SERPINB13

Gene of the species Homo sapiens
SERPINB13
Identifiers
AliasesSERPINB13, HSHUR7SEQ, HUR7, PI13, headpin, serpin family B member 13
External IDsOMIM: 604445; MGI: 3042250; HomoloGene: 22718; GeneCards: SERPINB13; OMA:SERPINB13 - orthologs
Gene location (Mouse)
Chromosome 1 (mouse)
Chr.Chromosome 1 (mouse)[1]
Chromosome 1 (mouse)
Genomic location for SERPINB13
Genomic location for SERPINB13
Band1|1 E2.1Start106,908,714 bp[1]
End106,928,925 bp[1]
RNA expression pattern
Bgee
HumanMouse (ortholog)
    n/a
Top expressed in
  • esophagus

  • lip

  • zone of skin

  • stomach
BioGPS




More reference expression data
Gene ontology
Molecular function
  • peptidase inhibitor activity
  • protease binding
  • cysteine-type endopeptidase inhibitor activity
  • serine-type endopeptidase inhibitor activity
Cellular component
  • cytoplasm
  • extracellular exosome
  • nucleolus
  • nucleoplasm
  • extracellular space
  • cytosol
  • nuclear speck
  • lysosomal lumen
Biological process
  • negative regulation of peptidase activity
  • response to UV
  • regulation of proteolysis
  • negative regulation of endopeptidase activity
  • negative regulation of keratinocyte apoptotic process
  • regulation of keratinocyte differentiation
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5275

241196

Ensembl

ENSG00000197641

ENSMUSG00000048775

UniProt

Q9UIV8

Q8CDC0

RefSeq (mRNA)

NM_001307923
NM_012397

NM_172852

RefSeq (protein)
NP_001294852
NP_036529
NP_001335196
NP_001335197
NP_001335198

NP_001335199

NP_766440

Location (UCSC)n/aChr 1: 106.91 – 106.93 Mb
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

Serpin B13 is a protein that in humans is encoded by the SERPINB13 gene.[4][5][6]

See also

References

  1. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000048775 – Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ Abts HF, Breuhahn K, Michel G, Kohrer K, Esser P, Ruzicka T (Oct 1997). "Analysis of UVB-modulated gene expression in human keratinocytes by mRNA differential display polymerase chain reaction". Photochem Photobiol. 66 (3): 363–7. doi:10.1111/j.1751-1097.1997.tb03159.x. PMID 9297979. S2CID 39471133.
  5. ^ Abts HF, Welss T, Mirmohammadsadegh A, Kohrer K, Michel G, Ruzicka T (Nov 1999). "Cloning and characterization of hurpin (protease inhibitor 13): A new skin-specific, UV-repressible serine proteinase inhibitor of the ovalbumin serpin family". J Mol Biol. 293 (1): 29–39. doi:10.1006/jmbi.1999.3159. PMID 10512713.
  6. ^ "Entrez Gene: SERPINB13 serpin peptidase inhibitor, clade B (ovalbumin), member 13".

Further reading

  • Spring P, Nakashima T, Frederick M, et al. (1999). "Identification and cDNA cloning of headpin, a novel differentially expressed serpin that maps to chromosome 18q". Biochem. Biophys. Res. Commun. 264 (1): 299–304. doi:10.1006/bbrc.1999.1453. PMID 10527881.
  • Nakashima T, Pak SC, Silverman GA, et al. (2000). "Genomic cloning, mapping, structure and promoter analysis of HEADPIN, a serpin which is down-regulated in head and neck cancer cells". Biochim. Biophys. Acta. 1492 (2–3): 441–6. doi:10.1016/s0167-4781(00)00100-7. PMID 11004515.
  • Abts HF, Welss T, Scheuring S, et al. (2001). "Sequence, organization, chromosomal localization, and alternative splicing of the human serine protease inhibitor gene hurpin (PI13) which is upregulated in psoriasis". DNA Cell Biol. 20 (3): 123–31. doi:10.1089/104454901300068924. PMID 11313015.
  • 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.
  • Jayakumar A, Kang Y, Frederick MJ, et al. (2003). "Inhibition of the cysteine proteinases cathepsins K and L by the serpin headpin (SERPINB13): a kinetic analysis". Arch. Biochem. Biophys. 409 (2): 367–74. doi:10.1016/S0003-9861(02)00635-5. PMID 12504904.
  • Welss T, Sun J, Irving JA, et al. (2003). "Hurpin is a selective inhibitor of lysosomal cathepsin L and protects keratinocytes from ultraviolet-induced apoptosis". Biochemistry. 42 (24): 7381–9. doi:10.1021/bi027307q. PMID 12809493.
  • 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.
  • Moussali H, Bylaite M, Welss T, et al. (2005). "Expression of hurpin, a serine proteinase inhibitor, in normal and pathological skin: overexpression and redistribution in psoriasis and cutaneous carcinomas". Exp. Dermatol. 14 (6): 420–8. doi:10.1111/j.0906-6705.2005.00300.x. PMID 15885077. S2CID 39830943.
  • Shellenberger TD, Mazumdar A, Henderson Y, et al. (2006). "Headpin: a serpin with endogenous and exogenous suppression of angiogenesis". Cancer Res. 65 (24): 11501–9. doi:10.1158/0008-5472.CAN-05-2262. PMID 16357159.
  • Bylaite M, Moussali H, Marciukaitiene I, et al. (2006). "Expression of cathepsin L and its inhibitor hurpin in inflammatory and neoplastic skin diseases". Exp. Dermatol. 15 (2): 110–8. doi:10.1111/j.1600-0625.2005.00389.x. PMID 16433682. S2CID 26784268.

External links

  • The MEROPS online database for peptidases and their inhibitors: I04.017
  • SERPINB13+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

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


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