CELA2B

Protein-coding gene in the species Homo sapiens
CELA2B
Identifiers
AliasesCELA2B, ELA2B, chymotrypsin like elastase family member 2B, chymotrypsin like elastase 2B
External IDsOMIM: 609444; HomoloGene: 88835; GeneCards: CELA2B; OMA:CELA2B - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for CELA2B
Genomic location for CELA2B
Band1p36.21Start15,465,909 bp[1]
End15,491,395 bp[1]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • body of pancreas

  • testicle

  • islet of Langerhans

  • pancreatic epithelial cell

  • pancreatic ductal cell

  • left adrenal cortex

  • right adrenal cortex

  • right hemisphere of cerebellum

  • left ovary

  • stromal cell of endometrium
    n/a
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • peptidase activity
  • serine-type peptidase activity
  • hydrolase activity
  • serine-type endopeptidase activity
Cellular component
  • extracellular region
  • extracellular space
Biological process
  • proteolysis
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

51032

n/a

Ensembl

ENSG00000215704

n/a

UniProt

P08218

n/a

RefSeq (mRNA)

NM_015849

n/a

RefSeq (protein)

NP_056933

n/a

Location (UCSC)Chr 1: 15.47 – 15.49 Mbn/a
PubMed search[2]n/a
Wikidata
View/Edit Human

Chymotrypsin-like elastase family member 2B is and enzyme that in humans is encoded by the CELA2B gene.[3][4][5]

Function

Elastases form a subfamily of serine proteases that hydrolyze many proteins in addition to elastin. Humans have six elastase genes which encode the structurally similar proteins elastase 1, 2, 2A, 2B, 3A, and 3B. Like most of the human elastases, elastase 2B is secreted from the pancreas as a zymogen. In other species, elastase 2B has been shown to preferentially cleave proteins after leucine, methionine, and phenylalanine residues.[5]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000215704 – Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ Kawashima I, Tani T, Shimoda K, Takiguchi Y (April 1987). "Characterization of pancreatic elastase II cDNAs: two elastase II mRNAs are expressed in human pancreas". DNA. 6 (2): 163–72. doi:10.1089/dna.1987.6.163. PMID 3646943.
  4. ^ Szepessy E, Sahin-Tóth M (2006). "Inactivity of Recombinant ELA2B Provides a New Example of Evolutionary Elastase Silencing in Humans". Pancreatology. 6 (1–2): 117–22. doi:10.1159/000090031. PMC 1447606. PMID 16327289.
  5. ^ a b "Entrez Gene: chymotrypsin-like elastase family".

External links

Further reading

  • Fletcher TS, Shen WF, Largman C (1987). "Primary structure of human pancreatic elastase 2 determined by sequence analysis of the cloned mRNA". Biochemistry. 26 (23): 7256–61. doi:10.1021/bi00397a010. PMID 3427074.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "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.
  • Hosgood HD, Zhang L, Shen M, et al. (2009). "Association between genetic variants in VEGF, ERCC3 and occupational benzene haematotoxicity". Occup Environ Med. 66 (12): 848–53. doi:10.1136/oem.2008.044024. PMC 2928224. PMID 19773279.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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