PARP2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PARP2_MOUSE
• UniProt AC: O88554
• Protein Name: Poly [ADP-ribose] polymerase 2
• Gene Name: Parp2
• Organism: Mus musculus (Mouse).
• Sequence Length: 559
• Subcellular Localization: Nucleus .
• Protein Description: Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. [PubMed: 10364231 This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks]
• Protein Sequence: MAPRRQRSGSGRRVLNEAKKVDNGNKATEDDSPPGKKMRTCQRKGPMAGGKDADRTKDNRDSVKTLLLKGKAPVDPECAAKLGKAHVYCEGDDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKTGQHSLVTCSGDLNKAKEIFQKKFLDKTKNNWEDRENFEKVPGKYDMLQMDYAASTQDESKTKEEETLKPESQLDLRVQELLKLICNVQTMEEMMIEMKYDTKRAPLGKLTVAQIKAGYQSLKKIEDCIRAGQHGRALVEACNEFYTRIPHDFGLSIPPVIRTEKELSDKVKLLEALGDIEIALKLVKSERQGLEHPLDQHYRNLHCALRPLDHESNEFKVISQYLQSTHAPTHKDYTMTLLDVFEVEKEGEKEAFREDLPNRMLLWHGSRLSNWVGILSHGLRVAPPEAPITGYMFGKGIYFADMSSKSANYCFASRLKNTGLLLLSEVALGQCNELLEANPKAQGLLRGKHSTKGMGKMAPSPAHFITLNGSTVPLGPASDTGILNPEGYTLNYNEFIVYSPNQVRMRYLLKIQFNFLQLW

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
5	Methylation	---MAPRRQRSGSGR ---CCCCCCCCCCCH	34.89	16289109
7	Methylation	-MAPRRQRSGSGRRV -CCCCCCCCCCCHHH	40.97	16289117
28	Phosphorylation	VDNGNKATEDDSPPG CCCCCCCCCCCCCCC	41.37	28285833
32	Phosphorylation	NKATEDDSPPGKKMR CCCCCCCCCCCHHHC	45.37	26824392
36	Acetylation	EDDSPPGKKMRTCQR CCCCCCCHHHCCCCC	49.52	18436469
36	ADP-ribosylation	EDDSPPGKKMRTCQR CCCCCCCHHHCCCCC	49.52	-
36	ADP-ribosylation	EDDSPPGKKMRTCQR CCCCCCCHHHCCCCC	49.52	18436469
37	Acetylation	DDSPPGKKMRTCQRK CCCCCCHHHCCCCCC	39.26	18436469
37	ADP-ribosylation	DDSPPGKKMRTCQRK CCCCCCHHHCCCCCC	39.26	-
37	ADP-ribosylation	DDSPPGKKMRTCQRK CCCCCCHHHCCCCCC	39.26	18436469
208	Phosphorylation	EETLKPESQLDLRVQ HHCCCCHHHHHHHHH	44.57	-
490	Phosphorylation	GLLRGKHSTKGMGKM HHHCCCCCCCCCCCC	34.99	28059163

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

Oops, there are no upstream regulatory protein records of PARP2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PARP2_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of PARP2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PARP2_MOUSE	Parp2	physical	11948190
PARP1_HUMAN	PARP1	physical	11948190
NPM_MOUSE	Npm1	physical	15615785

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Acetylation

"Identification of lysines 36 and 37 of PARP-2 as targets foracetylation and auto-ADP-ribosylation.";
Haenni S.S., Hassa P.O., Altmeyer M., Fey M., Imhof R., Hottiger M.O.;
Int. J. Biochem. Cell Biol. 40:2274-2283(2008).
Cited for: ACETYLATION AT LYS-36 AND LYS-37, ADP-RIBOSYLATION AT LYS-36 ANDLYS-37, AND MUTAGENESIS OF LYS-36 AND LYS-37.
PubMed: 18436469