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Protein FULL name: Protein with ubiquitin-like N terminus, subunit of Nuclear Excision Repair Factor 2 (NEF2) with Rad4p that recognizes and binds damaged DNA; enhances protein deglycosylation activity of Png1p; homolog of human HR23A and HR23B
Rad23p (Saccharomyces cerevisiae) is product of expression of
RAD23
gene.
Rad23p is involved in:
NER in Saccharomyces cerevisiae
FUNCTION: Plays a central role both in proteosomal degradation of
misfolded proteins and DNA repair. Central component of a complex
required to couple deglycosylation and proteasome-mediated
degradation of misfolded proteins in the endoplasmic reticulun
that are retrotranslocated in the cytosol. Involved in DNA
excision repair. May play a part in DNA damage recognition and/or
in altering chromatin structure to allow access by damage-
processing enzymes.
SUBUNIT: Interacts directly with PNG1.
INTERACTION:
P25347:-; NbExp=1; IntAct=EBI-14668, EBI-21836;
P18888:SNF6; NbExp=1; IntAct=EBI-14668, EBI-17550;
SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
MISCELLANEOUS: Present with 10900 molecules/cell in log phase SD
medium.
SIMILARITY: Contains 2 UBA domains.
SIMILARITY: Contains 1 ubiquitin-like domain.
Links to other databases:
Protein sequence:
MVSLTFKNFKKEKVPLDLEPSNTILETKTKLAQSISCEESQIKLIYSGKV
LQDSKTVSECGLKDGDQVVFMVSQKKSTKTKVTEPPIAPESATTPGRENS
TEASPSTDASAAPAATAPEGSQPQEEQTATTERTESASTPGFVVGTERNE
TIERIMEMGYQREEVERALRAAFNNPDRAVEYLLMGIPENLRQPEPQQQT
AAAAEQPSTAATTAEQPAEDDLFAQAAQGGNASSGALGTTGGATDAAQGG
PPGSIGLTVEDLLSLRQVVSGNPEALAPLLENISARYPQLREHIMANPEV
FVSMLLEAVGDNMQDVMEGADDMVEGEDIEVTGEAAAAGLGQGEGEGSFQ
VDYTPEDDQAISRLCELGFERDLVIQVYFACDKNEEAAANILFSDHAD
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Rad23p (Saccharomyces cerevisiae) belongs to following protein families:
References:
Title
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Authors
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Journal
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The gene clusters ARC and COR on chromosomes 5 and 10, respectively, of Saccharomyces cerevisiae share a common ancestry.
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Melnick L, Sherman F
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J Mol Biol
Oct. 5, 1993
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The Saccharomyces cerevisiae DNA repair gene RAD23 encodes a nuclear protein containing a ubiquitin-like domain required for biological function.
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Watkins JF, Sung P, Prakash L, Prakash S
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Mol Cell Biol
Dec. 1, 1993
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The nucleotide sequence of Saccharomyces cerevisiae chromosome V.
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Dietrich FS, Mulligan J, Hennessy K, Yelton MA, Allen E, Araujo R, Aviles E, Berno A, Brennan T, Carpenter J, Chen E, Cherry JM, Chung E, Duncan M, Guzman E, Hartzell G, Hunicke-Smith S, Hyman RW, Kayser A, Komp C, Lashkari D, Lew H, Lin D, Mosedale D, Davis RW, et al.
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Nature
May 1, 1997
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Global analysis of protein expression in yeast.
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Ghaemmaghami S, Huh WK, Bower K, Howson RW, Belle A, Dephoure N, O'Shea EK, Weissman JS
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Nature
Oct. 16, 2003
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Global analysis of protein localization in budding yeast.
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Huh WK, Falvo JV, Gerke LC, Carroll AS, Howson RW, Weissman JS, O'Shea EK
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Nature
Oct. 16, 2003
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The N-terminus of yeast peptide: N-glycanase interacts with the DNA repair protein Rad23.
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Biswas S, Katiyar S, Li G, Zhou X, Lennarz WJ, Schindelin H
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Biochem Biophys Res Commun
Oct. 8, 2004
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Structure of a peptide:N-glycanase-Rad23 complex: insight into the deglycosylation for denatured glycoproteins.
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Lee JH, Choi JM, Lee C, Yi KJ, Cho Y
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Proc Natl Acad Sci U S A
June 28, 2005
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Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.
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Li X, Gerber SA, Rudner AD, Beausoleil SA, Haas W, Villen J, Elias JE, Gygi SP
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J Proteome Res
March 1, 2007
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Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.
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Hu Y, Rolfs A, Bhullar B, Murthy TV, Zhu C, Berger MF, Camargo AA, Kelley F, McCarron S, Jepson D, Richardson A, Raphael J, Moreira D, Taycher E, Zuo D, Mohr S, Kane MF, Williamson J, Simpson A, Bulyk ML, Harlow E, Marsischky G, Kolodner RD, LaBaer J
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Genome Res
April 1, 2007
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A multidimensional chromatography technology for in-depth phosphoproteome analysis.
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Albuquerque CP, Smolka MB, Payne SH, Bafna V, Eng J, Zhou H
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Mol Cell Proteomics
July 1, 2008
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Last modification of this entry: Oct. 6, 2010.
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