PCNA_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PCNA_RAT
• UniProt AC: P04961
• Protein Name: Proliferating cell nuclear antigen
• Gene Name: Pcna
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 261
• Subcellular Localization: Nucleus . Forms nuclear foci representing sites of ongoing DNA replication and vary in morphology and number during S phase. Together with APEX2, is redistributed in discrete nuclear foci in presence of oxidative DNA damaging agents. Colocalizes with
• Protein Description: 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. Induces a robust stimulatory effect on the 3'-5' exonuclease and 3'-phosphodiesterase, but not apurinic-apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2. Plays a key role in DNA damage response (DDR) by being conveniently positioned at the replication fork to coordinate DNA replication with DNA repair and DNA damage tolerance pathways. Acts as a loading platform to recruit DDR proteins that allow completion of DNA replication after DNA damage and promote postreplication repair: Monoubiquitinated PCNA leads to recruitment of translesion (TLS) polymerases, while 'Lys-63'-linked polyubiquitination of PCNA is involved in error-free pathway and employs recombination mechanisms to synthesize across the lesion (By similarity)..
• Protein Sequence: MFEARLIQGSILKKVLEALKDLINEACWDISSGGVNLQSMDSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMDLDVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAKDGVKFSASGELGNGNIKLSQTSNVDKEEEAVSIEMNEPVQLTFALRYLNFFTKATPLSPTVTLSMSADVPLVVEYKIADMGHLKYYLAPKIEDEEGS

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
13	Acetylation	LIQGSILKKVLEALK HHCHHHHHHHHHHHH	38.88	22902405
14	Acetylation	IQGSILKKVLEALKD HCHHHHHHHHHHHHH	48.91	-
77	Acetylation	VNLTSMSKILKCAGN CCHHHHHHHHHHHCC	43.34	-
80	Acetylation	TSMSKILKCAGNEDI HHHHHHHHHHCCCCE	26.05	-
211	Phosphorylation	QLTFALRYLNFFTKA HHHHHHHHHHCCCCC	13.57	-
248	Acetylation	IADMGHLKYYLAPKI ECCCCCCEEEECCCC	26.61	-
261	Phosphorylation	KIEDEEGS------- CCCCCCCC-------	40.09	23984901

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
211	Y	Phosphorylation	Kinase	EGFR	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
13	K	Acetylation	Acetylated by CREBBP and p300/EP300; preferentially acetylated by CREBBP on Lys-80, Lys-13 and Lys-14 and on Lys-77 by p300/EP300 upon loading on chromatin in response to UV irradiation.	-
14	K	Acetylation	Acetylated by CREBBP and p300/EP300; preferentially acetylated by CREBBP on Lys-80, Lys-13 and Lys-14 and on Lys-77 by p300/EP300 upon loading on chromatin in response to UV irradiation.	-
63	K	ubiquitylation	An error-free pathway also exists and requires non-canonical polyubiquitination on Lys-164 through 'Lys-63' linkage of ubiquitin moieties by the E2 complex UBE2N-UBE2V2 and the E3 ligases, HLTF, RNF8 and SHPRH.	-
77	K	Acetylation	Acetylated by CREBBP and p300/EP300; preferentially acetylated by CREBBP on Lys-80, Lys-13 and Lys-14 and on Lys-77 by p300/EP300 upon loading on chromatin in response to UV irradiation.	-
80	K	Acetylation	Acetylated by CREBBP and p300/EP300; preferentially acetylated by CREBBP on Lys-80, Lys-13 and Lys-14 and on Lys-77 by p300/EP300 upon loading on chromatin in response to UV irradiation.	-
164	K	ubiquitylation	An error-free pathway also exists and requires non-canonical polyubiquitination on Lys-164 through 'Lys-63' linkage of ubiquitin moieties by the E2 complex UBE2N-UBE2V2 and the E3 ligases, HLTF, RNF8 and SHPRH.	-
164	K	ubiquitylation	Following induction of replication stress, monoubiquitinated by the UBE2B-RAD18 complex on Lys-164, leading to recruit translesion (TLS) polymerases, which are able to synthesize across DNA lesions in a potentially error-prone manner.	-
164	K	ubiquitylation	Monoubiquitination at Lys-164 also takes place in undamaged proliferating cells, and is mediated by the DCX(DTL) complex, leading to enhance PCNA-dependent translesion DNA synthesis.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of PCNA_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ESR2_RAT	Esr2	physical	19683557

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.