PARPT_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PARPT_HUMAN
• UniProt AC: Q7Z3E1
• Protein Name: TCDD-inducible poly [ADP-ribose] polymerase
• Gene Name: TIPARP
• Organism: Homo sapiens (Human).
• Sequence Length: 657
• Protein Description: Poly [ADP-ribose] polymerase using NAD(+) as a substrate to transfer ADP-ribose onto glutamic acid residues of a protein acceptor; repeated rounds of ADP-ribosylation leads to the formation of poly(ADPribose) chains on the protein, thereby altering the function of the target protein. May play a role in the adaptive response to chemical exposure (TCDD) and thereby mediates certain effects of the chemicals (By similarity)..
• Protein Sequence: MEMETTEPEPDCVVQPPSPPDDFSCQMRLSEKITPLKTCFKKKDQKRLGTGTLRSLRPILNTLLESGSLDGVFRSRNQSTDENSLHEPMMKKAMEINSSCPPAENNMSVLIPDRTNVGDQIPEAHPSTEAPERVVPIQDHSFPSETLSGTVADSTPAHFQTDLLHPVSSDVPTSPDCLDKVIDYVPGIFQENSFTIQYILDTSDKLSTELFQDKSEEASLDLVFELVNQLQYHTHQENGIEICMDFLQGTCIYGRDCLKHHTVLPYHWQIKRTTTQKWQSVFNDSQEHLERFYCNPENDRMRMKYGGQEFWADLNAMNVYETTEFDQLRRLSTPPSSNVNSIYHTVWKFFCRDHFGWREYPESVIRLIEEANSRGLKEVRFMMWNNHYILHNSFFRREIKRRPLFRSCFILLPYLQTLGGVPTQAPPPLEATSSSQIICPDGVTSANFYPETWVYMHPSQDFIQVPVSAEDKSYRIIYNLFHKTVPEFKYRILQILRVQNQFLWEKYKRKKEYMNRKMFGRDRIINERHLFHGTSQDVVDGICKHNFDPRVCGKHATMFGQGSYFAKKASYSHNFSKKSSKGVHFMFLAKVLTGRYTMGSHGMRRPPPVNPGSVTSDLYDSCVDNFFEPQIFVIFNDDQSYPYFVIQYEEVSNTVSI

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
32	Acetylation	CQMRLSEKITPLKTC HHHHHHCCCCCCHHH	48.80	25953088
32	Ubiquitination	CQMRLSEKITPLKTC HHHHHHCCCCCCHHH	48.80	-
39	ADP-ribosylation	KITPLKTCFKKKDQK CCCCCHHHHCCCCHH	4.50	30373764
62	Phosphorylation	SLRPILNTLLESGSL HHHHHHHHHHHHCCC	29.31	22468782
68	Phosphorylation	NTLLESGSLDGVFRS HHHHHHCCCCHHHCC	32.35	22468782
277	Ubiquitination	IKRTTTQKWQSVFND EEECCHHHHHHHHCC	45.14	-
332	Phosphorylation	FDQLRRLSTPPSSNV HHHHHCCCCCCCCCH	36.74	22210691
333	Phosphorylation	DQLRRLSTPPSSNVN HHHHCCCCCCCCCHH	43.75	22210691
336	Phosphorylation	RRLSTPPSSNVNSIY HCCCCCCCCCHHHHH	35.43	22210691
341	Phosphorylation	PPSSNVNSIYHTVWK CCCCCHHHHHHHHHH	21.90	22210691
345	Phosphorylation	NVNSIYHTVWKFFCR CHHHHHHHHHHHHCC	15.87	22210691
388	Phosphorylation	FMMWNNHYILHNSFF EEEECCEEEECHHHH	13.80	28450419
393	Phosphorylation	NHYILHNSFFRREIK CEEEECHHHHHHHHH	18.27	24719451
544	Ubiquitination	DVVDGICKHNFDPRV HHHHHHHHCCCCHHH	39.40	-
554	Ubiquitination	FDPRVCGKHATMFGQ CCHHHCCCCEEECCC	25.58	-
567	Ubiquitination	GQGSYFAKKASYSHN CCCHHHHHHHCCCCC	38.69	-
568	Ubiquitination	QGSYFAKKASYSHNF CCHHHHHHHCCCCCC	38.85	-
571	Phosphorylation	YFAKKASYSHNFSKK HHHHHHCCCCCCCCC	20.86	22817900
572	Phosphorylation	FAKKASYSHNFSKKS HHHHHCCCCCCCCCC	14.95	22817900
577	Ubiquitination	SYSHNFSKKSSKGVH CCCCCCCCCCCCCHH	53.16	-

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PARPT_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 PARPT_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of PARPT_HUMAN !!

Drug and Disease Associations

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