SEPX1

Protein-coding gene in the species Homo sapiens
MSRB1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

3MAO

Identifiers
AliasesMSRB1, SELR, SELX, SEPX1, SepR, HSPC270, methionine sulfoxide reductase B1, SELENOX, SELENOR
External IDsOMIM: 606216; MGI: 1351642; HomoloGene: 8455; GeneCards: MSRB1; OMA:MSRB1 - orthologs
Gene location (Human)
Chromosome 16 (human)
Chr.Chromosome 16 (human)[1]
Chromosome 16 (human)
Genomic location for MSRB1
Genomic location for MSRB1
Band16p13.3Start1,938,229 bp[1]
End1,943,199 bp[1]
Gene location (Mouse)
Chromosome 17 (mouse)
Chr.Chromosome 17 (mouse)[2]
Chromosome 17 (mouse)
Genomic location for MSRB1
Genomic location for MSRB1
Band17 A3.3|17 12.53 cMStart24,955,616 bp[2]
End24,961,752 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • blood

  • right lobe of liver

  • body of pancreas

  • trabecular bone

  • thoracic diaphragm

  • monocyte

  • granulocyte

  • bone marrow

  • periodontal fiber

  • human kidney
Top expressed in
  • granulocyte

  • left lobe of liver

  • parotid gland

  • sternocleidomastoid muscle

  • temporal muscle

  • triceps brachii muscle

  • tibiofemoral joint

  • interventricular septum

  • stroma of bone marrow

  • digastric muscle
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
  • oxidoreductase activity
  • actin binding
  • zinc ion binding
  • metal ion binding
  • methionine-R-sulfoxide reductase activity
  • peptide-methionine (R)-S-oxide reductase activity
  • L-methionine-(R)-S-oxide reductase activity
  • protein binding
Cellular component
  • cytoplasm
  • cytosol
  • cytoskeleton
  • nucleus
  • actin cytoskeleton
  • cellular component
Biological process
  • immune system process
  • actin filament polymerization
  • innate immune response
  • response to oxidative stress
  • protein repair
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

51734

27361

Ensembl

ENSG00000198736

ENSMUSG00000075705

UniProt

Q9NZV6

Q9JLC3

RefSeq (mRNA)

NM_016332
NM_001382264
NM_001382265

NM_013759
NM_001346668

RefSeq (protein)

NP_057416
NP_001369193
NP_001369194

NP_001333597
NP_038787

Location (UCSC)Chr 16: 1.94 – 1.94 MbChr 17: 24.96 – 24.96 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Methionine-R-sulfoxide reductase B1 is an enzyme that in humans is encoded by the SEPX1 gene.[5][6]

This gene encodes a selenoprotein, which contains a selenocysteine (Sec) residue at its active site. The selenocysteine is encoded by the UGA codon that normally signals translation termination. The 3' UTR of selenoprotein genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. This protein belongs to the methionine sulfoxide reductase B (MsrB) family, and it is expressed in a variety of adult and fetal tissues.[6]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000198736 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000075705 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Lescure A, Gautheret D, Carbon P, Krol A (Feb 2000). "Novel selenoproteins identified in silico and in vivo by using a conserved RNA structural motif". J Biol Chem. 274 (53): 38147–54. doi:10.1074/jbc.274.53.38147. PMID 10608886.
  6. ^ a b "Entrez Gene: SEPX1 selenoprotein X, 1".

Further reading

  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
  • Kryukov GV, Kryukov VM, Gladyshev VN (1999). "New mammalian selenocysteine-containing proteins identified with an algorithm that searches for selenocysteine insertion sequence elements". J. Biol. Chem. 274 (48): 33888–97. doi:10.1074/jbc.274.48.33888. PMID 10567350.
  • Zhang QH, Ye M, Wu XY, et al. (2001). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Res. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152.
  • Daniels RJ, Peden JF, Lloyd C, et al. (2001). "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16". Hum. Mol. Genet. 10 (4): 339–52. doi:10.1093/hmg/10.4.339. PMID 11157797.
  • Moskovitz J, Singh VK, Requena J, et al. (2002). "Purification and characterization of methionine sulfoxide reductases from mouse and Staphylococcus aureus and their substrate stereospecificity". Biochem. Biophys. Res. Commun. 290 (1): 62–5. doi:10.1006/bbrc.2001.6171. PMID 11779133.
  • 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.
  • Kim HY, Gladyshev VN (2004). "Methionine sulfoxide reduction in mammals: characterization of methionine-R-sulfoxide reductases". Mol. Biol. Cell. 15 (3): 1055–64. doi:10.1091/mbc.E03-08-0629. PMC 363075. PMID 14699060.
  • 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.


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