dbPTM

CHK2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CHK2_HUMAN
UniProt AC	O96017
Protein Name	Serine/threonine-protein kinase Chk2
Gene Name	CHEK2
Organism	Homo sapiens (Human).
Sequence Length	543
Subcellular Localization	Isoform 2: Nucleus. Isoform 10 is present throughout the cell. Isoform 4: Nucleus. Isoform 7: Nucleus. Isoform 9: Nucleus. Isoform 12: Nucleus. Nucleus, PML body. Nucleus, nucleoplasm. Recruited into PML bodies together with TP53.
Protein Description	Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest, activation of DNA repair and apoptosis in response to the presence of DNA double-strand breaks. May also negatively regulate cell cycle progression during unperturbed cell cycles. Following activation, phosphorylates numerous effectors preferentially at the consensus sequence [L-X-R-X-X-S/T]. Regulates cell cycle checkpoint arrest through phosphorylation of CDC25A, CDC25B and CDC25C, inhibiting their activity. Inhibition of CDC25 phosphatase activity leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and blocks cell cycle progression. May also phosphorylate NEK6 which is involved in G2/M cell cycle arrest. Regulates DNA repair through phosphorylation of BRCA2, enhancing the association of RAD51 with chromatin which promotes DNA repair by homologous recombination. Also stimulates the transcription of genes involved in DNA repair (including BRCA2) through the phosphorylation and activation of the transcription factor FOXM1. Regulates apoptosis through the phosphorylation of p53/TP53, MDM4 and PML. Phosphorylation of p53/TP53 at 'Ser-20' by CHEK2 may alleviate inhibition by MDM2, leading to accumulation of active p53/TP53. Phosphorylation of MDM4 may also reduce degradation of p53/TP53. Also controls the transcription of pro-apoptotic genes through phosphorylation of the transcription factor E2F1. Tumor suppressor, it may also have a DNA damage-independent function in mitotic spindle assembly by phosphorylating BRCA1. Its absence may be a cause of the chromosomal instability observed in some cancer cells. Promotes the CCAR2-SIRT1 association and is required for CCAR2-mediated SIRT1 inhibition. [PubMed: 25361978]
Protein Sequence	MSRESDVEAQQSHGSSACSQPHGSVTQSQGSSSQSQGISSSSTSTMPNSSQSSHSSSGTLSSLETVSTQELYSIPEDQEPEDQEPEEPTPAPWARLWALQDGFANLECVNDNYWFGRDKSCEYCFDEPLLKRTDKYRTYSKKHFRIFREVGPKNSYIAYIEDHSGNGTFVNTELVGKGKRRPLNNNSEIALSLSRNKVFVFFDLTVDDQSVYPKALRDEYIMSKTLGSGACGEVKLAFERKTCKKVAIKIISKRKFAIGSAREADPALNVETEIEILKKLNHPCIIKIKNFFDAEDYYIVLELMEGGELFDKVVGNKRLKEATCKLYFYQMLLAVQYLHENGIIHRDLKPENVLLSSQEEDCLIKITDFGHSKILGETSLMRTLCGTPTYLAPEVLVSVGTAGYNRAVDCWSLGVILFICLSGYPPFSEHRTQVSLKDQITSGKYNFIPEVWAEVSEKALDLVKKLLVVDPKARFTTEEALRHPWLQDEDMKRKFQDLLSEENESTALPQVLAQPSTSRKRPREGEAEGAETTKRPAVCAAVL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Ubiquitination	-----MSRESDVEAQ -----CCCHHHHHHH	46.25	29967540
12	Phosphorylation	SDVEAQQSHGSSACS HHHHHHHHHCCCCCC	20.10	17918214
15	Phosphorylation	EAQQSHGSSACSQPH HHHHHHCCCCCCCCC	14.89	17918214
19	Phosphorylation	SHGSSACSQPHGSVT HHCCCCCCCCCCCCC	46.60	16205633
24	Phosphorylation	ACSQPHGSVTQSQGS CCCCCCCCCCCCCCC	20.96	17918214
26	Phosphorylation	SQPHGSVTQSQGSSS CCCCCCCCCCCCCCC	24.97	10973490
28	Phosphorylation	PHGSVTQSQGSSSQS CCCCCCCCCCCCCCC	27.43	10973490
33	Phosphorylation	TQSQGSSSQSQGISS CCCCCCCCCCCCCCC	35.23	20160490
35	Phosphorylation	SQGSSSQSQGISSSS CCCCCCCCCCCCCCC	32.11	20160490
39	Phosphorylation	SSQSQGISSSSTSTM CCCCCCCCCCCCCCC	30.87	17918214
40	Phosphorylation	SQSQGISSSSTSTMP CCCCCCCCCCCCCCC	26.79	17918214
41	Phosphorylation	QSQGISSSSTSTMPN CCCCCCCCCCCCCCC	30.74	17918214
42	Phosphorylation	SQGISSSSTSTMPNS CCCCCCCCCCCCCCC	28.46	17918214
43	Phosphorylation	QGISSSSTSTMPNSS CCCCCCCCCCCCCCC	30.11	17918214
44	Phosphorylation	GISSSSTSTMPNSSQ CCCCCCCCCCCCCCC	25.34	17918214
45	Phosphorylation	ISSSSTSTMPNSSQS CCCCCCCCCCCCCCC	36.41	17918214
50	Phosphorylation	TSTMPNSSQSSHSSS CCCCCCCCCCCCCCC	40.50	10973490
52	Phosphorylation	TMPNSSQSSHSSSGT CCCCCCCCCCCCCCC	31.78	17918214
55	Phosphorylation	NSSQSSHSSSGTLSS CCCCCCCCCCCCCCC	28.31	17918214
58	Ubiquitination	QSSHSSSGTLSSLET CCCCCCCCCCCCEEE	32.40	29967540
62	Phosphorylation	SSSGTLSSLETVSTQ CCCCCCCCEEEECHH	33.08	16481012
65	Phosphorylation	GTLSSLETVSTQELY CCCCCEEEECHHHHC	25.67	17918214
66	Ubiquitination	TLSSLETVSTQELYS CCCCEEEECHHHHCC	4.21	29967540
67	Phosphorylation	LSSLETVSTQELYSI CCCEEEECHHHHCCC	31.62	17918214
68	Phosphorylation	SSLETVSTQELYSIP CCEEEECHHHHCCCC	23.02	21731742
73	Phosphorylation	VSTQELYSIPEDQEP ECHHHHCCCCCCCCC	44.27	16481012
119	Ubiquitination	NYWFGRDKSCEYCFD CCEECCCCCCCEECC	56.49	29967540
120	Phosphorylation	YWFGRDKSCEYCFDE CEECCCCCCCEECCC	19.23	25159151
123	Phosphorylation	GRDKSCEYCFDEPLL CCCCCCCEECCCHHH	11.62	27732954
131	Ubiquitination	CFDEPLLKRTDKYRT ECCCHHHHCCHHCCC	62.02	29967540
140	Phosphorylation	TDKYRTYSKKHFRIF CHHCCCCCHHHHEEE	34.32	18948271
153	Acetylation	IFREVGPKNSYIAYI EEHHHCCCCCEEEEE	53.23	26051181
163 (in isoform 9)	Phosphorylation	-	25.47	24719451
164	Phosphorylation	IAYIEDHSGNGTFVN EEEEEECCCCCEEEE	46.40	20126263
174	Ubiquitination	GTFVNTELVGKGKRR CEEEECEECCCCCCC	6.07	29967540
174 (in isoform 9)	Ubiquitination	-	6.07	-
192	Phosphorylation	NNSEIALSLSRNKVF CCCHHEEEECCCCEE	18.44	24719451
194	Phosphorylation	SEIALSLSRNKVFVF CHHEEEECCCCEEEE	30.36	17081983
204 (in isoform 2)	Phosphorylation	-	4.20	20049867
205	Phosphorylation	VFVFFDLTVDDQSVY EEEEEEEECCCCCCC	24.59	20126263
210	Phosphorylation	DLTVDDQSVYPKALR EEECCCCCCCCHHHH	30.52	20126263
223	Ubiquitination	LRDEYIMSKTLGSGA HHCHHHHHCCCCCCC	16.96	29967540
224	Ubiquitination	RDEYIMSKTLGSGAC HCHHHHHCCCCCCCC	30.32	29967540
225	Phosphorylation	DEYIMSKTLGSGACG CHHHHHCCCCCCCCC	29.10	25056879
235	Acetylation	SGACGEVKLAFERKT CCCCCHHHHHHCCCC	29.78	30587659
237	Ubiquitination	ACGEVKLAFERKTCK CCCHHHHHHCCCCCC	9.87	29967540
251	Ubiquitination	KKVAIKIISKRKFAI CHHHHHHHHCCCEEE	3.18	29967540
260	Phosphorylation	KRKFAIGSAREADPA CCCEEECCCCCCCCC	20.31	28355574
267	Ubiquitination	SAREADPALNVETEI CCCCCCCCCCHHHHH	16.59	29967540
267 (in isoform 9)	Ubiquitination	-	16.59	-
273	Ubiquitination	PALNVETEIEILKKL CCCCHHHHHHHHHHC	25.72	29967540
279	Ubiquitination	TEIEILKKLNHPCII HHHHHHHHCCCCEEE	51.59	29967540
287	Ubiquitination	LNHPCIIKIKNFFDA CCCCEEEEEECCCCH	27.93	29967540
303 (in isoform 9)	Phosphorylation	-	3.11	24719451
322	Ubiquitination	GNKRLKEATCKLYFY CCHHHHHHHHHHHHH	19.40	29967540
327	Phosphorylation	KEATCKLYFYQMLLA HHHHHHHHHHHHHHH	5.92	24043423
329	Phosphorylation	ATCKLYFYQMLLAVQ HHHHHHHHHHHHHHH	4.58	24043423
330	Ubiquitination	TCKLYFYQMLLAVQY HHHHHHHHHHHHHHH	13.22	29967540
337	Phosphorylation	QMLLAVQYLHENGII HHHHHHHHHHHCCCC	11.92	24043423
350 (in isoform 12)	Phosphorylation	-	45.77	29507054
356	Phosphorylation	KPENVLLSSQEEDCL CHHHEEECCCCCCCE	26.30	20873877
357	Phosphorylation	PENVLLSSQEEDCLI HHHEEECCCCCCCEE	41.39	20873877
372	Phosphorylation	KITDFGHSKILGETS EEECCCCCHHCCCHH	23.05	20713355
373	Ubiquitination	ITDFGHSKILGETSL EECCCCCHHCCCHHH	35.95	-
378	Phosphorylation	HSKILGETSLMRTLC CCHHCCCHHHHHHHH	25.92	17698850
379	Phosphorylation	SKILGETSLMRTLCG CHHCCCHHHHHHHHC	18.83	28355574
381	Sulfoxidation	ILGETSLMRTLCGTP HCCCHHHHHHHHCCC	2.85	21406390
383	Phosphorylation	GETSLMRTLCGTPTY CCHHHHHHHHCCCCC	16.66	17698850
387	Phosphorylation	LMRTLCGTPTYLAPE HHHHHHCCCCCCCCE	16.09	30278072
389	Phosphorylation	RTLCGTPTYLAPEVL HHHHCCCCCCCCEEE	30.88	28464451
390	Phosphorylation	TLCGTPTYLAPEVLV HHHCCCCCCCCEEEE	11.32	28464451
401	Phosphorylation	EVLVSVGTAGYNRAV EEEEEECCCCCCHHH	18.11	22210691
415	Ubiquitination	VDCWSLGVILFICLS HHHHHHHHHHHHHHH	4.10	29967540
416 (in isoform 9)	Ubiquitination	-	2.17	-
429	Ubiquitination	SGYPPFSEHRTQVSL HCCCCCCCCCCCCCH	37.46	29967540
430 (in isoform 9)	Phosphorylation	-	36.57	24719451
432	Phosphorylation	PPFSEHRTQVSLKDQ CCCCCCCCCCCHHHH	34.92	15213307
435	Phosphorylation	SEHRTQVSLKDQITS CCCCCCCCHHHHHHC	21.64	18538787
437	Ubiquitination	HRTQVSLKDQITSGK CCCCCCHHHHHHCCC	39.83	-
441	Phosphorylation	VSLKDQITSGKYNFI CCHHHHHHCCCCCCC	26.29	23403867
442	Phosphorylation	SLKDQITSGKYNFIP CHHHHHHCCCCCCCH	34.61	23403867
443	Ubiquitination	LKDQITSGKYNFIPE HHHHHHCCCCCCCHH	28.02	29967540
444	Ubiquitination	KDQITSGKYNFIPEV HHHHHCCCCCCCHHH	36.47	29967540
456	Phosphorylation	PEVWAEVSEKALDLV HHHHHHHHHHHHHHH	25.53	15535844
458	Ubiquitination	VWAEVSEKALDLVKK HHHHHHHHHHHHHHH	46.90	29967540
465	Ubiquitination	KALDLVKKLLVVDPK HHHHHHHHHCCCCCC	39.30	29967540
472	Ubiquitination	KLLVVDPKARFTTEE HHCCCCCCCCCCHHH	47.97	29967540
478 (in isoform 9)	Phosphorylation	-	37.91	24719451
480 (in isoform 9)	Ubiquitination	-	12.03	-
487	Ubiquitination	ALRHPWLQDEDMKRK HHHCCCCCCHHHHHH	48.45	29967540
494	Ubiquitination	QDEDMKRKFQDLLSE CCHHHHHHHHHHHHH	41.69	29967540
500	Phosphorylation	RKFQDLLSEENESTA HHHHHHHHHCCCCCC	50.60	23312004
501	Ubiquitination	KFQDLLSEENESTAL HHHHHHHHCCCCCCH	65.88	29967540
505	Phosphorylation	LLSEENESTALPQVL HHHHCCCCCCHHHHH	30.48	22210691
506	Phosphorylation	LSEENESTALPQVLA HHHCCCCCCHHHHHC	26.49	22210691
508 (in isoform 9)	Ubiquitination	-	2.86	-
515	Ubiquitination	LPQVLAQPSTSRKRP HHHHHCCCCCCCCCC	33.69	29967540
516	Phosphorylation	PQVLAQPSTSRKRPR HHHHCCCCCCCCCCC	27.25	25159151
517	Phosphorylation	QVLAQPSTSRKRPRE HHHCCCCCCCCCCCC	38.95	25159151
518	Phosphorylation	VLAQPSTSRKRPREG HHCCCCCCCCCCCCC	39.89	25850435
537	Ubiquitination	AETTKRPAVCAAVL- CCCCCCCCCEEEEC-	17.04	29967540
537 (in isoform 9)	Ubiquitination	-	17.04	-
559 (in isoform 9)	Phosphorylation	-		24719451
560 (in isoform 9)	Phosphorylation	-		27251275

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
19	S	Phosphorylation	Kinase	ATM	Q13315	PhosphoELM
19	S	Phosphorylation	Kinase	CHEK2	O96017	GPS
26	T	Phosphorylation	Kinase	ATM	Q13315	PSP
26	T	Phosphorylation	Kinase	PLK1	P53350	PhosphoELM
28	S	Phosphorylation	Kinase	ATM	Q13315	PSP
33	S	Phosphorylation	Kinase	ATM	Q13315	PSP
33	S	Phosphorylation	Kinase	CHEK2	O96017	GPS
35	S	Phosphorylation	Kinase	ATM	Q13315	PSP
35	S	Phosphorylation	Kinase	CHEK2	O96017	GPS
50	S	Phosphorylation	Kinase	ATM	Q13315	PhosphoELM
62	S	Phosphorylation	Kinase	PLK3	Q9H4B4	Uniprot
68	T	Phosphorylation	Kinase	CHEK2	O96017	GPS
68	T	Phosphorylation	Kinase	TTK	P33981	PSP
68	T	Phosphorylation	Kinase	ZAK	Q9NYL2	PSP
68	T	Phosphorylation	Kinase	PLK1	P53350	PSP
68	T	Phosphorylation	Kinase	PRKDC	P78527	GPS
68	T	Phosphorylation	Kinase	ATM	Q13315	Uniprot
68	T	Phosphorylation	Kinase	ATR	Q13535	PSP
73	S	Phosphorylation	Kinase	PLK3	Q9H4B4	Uniprot
120	S	Phosphorylation	Kinase	CHEK2	O96017	GPS
140	S	Phosphorylation	Kinase	CHEK2	O96017	GPS
164	S	Phosphorylation	Kinase	PLK1	P53350	PSP
205	T	Phosphorylation	Kinase	PLK1	P53350	PSP
210	S	Phosphorylation	Kinase	PLK1	P53350	PSP
225	T	Phosphorylation	Kinase	CHEK2	O96017	GPS
260	S	Phosphorylation	Kinase	CHEK2	O96017	GPS
379	S	Phosphorylation	Kinase	CHEK2	O96017	GPS
383	T	Phosphorylation	Kinase	CHEK2	O96017	GPS
383	T	Phosphorylation	Kinase	PRKDC	P78527	GPS
387	T	Phosphorylation	Kinase	CHEK2	O96017	GPS
387	T	Phosphorylation	Kinase	PRKDC	P78527	GPS
432	T	Phosphorylation	Kinase	CHEK2	O96017	GPS
435	S	Phosphorylation	Kinase	CHEK2	O96017	GPS
516	S	Phosphorylation	Kinase	CHEK2	O96017	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	RNF8	O76064	PMID:22266820
-	K	Ubiquitination	E3 ubiquitin ligase	RCHY1	Q96PM5	PMID:23449389
-	K	Ubiquitination	E3 ubiquitin ligase	SIAH2	O43255	PMID:26751770

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
68	T	Phosphorylation	10973490
Phosphorylation at Thr-68 induces homodimerization.
73	S	Phosphorylation	16481012
Phosphorylated at Ser-73 by PLK3 in response to DNA damage, promoting phosphorylation at Thr-68 by ATM and the G2/M transition checkpoint.
379	S	Phosphorylation	18644861
DNA damage-induced autophosphorylation at Ser-379 induces CUL1-mediated ubiquitination and regulates the pro-apoptotic function.
383	T	Phosphorylation	11390408
Autophosphorylates at Thr-383 and Thr-387 in the T-loop/activation segment upon dimerization to become fully active and phosphorylate its substrates like for instance CDC25C.
387	T	Phosphorylation	11390408
Autophosphorylates at Thr-383 and Thr-387 in the T-loop/activation segment upon dimerization to become fully active and phosphorylate its substrates like for instance CDC25C.
456	S	Phosphorylation	17715138
Phosphorylation at Ser-456 also regulates ubiquitination.

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
153	Acetylation	157 (4)	I ⇒ T	rs17879961	Lung cancer	24880342 29059683

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BRCA1_HUMAN	BRCA1	physical	10724175
MSH2_HUMAN	MSH2	physical	12447371
PLK3_HUMAN	PLK3	physical	12242661
PLK1_HUMAN	PLK1	physical	12493754
BRCA2_HUMAN	BRCA2	physical	17525332
RAD50_HUMAN	RAD50	physical	17525332
TP53B_HUMAN	TP53BP1	physical	17525332
PSF2_HUMAN	GINS2	physical	17525332
MUS81_HUMAN	MUS81	physical	11741546
BRCA1_HUMAN	BRCA1	physical	18804494
MPIP1_HUMAN	CDC25A	physical	18480045
MDM2_HUMAN	MDM2	physical	16943424
MDM4_HUMAN	MDM4	physical	16163388
FOXM1_HUMAN	FOXM1	physical	17101782
MPIP3_HUMAN	CDC25C	physical	16705183
REV3L_HUMAN	REV3L	physical	18622427
P53_HUMAN	TP53	physical	12810724
MPIP1_HUMAN	CDC25A	physical	12759351
AATF_HUMAN	AATF	physical	17157788
P53_HUMAN	TP53	physical	10673501
CHK2_HUMAN	CHEK2	physical	11901158
CHK2_HUMAN	CHEK2	physical	12024051
MPIP3_HUMAN	CDC25C	physical	12024051
2ABB_HUMAN	PPP2R2B	physical	15380617
2A5A_HUMAN	PPP2R5A	physical	15380617
2A5D_HUMAN	PPP2R5D	physical	15380617
2A5G_HUMAN	PPP2R5C	physical	15380617
2A5E_HUMAN	PPP2R5E	physical	15380617
2A5B_HUMAN	PPP2R5B	physical	15380617
2AAA_HUMAN	PPP2R1A	physical	15380617
PP2AA_HUMAN	PPP2CA	physical	15380617
TIF1B_HUMAN	TRIM28	physical	22496453
PSME3_HUMAN	PSME3	physical	19556897
LATS2_HUMAN	LATS2	physical	21118956
MDM2_HUMAN	MDM2	physical	19176998
KAT2B_HUMAN	KAT2B	physical	19176998
PML_HUMAN	PML	physical	12402044
MPIP3_HUMAN	CDC25C	physical	12402044
BRCA2_HUMAN	BRCA2	physical	14623252
BRCA1_HUMAN	BRCA1	physical	12438214
MDM2_HUMAN	MDM2	physical	15862297
P53_HUMAN	TP53	physical	15862297
UBR5_HUMAN	UBR5	physical	17074762
P53_HUMAN	TP53	physical	10710310
RB_HUMAN	RB1	physical	17380128
BRCA1_HUMAN	BRCA1	physical	17380128
IMA1_HUMAN	KPNA2	physical	12909615
CHK2_HUMAN	CHEK2	physical	12909615
MPIP3_HUMAN	CDC25C	physical	12909615
A4_HUMAN	APP	physical	21832049
STRAP_HUMAN	STRAP	physical	18833288
P53_HUMAN	TP53	physical	18833288
CHK2_HUMAN	CHEK2	physical	12676583
MPIP1_HUMAN	CDC25A	physical	12676583
CUL4A_HUMAN	CUL4A	physical	23109433
CUL1_HUMAN	CUL1	physical	23109433
MPIP3_HUMAN	CDC25C	physical	11438675
CHK2_HUMAN	CHEK2	physical	11438675
MPIP3_HUMAN	CDC25C	physical	10744722
ELAV1_HUMAN	ELAVL1	physical	17317627
MPIP1_HUMAN	CDC25A	physical	11298456
ZN363_HUMAN	RCHY1	physical	23449389
VHL_HUMAN	VHL	physical	22071692
CHK2_HUMAN	CHEK2	physical	16794575
NR4A1_HUMAN	NR4A1	physical	21988832
RPAB5_HUMAN	POLR2L	physical	21988832
SIR1_HUMAN	SIRT1	physical	25361978
CCAR2_HUMAN	CCAR2	physical	25361978
CHK2_HUMAN	CHEK2	physical	25361978
MPIP3_HUMAN	CDC25C	physical	25361978
PSME3_HUMAN	PSME3	physical	25361978
BEX1_HUMAN	BEX1	physical	25640309
CCL5_HUMAN	CCL5	physical	25640309
CAD13_HUMAN	CDH13	physical	25640309
CP17A_HUMAN	CYP17A1	physical	25640309
DIRA3_HUMAN	DIRAS3	physical	25640309
FA84B_HUMAN	FAM84B	physical	25640309
HXC6_HUMAN	HOXC6	physical	25640309
IL24_HUMAN	IL24	physical	25640309
ITIH5_HUMAN	ITIH5	physical	25640309
KLK7_HUMAN	KLK7	physical	25640309
KLK9_HUMAN	KLK9	physical	25640309
LYPD3_HUMAN	LYPD3	physical	25640309
PRD14_HUMAN	PRDM14	physical	25640309
HOP2_HUMAN	PSMC3IP	physical	25640309
RHBT2_HUMAN	RHOBTB2	physical	25640309
BRE1A_HUMAN	RNF20	physical	25640309
ST14_HUMAN	ST14	physical	25640309
NSD3_HUMAN	WHSC1L1	physical	25640309
BAALC_HUMAN	BAALC	physical	25640309
ENOA_HUMAN	ENO1	physical	25640309
GNAS3_HUMAN	GNAS	physical	25640309
GNAS2_HUMAN	GNAS	physical	25640309
ALEX_HUMAN	GNAS	physical	25640309
GNAS1_HUMAN	GNAS	physical	25640309
HMGN1_HUMAN	HMGN1	physical	25640309
ADT3_HUMAN	SLC25A6	physical	25640309
ANM2_HUMAN	PRMT2	physical	25640309
STMN1_HUMAN	STMN1	physical	25640309
TLR3_HUMAN	TLR3	physical	25640309
SIAH2_HUMAN	SIAH2	physical	26751770
ERBB2_HUMAN	ERBB2	genetic	28319113
KMT2D_HUMAN	KMT2D	genetic	28319113
WEE1_HUMAN	WEE1	genetic	27453043
CHK1_HUMAN	CHEK1	genetic	27453043
CDC6_HUMAN	CDC6	genetic	27453043
CDC73_HUMAN	CDC73	genetic	27453043
BLM_HUMAN	BLM	genetic	27453043
RFC1_HUMAN	RFC1	genetic	27453043
RAD17_HUMAN	RAD17	genetic	27453043
FZR1_HUMAN	FZR1	genetic	27453043
ATAD5_HUMAN	ATAD5	genetic	27453043
L2GL1_HUMAN	LLGL1	genetic	27453043
CC14A_HUMAN	CDC14A	genetic	27453043
RS10_HUMAN	RPS10	genetic	27453043
WRN_HUMAN	WRN	genetic	27453043
ATR_HUMAN	ATR	genetic	27453043
DAAM1_HUMAN	DAAM1	genetic	27453043
TITIN_HUMAN	TTN	genetic	27453043
BRD4_HUMAN	BRD4	genetic	27453043
MPIP3_HUMAN	CDC25C	physical	11053450
PPM1D_HUMAN	PPM1D	physical	16311512
MPIP3_HUMAN	CDC25C	physical	16311512

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
609265	Li-Fraumeni syndrome 2 (LFS2)
176807	Prostate cancer (PC)
259500	Osteogenic sarcoma (OSRC)
114480	Breast cancer (BC)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CHK2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Regulation of Chk2 ubiquitination and signaling throughautophosphorylation of serine 379."; Lovly C.M., Yan L., Ryan C.E., Takada S., Piwnica-Worms H.; Mol. Cell. Biol. 28:5874-5885(2008). Cited for: FUNCTION IN APOPTOSIS, AUTOPHOSPHORYLATION AT SER-379, MUTAGENESIS OFSER-379, UBIQUITINATION, AND INTERACTION WITH CUL1.	18644861 [Abstract]
"Stability of checkpoint kinase 2 is regulated via phosphorylation atserine 456."; Kass E.M., Ahn J., Tanaka T., Freed-Pastor W.A., Keezer S., Prives C.; J. Biol. Chem. 282:30311-30321(2007). Cited for: FUNCTION IN APOPTOSIS, PHOSPHORYLATION AT SER-456, UBIQUITINATION, ANDMUTAGENESIS OF SER-456.	17715138 [Abstract]
"Priming phosphorylation of Chk2 by polo-like kinase 3 (Plk3) mediatesits full activation by ATM and a downstream checkpoint in response toDNA damage."; Bahassi el M., Myer D.L., McKenney R.J., Hennigan R.F.,Stambrook P.J.; Mutat. Res. 596:166-176(2006). Cited for: PHOSPHORYLATION AT SER-62; THR-68 AND SER-73, AND MUTAGENESIS OFSER-73.	16481012 [Abstract]
"Regulation of the antioncogenic Chk2 kinase by the oncogenic Wip1phosphatase."; Fujimoto H., Onishi N., Kato N., Takekawa M., Xu X.Z., Kosugi A.,Kondo T., Imamura M., Oishi I., Yoda A., Minami Y.; Cell Death Differ. 13:1170-1180(2006). Cited for: PHOSPHORYLATION AT THR-68, AND DEPHOSPHORYLATION AT THR-68 BY PPM1D.	16311512 [Abstract]
"The stress kinase MRK contributes to regulation of DNA damagecheckpoints through a p38gamma-independent pathway."; Tosti E., Waldbaum L., Warshaw G., Gross E.A., Ruggieri R.; J. Biol. Chem. 279:47652-47660(2004). Cited for: ENZYME REGULATION, PHOSPHORYLATION AT THR-68 BY MLTK, AND MUTAGENESISOF THR-68 AND ASP-368.	15342622 [Abstract]
"The hCds1 (Chk2)-FHA domain is essential for a chain ofphosphorylation events on hCds1 that is induced by ionizingradiation."; Lee C.H., Chung J.H.; J. Biol. Chem. 276:30537-30541(2001). Cited for: AUTOPHOSPHORYLATION AT THR-383 AND THR-387, AND MUTAGENESIS OF THR-383AND THR-387.	11390408 [Abstract]

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