REPAIRtoire - a database of DNA repair pathways

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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;


MISCELLANEOUS: Present with 10900 molecules/cell in log phase SD medium.

SIMILARITY: Contains 2 UBA domains.

SIMILARITY: Contains 1 ubiquitin-like domain.

NCBI GenPept GI number(s): 6320798
Species: Saccharomyces cerevisiae

Links to other databases:

Database ID Link
Uniprot P32628 P32628
PFAM: - P32628 (Link - using uniprot id)
InterPro: - P32628 (Link - using uniprot id)
CATH: - -
SCOP: - -
PDB: - -

Protein sequence:

Rad23p (Saccharomyces cerevisiae) belongs to following protein families:

Title Authors Journal
The gene clusters ARC and COR on chromosomes 5 and 10, respectively, of Saccharomyces cerevisiae share a common ancestry. Melnick L, Sherman F J Mol Biol Oct. 5, 1993
The Saccharomyces cerevisiae DNA repair gene RAD23 encodes a nuclear protein containing a ubiquitin-like domain required for biological function. Watkins JF, Sung P, Prakash L, Prakash S Mol Cell Biol Dec. 1, 1993
The nucleotide sequence of Saccharomyces cerevisiae chromosome V. 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. Nature May 1, 1997
Global analysis of protein expression in yeast. Ghaemmaghami S, Huh WK, Bower K, Howson RW, Belle A, Dephoure N, O'Shea EK, Weissman JS Nature Oct. 16, 2003
Global analysis of protein localization in budding yeast. Huh WK, Falvo JV, Gerke LC, Carroll AS, Howson RW, Weissman JS, O'Shea EK Nature Oct. 16, 2003
The N-terminus of yeast peptide: N-glycanase interacts with the DNA repair protein Rad23. Biswas S, Katiyar S, Li G, Zhou X, Lennarz WJ, Schindelin H Biochem Biophys Res Commun Oct. 8, 2004
Structure of a peptide:N-glycanase-Rad23 complex: insight into the deglycosylation for denatured glycoproteins. Lee JH, Choi JM, Lee C, Yi KJ, Cho Y Proc Natl Acad Sci U S A June 28, 2005
Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae. Li X, Gerber SA, Rudner AD, Beausoleil SA, Haas W, Villen J, Elias JE, Gygi SP J Proteome Res March 1, 2007
Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae. 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 Genome Res April 1, 2007
A multidimensional chromatography technology for in-depth phosphoproteome analysis. Albuquerque CP, Smolka MB, Payne SH, Bafna V, Eng J, Zhou H Mol Cell Proteomics July 1, 2008

Last modification of this entry: Oct. 6, 2010.

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