation of keratinocytes.^[6]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000178372 - Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000033765 - Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Mehul B, Bernard D, Simonetti L, Bernard MA, Schmidt R (Jun 2000). "Identification and cloning of a new calmodulin-like protein from human epidermis". J Biol Chem. 275 (17): 12841–7. doi:10.1074/jbc.275.17.12841. PMID 10777582.
^ ^a ^b "Entrez Gene: CALML5 calmodulin-like 5".

External links

Human CALML5 genome location and CALML5 gene details page in the UCSC Genome Browser.
Overview of all the structural information available in the PDB for UniProt: Q9NZT1 (Human Calmodulin-like protein 5) at the PDBe-KB.

Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Méhul B, Bernard D, Schmidt R (2001). "Calmodulin-like skin protein: a new marker of keratinocyte differentiation". J. Invest. Dermatol. 116 (6): 905–9. doi:10.1046/j.0022-202x.2001.01376.x. PMID 11407979.
Durussel I, Méhul B, Bernard D, et al. (2002). "Cation- and peptide-binding properties of human calmodulin-like skin protein". Biochemistry. 41 (17): 5439–48. doi:10.1021/bi016062z. PMID 11969404.
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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
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.
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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
Méhul B, Bernard D, Brouard M, et al. (2006). "Influence of calcium on the proteolytic degradation of the calmodulin-like skin protein (calmodulin-like protein 5) in psoriatic epidermis". Exp. Dermatol. 15 (6): 469–77. doi:10.1111/j.1600-0625.2006.00433.x. PMID 16689864. S2CID 32717375.
Babini E, Bertini I, Capozzi F, et al. (2006). "A structural and dynamic characterization of the EF-hand protein CLSP". Structure. 14 (6): 1029–38. doi:10.1016/j.str.2006.04.004. PMID 16765896.
Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

v t e PDB gallery
2b1u: Solution structure of Calmodulin-like Skin Protein C terminal domain

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This page was last edited on 13 October 2022, at 20:19

CALML5

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References

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