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LTN1

From Wikipedia, the free encyclopedia
LTN1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesLTN1, C21orf10, C21orf98, RNF160, ZNF294, listerin E3 ubiquitin protein ligase 1
External IDsOMIM: 613083; MGI: 1926163; HomoloGene: 32272; GeneCards: LTN1; OMA:LTN1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_015565
NM_001320766

NM_001081068

RefSeq (protein)

NP_001307695
NP_056380

NP_001074537

Location (UCSC)Chr 21: 28.93 – 28.99 MbChr 16: 87.17 – 87.23 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Listerin E3 ubiquitin protein ligase 1 (LTN1), otherwise known as listerin, is a protein that in humans is encoded by the LTN1 gene.[5]

Function

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Like most RING finger proteins, listerin functions as an E3 ubiquitin ligase.[6] Listerin is a component of the ribosome quality control complex.[7][8]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000198862Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000052299Ensembl, 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. ^ "Entrez Gene: Listerin E3 ubiquitin protein ligase 1".
  6. ^ Chu J, Hong NA, Masuda CA, Jenkins BV, Nelms KA, Goodnow CC, Glynne RJ, Wu H, Masliah E, Joazeiro CA, Kay SA (February 2009). "A mouse forward genetics screen identifies LISTERIN as an E3 ubiquitin ligase involved in neurodegeneration". Proceedings of the National Academy of Sciences of the United States of America. 106 (7): 2097–103. doi:10.1073/pnas.0812819106. PMC 2650114. PMID 19196968.
  7. ^ Shao S, Brown A, Santhanam B, Hegde RS (February 2015). "Structure and assembly pathway of the ribosome quality control complex". Molecular Cell. 57 (3): 433–44. doi:10.1016/j.molcel.2014.12.015. PMC 4321881. PMID 25578875.
  8. ^ Shao S, von der Malsburg K, Hegde RS (June 2013). "Listerin-dependent nascent protein ubiquitination relies on ribosome subunit dissociation". Molecular Cell. 50 (5): 637–48. doi:10.1016/j.molcel.2013.04.015. PMC 3719020. PMID 23685075.

Further reading

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