UBR1

Mammalian protein found in Homo sapiens
UBR1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

3NY1

Identifiers
AliasesUBR1, JBS, ubiquitin protein ligase E3 component n-recognin 1
External IDsOMIM: 605981; MGI: 1277977; HomoloGene: 7582; GeneCards: UBR1; OMA:UBR1 - orthologs
Gene location (Human)
Chromosome 15 (human)
Chr.Chromosome 15 (human)[1]
Chromosome 15 (human)
Genomic location for UBR1
Genomic location for UBR1
Band15q15.2Start42,942,897 bp[1]
End43,106,113 bp[1]
Gene location (Mouse)
Chromosome 2 (mouse)
Chr.Chromosome 2 (mouse)[2]
Chromosome 2 (mouse)
Genomic location for UBR1
Genomic location for UBR1
Band2 E5|2 60.37 cMStart120,690,750 bp[2]
End120,801,196 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • pancreatic epithelial cell

  • germinal epithelium

  • visceral pleura

  • endothelial cell

  • parietal pleura

  • Brodmann area 23

  • thymus

  • pancreatic ductal cell

  • epithelium of nasopharynx

  • tibia
Top expressed in
  • ascending aorta

  • aortic valve

  • supraoptic nucleus

  • retinal pigment epithelium

  • ciliary body

  • pineal gland

  • cumulus cell

  • iris

  • genital tubercle

  • tail of embryo
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • ubiquitin-protein transferase activity
  • zinc ion binding
  • leucine binding
  • metal ion binding
  • ubiquitin protein ligase activity
  • transferase activity
  • protein binding
Cellular component
  • cytoplasm
  • proteasome complex
  • cytosol
  • ubiquitin ligase complex
Biological process
  • negative regulation of TOR signaling
  • cellular response to leucine
  • ubiquitin-dependent protein catabolic process via the N-end rule pathway
  • protein catabolic process
  • protein ubiquitination
  • ubiquitin-dependent protein catabolic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

197131

22222

Ensembl

ENSG00000159459

ENSMUSG00000027272

UniProt

Q8IWV7

O70481

RefSeq (mRNA)

NM_174916

NM_009461

RefSeq (protein)

NP_777576

NP_033487

Location (UCSC)Chr 15: 42.94 – 43.11 MbChr 2: 120.69 – 120.8 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

The human gene UBR1 encodes the enzyme ubiquitin-protein ligase E3 component n-recognin 1.[5][6]

The N-end rule pathway is one proteolytic pathway of the ubiquitin system. The recognition component of this pathway, encoded by this gene, binds to a destabilizing N-terminal residue of a substrate protein and participates in the formation of a substrate-linked multiubiquitin chain. This leads to the eventual degradation of the substrate protein. The protein described in this record has a RING-type zinc finger and a UBR-type zinc finger. Mutations in this gene have been associated with Johanson–Blizzard syndrome.[6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000159459 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027272 – 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. ^ Kwon YT, Reiss Y, Fried VA, Hershko A, Yoon JK, Gonda DK, Sangan P, Copeland NG, Jenkins NA, Varshavsky A (Aug 1998). "The mouse and human genes encoding the recognition component of the N-end rule pathway". Proc Natl Acad Sci U S A. 95 (14): 7898–903. Bibcode:1998PNAS...95.7898K. doi:10.1073/pnas.95.14.7898. PMC 20901. PMID 9653112.
  6. ^ a b "Entrez Gene: UBR1 ubiquitin protein ligase E3 component n-recognin 1".

Further reading

  • Varshavsky A (1996). "The N-end rule: functions, mysteries, uses". Proc. Natl. Acad. Sci. U.S.A. 93 (22): 12142–9. Bibcode:1996PNAS...9312142V. doi:10.1073/pnas.93.22.12142. PMC 37957. PMID 8901547.
  • Chiannilkulchai N, Pasturaud P, Richard I, et al. (1995). "A primary expression map of the chromosome 15q15 region containing the recessive form of limb-girdle muscular dystrophy (LGMD2A) gene". Hum. Mol. Genet. 4 (4): 717–25. doi:10.1093/hmg/4.4.717. PMID 7633422.
  • Dgany O, Avidan N, Delaunay J, et al. (2003). "Congenital Dyserythropoietic Anemia Type I Is Caused by Mutations in Codanin-1". Am. J. Hum. Genet. 71 (6): 1467–74. doi:10.1086/344781. PMC 378595. PMID 12434312.
  • 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.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
  • Yin J, Kwon YT, Varshavsky A, Wang W (2005). "RECQL4, mutated in the Rothmund-Thomson and RAPADILINO syndromes, interacts with ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway". Hum. Mol. Genet. 13 (20): 2421–30. doi:10.1093/hmg/ddh269. PMID 15317757.
  • 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.
  • Kwak KS, Zhou X, Solomon V, et al. (2005). "Regulation of protein catabolism by muscle-specific and cytokine-inducible ubiquitin ligase E3alpha-II during cancer cachexia". Cancer Res. 64 (22): 8193–8. doi:10.1158/0008-5472.CAN-04-2102. PMID 15548684. S2CID 20424565.
  • Tasaki T, Mulder LC, Iwamatsu A, et al. (2005). "A Family of Mammalian E3 Ubiquitin Ligases That Contain the UBR Box Motif and Recognize N-Degrons". Mol. Cell. Biol. 25 (16): 7120–36. doi:10.1128/MCB.25.16.7120-7136.2005. PMC 1190250. PMID 16055722.
  • Stelzl U, Worm U, Lalowski M, et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
  • Zenker M, Mayerle J, Lerch MM, et al. (2006). "Deficiency of UBR1, a ubiquitin ligase of the N-end rule pathway, causes pancreatic dysfunction, malformations and mental retardation (Johanson-Blizzard syndrome)" (PDF). Nat. Genet. 37 (12): 1345–50. doi:10.1038/ng1681. PMID 16311597. S2CID 23050042.
  • Sasaki T, Kojima H, Kishimoto R, et al. (2006). "Spatiotemporal regulation of c-Fos by ERK5 and the E3 ubiquitin ligase UBR1, and its biological role". Mol. Cell. 24 (1): 63–75. doi:10.1016/j.molcel.2006.08.005. PMID 17018293.
  • Zou W, Wang J, Zhang DE (2007). "Negative Regulation of ISG15 E3 ligase EFP through its autoISGylation". Biochem. Biophys. Res. Commun. 354 (1): 321–7. doi:10.1016/j.bbrc.2006.12.210. PMC 1858649. PMID 17222803.
  • Sakane A, Hatakeyama S, Sasaki T (2007). "Involvement of Rabring7 in EGF receptor degradation as an E3 ligase". Biochem. Biophys. Res. Commun. 357 (4): 1058–64. doi:10.1016/j.bbrc.2007.04.052. PMID 17462600.
  • Wei S, Lin LF, Yang CC, et al. (2007). "Thiazolidinediones modulate the expression of beta-catenin and other cell-cycle regulatory proteins by targeting the F-box proteins of Skp1-Cul1-F-box protein E3 ubiquitin ligase independently of peroxisome proliferator-activated receptor gamma" (PDF). Mol. Pharmacol. 72 (3): 725–33. doi:10.1124/mol.107.035287. PMID 17569795. S2CID 38439682.


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Chaperones/
protein folding
Heat shock proteins/
Chaperonins
Other
Protein targeting
Ubiquitin
(ubiquitylation)
Ubiquitin-like proteins
(UBL)
SUMO protein
(SUMOylation)
  • E1 SUMO-activating enzyme
  • E2 SUMO-conjugating enzyme
Other


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