Ubiquitin-Protein-Ligase UBR1

Ubiquitin-Protein-Ligase UBR1
UBR1

Masse/Länge Primärstruktur 1749 aa
Isoformen 2
Bezeichner
Gen-Name UBR1
Externe IDs OMIM605981 UniProtQ8IWV7   MGI1277977
Enzymklassifikation
EC, Kategorie 6.3.2.-  Ligase
Reaktionsart Erzeugung einer Peptidbindung
Substrat ATP + Ubiquitin + (Protein-)Aminosäure
Produkte AMP + Diphosphat + (Protein-N-)Ubiquitinyl-Aminosäure
Vorkommen
Übergeordnetes Taxon Wirbeltiere[1]
Orthologe
Mensch Maus
Entrez 197131 22222
Ensembl ENSG00000159459 ENSMUSG00000027272
UniProt Q8IWV7 Q2M4I1
Refseq (mRNA) NM_174916 NM_009461
Refseq (Protein) NP_777576 NP_033487


PubMed Suche [1] [2]

Das menschliche Gen UBR1 codiert für das Enzym Ubiquitin--ligase E3 component n-recognin 1.[2][3]

Funktion

Der sog. "N-end rule" Pfad ist ein proteolytischer Pfad des Ubiquitin-Systems. Die sogenannte Recognition-Komponente dieses Pfades, die diesem Protein entspricht, bindet an den N-terminalen Aminosäure-Rest des Zielproteins und vermittelt so die Erzeugung der substratgebundenen Multiubiquitin-Kette (sog. Polyubiquinierung). Dies führt zum Abbau des Zielproteins. Das hier beschriebene Protein besitzt zwei Zinc-Finger-Domänen. Mutationen in diesem Gen wurden mit der Entstehung des Johanson-Blizzard-Syndroms in Verbindung gebracht.[3]

Literatur

  • Varshavsky A: The N-end rule: functions, mysteries, uses.. In: Proc. Natl. Acad. Sci. U.S.A.. 93, Nr. 22, 1996, S. 12142–9. doi:10.1073/pnas.93.22.12142. PMID 8901547.
  • Chiannilkulchai N, Pasturaud P, Richard I, et al.: A primary expression map of the chromosome 15q15 region containing the recessive form of limb-girdle muscular dystrophy (LGMD2A) gene.. In: Hum. Mol. Genet.. 4, Nr. 4, 1995, S. 717–25. doi:10.1093/hmg/4.4.717. PMID 7633422.
  • Dgany O, Avidan N, Delaunay J, et al.: Congenital dyserythropoietic anemia type I is caused by mutations in codanin-1.. In: Am. J. Hum. Genet.. 71, Nr. 6, 2003, S. 1467–74. doi:10.1086/344781. PMID 12434312.
  • Strausberg RL, Feingold EA, Grouse LH, et al.: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.. In: Proc. Natl. Acad. Sci. U.S.A.. 99, Nr. 26, 2003, S. 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Ota T, Suzuki Y, Nishikawa T, et al.: Complete sequencing and characterization of 21,243 full-length human cDNAs.. In: Nat. Genet.. 36, Nr. 1, 2004, S. 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Beausoleil SA, Jedrychowski M, Schwartz D, et al.: Large-scale characterization of HeLa cell nuclear phosphoproteins.. In: Proc. Natl. Acad. Sci. U.S.A.. 101, Nr. 33, 2004, S. 12130–5. doi:10.1073/pnas.0404720101. PMID 15302935.
  • Yin J, Kwon YT, Varshavsky A, Wang W: RECQL4, mutated in the Rothmund-Thomson and RAPADILINO syndromes, interacts with ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway.. In: Hum. Mol. Genet.. 13, Nr. 20, 2005, S. 2421–30. doi:10.1093/hmg/ddh269. PMID 15317757.
  • Gerhard DS, Wagner L, Feingold EA, et al.: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).. In: Genome Res.. 14, Nr. 10B, 2004, S. 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
  • Kwak KS, Zhou X, Solomon V, et al.: Regulation of protein catabolism by muscle-specific and cytokine-inducible ubiquitin ligase E3alpha-II during cancer cachexia.. In: Cancer Res.. 64, Nr. 22, 2005, S. 8193–8. doi:10.1158/0008-5472.CAN-04-2102. PMID 15548684.
  • Tasaki T, Mulder LC, Iwamatsu A, et al.: A family of mammalian E3 ubiquitin ligases that contain the UBR box motif and recognize N-degrons.. In: Mol. Cell. Biol.. 25, Nr. 16, 2005, S. 7120–36. doi:10.1128/MCB.25.16.7120-7136.2005. PMID 16055722.
  • Stelzl U, Worm U, Lalowski M, et al.: A human protein-protein interaction network: a resource for annotating the proteome.. In: Cell. 122, Nr. 6, 2005, S. 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
  • Zenker M, Mayerle J, Lerch MM, et al.: Deficiency of UBR1, a ubiquitin ligase of the N-end rule pathway, causes pancreatic dysfunction, malformations and mental retardation (Johanson-Blizzard syndrome).. In: Nat. Genet.. 37, Nr. 12, 2006, S. 1345–50. doi:10.1038/ng1681. PMID 16311597.
  • Sasaki T, Kojima H, Kishimoto R, et al.: Spatiotemporal regulation of c-Fos by ERK5 and the E3 ubiquitin ligase UBR1, and its biological role.. In: Mol. Cell. 24, Nr. 1, 2006, S. 63–75. doi:10.1016/j.molcel.2006.08.005. PMID 17018293.
  • Zou W, Wang J, Zhang DE: Negative regulation of ISG15 E3 ligase EFP through its autoISGylation.. In: Biochem. Biophys. Res. Commun.. 354, Nr. 1, 2007, S. 321–7. doi:10.1016/j.bbrc.2006.12.210. PMID 17222803.
  • Sakane A, Hatakeyama S, Sasaki T: Involvement of Rabring7 in EGF receptor degradation as an E3 ligase.. In: Biochem. Biophys. Res. Commun.. 357, Nr. 4, 2007, S. 1058–64. doi:10.1016/j.bbrc.2007.04.052. PMID 17462600.
  • Wei S, Lin LF, Yang CC, et al.: 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.. In: Mol. Pharmacol.. 72, Nr. 3, 2007, S. 725–33. doi:10.1124/mol.107.035287. PMID 17569795.

Einzelnachweise

  1. Homologe bei OMA
  2. Kwon YT, Reiss Y, Fried VA, Hershko A, Yoon JK, Gonda DK, Sangan P, Copeland NG, Jenkins NA, Varshavsky A: The mouse and human genes encoding the recognition component of the N-end rule pathway. In: Proc Natl Acad Sci U S A. 95, Nr. 14, August 1998, S. 7898-903. PMID 9653112. Volltext bei PMC: 20901.
  3. a b Entrez Gene: UBR1 ubiquitin protein ligase E3 component n-recognin 1. Abgerufen am 5. März 2011.

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