UBR1

UBR1

Ubiquitin protein ligase E3 component n-recognin 1, also known as UBR1, is a human gene.cite web | title = Entrez Gene: UBR1 ubiquitin protein ligase E3 component n-recognin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=197131| accessdate = ]

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: UBR1 ubiquitin protein ligase E3 component n-recognin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=197131| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Varshavsky A |title=The N-end rule: functions, mysteries, uses. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 22 |pages= 12142–9 |year= 1996 |pmid= 8901547 |doi=
*cite journal | author=Chiannilkulchai N, Pasturaud P, Richard I, "et al." |title=A primary expression map of the chromosome 15q15 region containing the recessive form of limb-girdle muscular dystrophy (LGMD2A) gene. |journal=Hum. Mol. Genet. |volume=4 |issue= 4 |pages= 717–25 |year= 1995 |pmid= 7633422 |doi=
*cite journal | author=Kwon YT, Reiss Y, Fried VA, "et al." |title=The mouse and human genes encoding the recognition component of the N-end rule pathway. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 14 |pages= 7898–903 |year= 1998 |pmid= 9653112 |doi=
*cite journal | author=Dgany O, Avidan N, Delaunay J, "et al." |title=Congenital dyserythropoietic anemia type I is caused by mutations in codanin-1. |journal=Am. J. Hum. Genet. |volume=71 |issue= 6 |pages= 1467–74 |year= 2003 |pmid= 12434312 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Beausoleil SA, Jedrychowski M, Schwartz D, "et al." |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130–5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101
*cite journal | author=Yin J, Kwon YT, Varshavsky A, Wang W |title=RECQL4, mutated in the Rothmund-Thomson and RAPADILINO syndromes, interacts with ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway. |journal=Hum. Mol. Genet. |volume=13 |issue= 20 |pages= 2421–30 |year= 2005 |pmid= 15317757 |doi= 10.1093/hmg/ddh269
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Kwak KS, Zhou X, Solomon V, "et al." |title=Regulation of protein catabolism by muscle-specific and cytokine-inducible ubiquitin ligase E3alpha-II during cancer cachexia. |journal=Cancer Res. |volume=64 |issue= 22 |pages= 8193–8 |year= 2005 |pmid= 15548684 |doi= 10.1158/0008-5472.CAN-04-2102
*cite journal | author=Tasaki T, Mulder LC, Iwamatsu A, "et al." |title=A family of mammalian E3 ubiquitin ligases that contain the UBR box motif and recognize N-degrons. |journal=Mol. Cell. Biol. |volume=25 |issue= 16 |pages= 7120–36 |year= 2005 |pmid= 16055722 |doi= 10.1128/MCB.25.16.7120-7136.2005
*cite journal | author=Stelzl U, Worm U, Lalowski M, "et al." |title=A human protein-protein interaction network: a resource for annotating the proteome. |journal=Cell |volume=122 |issue= 6 |pages= 957–68 |year= 2005 |pmid= 16169070 |doi= 10.1016/j.cell.2005.08.029
*cite journal | author=Zenker M, Mayerle J, Lerch MM, "et al." |title=Deficiency of UBR1, a ubiquitin ligase of the N-end rule pathway, causes pancreatic dysfunction, malformations and mental retardation (Johanson-Blizzard syndrome). |journal=Nat. Genet. |volume=37 |issue= 12 |pages= 1345–50 |year= 2006 |pmid= 16311597 |doi= 10.1038/ng1681
*cite journal | author=Sasaki T, Kojima H, Kishimoto R, "et al." |title=Spatiotemporal regulation of c-Fos by ERK5 and the E3 ubiquitin ligase UBR1, and its biological role. |journal=Mol. Cell |volume=24 |issue= 1 |pages= 63–75 |year= 2006 |pmid= 17018293 |doi= 10.1016/j.molcel.2006.08.005
*cite journal | author=Zou W, Wang J, Zhang DE |title=Negative regulation of ISG15 E3 ligase EFP through its autoISGylation. |journal=Biochem. Biophys. Res. Commun. |volume=354 |issue= 1 |pages= 321–7 |year= 2007 |pmid= 17222803 |doi= 10.1016/j.bbrc.2006.12.210
*cite journal | author=Sakane A, Hatakeyama S, Sasaki T |title=Involvement of Rabring7 in EGF receptor degradation as an E3 ligase. |journal=Biochem. Biophys. Res. Commun. |volume=357 |issue= 4 |pages= 1058–64 |year= 2007 |pmid= 17462600 |doi= 10.1016/j.bbrc.2007.04.052
*cite journal | author=Wei S, Lin LF, Yang CC, "et al." |title=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. |journal=Mol. Pharmacol. |volume=72 |issue= 3 |pages= 725–33 |year= 2007 |pmid= 17569795 |doi= 10.1124/mol.107.035287

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes


Wikimedia Foundation. 2010.

Игры ⚽ Нужен реферат?

Look at other dictionaries:

  • Ubiquitin-Protein-Ligase UBR1 — UBR1 Masse/Länge Primärstruktur 1749 aa I …   Deutsch Wikipedia

  • Johanson-Blizzard-Syndrom — Klassifikation nach ICD 10 Q45.0 Sonstige angeborene Fehlbildungen des Verdauungssystems …   Deutsch Wikipedia

  • Mdm2 — p53 binding protein homolog (mouse) Solution structure of Mdm2. [1] …   Wikipedia

  • UBR4 — Zinc finger, UBR1 type 1, also known as ZUBR1, is a human gene.cite web | title = Entrez Gene: ZUBR1 zinc finger, UBR1 type 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene Cmd=ShowDetailView TermToSearch=23352| accessdate = ] PBB… …   Wikipedia

  • UBR2 — Ubiquitin protein ligase E3 component n recognin 2, also known as UBR2, is a human gene.cite web | title = Entrez Gene: UBR2 ubiquitin protein ligase E3 component n recognin 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene… …   Wikipedia

  • Cullin — structure of the cul1 rbx1 skp1 f boxskp2 scf ubiquitin ligase complex Identifiers Symbol Cullin Pfam …   Wikipedia

  • André Reis — (* 1960) ist ein deutscher Mediziner. Er ist Direktor des Humangenetischen Institutes an der Universität Erlangen und Mitglied der Akademie der Wissenschaften und der Literatur in Mainz. Inhaltsverzeichnis 1 Werdegang 2 Aktuelle… …   Deutsch Wikipedia

  • Protein targeting — This article deals with protein targeting in eukaryotes except where noted. Protein targeting or protein sorting is the mechanism by which a cell transports proteins to the appropriate positions in the cell or outside of it. Sorting targets can… …   Wikipedia

  • Protein folding — Protein thermodynamics redirects here. For the thermodynamics of reactions catalyzed by proteins, see Enzyme. Protein before and after folding. Protein folding is the process by which a protein structure assumes its functional shape or… …   Wikipedia

  • Chaperone (protein) — A top view of the GroES/GroEL bacterial chaperone complex model In molecular biology, chaperones are proteins that assist the non covalent folding or unfolding and the assembly or disassembly of other macromolecular structures, but do not occur… …   Wikipedia

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”