dbPTM

PCNA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PCNA_HUMAN
UniProt AC	P12004
Protein Name	Proliferating cell nuclear antigen
Gene Name	PCNA
Organism	Homo sapiens (Human).
Sequence Length	261
Subcellular Localization	Nucleus . Colocalizes with CREBBP, EP300 and POLD1 to sites of DNA damage (PubMed:24939902). Forms nuclear foci representing sites of ongoing DNA replication and vary in morphology and number during S phase. Together with APEX2, is redistributed in d
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. [PubMed: 24939902 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.]
Protein Sequence	MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSMDSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMDLDVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAKDGVKFSASGELGNGNIKLSQTSNVDKEEEAVTIEMNEPVQLTFALRYLNFFTKATPLSSTVTLSMSADVPLVVEYKIADMGHLKYYLAPKIEDEEGS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Methylation	---MFEARLVQGSIL ---CCCHHHHCHHHH	28.35	115486671
10	Phosphorylation	EARLVQGSILKKVLE CHHHHCHHHHHHHHH	13.99	24719451
10	O-linked_Glycosylation	EARLVQGSILKKVLE CHHHHCHHHHHHHHH	13.99	23301498
13	Succinylation	LVQGSILKKVLEALK HHCHHHHHHHHHHHH	38.88	23954790
13	Acetylation	LVQGSILKKVLEALK HHCHHHHHHHHHHHH	38.88	23749302
13	Ubiquitination	LVQGSILKKVLEALK HHCHHHHHHHHHHHH	38.88	23000965
14	Ubiquitination	VQGSILKKVLEALKD HCHHHHHHHHHHHHH	48.91	23000965
14	Acetylation	VQGSILKKVLEALKD HCHHHHHHHHHHHHH	48.91	19419956
14	2-Hydroxyisobutyrylation	VQGSILKKVLEALKD HCHHHHHHHHHHHHH	48.91	-
20	Ubiquitination	KKVLEALKDLINEAC HHHHHHHHHHHHHHH	58.50	PubMed
60	Phosphorylation	RSEGFDTYRCDRNLA CCCCCCEEECCCCCC	15.87	-
60	Nitration	RSEGFDTYRCDRNLA CCCCCCEEECCCCCC	15.87	-
61	Methylation	SEGFDTYRCDRNLAM CCCCCEEECCCCCCC	20.25	115486687
68	Sulfoxidation	RCDRNLAMGVNLTSM ECCCCCCCCCCHHHH	7.49	21406390
73	Phosphorylation	LAMGVNLTSMSKILK CCCCCCHHHHHHHHH	19.72	21406692
74	Phosphorylation	AMGVNLTSMSKILKC CCCCCHHHHHHHHHH	24.99	21406692
76	Phosphorylation	GVNLTSMSKILKCAG CCCHHHHHHHHHHHC	19.13	21406692
77	Malonylation	VNLTSMSKILKCAGN CCHHHHHHHHHHHCC	43.34	26320211
77	Ubiquitination	VNLTSMSKILKCAGN CCHHHHHHHHHHHCC	43.34	23000965
77	Acetylation	VNLTSMSKILKCAGN CCHHHHHHHHHHHCC	43.34	19608861
80	Malonylation	TSMSKILKCAGNEDI HHHHHHHHHHCCCCE	26.05	26320211
80	2-Hydroxyisobutyrylation	TSMSKILKCAGNEDI HHHHHHHHHHCCCCE	26.05	-
80	Ubiquitination	TSMSKILKCAGNEDI HHHHHHHHHHCCCCE	26.05	23000965
80	Acetylation	TSMSKILKCAGNEDI HHHHHHHHHHCCCCE	26.05	19608861
81	S-nitrosocysteine	SMSKILKCAGNEDII HHHHHHHHHCCCCEE	5.41	-
81	Glutathionylation	SMSKILKCAGNEDII HHHHHHHHHCCCCEE	5.41	22555962
81	S-nitrosylation	SMSKILKCAGNEDII HHHHHHHHHCCCCEE	5.41	22178444
110	Ubiquitination	FEAPNQEKVSDYEMK EECCCCCCCCCHHEE	36.96	21906983
114	Phosphorylation	NQEKVSDYEMKLMDL CCCCCCCHHEEECCC	15.49	29116813
117	Ubiquitination	KVSDYEMKLMDLDVE CCCCHHEEECCCCHH	28.81	21963094
117	Neddylation	KVSDYEMKLMDLDVE CCCCHHEEECCCCHH	28.81	32015554
119	Sulfoxidation	SDYEMKLMDLDVEQL CCHHEEECCCCHHHH	3.92	28465586
133	Phosphorylation	LGIPEQEYSCVVKMP HCCCCCEEEEEEECC	13.68	29116813
134	Phosphorylation	GIPEQEYSCVVKMPS CCCCCEEEEEEECCC	10.32	29116813
135	Glutathionylation	IPEQEYSCVVKMPSG CCCCEEEEEEECCCC	3.90	22555962
138	Ubiquitination	QEYSCVVKMPSGEFA CEEEEEEECCCCHHH	25.38	21963094
139	Sulfoxidation	EYSCVVKMPSGEFAR EEEEEEECCCCHHHH	1.84	21406390
146	Methylation	MPSGEFARICRDLSH CCCCHHHHHHHHHHH	33.58	115486679
152	Phosphorylation	ARICRDLSHIGDAVV HHHHHHHHHCCCEEE	19.83	21712546
161	Phosphorylation	IGDAVVISCAKDGVK CCCEEEEEECCCCCE	9.08	28258704
162	S-palmitoylation	GDAVVISCAKDGVKF CCEEEEEECCCCCEE	3.61	26865113
162	S-nitrosocysteine	GDAVVISCAKDGVKF CCEEEEEECCCCCEE	3.61	-
162	Glutathionylation	GDAVVISCAKDGVKF CCEEEEEECCCCCEE	3.61	22555962
162	S-nitrosylation	GDAVVISCAKDGVKF CCEEEEEECCCCCEE	3.61	22178444
164	Sumoylation	AVVISCAKDGVKFSA EEEEEECCCCCEEEE	60.38	28112733
164	Acetylation	AVVISCAKDGVKFSA EEEEEECCCCCEEEE	60.38	23954790
164	Sumoylation	AVVISCAKDGVKFSA EEEEEECCCCCEEEE	60.38	-
164	2-Hydroxyisobutyrylation	AVVISCAKDGVKFSA EEEEEECCCCCEEEE	60.38	-
164	Ubiquitination	AVVISCAKDGVKFSA EEEEEECCCCCEEEE	60.38	27667366
164	Neddylation	AVVISCAKDGVKFSA EEEEEECCCCCEEEE	60.38	32015554
168	Acetylation	SCAKDGVKFSASGEL EECCCCCEEEECCCC	38.85	26051181
168	Ubiquitination	SCAKDGVKFSASGEL EECCCCCEEEECCCC	38.85	23000965
170	Phosphorylation	AKDGVKFSASGELGN CCCCCEEEECCCCCC	18.79	28509920
172	Phosphorylation	DGVKFSASGELGNGN CCCEEEECCCCCCCC	31.44	28509920
181	Ubiquitination	ELGNGNIKLSQTSNV CCCCCCEEEEECCCC	46.19	22817900
183	Phosphorylation	GNGNIKLSQTSNVDK CCCCEEEEECCCCCC	26.81	21406692
185	Phosphorylation	GNIKLSQTSNVDKEE CCEEEEECCCCCCCC	20.92	21406692
186	Phosphorylation	NIKLSQTSNVDKEEE CEEEEECCCCCCCCC	27.50	21406692
190	Ubiquitination	SQTSNVDKEEEAVTI EECCCCCCCCCCEEE	63.84	33845483
190	Acetylation	SQTSNVDKEEEAVTI EECCCCCCCCCCEEE	63.84	7367671
199	Sulfoxidation	EEAVTIEMNEPVQLT CCCEEEECCCCCHHH	6.43	28183972
210	Methylation	VQLTFALRYLNFFTK CHHHHHHHHHHCCCC	30.39	115486663
211	Phosphorylation	QLTFALRYLNFFTKA HHHHHHHHHHCCCCC	13.57	17115032
216	Phosphorylation	LRYLNFFTKATPLSS HHHHHCCCCCCCCCC	18.68	21712546
217	Ubiquitination	RYLNFFTKATPLSST HHHHCCCCCCCCCCE	45.14	33845483
217	Acetylation	RYLNFFTKATPLSST HHHHCCCCCCCCCCE	45.14	7367681
219	Phosphorylation	LNFFTKATPLSSTVT HHCCCCCCCCCCEEE	26.73	26503514
222	Phosphorylation	FTKATPLSSTVTLSM CCCCCCCCCEEEEEE	25.76	30576142
223	Phosphorylation	TKATPLSSTVTLSMS CCCCCCCCEEEEEEC	34.28	30576142
228	Phosphorylation	LSSTVTLSMSADVPL CCCEEEEEECCCCCE	11.00	26503514
229	Sulfoxidation	SSTVTLSMSADVPLV CCEEEEEECCCCCEE	4.27	28183972
230	Phosphorylation	STVTLSMSADVPLVV CEEEEEECCCCCEEE	20.24	26503514
239	Phosphorylation	DVPLVVEYKIADMGH CCCEEEEEEECCCCC	8.97	26503514
244	Sulfoxidation	VEYKIADMGHLKYYL EEEEECCCCCCEEEE	2.42	30846556
248	Acetylation	IADMGHLKYYLAPKI ECCCCCCEEEECCCC	26.61	19608861
248	Ubiquitination	IADMGHLKYYLAPKI ECCCCCCEEEECCCC	26.61	23000965
248	2-Hydroxyisobutyrylation	IADMGHLKYYLAPKI ECCCCCCEEEECCCC	26.61	-
248	Neddylation	IADMGHLKYYLAPKI ECCCCCCEEEECCCC	26.61	32015554
250	Phosphorylation	DMGHLKYYLAPKIED CCCCCEEEECCCCCC	8.52	17081983
254	Sumoylation	LKYYLAPKIEDEEGS CEEEECCCCCCCCCC	53.79	28112733
254	Ubiquitination	LKYYLAPKIEDEEGS CEEEECCCCCCCCCC	53.79	23000965
254	Sumoylation	LKYYLAPKIEDEEGS CEEEECCCCCCCCCC	53.79	-
254	Acetylation	LKYYLAPKIEDEEGS CEEEECCCCCCCCCC	53.79	26051181
261	Phosphorylation	KIEDEEGS------- CCCCCCCC-------	40.09	22617229

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
60	Y	Phosphorylation	Kinase	IGF1R	P08069	PSP
133	Y	Phosphorylation	Kinase	IGF1R	P08069	PSP
211	Y	Phosphorylation	Kinase	EGFR	P00533	Uniprot
250	Y	Phosphorylation	Kinase	IGF1R	P08069	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	DTL	Q9NZJ0	PMID:20129063
-	K	Ubiquitination	E3 ubiquitin ligase	HUWE1	Q7Z6Z7	PMID:22203964
-	K	Ubiquitination	E3 ubiquitin ligase	RNF8	O76064	PMID:18948756
-	K	Ubiquitination	E3 ubiquitin ligase	RAD18	Q9NS91	PMID:12226657
-	K	Ubiquitination	E3 ubiquitin ligase	HLTF	Q14527	PMID:18719106
-	K	Ubiquitination	E3 ubiquitin ligase	PAXIP1	Q6ZW49	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	SHPRH	Q149N8	PMID:17130289

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
13	K	Acetylation	24939902
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	19419956
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	18316726
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	19608861
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	19608861
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	17130289
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	17130289
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	17130289
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.

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GA45A_HUMAN	GADD45A	physical	7973727
GA45G_HUMAN	GADD45G	physical	11022036
GA45A_HUMAN	GADD45A	physical	10973963
GA45A_HUMAN	GADD45A	physical	10828065
GA45B_MOUSE	Gadd45b	physical	10828065
XRCC1_HUMAN	XRCC1	physical	15107487
FEN1_HUMAN	FEN1	physical	12853968
WRN_HUMAN	WRN	physical	12633936
DNMT1_HUMAN	DNMT1	physical	10888872
HDAC1_HUMAN	HDAC1	physical	11929879
EP300_HUMAN	EP300	physical	11268218
PDIP2_HUMAN	POLDIP2	physical	12522211
RFC2_HUMAN	RFC2	physical	9228079
RFC4_HUMAN	RFC4	physical	9228079
RFC5_HUMAN	RFC5	physical	9228079
RFC1_HUMAN	RFC1	physical	8861969
CDN1A_HUMAN	CDKN1A	physical	8861969
PCNA_HUMAN	PCNA	physical	9545252
FEN1_HUMAN	FEN1	physical	9545252
CDN1A_HUMAN	CDKN1A	physical	9545252
BACD1_HUMAN	KCTD13	physical	11593007
CDC6_HUMAN	CDC6	physical	9566895
FEN1_HUMAN	FEN1	physical	9305916
RFC1_HUMAN	RFC1	physical	10353443
MCL1_HUMAN	MCL1	physical	10978339
MPIP3_HUMAN	CDC25C	physical	11896603
RFC2_HUMAN	RFC2	physical	8093561
DPOLL_HUMAN	POLL	physical	12368291
DPOD2_HUMAN	POLD2	physical	11986310
WRN_HUMAN	WRN	physical	10871373
FEN1_HUMAN	FEN1	physical	8876181
APEX1_HUMAN	APEX1	physical	11601988
MSH6_HUMAN	MSH6	physical	12171929
XRCC5_HUMAN	XRCC5	physical	12171929
CTF18_HUMAN	CHTF18	physical	12171929
DPOE1_HUMAN	POLE	physical	12171929
DPOD1_HUMAN	POLD1	physical	12171929
RFC3_HUMAN	RFC3	physical	12171929
PRKDC_HUMAN	PRKDC	physical	12171929
RUVB2_HUMAN	RUVBL2	physical	12171929
RFC5_HUMAN	RFC5	physical	12171929
RFC2_HUMAN	RFC2	physical	12171929
DPOD3_HUMAN	POLD3	physical	12171929
MBB1A_HUMAN	MYBBP1A	physical	12171929
MSH3_HUMAN	MSH3	physical	12171929
XRCC6_HUMAN	XRCC6	physical	12171929
ANXA2_HUMAN	ANXA2	physical	12171929
MSH2_HUMAN	MSH2	physical	12171929
RFC4_HUMAN	RFC4	physical	12171929
RFA1_HUMAN	RPA1	physical	12171929
CCNO_HUMAN	CCNO	physical	12171929
DNLI1_HUMAN	LIG1	physical	12171929
RFC1_HUMAN	RFC1	physical	12171929
DNMT1_HUMAN	DNMT1	physical	9302295
CDN1A_HUMAN	CDKN1A	physical	11350925
XRCC6_HUMAN	XRCC6	physical	11239001
XRCC5_HUMAN	XRCC5	physical	11239001
HUS1_HUMAN	HUS1	physical	11077446
FEN1_HUMAN	FEN1	physical	11313979
PAF15_HUMAN	KIAA0101	physical	11313979
CDN1A_HUMAN	CDKN1A	physical	11313979
POLK_MOUSE	Polk	physical	18162470
POLH_HUMAN	POLH	physical	15149598
CDN1A_HUMAN	CDKN1A	physical	17588519
POLK_HUMAN	POLK	physical	16611994
CDT1_HUMAN	CDT1	physical	16407252
ING2_HUMAN	ING2	physical	19730436
EGFR_HUMAN	EGFR	physical	17115032
FEN1_HUMAN	FEN1	physical	17115032
CDN1A_HUMAN	CDKN1A	physical	17115032
CAF1A_HUMAN	CHAF1A	physical	16826239
DDX11_HUMAN	DDX11	physical	18499658
PCNA_HUMAN	PCNA	physical	15805117
CAF1A_HUMAN	CHAF1A	physical	15805117
DPOD1_HUMAN	POLD1	physical	15805117
CHK1_HUMAN	CHEK1	physical	18448427
BAZ1B_HUMAN	BAZ1B	physical	15543136
MBD1_HUMAN	MBD1	physical	15327775
SETB1_HUMAN	SETDB1	physical	15327775
CAF1A_HUMAN	CHAF1A	physical	15327775
DPOLB_HUMAN	POLB	physical	14988403
DPOD1_HUMAN	POLD1	physical	14988403
HDAC1_HUMAN	HDAC1	physical	14988403
EP300_HUMAN	EP300	physical	14988403
FANCL_HUMAN	FANCL	physical	20937699
FANCA_HUMAN	FANCA	physical	20937699
FANCE_HUMAN	FANCE	physical	20937699
ATAD5_HUMAN	ATAD5	physical	20147293
CCL2_HUMAN	CCL2	physical	21383955
SETMR_HUMAN	SETMAR	physical	20457750
CDN1A_HUMAN	CDKN1A	physical	19704162
FACD2_HUMAN	FANCD2	physical	19704162
DPOLN_HUMAN	POLN	physical	16611994
POLH_HUMAN	POLH	physical	20159558
MK15_HUMAN	MAPK15	physical	20733054
MDM2_HUMAN	MDM2	physical	20733054
CDN1A_HUMAN	CDKN1A	physical	19895794
RFA1_HUMAN	RPA1	physical	20227374
XRCC1_HUMAN	XRCC1	physical	20227374
POLK_HUMAN	POLK	physical	20227374
DPOD1_HUMAN	POLD1	physical	20227374
DPOE1_HUMAN	POLE	physical	20227374
CDN2A_HUMAN	CDKN2A	physical	17955473
ARF_HUMAN	CDKN2A	physical	17955473
DPOD3_HUMAN	POLD3	physical	11328591
DPOD1_HUMAN	POLD1	physical	11328591
DPOD2_HUMAN	POLD2	physical	11328591
G3P_HUMAN	GAPDH	physical	20849852
ALDOA_HUMAN	ALDOA	physical	20849852
ENOA_HUMAN	ENO1	physical	20849852
SPAG1_HUMAN	SPAG1	physical	20849852
PGK1_HUMAN	PGK1	physical	20849852
PGAM1_HUMAN	PGAM1	physical	20849852
RSSA_HUMAN	RPSA	physical	20849852
CAH2_HUMAN	CA2	physical	20849852
PRDX6_HUMAN	PRDX6	physical	20849852
MDHM_HUMAN	MDH2	physical	20849852
K2C7_HUMAN	KRT7	physical	20849852
ANXA2_HUMAN	ANXA2	physical	20849852
PPIA_HUMAN	PPIA	physical	20849852
EF1A1_HUMAN	EEF1A1	physical	20849852
HXK4_HUMAN	GCK	physical	20849852
G6PI_HUMAN	GPI	physical	20849852
PFKAM_HUMAN	PFKM	physical	20849852
TPIS_HUMAN	TPI1	physical	20849852
KPYR_HUMAN	PKLR	physical	20849852
LDHA_HUMAN	LDHA	physical	20849852
MPIP3_HUMAN	CDC25C	physical	11559705
CDN1A_HUMAN	CDKN1A	physical	11559705
RFA1_HUMAN	RPA1	physical	11254741
RFA2_HUMAN	RPA2	physical	11254741
RFA3_HUMAN	RPA3	physical	11254741
DHX9_HUMAN	DHX9	physical	11254741
CDK4_HUMAN	CDK4	physical	11254741
CDK5_HUMAN	CDK5	physical	11254741
TOP1_HUMAN	TOP1	physical	11254741
CDN1A_HUMAN	CDKN1A	physical	11254741
RAD9A_HUMAN	RAD9A	physical	12400013
RFC1_HUMAN	RFC1	physical	12400013
EXO1_HUMAN	EXO1	physical	14676842
PIDD1_HUMAN	PIDD1	physical	21415862
CDN1A_HUMAN	CDKN1A	physical	21415862
CDN1A_HUMAN	CDKN1A	physical	20605778
FEN1_HUMAN	FEN1	physical	15576034
DPOD3_HUMAN	POLD3	physical	15576034
CDN1A_HUMAN	CDKN1A	physical	15576034
POLH_HUMAN	POLH	physical	21791603
DTL_HUMAN	DTL	physical	21725088
MSH6_HUMAN	MSH6	physical	21725088
REV1_HUMAN	REV1	physical	21690293
PARP1_HUMAN	PARP1	physical	21690293
POLH_HUMAN	POLH	physical	21855803
KDM5C_HUMAN	KDM5C	physical	21996408
FEN1_HUMAN	FEN1	physical	22592530
KMT5A_HUMAN	SETD8	physical	22556262
FEN1_HUMAN	FEN1	physical	22556262
H32_HUMAN	HIST2H3C	physical	22387026
POLI_HUMAN	POLI	physical	18931444
POLI_HUMAN	POLI	physical	15342632
POLH_HUMAN	POLH	physical	15342632
POLI_HUMAN	POLI	physical	11724965
DCR1A_HUMAN	DCLRE1A	physical	20385554
CUL4A_HUMAN	CUL4A	physical	22692198
POLH_HUMAN	POLH	physical	20129057
PARP1_HUMAN	PARP1	physical	20129057
P53_HUMAN	TP53	physical	16861890
DPOLN_HUMAN	POLN	physical	22456510
PRKN_HUMAN	PARK2	physical	19285961
SPRTN_HUMAN	SPRTN	physical	22902628
SPRTN_HUMAN	SPRTN	physical	22894931
FOXO3_HUMAN	FOXO3	physical	22451935
BACD3_HUMAN	KCTD10	physical	19125419
SPRTN_HUMAN	SPRTN	physical	23042605
DNMT1_HUMAN	DNMT1	physical	20613874
CTIP_HUMAN	RBBP8	physical	19342888
WRN_HUMAN	WRN	physical	12750383
RFC4_HUMAN	RFC4	physical	22939629
RFC1_HUMAN	RFC1	physical	22939629
RAD21_HUMAN	RAD21	physical	22939629
PAF15_HUMAN	KIAA0101	physical	16288740
DNLI1_HUMAN	LIG1	physical	9649448
RFC1_HUMAN	RFC1	physical	9649448
CDK2_HUMAN	CDK2	physical	9545286
CDK5_HUMAN	CDK5	physical	9545286
FEN1_HUMAN	FEN1	physical	8668533
CDN1A_HUMAN	CDKN1A	physical	7780738
PCNA_SCHPO	pcn1	physical	7780738
CDN1A_HUMAN	CDKN1A	physical	9546435
RFA1_HUMAN	RPA1	physical	15831485
KIN17_HUMAN	KIN	physical	15831485
POLH_HUMAN	POLH	physical	23345618
RAD18_HUMAN	RAD18	physical	23345618
SIVA_HUMAN	SIVA1	physical	21988832
TIRAP_HUMAN	TIRAP	physical	21988832
CALU_HUMAN	CALU	physical	22863883
DCTP1_HUMAN	DCTPP1	physical	22863883
DHX15_HUMAN	DHX15	physical	22863883
GNPI1_HUMAN	GNPDA1	physical	22863883
H2AV_HUMAN	H2AFV	physical	22863883
HERC4_HUMAN	HERC4	physical	22863883
RD23A_HUMAN	RAD23A	physical	22863883
PAR10_HUMAN	PARP10	physical	24695737
DPOD3_HUMAN	POLD3	physical	24695737
XRCC6_HUMAN	XRCC6	physical	24695737
MAGD1_HUMAN	MAGED1	physical	24710624
TRI25_HUMAN	TRIM25	physical	24768535
UBP10_HUMAN	USP10	physical	24768535
DPOLN_HUMAN	POLN	physical	24768535
UBP18_HUMAN	USP18	physical	24768535
DPOD1_HUMAN	POLD1	physical	24768535
FBH1_HUMAN	FBXO18	physical	23677613
PAF15_HUMAN	KIAA0101	physical	24958773
RFC5_HUMAN	RFC5	physical	24958773
RFC2_HUMAN	RFC2	physical	24958773
RFC3_HUMAN	RFC3	physical	24958773
RFC4_HUMAN	RFC4	physical	24958773
RFC1_HUMAN	RFC1	physical	24958773
CTF18_HUMAN	CHTF18	physical	24958773
FEN1_HUMAN	FEN1	physical	24958773
DPOD1_HUMAN	POLD1	physical	24958773
SIVA_HUMAN	SIVA1	physical	24958773
MSH6_HUMAN	MSH6	physical	24958773
DNMT1_HUMAN	DNMT1	physical	24958773
ZRAB3_HUMAN	ZRANB3	physical	24958773
DNLI1_HUMAN	LIG1	physical	24958773
RFA1_HUMAN	RPA1	physical	24958773
MCM7_HUMAN	MCM7	physical	24958773
MCM4_HUMAN	MCM4	physical	24958773
DPOE1_HUMAN	POLE	physical	24958773
TDG_HUMAN	TDG	physical	24962565
RAD18_HUMAN	RAD18	physical	24958773
DTL_HUMAN	DTL	physical	25154416
PCNA_HUMAN	PCNA	physical	25416956
TM218_HUMAN	TMEM218	physical	25416956
CDN1A_HUMAN	CDKN1A	physical	23223023
UBP1_HUMAN	USP1	physical	21768287
PCNA_HUMAN	PCNA	physical	21364740
CDK2_HUMAN	CDK2	physical	26186194
PAF15_HUMAN	KIAA0101	physical	26186194
CCNE2_HUMAN	CCNE2	physical	26186194
CCNA2_HUMAN	CCNA2	physical	26186194
CDN1A_HUMAN	CDKN1A	physical	26186194
CCNE1_HUMAN	CCNE1	physical	26186194
POLH_HUMAN	POLH	physical	25766642
DPOD2_HUMAN	POLD2	physical	24939902
GDIR1_HUMAN	ARHGDIA	physical	26344197
CDC45_HUMAN	CDC45	physical	26344197
CAF1B_HUMAN	CHAF1B	physical	26344197
CTF18_HUMAN	CHTF18	physical	26344197
NACA2_HUMAN	NACA2	physical	26344197
PDIA1_HUMAN	P4HB	physical	26344197
PACN3_HUMAN	PACSIN3	physical	26344197
DPOLA_HUMAN	POLA1	physical	26344197
DPOE1_HUMAN	POLE	physical	26344197
PPIB_HUMAN	PPIB	physical	26344197
TRUA_HUMAN	PUS1	physical	26344197
RAD21_HUMAN	RAD21	physical	26344197
RFC3_HUMAN	RFC3	physical	26344197
ANK3_HUMAN	ANK3	physical	26496610
CDN1A_HUMAN	CDKN1A	physical	26496610
DNMT1_HUMAN	DNMT1	physical	26496610
FEN1_HUMAN	FEN1	physical	26496610
GOGA1_HUMAN	GOLGA1	physical	26496610
DPOD1_HUMAN	POLD1	physical	26496610
DPOD2_HUMAN	POLD2	physical	26496610
RBBP6_HUMAN	RBBP6	physical	26496610
RFC1_HUMAN	RFC1	physical	26496610
RFC2_HUMAN	RFC2	physical	26496610
RFC4_HUMAN	RFC4	physical	26496610
UTY_HUMAN	UTY	physical	26496610
PABP2_HUMAN	PABPN1	physical	26496610
EEA1_HUMAN	EEA1	physical	26496610
ARK72_HUMAN	AKR7A2	physical	26496610
FIBP_HUMAN	FIBP	physical	26496610
CAPON_HUMAN	NOS1AP	physical	26496610
PAF15_HUMAN	KIAA0101	physical	26496610
CAF1A_HUMAN	CHAF1A	physical	26496610
FA13A_HUMAN	FAM13A	physical	26496610
RBM7_HUMAN	RBM7	physical	26496610
SIVA_HUMAN	SIVA1	physical	26496610
DPOD3_HUMAN	POLD3	physical	26496610
PRDX3_HUMAN	PRDX3	physical	26496610
S27A4_HUMAN	SLC27A4	physical	26496610
B4GT7_HUMAN	B4GALT7	physical	26496610
CYFP1_HUMAN	CYFIP1	physical	26496610
SC22A_HUMAN	SEC22A	physical	26496610
UHRF1_HUMAN	UHRF1	physical	26496610
RM04_HUMAN	MRPL4	physical	26496610
URFB1_HUMAN	UHRF1BP1	physical	26496610
BRE1A_HUMAN	RNF20	physical	26496610
K1522_HUMAN	KIAA1522	physical	26496610
RT25_HUMAN	MRPS25	physical	26496610
ELMO3_HUMAN	ELMO3	physical	26496610
ATAD5_HUMAN	ATAD5	physical	26496610
OBSCN_HUMAN	OBSCN	physical	26496610
ACOT1_HUMAN	ACOT1	physical	26496610
RAD51_HUMAN	RAD51	physical	25893307
NSD2_HUMAN	WHSC1	physical	26771714
TRAIP_HUMAN	TRAIP	physical	26711499
WRIP1_HUMAN	WRNIP1	physical	26549024
HUWE1_HUMAN	HUWE1	physical	27146073
DPOLB_HUMAN	POLB	physical	25184665
CDN1A_HUMAN	CDKN1A	physical	28514442
PAF15_HUMAN	KIAA0101	physical	28514442
CCNE1_HUMAN	CCNE1	physical	28514442
CCNA2_HUMAN	CCNA2	physical	28514442
CDK2_HUMAN	CDK2	physical	28514442
CCNB1_HUMAN	CCNB1	physical	28514442
CCNE2_HUMAN	CCNE2	physical	28514442
PARI_HUMAN	PARPBP	physical	22153967
SUMO1_HUMAN	SUMO1	physical	22153967
UHRF2_HUMAN	UHRF2	physical	28951215
SENP8_HUMAN	SENP8	physical	28831681
POLH_HUMAN	POLH	physical	28831681
PRKN_HUMAN	PARK2	physical	28430587
CDN1A_HUMAN	CDKN1A	physical	11463845
DNLI1_HUMAN	LIG1	physical	28803780

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615919	Ataxia-telangiectasia-like disorder 2 (ATLD2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PCNA_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-77; LYS-80 AND LYS-248, ANDMASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Tyrosine phosphorylation controls PCNA function through proteinstability."; Wang S.C., Nakajima Y., Yu Y.L., Xia W., Chen C.T., Yang C.C.,McIntush E.W., Li L.Y., Hawke D.H., Kobayashi R., Hung M.C.; Nat. Cell Biol. 8:1359-1368(2006). Cited for: PHOSPHORYLATION AT TYR-211 BY EGFR, MUTAGENESIS OF TYR-211, ANDINTERACTION WITH EGFR.	17115032 [Abstract]
Ubiquitylation
Reference	PubMed
"Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependentpolyubiquitylation of proliferating cell nuclear antigen."; Unk I., Hajdu I., Fatyol K., Szakal B., Blastyak A., Bermudez V.,Hurwitz J., Prakash L., Prakash S., Haracska L.; Proc. Natl. Acad. Sci. U.S.A. 103:18107-18112(2006). Cited for: UBIQUITINATION AT LYS-164, AND MUTAGENESIS OF LYS-164.	17108083 [Abstract]
"Human SHPRH suppresses genomic instability through proliferating cellnuclear antigen polyubiquitination."; Motegi A., Sood R., Moinova H., Markowitz S.D., Liu P.P., Myung K.; J. Cell Biol. 175:703-708(2006). Cited for: INTERACTION WITH SHPRH, UBIQUITINATION AT LYS-164, AND MUTAGENESIS OFLYS-164.	17130289 [Abstract]

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