dbPTM

PNKP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PNKP_HUMAN
UniProt AC	Q96T60
Protein Name	Bifunctional polynucleotide phosphatase/kinase
Gene Name	PNKP
Organism	Homo sapiens (Human).
Sequence Length	521
Subcellular Localization	Nucleus .
Protein Description	Plays a key role in the repair of DNA damage, functioning as part of both the non-homologous end-joining (NHEJ) and base excision repair (BER) pathways. Through its two catalytic activities, PNK ensures that DNA termini are compatible with extension and ligation by either removing 3'-phosphates from, or by phosphorylating 5'-hydroxyl groups on, the ribose sugar of the DNA backbone..
Protein Sequence	MGEVEAPGRLWLESPPGGAPPIFLPSDGQALVLGRGPLTQVTDRKCSRTQVELVADPETRTVAVKQLGVNPSTTGTQELKPGLEGSLGVGDTLYLVNGLHPLTLRWEETRTPESQPDTPPGTPLVSQDEKRDAELPKKRMRKSNPGWENLEKLLVFTAAGVKPQGKVAGFDLDGTLITTRSGKVFPTGPSDWRILYPEIPRKLRELEAEGYKLVIFTNQMSIGRGKLPAEEFKAKVEAVVEKLGVPFQVLVATHAGLYRKPVTGMWDHLQEQANDGTPISIGDSIFVGDAAGRPANWAPGRKKKDFSCADRLFALNLGLPFATPEEFFLKWPAAGFELPAFDPRTVSRSGPLCLPESRALLSASPEVVVAVGFPGAGKSTFLKKHLVSAGYVHVNRDTLGSWQRCVTTCETALKQGKRVAIDNTNPDAASRARYVQCARAAGVPCRCFLFTATLEQARHNNRFREMTDSSHIPVSDMVMYGYRKQFEAPTLAEGFSAILEIPFRLWVEPRLGRLYCQFSEG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MGEVEAPG -------CCCCCCCC	10.48	22814378
14	Phosphorylation	PGRLWLESPPGGAPP CCCEEEECCCCCCCC	33.94	25159151
109	Phosphorylation	LTLRWEETRTPESQP EEEEEEECCCCCCCC	28.47	23927012
111	Phosphorylation	LRWEETRTPESQPDT EEEEECCCCCCCCCC	38.54	23927012
114	Phosphorylation	EETRTPESQPDTPPG EECCCCCCCCCCCCC	48.49	23927012
118	Phosphorylation	TPESQPDTPPGTPLV CCCCCCCCCCCCCCC	37.76	19664994
122	Phosphorylation	QPDTPPGTPLVSQDE CCCCCCCCCCCCHHH	21.15	23927012
126	Phosphorylation	PPGTPLVSQDEKRDA CCCCCCCCHHHHCCC	39.33	17525332
142	Ubiquitination	LPKKRMRKSNPGWEN CCHHHHHHCCCCCHH	45.29	29967540
143	Phosphorylation	PKKRMRKSNPGWENL CHHHHHHCCCCCHHH	37.58	25159151
162	Ubiquitination	VFTAAGVKPQGKVAG HHHHCCCCCCCEEEC	30.61	-
183	Acetylation	LITTRSGKVFPTGPS EEECCCCCEECCCCC	41.78	23749302
183	Ubiquitination	LITTRSGKVFPTGPS EEECCCCCEECCCCC	41.78	29967540
183	Sumoylation	LITTRSGKVFPTGPS EEECCCCCEECCCCC	41.78	-
183	Malonylation	LITTRSGKVFPTGPS EEECCCCCEECCCCC	41.78	26320211
183	Sumoylation	LITTRSGKVFPTGPS EEECCCCCEECCCCC	41.78	-
187	Phosphorylation	RSGKVFPTGPSDWRI CCCCEECCCCCCCCH	50.70	28555341
224	Methylation	TNQMSIGRGKLPAEE ECCCCCCCCCCCHHH	37.09	54558089
226	Malonylation	QMSIGRGKLPAEEFK CCCCCCCCCCHHHHH	50.35	26320211
226	Ubiquitination	QMSIGRGKLPAEEFK CCCCCCCCCCHHHHH	50.35	33845483
226	Acetylation	QMSIGRGKLPAEEFK CCCCCCCCCCHHHHH	50.35	23749302
323	Phosphorylation	NLGLPFATPEEFFLK HCCCCCCCHHHHCHH	31.45	30387612
362	Phosphorylation	PESRALLSASPEVVV HHHHHHHCCCCCEEE	27.79	28348404
364	Phosphorylation	SRALLSASPEVVVAV HHHHHCCCCCEEEEE	20.44	27251275
379	Phosphorylation	GFPGAGKSTFLKKHL CCCCCCHHHHHHHHH	24.39	-
414	Ubiquitination	TTCETALKQGKRVAI HHHHHHHHCCCEEEE	55.32	33845483
484	Ubiquitination	MVMYGYRKQFEAPTL HHHHCCCCCCCCCCH	51.35	-

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
114	S	Phosphorylation	Kinase	ATM	Q13315	PSP
114	S	Phosphorylation	Kinase	PRKDC	P78527	GPS
126	S	Phosphorylation	Kinase	ATM	Q13315	PSP
126	S	Phosphorylation	Kinase	PRKDC	P78527	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PNKP_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of PNKP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KR412_HUMAN	KRTAP4-12	physical	16189514
MYOZ1_HUMAN	MYOZ1	physical	16189514
DNLI4_HUMAN	LIG4	physical	17353931
DNLI3_HUMAN	LIG3	physical	17353931
XRCC1_HUMAN	XRCC1	physical	17353931
MCM3_HUMAN	MCM3	physical	17353931
NOM1_HUMAN	NOM1	physical	17353931
XRCC4_HUMAN	XRCC4	physical	17353931
NOL3_HUMAN	NOL3	physical	17353931
LAS1L_HUMAN	LAS1L	physical	17353931
NUP93_HUMAN	NUP93	physical	17353931
CMC1_HUMAN	SLC25A12	physical	17353931
DAAF5_HUMAN	DNAAF5	physical	17353931
ATD3B_HUMAN	ATAD3B	physical	17353931
DDX20_HUMAN	DDX20	physical	17353931
XRCC1_HUMAN	XRCC1	physical	11163244
DPOLB_HUMAN	POLB	physical	11163244
DNLI3_HUMAN	LIG3	physical	11163244
A4_HUMAN	APP	physical	21832049
TRI18_HUMAN	MID1	physical	22939629
XRCC4_HUMAN	XRCC4	physical	15385968
CR025_HUMAN	C18orf25	physical	15385968
TRI26_HUMAN	TRIM26	physical	15385968
NASP_HUMAN	NASP	physical	15385968
XRCC6_HUMAN	XRCC6	physical	15385968
XRCC5_HUMAN	XRCC5	physical	15385968
XRCC1_HUMAN	XRCC1	physical	15385968
SSRP1_HUMAN	SSRP1	physical	15385968
MCM5_HUMAN	MCM5	physical	15385968
MCM3_HUMAN	MCM3	physical	15385968
GEMI4_HUMAN	GEMIN4	physical	15385968
CD11B_HUMAN	CDK11B	physical	15385968
PARP1_HUMAN	PARP1	physical	15385968
HNRPU_HUMAN	HNRNPU	physical	15385968
NOLC1_HUMAN	NOLC1	physical	15385968
SP16H_HUMAN	SUPT16H	physical	15385968
NRDC_HUMAN	NRD1	physical	15385968
CBPC1_HUMAN	AGTPBP1	physical	15385968
TCOF_HUMAN	TCOF1	physical	15385968
DCAF1_HUMAN	VPRBP	physical	15385968
UBE2O_HUMAN	UBE2O	physical	15385968
PRKDC_HUMAN	PRKDC	physical	15385968
DNLI4_HUMAN	LIG4	physical	15385968
KDM1A_HUMAN	KDM1A	physical	23455924
SUV91_HUMAN	SUV39H1	physical	23455924
ZN639_HUMAN	ZNF639	physical	25416956
DCPS_HUMAN	DCPS	physical	26344197
SBDS_HUMAN	SBDS	physical	26344197
ATX3_HUMAN	ATXN3	physical	25590633
HBB_HUMAN	HBB	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613402	Microcephaly, seizures, and developmental delay (MCSZ)
616267	Ataxia-oculomotor apraxia 4 (AOA4)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PNKP_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; THR-118 ANDSER-126, AND MASS SPECTROMETRY.	17525332 [Abstract]
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-118 AND THR-122, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-118 AND THR-122, ANDMASS SPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-118 AND THR-122, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-118 AND THR-122, ANDMASS SPECTROMETRY.	17081983 [Abstract]