LTN1

Last updated
LTN1
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases LTN1 , C21orf10, C21orf98, RNF160, ZNF294, listerin E3 ubiquitin protein ligase 1
External IDs OMIM: 613083 MGI: 1926163 HomoloGene: 32272 GeneCards: LTN1
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 Mb Chr 16: 87.17 – 87.23 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/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]

Contents

Function

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]

Related Research Articles

<span class="mw-page-title-main">Ubiquitin ligase</span> Protein

A ubiquitin ligase is a protein that recruits an E2 ubiquitin-conjugating enzyme that has been loaded with ubiquitin, recognizes a protein substrate, and assists or directly catalyzes the transfer of ubiquitin from the E2 to the protein substrate. In simple and more general terms, the ligase enables movement of ubiquitin from a ubiquitin carrier to another thing by some mechanism. The ubiquitin, once it reaches its destination, ends up being attached by an isopeptide bond to a lysine residue, which is part of the target protein. E3 ligases interact with both the target protein and the E2 enzyme, and so impart substrate specificity to the E2. Commonly, E3s polyubiquitinate their substrate with Lys48-linked chains of ubiquitin, targeting the substrate for destruction by the proteasome. However, many other types of linkages are possible and alter a protein's activity, interactions, or localization. Ubiquitination by E3 ligases regulates diverse areas such as cell trafficking, DNA repair, and signaling and is of profound importance in cell biology. E3 ligases are also key players in cell cycle control, mediating the degradation of cyclins, as well as cyclin dependent kinase inhibitor proteins. The human genome encodes over 600 putative E3 ligases, allowing for tremendous diversity in substrates.

<span class="mw-page-title-main">ITCH</span> Protein-coding gene in the species Homo sapiens

ITCH is a HECT domain E3 ubiquitin ligase that is ablated in non-agouti-lethal 18H mice. Itchy mice develop a severe immunological phenotype after birth that includes hyperplasia of lymphoid and hematopoietic cells, and stomach and lung inflammation. In humans ITCH deficiency causes altered physical growth, craniofacial morphology defects, defective muscle development, and aberrant immune system function. ITCH contains a C2 domain, proline-rich region, WW domains, HECT domain, and multiple amino acids that are phosphorylated and ubiquitinated.

<span class="mw-page-title-main">BTRC (gene)</span> Protein-coding gene in the species Homo sapiens

F-box/WD repeat-containing protein 1A (FBXW1A) also known as βTrCP1 or Fbxw1 or hsSlimb or pIkappaBalpha-E3 receptor subunit is a protein that in humans is encoded by the BTRC gene.

<span class="mw-page-title-main">UBE2L3</span> Protein-coding gene in humans

Ubiquitin-conjugating enzyme E2 L3 (UBE2L3), also called UBCH7, is a protein that in humans is encoded by the UBE2L3 gene. As an E2 enzyme, UBE2L3 participates in ubiquitination to target proteins for degradation. The role of UBE2L3 in the ubiquitination of the NF-κB precursor implicated it in various major autoimmune diseases, including rheumatoid arthritis (RA), celiac disease, Crohn's disease (CD), and systemic lupus erythematosus.

<span class="mw-page-title-main">SMURF1</span> Mammalian protein found in Homo sapiens

E3 ubiquitin-protein ligase SMURF1 is an enzyme that in humans is encoded by the SMURF1 gene. The SMURF1 Gene encodes a protein with a size of 757 amino acids and the molecular mass of this protein is 86114 Da.

<span class="mw-page-title-main">USP7</span> Protein-coding gene in the species Homo sapiens

Ubiquitin-specific-processing protease 7 (USP7), also known as ubiquitin carboxyl-terminal hydrolase 7 or herpesvirus-associated ubiquitin-specific protease (HAUSP), is an enzyme that in humans is encoded by the USP7 gene.

<span class="mw-page-title-main">CUL3</span> Protein-coding gene in humans

Cullin 3 is a protein that in humans is encoded by the CUL3 gene.

<span class="mw-page-title-main">SMURF2</span>

E3 ubiquitin-protein ligase SMURF2 is an enzyme that in humans is encoded by the SMURF2 gene which is located at chromosome 17q23.3-q24.1.

<span class="mw-page-title-main">SYVN1</span> Protein-coding gene in the species Homo sapiens

E3 ubiquitin-protein ligase synoviolin is an enzyme that in humans is encoded by the SYVN1 gene.

<span class="mw-page-title-main">UBR1</span> Mammalian protein found in Homo sapiens

The human gene UBR1 encodes the enzyme ubiquitin-protein ligase E3 component n-recognin 1.

<span class="mw-page-title-main">FANCL</span> Protein-coding gene in the species Homo sapiens

E3 ubiquitin-protein ligase FANCL is an enzyme that in humans is encoded by the FANCL gene.

<span class="mw-page-title-main">RNF20</span> Protein-coding gene in the species Homo sapiens

E3 ubiquitin-protein ligase BRE1A is an enzyme that in humans is encoded by the RNF20 gene.

<span class="mw-page-title-main">FBXW11</span> Protein-coding gene in the species Homo sapiens

βTrCP2 is a protein that in humans is encoded by the FBXW11 gene.

<span class="mw-page-title-main">FBXO11</span> Protein-coding gene in the species Homo sapiens

F-box only protein 11 is a protein that in humans is encoded by the FBXO11 gene.

<span class="mw-page-title-main">MARCH5</span> Protein-coding gene in the species Homo sapiens

E3 ubiquitin-protein ligase MARCH5, also known as membrane-associated ring finger (C3HC4) 5, is an enzyme that, in humans, is encoded by the MARCH5 gene. It is localized in the mitochondrial outer membrane and has four transmembrane domains.

<span class="mw-page-title-main">PCGF1</span> Protein-coding gene in the species Homo sapiens

Polycomb group RING finger protein 1, PCGF1, also known as NSPC1 or RNF68 is a RING finger domain protein that in humans is encoded by the PCGF1 gene.

<span class="mw-page-title-main">DTX3L</span> Protein-coding gene in the species Homo sapiens

Deltex E3 ubiquitin ligase 3L is a protein that in humans is encoded by the DTX3L gene.

<span class="mw-page-title-main">ZNF598</span> Protein-coding gene in the species Homo sapiens

Zinc finger protein 598 (ZNF598) is a protein that in humans is encoded by the ZNF598 gene.

<span class="mw-page-title-main">NEMF (gene)</span> Protein-coding gene in the species Homo sapiens

Nuclear export mediator factor (NEMF) is a protein that in humans is encoded by the NEMF gene.

<span class="mw-page-title-main">RNF144A</span> Protein-coding gene in the species Homo sapiens

RNF144A is an E3 ubiquitin ligase belonging to the RING-between RING (RBR) family of ubiquitin ligases, whose specific members have been shown to function as RING-HECT hybrid E3 ligases. RNF144A is most closely related to RNF144B at the protein level, and the two proteins together comprise a subdomain within the RBR family of proteins. The ubiquitin ligase activity of RNF144A catalyzes ubiquitin linkages at the K6-, K11- and K48- positions of ubiquitin in vitro, and is regulated by self-association through its transmembrane domain.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000198862 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000052299 - 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. "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

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