dbPTM

CHK1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CHK1_HUMAN
UniProt AC	O14757
Protein Name	Serine/threonine-protein kinase Chk1
Gene Name	CHEK1
Organism	Homo sapiens (Human).
Sequence Length	476
Subcellular Localization	Nucleus. Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nuclear export is mediated at least in part by XPO1/CRM1. Also localizes to the centrosome specifically during interphase, where it may protect centrosomal CDC2 k
Protein Description	Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA. May also negatively regulate cell cycle progression during unperturbed cell cycles. This regulation is achieved by a number of mechanisms that together help to preserve the integrity of the genome. Recognizes the substrate consensus sequence [R-X-X-S/T]. Binds to and phosphorylates CDC25A, CDC25B and CDC25C. Phosphorylation of CDC25A at 'Ser-178' and 'Thr-507' and phosphorylation of CDC25C at 'Ser-216' creates binding sites for 14-3-3 proteins which inhibit CDC25A and CDC25C. Phosphorylation of CDC25A at 'Ser-76', 'Ser-124', 'Ser-178', 'Ser-279' and 'Ser-293' promotes proteolysis of CDC25A. Phosphorylation of CDC25A at 'Ser-76' primes the protein for subsequent phosphorylation at 'Ser-79', 'Ser-82' and 'Ser-88' by NEK11, which is required for polyubiquitination and degradation of CDCD25A. Inhibition of CDC25 leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and blocks cell cycle progression. Also phosphorylates NEK6. Binds to and phosphorylates RAD51 at 'Thr-309', which promotes the release of RAD51 from BRCA2 and enhances the association of RAD51 with chromatin, thereby promoting DNA repair by homologous recombination. Phosphorylates multiple sites within the C-terminus of TP53, which promotes activation of TP53 by acetylation and promotes cell cycle arrest and suppression of cellular proliferation. Also promotes repair of DNA cross-links through phosphorylation of FANCE. Binds to and phosphorylates TLK1 at 'Ser-743', which prevents the TLK1-dependent phosphorylation of the chromatin assembly factor ASF1A. This may enhance chromatin assembly both in the presence or absence of DNA damage. May also play a role in replication fork maintenance through regulation of PCNA. May regulate the transcription of genes that regulate cell-cycle progression through the phosphorylation of histones. Phosphorylates histone H3.1 (to form H3T11ph), which leads to epigenetic inhibition of a subset of genes. May also phosphorylate RB1 to promote its interaction with the E2F family of transcription factors and subsequent cell cycle arrest.; Isoform 2: Endogenous repressor of isoform 1, interacts with, and antagonizes CHK1 to promote the S to G2/M phase transition..
Protein Sequence	MAVPFVEDWDLVQTLGEGAYGEVQLAVNRVTEEAVAVKIVDMKRAVDCPENIKKEICINKMLNHENVVKFYGHRREGNIQYLFLEYCSGGELFDRIEPDIGMPEPDAQRFFHQLMAGVVYLHGIGITHRDIKPENLLLDERDNLKISDFGLATVFRYNNRERLLNKMCGTLPYVAPELLKRREFHAEPVDVWSCGIVLTAMLAGELPWDQPSDSCQEYSDWKEKKTYLNPWKKIDSAPLALLHKILVENPSARITIPDIKKDRWYNKPLKKGAKRPRVTSGGVSESPSGFSKHIQSNLDFSPVNSASSEENVKYSSSQPEPRTGLSLWDTSPSYIDKLVQGISFSQPTCPDHMLLNSQLLGTPGSSQNPWQRLVKRMTRFFTKLDADKSYQCLKETCEKLGYQWKKSCMNQVTISTTDRRNNKLIFKVNLLEMDDKILVDFRLSKGDGLEFKRHFLKIKGKLIDIVSSQKIWLPAT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
43	Ubiquitination	AVKIVDMKRAVDCPE EEEEECCCHHCCCCH	32.51	-
53	Acetylation	VDCPENIKKEICINK CCCCHHHCHHHHHHH	56.80	23749302
53	Ubiquitination	VDCPENIKKEICINK CCCCHHHCHHHHHHH	56.80	-
54	Ubiquitination	DCPENIKKEICINKM CCCHHHCHHHHHHHH	48.81	-
54	Acetylation	DCPENIKKEICINKM CCCHHHCHHHHHHHH	48.81	23749302
60	Ubiquitination	KKEICINKMLNHENV CHHHHHHHHCCCCCC	25.50	-
132	Ubiquitination	GITHRDIKPENLLLD CCCCCCCCHHHCCCC	51.04	-
145	Ubiquitination	LDERDNLKISDFGLA CCCCCCCCCCCCCCH	46.55	21906983
153	Phosphorylation	ISDFGLATVFRYNNR CCCCCCHHEEECCCH	25.81	27050516
166	Ubiquitination	NRERLLNKMCGTLPY CHHHHHHHHHCCCCC	35.22	-
166	Acetylation	NRERLLNKMCGTLPY CHHHHHHHHHCCCCC	35.22	25953088
180	Ubiquitination	YVAPELLKRREFHAE CCCHHHHHCCCCCCC	63.13	-
225	Ubiquitination	YSDWKEKKTYLNPWK CCHHHHHHHCCCCCH	43.42	-
233	Ubiquitination	TYLNPWKKIDSAPLA HCCCCCHHCCCHHHH	48.12	-
244	Ubiquitination	APLALLHKILVENPS HHHHHHHHHHHHCCC	37.39	-
260	Ubiquitination	RITIPDIKKDRWYNK CCCCCCCCCCCCCCC	56.87	-
261	Ubiquitination	ITIPDIKKDRWYNKP CCCCCCCCCCCCCCC	53.51	-
267	Ubiquitination	KKDRWYNKPLKKGAK CCCCCCCCCCCCCCC	35.71	-
279	Phosphorylation	GAKRPRVTSGGVSES CCCCCCCCCCCCCCC	23.96	30266825
280	Phosphorylation	AKRPRVTSGGVSESP CCCCCCCCCCCCCCC	30.60	29255136
284	Phosphorylation	RVTSGGVSESPSGFS CCCCCCCCCCCCCHH	35.31	30266825
286	Phosphorylation	TSGGVSESPSGFSKH CCCCCCCCCCCHHHH	19.50	30266825
288	Phosphorylation	GGVSESPSGFSKHIQ CCCCCCCCCHHHHHH	62.85	21712546
291	Phosphorylation	SESPSGFSKHIQSNL CCCCCCHHHHHHHCC	27.18	23403867
292	Ubiquitination	ESPSGFSKHIQSNLD CCCCCHHHHHHHCCC	42.33	21906983
296	Phosphorylation	GFSKHIQSNLDFSPV CHHHHHHHCCCCCCC	38.46	23401153
301	Phosphorylation	IQSNLDFSPVNSASS HHHCCCCCCCCCCCC	27.83	25159151
305	Phosphorylation	LDFSPVNSASSEENV CCCCCCCCCCCHHCC	29.75	22322096
307	Phosphorylation	FSPVNSASSEENVKY CCCCCCCCCHHCCCC	37.80	25159151
308	Phosphorylation	SPVNSASSEENVKYS CCCCCCCCHHCCCCC	48.96	17525332
313	Ubiquitination	ASSEENVKYSSSQPE CCCHHCCCCCCCCCC	51.50	21906983
314	Phosphorylation	SSEENVKYSSSQPEP CCHHCCCCCCCCCCC	14.98	26074081
315	Phosphorylation	SEENVKYSSSQPEPR CHHCCCCCCCCCCCC	20.14	22322096
316	Phosphorylation	EENVKYSSSQPEPRT HHCCCCCCCCCCCCC	29.87	22322096
317	Phosphorylation	ENVKYSSSQPEPRTG HCCCCCCCCCCCCCC	43.76	22322096
323	Phosphorylation	SSQPEPRTGLSLWDT CCCCCCCCCCCCCCC	53.87	29396449
326	Phosphorylation	PEPRTGLSLWDTSPS CCCCCCCCCCCCCHH	28.85	29396449
330	Phosphorylation	TGLSLWDTSPSYIDK CCCCCCCCCHHHHHH	30.84	25159151
331	Phosphorylation	GLSLWDTSPSYIDKL CCCCCCCCHHHHHHH	14.91	25159151
333	Phosphorylation	SLWDTSPSYIDKLVQ CCCCCCHHHHHHHHH	34.19	25159151
334	Phosphorylation	LWDTSPSYIDKLVQG CCCCCHHHHHHHHHC	19.27	29396449
343	Phosphorylation	DKLVQGISFSQPTCP HHHHHCCCCCCCCCC	26.18	26074081
345	Phosphorylation	LVQGISFSQPTCPDH HHHCCCCCCCCCCCH	28.58	21731742
348	Phosphorylation	GISFSQPTCPDHMLL CCCCCCCCCCCHHCC	29.09	26074081
357	Phosphorylation	PDHMLLNSQLLGTPG CCHHCCCCHHCCCCC	23.36	27251275
362	Phosphorylation	LNSQLLGTPGSSQNP CCCHHCCCCCCCCCH	25.17	-
365	Phosphorylation	QLLGTPGSSQNPWQR HHCCCCCCCCCHHHH	29.92	27282143
366	Phosphorylation	LLGTPGSSQNPWQRL HCCCCCCCCCHHHHH	39.63	-
378	Phosphorylation	QRLVKRMTRFFTKLD HHHHHHHHHHHHHCC	28.49	-
382	Phosphorylation	KRMTRFFTKLDADKS HHHHHHHHHCCCCHH	28.17	20873877
383	Ubiquitination	RMTRFFTKLDADKSY HHHHHHHHCCCCHHH	38.93	21906983
388	Ubiquitination	FTKLDADKSYQCLKE HHHCCCCHHHHHHHH	53.43	-
389	Phosphorylation	TKLDADKSYQCLKET HHCCCCHHHHHHHHH	22.45	28152594
390	Phosphorylation	KLDADKSYQCLKETC HCCCCHHHHHHHHHH	14.69	28152594
399	Ubiquitination	CLKETCEKLGYQWKK HHHHHHHHHCCHHHH	49.73	21890473
399	Ubiquitination	CLKETCEKLGYQWKK HHHHHHHHHCCHHHH	49.73	21890473
399	Ubiquitination	CLKETCEKLGYQWKK HHHHHHHHHCCHHHH	49.73	21890473
399	Ubiquitination	CLKETCEKLGYQWKK HHHHHHHHHCCHHHH	49.73	21890473
402	Phosphorylation	ETCEKLGYQWKKSCM HHHHHHCCHHHHHHH	22.95	29978859
405	Ubiquitination	EKLGYQWKKSCMNQV HHHCCHHHHHHHCEE	21.20	-
405	Acetylation	EKLGYQWKKSCMNQV HHHCCHHHHHHHCEE	21.20	25953088
406	Ubiquitination	KLGYQWKKSCMNQVT HHCCHHHHHHHCEEE	46.02	-
407	Phosphorylation	LGYQWKKSCMNQVTI HCCHHHHHHHCEEEE	18.18	29978859
409	Sulfoxidation	YQWKKSCMNQVTIST CHHHHHHHCEEEEEC	5.19	21406390
413	Phosphorylation	KSCMNQVTISTTDRR HHHHCEEEEECCCCC	10.23	29978859
415	Phosphorylation	CMNQVTISTTDRRNN HHCEEEEECCCCCCC	18.85	29978859
416	Phosphorylation	MNQVTISTTDRRNNK HCEEEEECCCCCCCE	28.94	29978859
417	O-linked_Glycosylation	NQVTISTTDRRNNKL CEEEEECCCCCCCEE	22.25	30379171
417	Phosphorylation	NQVTISTTDRRNNKL CEEEEECCCCCCCEE	22.25	29978859
423	Ubiquitination	TTDRRNNKLIFKVNL CCCCCCCEEEEEEEE	46.65	-
436	Ubiquitination	NLLEMDDKILVDFRL EEEECCCEEEEEEEE	33.40	17370265
445	Ubiquitination	LVDFRLSKGDGLEFK EEEEEECCCCCCHHH	66.66	-
452	Acetylation	KGDGLEFKRHFLKIK CCCCCHHHHHHHEEC	35.27	19824847
452	Ubiquitination	KGDGLEFKRHFLKIK CCCCCHHHHHHHEEC	35.27	-
461	Ubiquitination	HFLKIKGKLIDIVSS HHHEECCEEEEEECC	36.95	-
461	Acetylation	HFLKIKGKLIDIVSS HHHEECCEEEEEECC	36.95	25953088
467	Phosphorylation	GKLIDIVSSQKIWLP CEEEEEECCCCCEEE	27.64	17001009
468	Phosphorylation	KLIDIVSSQKIWLPA EEEEEECCCCCEEEC	25.30	22167270

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
280	S	Phosphorylation	Kinase	PKB_GROUP	-	PhosphoELM
280	S	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
280	S	Phosphorylation	Kinase	RPS6KA1	Q15418	GPS
280	S	Phosphorylation	Kinase	AKT1	P31749	PSP
286	S	Phosphorylation	Kinase	CDK1	P06493	PSP
286	S	Phosphorylation	Kinase	CDK2	P24941	PSP
291	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
296	S	Phosphorylation	Kinase	ATR	Q13535	PSP
296	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
301	S	Phosphorylation	Kinase	CDK2	P24941	PSP
301	S	Phosphorylation	Kinase	CDK1	P06493	PSP
316	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
317	S	Phosphorylation	Kinase	ATR	Q13535	Uniprot
317	S	Phosphorylation	Kinase	ATM	Q13315	Uniprot
345	S	Phosphorylation	Kinase	ATR	Q13535	Uniprot
345	S	Phosphorylation	Kinase	MAP3K8	P41279	GPS
345	S	Phosphorylation	Kinase	ATM	Q13315	Uniprot
378	T	Phosphorylation	Kinase	CHK1	O14757	PSP
382	T	Phosphorylation	Kinase	CHK1	O14757	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	DTL	Q9NZJ0	PMID:23533280
-	K	Ubiquitination	E3 ubiquitin ligase	FBXO6	Q9NRD1	PMID:19716789

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
280	S	Phosphorylation	23186163
Phosphorylation at Ser-280 by AKT1/PKB, may promote mono and/or diubiquitination.
280	S	ubiquitylation	23186163
Phosphorylation at Ser-280 by AKT1/PKB, may promote mono and/or diubiquitination.
317	S	Phosphorylation	11390642
ATM and ATR can both phosphorylate Ser-317 and Ser-345 and this results in enhanced kinase activity.
345	S	Phosphorylation	10859164
ATM and ATR can both phosphorylate Ser-317 and Ser-345 and this results in enhanced kinase activity.
345	S	Phosphorylation	10859164
Conversely, dephosphorylation at Ser-345 by PPM1D may contribute to exit from checkpoint mediated cell cycle arrest.
345	S	Phosphorylation	10859164
Phosphorylation at Ser-345 also increases binding to 14-3-3 proteins and promotes nuclear retention.
345	S	Phosphorylation	10859164
Phosphorylation at Ser-345 induces a change in the conformation of the protein, activates the kinase activity and is a prerequisite for interaction with FBXO6 and subsequent ubiquitination at Lys-436.
345	S	Phosphorylation	10859164
The activated form (phosphorylated on Ser-345) is polyubiquitinated at Lys-436 by some SCF-type E3 ubiquitin ligase complex containing FBXO6 promoting its degradation.
345	S	ubiquitylation	10859164
Phosphorylation at Ser-345 induces a change in the conformation of the protein, activates the kinase activity and is a prerequisite for interaction with FBXO6 and subsequent ubiquitination at Lys-436.
345	S	ubiquitylation	10859164
The activated form (phosphorylated on Ser-345) is polyubiquitinated at Lys-436 by some SCF-type E3 ubiquitin ligase complex containing FBXO6 promoting its degradation.
436	K	Phosphorylation	19716789
Phosphorylation at Ser-345 induces a change in the conformation of the protein, activates the kinase activity and is a prerequisite for interaction with FBXO6 and subsequent ubiquitination at Lys-436.
436	K	Phosphorylation	19716789
The activated form (phosphorylated on Ser-345) is polyubiquitinated at Lys-436 by some SCF-type E3 ubiquitin ligase complex containing FBXO6 promoting its degradation.
436	K	ubiquitylation	19716789
Phosphorylation at Ser-345 induces a change in the conformation of the protein, activates the kinase activity and is a prerequisite for interaction with FBXO6 and subsequent ubiquitination at Lys-436.
436	K	ubiquitylation	19716789
The activated form (phosphorylated on Ser-345) is polyubiquitinated at Lys-436 by some SCF-type E3 ubiquitin ligase complex containing FBXO6 promoting its degradation.

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 CHK1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MPIP1_HUMAN	CDC25A	physical	12963847
CSK21_HUMAN	CSNK2A1	physical	15225637
1433S_HUMAN	SFN	physical	11896572
CDN1A_HUMAN	CDKN1A	physical	11896572
P53_HUMAN	TP53	physical	11896572
BLM_HUMAN	BLM	physical	15364958
XIAP_HUMAN	XIAP	physical	14759516
PRKDC_HUMAN	PRKDC	physical	12756247
CLSPN_HUMAN	CLSPN	physical	12766152
P53_HUMAN	TP53	physical	12756247
XRCC6_HUMAN	XRCC6	physical	12756247
XRCC5_HUMAN	XRCC5	physical	12756247
MPIP1_HUMAN	CDC25A	physical	9278511
MPIP2_HUMAN	CDC25B	physical	9278511
MPIP3_HUMAN	CDC25C	physical	9278511
MPIP1_HUMAN	CDC25A	physical	12399544
MPIP1_HUMAN	CDC25A	physical	18480045
SCC1_YEAST	MCD1	physical	18614046
MSH6_HUMAN	MSH6	physical	20029092
MDM4_HUMAN	MDM4	physical	16511572
DPOLA_HUMAN	POLA1	physical	19177015
MDM4_HUMAN	MDM4	physical	16163388
MPIP3_HUMAN	CDC25C	physical	17035231
CLSPN_HUMAN	CLSPN	physical	16963448
MCPH1_HUMAN	MCPH1	physical	16783362
MPIP3_HUMAN	CDC25C	physical	16705183
XPO1_HUMAN	XPO1	physical	12676962
MPIP3_HUMAN	CDC25C	physical	15705874
MPIP1_HUMAN	CDC25A	physical	12759351
DNMT1_HUMAN	DNMT1	physical	17991895
DDB1_HUMAN	DDB1	physical	19276361
CUL4A_HUMAN	CUL4A	physical	19276361
FANCE_HUMAN	FANCE	physical	17296736
MEN1_HUMAN	MEN1	physical	20969866
P53_HUMAN	TP53	physical	10673501
LATS2_HUMAN	LATS2	physical	21118956
MEPE_HUMAN	MEPE	physical	19808933
MPIP3_HUMAN	CDC25C	physical	11836499
BRCA1_HUMAN	BRCA1	physical	11836499
MPIP3_HUMAN	CDC25C	physical	11016625
FEM1B_HUMAN	FEM1B	physical	19330022
MPIP3_HUMAN	CDC25C	physical	19330022
RB_HUMAN	RB1	physical	17380128
BRCA1_HUMAN	BRCA1	physical	17380128
TLK1_HUMAN	TLK1	physical	12955071
MPIP3_HUMAN	CDC25C	physical	11390642
NEK2_HUMAN	NEK2	physical	15311285
MPIP3_HUMAN	CDC25C	physical	12660173
A4_HUMAN	APP	physical	21832049
MED15_HUMAN	MED15	physical	22939629
TF65_HUMAN	RELA	physical	15775976
MPIP3_HUMAN	CDC25C	physical	10681541
MPIP1_HUMAN	CDC25A	physical	12676583
CUL4A_HUMAN	CUL4A	physical	23109433
CUL1_HUMAN	CUL1	physical	23109433
DTL_HUMAN	DTL	physical	23109433
DDB1_HUMAN	DDB1	physical	23109433
CLSPN_HUMAN	CLSPN	physical	23109433
CUL1_HUMAN	CUL1	physical	16137618
CUL4A_HUMAN	CUL4A	physical	16137618
MPIP3_HUMAN	CDC25C	physical	16330544
HS90A_HUMAN	HSP90AA1	physical	16330544
RAD51_HUMAN	RAD51	physical	15665856
BTG3_HUMAN	BTG3	physical	23533280
CLSPN_HUMAN	CLSPN	physical	16123041
PIGM_HUMAN	PIGM	physical	21988832
DDB1_HUMAN	DDB1	physical	25024738
SETMR_HUMAN	SETMAR	physical	25024738
LATS2_HUMAN	LATS2	physical	23886938
FUS_HUMAN	FUS	physical	25852190
RD23A_HUMAN	RAD23A	physical	26296656
UBP7_HUMAN	USP7	physical	26296656
FACD2_HUMAN	FANCD2	physical	19861535
UBE2T_HUMAN	UBE2T	physical	28162934
IGF1R_HUMAN	IGF1R	genetic	28319113
VEGFA_HUMAN	VEGFA	genetic	28319113
PTEN_HUMAN	PTEN	genetic	28319113
MTOR_HUMAN	MTOR	genetic	28319113
SMO_HUMAN	SMO	genetic	28319113
PARP1_HUMAN	PARP1	genetic	28319113
PRKDC_HUMAN	PRKDC	genetic	28319113
TYSY_HUMAN	TYMS	genetic	28319113
PK3CA_HUMAN	PIK3CA	genetic	28319113
SMCA4_HUMAN	SMARCA4	genetic	28319113
VHL_HUMAN	VHL	genetic	28319113
MP2K1_HUMAN	MAP2K1	genetic	28319113
SRC_HUMAN	SRC	genetic	28319113
MET_HUMAN	MET	genetic	28319113
KCTD3_HUMAN	KCTD3	physical	27173435
KI13B_HUMAN	KIF13B	physical	27173435
ZBT21_HUMAN	ZBTB21	physical	27173435
GGYF1_HUMAN	GIGYF1	physical	27173435
LRFN1_HUMAN	LRFN1	physical	27173435
DEN1A_HUMAN	DENND1A	physical	27173435
SRGP2_HUMAN	SRGAP2	physical	27173435
CBY1_HUMAN	CBY1	physical	27173435
WEE1_HUMAN	WEE1	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
MTOR_HUMAN	MTOR	genetic	27453043
SMRC1_HUMAN	SMARCC1	genetic	27453043
TUSC3_HUMAN	TUSC3	genetic	27453043
TCEA1_HUMAN	TCEA1	genetic	27453043
FHIT_HUMAN	FHIT	genetic	27453043
UBP11_HUMAN	USP11	genetic	27453043
B2CL1_HUMAN	BCL2L1	physical	22617334

Drug and Disease Associations

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

Regulatory Network of CHK1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-280 AND SER-301, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-279; SER-280; SER-296AND SER-307, AND MASS SPECTROMETRY.	19369195 [Abstract]
"The F box protein Fbx6 regulates Chk1 stability and cellularsensitivity to replication stress."; Zhang Y.-W., Brognard J., Coughlin C., You Z., Dolled-Filhart M.,Aslanian A., Manning G., Abraham R.T., Hunter T.; Mol. Cell 35:442-453(2009). Cited for: PHOSPHORYLATION AT SER-345, UBIQUITINATION AT LYS-436, INTERACTIONWITH FBXO6, AND MUTAGENESIS OF SER-345; ARG-372; ARG-376; ARG-379 ANDLYS-436.	19716789 [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-279; SER-280; SER-284AND SER-286, AND MASS 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 SER-286; SER-296 ANDSER-301, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286; SER-301; SER-308;SER-317; SER-331 AND SER-468, AND MASS SPECTROMETRY.	18691976 [Abstract]
"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-308 AND SER-317, ANDMASS SPECTROMETRY.	17525332 [Abstract]
"DNA damage-induced mitotic catastrophe is mediated by the Chk1-dependent mitotic exit DNA damage checkpoint."; Huang X., Tran T., Zhang L., Hatcher R., Zhang P.; Proc. Natl. Acad. Sci. U.S.A. 102:1065-1070(2005). Cited for: FUNCTION IN MITOTIC EXIT, AND PHOSPHORYLATION AT SER-345.	15650047 [Abstract]
"PPM1D dephosphorylates Chk1 and p53 and abrogates cell cyclecheckpoints."; Lu X., Nannenga B., Donehower L.A.; Genes Dev. 19:1162-1174(2005). Cited for: INTERACTION WITH PPM1D, PHOSPHORYLATION AT SER-317 AND SER-345, ANDDEPHOSPHORYLATION BY PPM1D.	15870257 [Abstract]
"DNA-dependent phosphorylation of Chk1 and claspin in a human cell-free system."; Clarke C.A.L., Clarke P.R.; Biochem. J. 388:705-712(2005). Cited for: INTERACTION WITH CLSPN, AND PHOSPHORYLATION AT SER-296; SER-317 ANDSER-345.	15707391 [Abstract]
"Differential mode of regulation of the checkpoint kinases CHK1 andCHK2 by their regulatory domains."; Ng C.-P., Lee H.C., Ho C.W., Arooz T., Siu W.Y., Lau A., Poon R.Y.C.; J. Biol. Chem. 279:8808-8819(2004). Cited for: DOMAIN, MITOTIC PHOSPHORYLATION, PHOSPHORYLATION AT SER-345, ANDMUTAGENESIS OF LYS-38.	14681223 [Abstract]
"The DNA crosslink-induced S-phase checkpoint depends on ATR-CHK1 andATR-NBS1-FANCD2 pathways."; Pichierri P., Rosselli F.; EMBO J. 23:1178-1187(2004). Cited for: FUNCTION, AND PHOSPHORYLATION AT SER-345.	14988723 [Abstract]
"MSH2 and ATR form a signaling module and regulate two branches of thedamage response to DNA methylation."; Wang Y., Qin J.; Proc. Natl. Acad. Sci. U.S.A. 100:15387-15392(2003). Cited for: PHOSPHORYLATION AT SER-317.	14657349 [Abstract]
"Regulation of Chk1 includes chromatin association and 14-3-3 bindingfollowing phosphorylation on ser-345."; Jiang K., Pereira E., Maxfield M., Russell B., Goudelock D.M.,Sanchez Y.; J. Biol. Chem. 278:25207-25217(2003). Cited for: INTERACTION WITH YWHAZ AND XPO1, SUBCELLULAR LOCATION, ASSOCIATIONWITH CHROMATIN, PHOSPHORYLATION AT SER-317 AND SER-345, ANDMUTAGENESIS OF SER-317; PHE-344; SER-345 AND MET-353.	12676962 [Abstract]
"Chk1 mediates S and G2 arrests through Cdc25A degradation in responseto DNA-damaging agents."; Xiao Z., Chen Z., Gunasekera A.H., Sowin T.J., Rosenberg S.H.,Fesik S., Zhang H.; J. Biol. Chem. 278:21767-21773(2003). Cited for: FUNCTION IN CDC25A TURNOVER, AND PHOSPHORYLATION AT SER-345.	12676925 [Abstract]
"Ataxia-telangiectasia-mutated (ATM) and NBS1-dependentphosphorylation of Chk1 on ser-317 in response to ionizingradiation."; Gatei M., Sloper K., Soerensen C., Syljuaesen R., Falck J., Hobson K.,Savage K., Lukas J., Zhou B.-B., Bartek J., Khanna K.K.; J. Biol. Chem. 278:14806-14811(2003). Cited for: PHOSPHORYLATION AT SER-317, AND MUTAGENESIS OF ASP-130; SER-317 ANDSER-345.	12588868 [Abstract]
"Human tousled like kinases are targeted by an ATM- and Chk1-dependentDNA damage checkpoint."; Groth A., Lukas J., Nigg E.A., Sillje H.H.W., Wernstedt C., Bartek J.,Hansen K.; EMBO J. 22:1676-1687(2003). Cited for: FUNCTION IN PHOSPHORYLATION OF TLK1, AND PHOSPHORYLATION AT SER-317.	12660173 [Abstract]
"Chk1 regulates the S phase checkpoint by coupling the physiologicalturnover and ionizing radiation-induced accelerated proteolysis ofCdc25A."; Soerensen C.S., Syljuaesen R.G., Falck J., Schroeder T.,Roennstrand L., Khanna K.K., Zhou B.-B., Bartek J., Lukas J.; Cancer Cell 3:247-258(2003). Cited for: FUNCTION IN CDC25A TURNOVER, PHOSPHORYLATION AT SER-317 AND SER-345,AND MUTAGENESIS OF SER-317 AND SER-345.	12676583 [Abstract]
"An ATR- and Chk1-dependent S checkpoint inhibits replicon initiationfollowing UVC-induced DNA damage."; Heffernan T.P., Simpson D.A., Frank A.R., Heinloth A.N., Paules R.S.,Cordeiro-Stone M., Kaufmann W.K.; Mol. Cell. Biol. 22:8552-8561(2002). Cited for: FUNCTION IN DNA DAMAGE RESPONSE, PHOSPHORYLATION AT SER-317 ANDSER-345, AND MUTAGENESIS OF LYS-38.	12446774 [Abstract]
"ATR-mediated checkpoint pathways regulate phosphorylation andactivation of human Chk1."; Zhao H., Piwnica-Worms H.; Mol. Cell. Biol. 21:4129-4139(2001). Cited for: PHOSPHORYLATION AT SER-317 AND SER-345, AND MUTAGENESIS OF ASP-130;SER-317; SER-345; SER-357; SER-366 AND SER-468.	11390642 [Abstract]
"Chk1 is an essential kinase that is regulated by Atr and required forthe G(2)/M DNA damage checkpoint."; Liu Q., Guntuku S., Cui X.-S., Matsuoka S., Cortez D., Tamai K.,Luo G., Carattini-Rivera S., DeMayo F., Bradley A., Donehower L.A.,Elledge S.J.; Genes Dev. 14:1448-1459(2000). Cited for: PHOSPHORYLATION AT SER-345 BY ATR.	10859164 [Abstract]
Ubiquitylation
Reference	PubMed
"The F box protein Fbx6 regulates Chk1 stability and cellularsensitivity to replication stress."; Zhang Y.-W., Brognard J., Coughlin C., You Z., Dolled-Filhart M.,Aslanian A., Manning G., Abraham R.T., Hunter T.; Mol. Cell 35:442-453(2009). Cited for: PHOSPHORYLATION AT SER-345, UBIQUITINATION AT LYS-436, INTERACTIONWITH FBXO6, AND MUTAGENESIS OF SER-345; ARG-372; ARG-376; ARG-379 ANDLYS-436.	19716789 [Abstract]
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry."; Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.; Proteomics 7:868-874(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-436, AND MASSSPECTROMETRY.	17370265 [Abstract]

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