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Pol30p

Protein FULL name:

PCNA


Pol30p (Saccharomyces cerevisiae) is product of expression of POL30 gene.


Pol30p is involved in:

BER in Saccharomyces cerevisiae MMR in Saccharomyces cerevisiae NER in Saccharomyces cerevisiae




FUNCTION: This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Involved in DNA repair.

SUBUNIT: Homotrimer. Interacts with RAD30 and MCM10.

INTERACTION: P32354:MCM10; NbExp=3; IntAct=EBI-12993, EBI-5965; P26793:RAD27; NbExp=1; IntAct=EBI-12993, EBI-14693; Q04049:RAD30; NbExp=2; IntAct=EBI-12993, EBI-36214;

SUBCELLULAR LOCATION: Nucleus.

PTM: Sumoylated on Lys-164, and to a lesser extent on Lys-127 by the UBC9/SIZ1 complex during S-phase; which impairs ubiquitination and function in DNA repair.

PTM: Monoubiquitinated on Lys-164 by the UBC2/RAD18 complex upon DNA damage, and then polyubiquitinated through 'Lys-63'-linkage by UBC13/MMS2. Ubiquitination is required for UBC2-mediated DNA repair.

SIMILARITY: Belongs to the PCNA family.


NCBI GenPept GI number(s): 6319564
Species: Saccharomyces cerevisiae

Links to other databases:

Database ID Link
Uniprot P15873 P15873
PFAM: - P15873 (Link - using uniprot id)
InterPro: - P15873 (Link - using uniprot id)
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MLEAKFEEASLFKRIIDGFKDCVQLVNFQCKEDGIIAQAVDDSRVLLVSL
EIGVEAFQEYRCDHPVTLGMDLTSLSKILRCGNNTDTLTLIADNTPDSII
LLFEDTKKDRIAEYSLKLMDIDADFLKIEELQYDSTLSLPSSEFSKIVRD
LSQLSDSINIMITKETIKFVADGDIGSGSVIIKPFVDMEHPETSIKLEMD
QPVDLTFGAKYLLDIIKGSSLSDRVGIRLSSEAPALFQFDLKSGFLQFFL
APKFNDEE

Pol30p (Saccharomyces cerevisiae) is able to recognize following damages:
Pol30p (Saccharomyces cerevisiae) belongs to following protein families:
References:

Title Authors Journal
Molecular cloning, structure and expression of the yeast proliferating cell nuclear antigen gene. Bauer GA, Burgers PM Nucleic Acids Res Feb. 25, 1990
Analysis of a 70 kb region on the right arm of yeast chromosome II. Mannhaupt G, Stucka R, Ehnle S, Vetter I, Feldmann H Yeast Oct. 1, 1994
Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA. Krishna TS, Kong XP, Gary S, Burgers PM, Kuriyan J Cell Dec. 1, 1994
Complete DNA sequence of yeast chromosome II. Feldmann H, Aigle M, Aljinovic G, Andre B, Baclet MC, Barthe C, Baur A, Becam AM, Biteau N, Boles E, et al. EMBO J Dec. 15, 1994
Interaction with PCNA is essential for yeast DNA polymerase eta function. Haracska L, Kondratick CM, Unk I, Prakash S, Prakash L Mol Cell Aug. 1, 2001
RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Hoege C, Pfander B, Moldovan GL, Pyrowolakis G, Jentsch S Nature Sept. 12, 2002
Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex. Bowman GD, O'Donnell M, Kuriyan J Nature June 17, 2004
Global analyses of sumoylated proteins in Saccharomyces cerevisiae. Induction of protein sumoylation by cellular stresses. Zhou W, Ryan JJ, Zhou H J Biol Chem July 1, 2004
A proteomic strategy for gaining insights into protein sumoylation in yeast. Denison C, Rudner AD, Gerber SA, Bakalarski CE, Moazed D, Gygi SP Mol Cell Proteomics March 1, 2005
Interaction between PCNA and diubiquitinated Mcm10 is essential for cell growth in budding yeast. Das-Bradoo S, Ricke RM, Bielinsky AK Mol Cell Biol July 1, 2006
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


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

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