PARP3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PARP3_HUMAN
• UniProt AC: Q9Y6F1
• Protein Name: Poly [ADP-ribose] polymerase 3
• Gene Name: PARP3
• Organism: Homo sapiens (Human).
• Sequence Length: 533
• Subcellular Localization: Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Core component of the centrosome. Preferentially localized to the daughter centriole throughou
• 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. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. May link the DNA damage surveillance network to the mitotic fidelity checkpoint. Negatively influences the G1/S cell cycle progression without interfering with centrosome duplication. Binds DNA. May be involved in the regulation of PRC2 and PRC3 complex-dependent gene silencing..
• Protein Sequence: MAPKPKPWVQTEGPEKKKGRQAGREEDPFRSTAEALKAIPAEKRIIRVDPTCPLSSNPGTQVYEDYNCTLNQTNIENNNNKFYIIQLLQDSNRFFTCWNRWGRVGEVGQSKINHFTRLEDAKKDFEKKFREKTKNNWAERDHFVSHPGKYTLIEVQAEDEAQEAVVKVDRGPVRTVTKRVQPCSLDPATQKLITNIFSKEMFKNTMALMDLDVKKMPLGKLSKQQIARGFEALEALEEALKGPTDGGQSLEELSSHFYTVIPHNFGHSQPPPINSPELLQAKKDMLLVLADIELAQALQAVSEQEKTVEEVPHPLDRDYQLLKCQLQLLDSGAPEYKVIQTYLEQTGSNHRCPTLQHIWKVNQEGEEDRFQAHSKLGNRKLLWHGTNMAVVAAILTSGLRIMPHSGGRVGKGIYFASENSKSAGYVIGMKCGAHHVGYMFLGEVALGREHHINTDNPSLKSPPPGFDSVIARGHTEPDPTQDTELELDGQQVVVPQGQPVPCPEFSSSTFSQSEYLIYQESQCRLRYLLEVHL

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
6	ADP-ribosylation	--MAPKPKPWVQTEG --CCCCCCCCCCCCC	58.60	25043379
12	ADP-ribosylation	PKPWVQTEGPEKKKG CCCCCCCCCCCCCCC	56.51	25043379
15	ADP-ribosylation	WVQTEGPEKKKGRQA CCCCCCCCCCCCCCC	84.26	25043379
26	ADP-ribosylation	GRQAGREEDPFRSTA CCCCCCCCCCCHHHH	70.40	25043379
31	Phosphorylation	REEDPFRSTAEALKA CCCCCCHHHHHHHHC	32.14	29083192
32	Phosphorylation	EEDPFRSTAEALKAI CCCCCHHHHHHHHCC	25.02	29083192
34	ADP-ribosylation	DPFRSTAEALKAIPA CCCHHHHHHHHCCCH	55.40	25043379
37	ADP-ribosylation	RSTAEALKAIPAEKR HHHHHHHHCCCHHHC	51.85	25043379
37	Ubiquitination	RSTAEALKAIPAEKR HHHHHHHHCCCHHHC	51.85	-
141	ADP-ribosylation	KNNWAERDHFVSHPG CCCHHHHHHCCCCCC	30.95	25043379
163	ADP-ribosylation	QAEDEAQEAVVKVDR EECHHHHHHEEEEEC	50.94	25043379
198	Phosphorylation	KLITNIFSKEMFKNT HHHHHHCCHHHHHCH	24.74	24719451
199	Ubiquitination	LITNIFSKEMFKNTM HHHHHCCHHHHHCHH	42.31	-
205	Phosphorylation	SKEMFKNTMALMDLD CHHHHHCHHHHHCCC	12.38	-
210	ADP-ribosylation	KNTMALMDLDVKKMP HCHHHHHCCCCCCCC	40.33	25043379
220	Acetylation	VKKMPLGKLSKQQIA CCCCCCCCCCHHHHH	58.22	19823141
220	Ubiquitination	VKKMPLGKLSKQQIA CCCCCCCCCCHHHHH	58.22	-
222	Phosphorylation	KMPLGKLSKQQIARG CCCCCCCCHHHHHHH	31.72	25159151
223	Acetylation	MPLGKLSKQQIARGF CCCCCCCHHHHHHHH	57.57	25953088
231	ADP-ribosylation	QQIARGFEALEALEE HHHHHHHHHHHHHHH	55.99	25043379
309	ADP-ribosylation	SEQEKTVEEVPHPLD HHCCCCHHCCCCCCC	59.51	25043379
310	ADP-ribosylation	EQEKTVEEVPHPLDR HCCCCHHCCCCCCCH	57.94	25043379
323	Ubiquitination	DRDYQLLKCQLQLLD CHHHHHHHHHHHHHH	28.64	-
344	ADP-ribosylation	KVIQTYLEQTGSNHR HHHHHHHHHHCCCCC	35.37	25043379
405	Phosphorylation	GLRIMPHSGGRVGKG CCEECCCCCCCCCCE	36.75	24719451
449	ADP-ribosylation	GEVALGREHHINTDN HHHHHCCCCCCCCCC	37.71	25043379
461	Phosphorylation	TDNPSLKSPPPGFDS CCCCCCCCCCCCCCC	48.18	-

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

Oops, there are no upstream regulatory protein records of PARP3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PARP3_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of PARP3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RFA3_HUMAN	RPA3	physical	17353931
MTDC_HUMAN	MTHFD2	physical	17353931
H2B2E_HUMAN	HIST2H2BE	physical	17353931
H32_HUMAN	HIST2H3C	physical	17353931
PARP1_HUMAN	PARP1	physical	12640039
PARP3_HUMAN	PARP3	physical	20064938
H11_HUMAN	HIST1H1A	physical	20064938
A4_HUMAN	APP	physical	21832049

Drug and Disease Associations

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