dbPTM

CDK1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CDK1_HUMAN
UniProt AC	P06493
Protein Name	Cyclin-dependent kinase 1
Gene Name	CDK1
Organism	Homo sapiens (Human).
Sequence Length	297
Subcellular Localization	Nucleus. Cytoplasm. Mitochondrion. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Cytoplasmic during the interphase. Colocalizes with SIRT2 on centrosome during prophase and on splindle fibers du
Protein Description	Plays a key role in the control of the eukaryotic cell cycle by modulating the centrosome cycle as well as mitotic onset; promotes G2-M transition, and regulates G1 progress and G1-S transition via association with multiple interphase cyclins. Required in higher cells for entry into S-phase and mitosis. Phosphorylates PARVA/actopaxin, APC, AMPH, APC, BARD1, Bcl-xL/BCL2L1, BRCA2, CALD1, CASP8, CDC7, CDC20, CDC25A, CDC25C, CC2D1A, CENPA, CSNK2 proteins/CKII, FZR1/CDH1, CDK7, CEBPB, CHAMP1, DMD/dystrophin, EEF1 proteins/EF-1, EZH2, KIF11/EG5, EGFR, FANCG, FOS, GFAP, GOLGA2/GM130, GRASP1, UBE2A/hHR6A, HIST1H1 proteins/histone H1, HMGA1, HIVEP3/KRC, LMNA, LMNB, LMNC, LBR, LATS1, MAP1B, MAP4, MARCKS, MCM2, MCM4, MKLP1, MYB, NEFH, NFIC, NPC/nuclear pore complex, PITPNM1/NIR2, NPM1, NCL, NUCKS1, NPM1/numatrin, ORC1, PRKAR2A, EEF1E1/p18, EIF3F/p47, p53/TP53, NONO/p54NRB, PAPOLA, PLEC/plectin, RB1, UL40/R2, RAB4A, RAP1GAP, RCC1, RPS6KB1/S6K1, KHDRBS1/SAM68, ESPL1, SKI, BIRC5/survivin, STIP1, TEX14, beta-tubulins, MAPT/TAU, NEDD1, VIM/vimentin, TK1, FOXO1, RUNX1/AML1, SIRT2 and RUNX2. CDK1/CDC2-cyclin-B controls pronuclear union in interphase fertilized eggs. Essential for early stages of embryonic development. During G2 and early mitosis, CDC25A/B/C-mediated dephosphorylation activates CDK1/cyclin complexes which phosphorylate several substrates that trigger at least centrosome separation, Golgi dynamics, nuclear envelope breakdown and chromosome condensation. Once chromosomes are condensed and aligned at the metaphase plate, CDK1 activity is switched off by WEE1- and PKMYT1-mediated phosphorylation to allow sister chromatid separation, chromosome decondensation, reformation of the nuclear envelope and cytokinesis. Inactivated by PKR/EIF2AK2- and WEE1-mediated phosphorylation upon DNA damage to stop cell cycle and genome replication at the G2 checkpoint thus facilitating DNA repair. Reactivated after successful DNA repair through WIP1-dependent signaling leading to CDC25A/B/C-mediated dephosphorylation and restoring cell cycle progression. In proliferating cells, CDK1-mediated FOXO1 phosphorylation at the G2-M phase represses FOXO1 interaction with 14-3-3 proteins and thereby promotes FOXO1 nuclear accumulation and transcription factor activity, leading to cell death of postmitotic neurons. The phosphorylation of beta-tubulins regulates microtubule dynamics during mitosis. NEDD1 phosphorylation promotes PLK1-mediated NEDD1 phosphorylation and subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation. In addition, CC2D1A phosphorylation regulates CC2D1A spindle pole localization and association with SCC1/RAD21 and centriole cohesion during mitosis. The phosphorylation of Bcl-xL/BCL2L1 after prolongated G2 arrest upon DNA damage triggers apoptosis. In contrast, CASP8 phosphorylation during mitosis prevents its activation by proteolysis and subsequent apoptosis. This phosphorylation occurs in cancer cell lines, as well as in primary breast tissues and lymphocytes. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. CALD1 phosphorylation promotes Schwann cell migration during peripheral nerve regeneration. CDK1-cyclin-B complex phosphorylates NCKAP5L and mediates its dissociation from centrosomes during mitosis. [PubMed: 26549230; (Microbial infection) Acts as a receptor for hepatitis C virus (HCV) in hepatocytes and facilitates its cell entry.]
Protein Sequence	MEDYTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLESEEEGVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLIFEFLSMDLKKYLDSIPPGQYMDSSLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFGLARAFGIPIRVYTHEVVTLWYRSPEVLLGSARYSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLFRIFRALGTPNNEVWPEVESLQDYKNTFPKWKPGSLASHVKNLDENGLDLLSKMLIYDPAKRISGKMALNHPYFNDLDNQIKKM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEDYTKIE -------CCCCCEEE	8.80	19369195
4	Phosphorylation	----MEDYTKIEKIG ----CCCCCEEEECC	9.16	18691976
4 (in isoform 2)	Phosphorylation	-	9.16	-
5	Phosphorylation	---MEDYTKIEKIGE ---CCCCCEEEECCC	37.56	17192257
5 (in isoform 2)	Phosphorylation	-	37.56	-
6	Sumoylation	--MEDYTKIEKIGEG --CCCCCEEEECCCC	42.51	-
6	Acetylation	--MEDYTKIEKIGEG --CCCCCEEEECCCC	42.51	19608861
6	Sumoylation	--MEDYTKIEKIGEG --CCCCCEEEECCCC	42.51	28112733
6	Ubiquitination	--MEDYTKIEKIGEG --CCCCCEEEECCCC	42.51	19608861
6 (in isoform 2)	Acetylation	-	42.51	-
9	Ubiquitination	EDYTKIEKIGEGTYG CCCCEEEECCCCCCE	60.53	21890473
9	Sumoylation	EDYTKIEKIGEGTYG CCCCEEEECCCCCCE	60.53	-
9	Acetylation	EDYTKIEKIGEGTYG CCCCEEEECCCCCCE	60.53	23954790
9	Sumoylation	EDYTKIEKIGEGTYG CCCCEEEECCCCCCE	60.53	28112733
9	Ubiquitination	EDYTKIEKIGEGTYG CCCCEEEECCCCCCE	60.53	21890473
9 (in isoform 1)	Ubiquitination	-	60.53	21890473
9 (in isoform 2)	Ubiquitination	-	60.53	21890473
14	Dephosphorylation	IEKIGEGTYGVVYKG EEECCCCCCEEEEEE	16.89	9585407
14	Phosphorylation	IEKIGEGTYGVVYKG EEECCCCCCEEEEEE	16.89	19664994
14 (in isoform 2)	Phosphorylation	-	16.89	-
15	Dephosphorylation	EKIGEGTYGVVYKGR EECCCCCCEEEEEEE	20.84	9585407
15	Phosphorylation	EKIGEGTYGVVYKGR EECCCCCCEEEEEEE	20.84	19664994
15 (in isoform 2)	Phosphorylation	-	20.84	-
19	Phosphorylation	EGTYGVVYKGRHKTT CCCCEEEEEEECCCC	12.81	22322096
19 (in isoform 2)	Phosphorylation	-	12.81	-
20	Ubiquitination	GTYGVVYKGRHKTTG CCCEEEEEEECCCCC	37.55	21890473
20	Acetylation	GTYGVVYKGRHKTTG CCCEEEEEEECCCCC	37.55	23236377
20	Sumoylation	GTYGVVYKGRHKTTG CCCEEEEEEECCCCC	37.55	28112733
20	Ubiquitination	GTYGVVYKGRHKTTG CCCEEEEEEECCCCC	37.55	21890473
20 (in isoform 1)	Ubiquitination	-	37.55	21890473
20 (in isoform 2)	Ubiquitination	-	37.55	21890473
24	Sumoylation	VVYKGRHKTTGQVVA EEEEEECCCCCCEEE	46.55	-
24	Sumoylation	VVYKGRHKTTGQVVA EEEEEECCCCCCEEE	46.55	-
24	Ubiquitination	VVYKGRHKTTGQVVA EEEEEECCCCCCEEE	46.55	21906983
24 (in isoform 1)	Ubiquitination	-	46.55	21890473
24 (in isoform 2)	Ubiquitination	-	46.55	21890473
25	Phosphorylation	VYKGRHKTTGQVVAM EEEEECCCCCCEEEE	29.99	29083192
26	Phosphorylation	YKGRHKTTGQVVAMK EEEECCCCCCEEEEE	30.35	29083192
33	Sumoylation	TGQVVAMKKIRLESE CCCEEEEEEEECCCC	35.00	-
33	Acetylation	TGQVVAMKKIRLESE CCCEEEEEEEECCCC	35.00	23954790
33	Sumoylation	TGQVVAMKKIRLESE CCCEEEEEEEECCCC	35.00	19608861
33	Ubiquitination	TGQVVAMKKIRLESE CCCEEEEEEEECCCC	35.00	21906983
33 (in isoform 1)	Ubiquitination	-	35.00	21890473
33 (in isoform 2)	Acetylation	-	35.00	-
33 (in isoform 2)	Ubiquitination	-	35.00	21890473
34	Sumoylation	GQVVAMKKIRLESEE CCEEEEEEEECCCCC	21.70	-
34	Acetylation	GQVVAMKKIRLESEE CCEEEEEEEECCCCC	21.70	88621
34	Sumoylation	GQVVAMKKIRLESEE CCEEEEEEEECCCCC	21.70	-
34	Ubiquitination	GQVVAMKKIRLESEE CCEEEEEEEECCCCC	21.70	-
39	Phosphorylation	MKKIRLESEEEGVPS EEEEECCCCCCCCCH	55.70	25159151
39 (in isoform 2)	Phosphorylation	-	55.70	-
46	Phosphorylation	SEEEGVPSTAIREIS CCCCCCCHHHHHHHH	28.23	18691976
46 (in isoform 2)	Phosphorylation	-	28.23	-
53	Phosphorylation	STAIREISLLKELRH HHHHHHHHHHHHCCC	23.93	24719451
56	Ubiquitination	IREISLLKELRHPNI HHHHHHHHHCCCCCC	61.06	21890473
56	Acetylation	IREISLLKELRHPNI HHHHHHHHHCCCCCC	61.06	26051181
56	Ubiquitination	IREISLLKELRHPNI HHHHHHHHHCCCCCC	61.06	21890473
56 (in isoform 2)	Ubiquitination	-	61.06	21890473
58 (in isoform 1)	Ubiquitination	-	6.11	21890473
77	Phosphorylation	LMQDSRLYLIFEFLS HHCCCHHHHHHHHHH	9.17	17192257
77 (in isoform 2)	Phosphorylation	-	9.17	-
89	Ubiquitination	FLSMDLKKYLDSIPP HHHCCHHHHHHCCCC	59.34	18655026
121	Phosphorylation	QGIVFCHSRRVLHRD HHHHHHCCCCEECCC	23.98	18691976
121 (in isoform 2)	Phosphorylation	-	23.98	-
130	Ubiquitination	RVLHRDLKPQNLLID CEECCCCCCCCEEEC	49.17	21890473
130	Sumoylation	RVLHRDLKPQNLLID CEECCCCCCCCEEEC	49.17	-
130	Acetylation	RVLHRDLKPQNLLID CEECCCCCCCCEEEC	49.17	27452117
130	Sumoylation	RVLHRDLKPQNLLID CEECCCCCCCCEEEC	49.17	-
130	Ubiquitination	RVLHRDLKPQNLLID CEECCCCCCCCEEEC	49.17	21890473
136 (in isoform 1)	Ubiquitination	-	7.89	21890473
139	Ubiquitination	QNLLIDDKGTIKLAD CCEEECCCCCEEEHH	54.96	21890473
139	Sumoylation	QNLLIDDKGTIKLAD CCEEECCCCCEEEHH	54.96	-
139	Acetylation	QNLLIDDKGTIKLAD CCEEECCCCCEEEHH	54.96	25953088
139	Sumoylation	QNLLIDDKGTIKLAD CCEEECCCCCEEEHH	54.96	28112733
139	Ubiquitination	QNLLIDDKGTIKLAD CCEEECCCCCEEEHH	54.96	18655026
141	Phosphorylation	LLIDDKGTIKLADFG EEECCCCCEEEHHHH	22.22	19369195
143	Ubiquitination	IDDKGTIKLADFGLA ECCCCCEEEHHHHHH	37.14	21890473
143	Acetylation	IDDKGTIKLADFGLA ECCCCCEEEHHHHHH	37.14	27452117
143	Ubiquitination	IDDKGTIKLADFGLA ECCCCCEEEHHHHHH	37.14	21890473
144 (in isoform 2)	Ubiquitination	-	4.96	21890473
145 (in isoform 1)	Ubiquitination	-	12.70	21890473
149 (in isoform 1)	Ubiquitination	-	2.70	21890473
160	Phosphorylation	FGIPIRVYTHEVVTL HCCCEEEEECEEEEE	7.79	27273156
161	Phosphorylation	GIPIRVYTHEVVTLW CCCEEEEECEEEEEE	14.54	22167270
165 (in isoform 2)	Phosphorylation	-	3.11	-
166	Phosphorylation	VYTHEVVTLWYRSPE EEECEEEEEEECCHH	19.42	22167270
169	Phosphorylation	HEVVTLWYRSPEVLL CEEEEEEECCHHHHH	12.34	23403867
171	Phosphorylation	VVTLWYRSPEVLLGS EEEEEECCHHHHHCC	15.09	21406692
178	Phosphorylation	SPEVLLGSARYSTPV CHHHHHCCCCCCCCC	15.00	18691976
181	Phosphorylation	VLLGSARYSTPVDIW HHHCCCCCCCCCHHH	19.33	19060867
181 (in isoform 2)	Ubiquitination	-	19.33	21890473
182	Phosphorylation	LLGSARYSTPVDIWS HHCCCCCCCCCHHHH	22.23	24719451
183	Phosphorylation	LGSARYSTPVDIWSI HCCCCCCCCCHHHHH	20.56	24719451
188 (in isoform 2)	Ubiquitination	-	4.57	21890473
197 (in isoform 2)	Ubiquitination	-	7.04	21890473
201	Ubiquitination	FAELATKKPLFHGDS HHHHHHCCCCCCCCH	42.47	21890473
201	Sumoylation	FAELATKKPLFHGDS HHHHHHCCCCCCCCH	42.47	-
201	Acetylation	FAELATKKPLFHGDS HHHHHHCCCCCCCCH	42.47	26051181
201	Sumoylation	FAELATKKPLFHGDS HHHHHHCCCCCCCCH	42.47	-
201	Ubiquitination	FAELATKKPLFHGDS HHHHHHCCCCCCCCH	42.47	21890473
207 (in isoform 1)	Ubiquitination	-	34.23	21890473
208	Phosphorylation	KPLFHGDSEIDQLFR CCCCCCCHHHHHHHH	40.83	-
209 (in isoform 2)	Ubiquitination	-	56.15	21890473
217 (in isoform 2)	Ubiquitination	-	3.05	21890473
222	Phosphorylation	RIFRALGTPNNEVWP HHHHHHCCCCCCCCC	24.56	25159151
222 (in isoform 2)	Ubiquitination	-	24.56	21890473
233	Phosphorylation	EVWPEVESLQDYKNT CCCCCHHHHHHHHHC	36.18	28450419
237	Phosphorylation	EVESLQDYKNTFPKW CHHHHHHHHHCCCCC	7.99	26714015
238	Ubiquitination	VESLQDYKNTFPKWK HHHHHHHHHCCCCCC	58.77	21890473
238	Sumoylation	VESLQDYKNTFPKWK HHHHHHHHHCCCCCC	58.77	-
238	Ubiquitination	VESLQDYKNTFPKWK HHHHHHHHHCCCCCC	58.77	21890473
238 (in isoform 2)	Ubiquitination	-	58.77	21890473
240	Phosphorylation	SLQDYKNTFPKWKPG HHHHHHHCCCCCCCC	36.84	28450419
243	Ubiquitination	DYKNTFPKWKPGSLA HHHHCCCCCCCCCHH	64.75	-
244 (in isoform 1)	Ubiquitination	-	16.59	21890473
245	Ubiquitination	KNTFPKWKPGSLASH HHCCCCCCCCCHHHH	45.70	21890473
245	Succinylation	KNTFPKWKPGSLASH HHCCCCCCCCCHHHH	45.70	-
245	Succinylation	KNTFPKWKPGSLASH HHCCCCCCCCCHHHH	45.70	21890473
245	Sumoylation	KNTFPKWKPGSLASH HHCCCCCCCCCHHHH	45.70	-
245	Ubiquitination	KNTFPKWKPGSLASH HHCCCCCCCCCHHHH	45.70	21890473
248	Phosphorylation	FPKWKPGSLASHVKN CCCCCCCCHHHHHCC	29.32	28112733
251	Phosphorylation	WKPGSLASHVKNLDE CCCCCHHHHHCCCCC	33.82	20873877
251 (in isoform 1)	Ubiquitination	-	33.82	21890473
254	Ubiquitination	GSLASHVKNLDENGL CCHHHHHCCCCCCCH	46.50	21890473
254	Acetylation	GSLASHVKNLDENGL CCHHHHHCCCCCCCH	46.50	26051181
254	Sumoylation	GSLASHVKNLDENGL CCHHHHHCCCCCCCH	46.50	-
254	Ubiquitination	GSLASHVKNLDENGL CCHHHHHCCCCCCCH	46.50	21890473
260 (in isoform 1)	Ubiquitination	-	20.65	21890473
265	Phosphorylation	ENGLDLLSKMLIYDP CCCHHHHHHHHHCCH	24.26	21712546
266	Ubiquitination	NGLDLLSKMLIYDPA CCHHHHHHHHHCCHH	37.38	21890473
266	Ubiquitination	NGLDLLSKMLIYDPA CCHHHHHHHHHCCHH	37.38	21890473
267	Sulfoxidation	GLDLLSKMLIYDPAK CHHHHHHHHHCCHHH	2.18	28183972
270	Phosphorylation	LLSKMLIYDPAKRIS HHHHHHHCCHHHHCC	16.35	20068231
272 (in isoform 1)	Ubiquitination	-	23.78	21890473
274	Acetylation	MLIYDPAKRISGKMA HHHCCHHHHCCCHHH	56.50	25953088
274	Ubiquitination	MLIYDPAKRISGKMA HHHCCHHHHCCCHHH	56.50	21906983
277	Phosphorylation	YDPAKRISGKMALNH CCHHHHCCCHHHHCC	36.07	24719451
279	Ubiquitination	PAKRISGKMALNHPY HHHHCCCHHHHCCCC	17.76	21890473
279	Sumoylation	PAKRISGKMALNHPY HHHHCCCHHHHCCCC	17.76	-
279	Acetylation	PAKRISGKMALNHPY HHHHCCCHHHHCCCC	17.76	25953088
279	Sumoylation	PAKRISGKMALNHPY HHHHCCCHHHHCCCC	17.76	-
279	Ubiquitination	PAKRISGKMALNHPY HHHHCCCHHHHCCCC	17.76	21890473
280	Sulfoxidation	AKRISGKMALNHPYF HHHCCCHHHHCCCCH	6.14	28183972
280 (in isoform 1)	Ubiquitination	-	6.14	21890473
285 (in isoform 1)	Ubiquitination	-	34.05	21890473
286	Phosphorylation	KMALNHPYFNDLDNQ HHHHCCCCHHHHHHH	13.89	29496907
295	Ubiquitination	NDLDNQIKKM----- HHHHHHHHCC-----	32.78	21890473
295	Sumoylation	NDLDNQIKKM----- HHHHHHHHCC-----	32.78	-
295	Acetylation	NDLDNQIKKM----- HHHHHHHHCC-----	32.78	25953088
295	Sumoylation	NDLDNQIKKM----- HHHHHHHHCC-----	32.78	-
295	Ubiquitination	NDLDNQIKKM----- HHHHHHHHCC-----	32.78	21890473
296	Ubiquitination	DLDNQIKKM------ HHHHHHHCC------	52.01	-
301 (in isoform 1)	Ubiquitination	-		21890473

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
4	Y	Phosphorylation	Kinase	EIF2AK2	P19525	GPS
14	T	Phosphorylation	Kinase	MYT1	Q99640	PSP
15	Y	Phosphorylation	Kinase	ERBB2	P04626	GPS
15	Y	Phosphorylation	Kinase	PRKCD	Q05655	Uniprot
15	Y	Phosphorylation	Kinase	MYT1	Q99640	PSP
15	Y	Phosphorylation	Kinase	SRC	P00523	PSP
15	Y	Phosphorylation	Kinase	SRC	P12931	PSP
15	Y	Phosphorylation	Kinase	WEE1	P30291	Uniprot
15	Y	Phosphorylation	Kinase	WEE2	P0C1S8	Uniprot
39	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
39	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
39	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
161	T	Phosphorylation	Kinase	CDK7	P50613	PSP
161	T	Phosphorylation	Kinase	MAP3K8	P41279	GPS
208	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:25149538

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
14	T	Phosphorylation	7569953
Dephosphorylation by active CDC25A and CDC25B at Thr-14 and Tyr-15, leads to CDK1 activation at the G2-M transition.
14	T	Phosphorylation	7569953
Phosphorylation at Thr-14 and Tyr-15 by PKMYT1 prevents nuclear translocation.
161	T	Phosphorylation	19690332
Phosphorylation at Thr-161 by CAK/CDK7 activates kinase activity.

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 CDK1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FANCG_HUMAN	FANCG	physical	15367677
GA45A_HUMAN	GADD45A	physical	10747892
GA45A_HUMAN	GADD45A	physical	10973963
DAB2_HUMAN	DAB2	physical	12881709
FEN1_HUMAN	FEN1	physical	12853968
NSF1C_HUMAN	NSFL1C	physical	12810701
LYN_HUMAN	LYN	physical	8051175
CDKN3_HUMAN	CDKN3	physical	8127873
P53_HUMAN	TP53	physical	10884347
CUX1_HUMAN	CUX1	physical	11584018
CASP_HUMAN	CUX1	physical	11584018
KI67_HUMAN	MKI67	physical	10502411
TSC1_HUMAN	TSC1	physical	14551205
P53_HUMAN	TP53	physical	11327730
CCNB1_HUMAN	CCNB1	physical	10973963
SPAG5_HUMAN	SPAG5	physical	11549262
CCNF_HUMAN	CCNF	physical	10716937
CCNB1_HUMAN	CCNB1	physical	10716937
MAP4_HUMAN	MAP4	physical	7876309
C2TA_HUMAN	CIITA	physical	18245089
CDN1A_HUMAN	CDKN1A	physical	17679094
HMGB1_HUMAN	HMGB1	physical	2013279
CCNA1_HUMAN	CCNA1	physical	1628647
CDCA2_HUMAN	CDCA2	physical	16998479
TSYL2_HUMAN	TSPYL2	physical	11395479
FOXM1_HUMAN	FOXM1	physical	15024056
KMT2E_HUMAN	KMT2E	physical	20439461
EZH2_HUMAN	EZH2	physical	20935635
EZH2_HUMAN	EZH2	physical	21135039
H13_HUMAN	HIST1H1D	physical	21131960
EZH2_HUMAN	EZH2	physical	21131960
EZH2_HUMAN	EZH2	physical	21123648
CCNB1_HUMAN	CCNB1	physical	20367638
RUNX1_HUMAN	RUNX1	physical	21059642
KAT5_HUMAN	KAT5	physical	12468530
PAH1_YEAST	PAH1	physical	21081492
CCND1_HUMAN	CCND1	physical	7903056
SSBP_HUMAN	SSBP1	physical	19786724
CND1_HUMAN	NCAPD2	physical	11136719
CND3_HUMAN	NCAPG	physical	11136719
CND2_HUMAN	NCAPH	physical	11136719
H15_HUMAN	HIST1H1B	physical	16205633
RPB1_YEAST	RPO21	physical	22689984
H11_HUMAN	HIST1H1A	physical	10362260
GA45A_HUMAN	GADD45A	physical	10362260
MARCS_HUMAN	MARCKS	physical	10359664
CDN1B_HUMAN	CDKN1B	physical	18615582
LMNB1_RAT	Lmnb1	physical	9053846
RB_HUMAN	RB1	physical	9053846
H11_HUMAN	HIST1H1A	physical	9053846
SP1_HUMAN	SP1	physical	22266860
H11_HUMAN	HIST1H1A	physical	8397207
CCNB1_HUMAN	CCNB1	physical	8397207
RFA1_HUMAN	RPA1	physical	8397207
CCNB1_HUMAN	CCNB1	physical	8397206
RFA1_HUMAN	RPA1	physical	8397206
H11_HUMAN	HIST1H1A	physical	8397206
KI26B_HUMAN	KIF26B	physical	22768111
FZR1_HUMAN	FZR1	physical	20581839
UBC9_HUMAN	UBE2I	physical	22407595
FBX5_HUMAN	FBXO5	physical	21454540
H15_HUMAN	HIST1H1B	physical	18560763
H10_HUMAN	H1F0	physical	12190313
CKS1_HUMAN	CKS1B	physical	18471975
CKS2_HUMAN	CKS2	physical	18471975
LATS1_HUMAN	LATS1	physical	12372621
H11_HUMAN	HIST1H1A	physical	11836499
CASB_HUMAN	CSN2	physical	7790358
H11_HUMAN	HIST1H1A	physical	7790358
BUB1_HUMAN	BUB1	physical	16760428
CCNA2_HUMAN	CCNA2	physical	21308745
CDK1_HUMAN	CDK1	physical	21308745
CDN1A_HUMAN	CDKN1A	physical	21308745
REPS2_HUMAN	REPS2	physical	10764745
EPN1_HUMAN	EPN1	physical	10764745
CCNB1_HUMAN	CCNB1	physical	7799941
CCNA1_HUMAN	CCNA1	physical	7799941
H10_HUMAN	H1F0	physical	15147269
MBP_HUMAN	MBP	physical	17906618
HTRA2_HUMAN	HTRA2	physical	17906618
KIF11_HUMAN	KIF11	physical	8548803
WEE1_HUMAN	WEE1	physical	15070733
TFDP1_HUMAN	TFDP1	physical	9199321
E2F1_HUMAN	E2F1	physical	9199321
RB_HUMAN	RB1	physical	1756735
RGAP1_HUMAN	RACGAP1	physical	18201571
CKS1_HUMAN	CKS1B	physical	22939629
HMGA2_MOUSE	Hmga2	physical	10636877
RB_HUMAN	RB1	physical	8626527
PRC1_HUMAN	PRC1	physical	9885575
RB_HUMAN	RB1	physical	9885575
H11_HUMAN	HIST1H1A	physical	9885575
RARA_MOUSE	Rara	physical	10383391
LMNB1_HUMAN	LMNB1	physical	8034666
H10_HUMAN	H1F0	physical	8034666
RB_HUMAN	RB1	physical	9258347
CP110_HUMAN	CCP110	physical	12361598
RB_HUMAN	RB1	physical	12361598
IL16_HUMAN	IL16	physical	12450396
H15_HUMAN	HIST1H1B	physical	11980914
EF2K_HUMAN	EEF2K	physical	18337751
CCNB1_HUMAN	CCNB1	physical	18337751
PML_HUMAN	PML	physical	21840486
CDC6_HUMAN	CDC6	physical	10339564
CDK7_HUMAN	CDK7	physical	11113184
RB_HUMAN	RB1	physical	9315635
H15_HUMAN	HIST1H1B	physical	23543736
CKS1_HUMAN	CKS1B	physical	9774639
H15_HUMAN	HIST1H1B	physical	9668078
BCL2_HUMAN	BCL2	physical	9668078
H15_HUMAN	HIST1H1B	physical	8663071
H15_HUMAN	HIST1H1B	physical	11516829
CDCA5_HUMAN	CDCA5	physical	21987589
H11_HUMAN	HIST1H1A	physical	11687586
RGCC_HUMAN	RGCC	physical	11687586
HMGA1_HUMAN	HMGA1	physical	11034995
TP53B_HUMAN	TP53BP1	physical	20126263
DPOLA_HUMAN	POLA1	physical	11259605
DCTN6_BOVIN	DCTN6	physical	23455152
DCTN6_HUMAN	DCTN6	physical	23455152
RGCC_HUMAN	RGCC	physical	19162005
CCNB1_HUMAN	CCNB1	physical	19162005
H11_HUMAN	HIST1H1A	physical	23933584
SQSTM_HUMAN	SQSTM1	physical	20974803
CCNB1_HUMAN	CCNB1	physical	20974803
H11_HUMAN	HIST1H1A	physical	20974803
IL3RA_HUMAN	IL3RA	physical	21988832
CXCR1_HUMAN	CXCR1	physical	21988832
JAK3_HUMAN	JAK3	physical	21988832
RELB_HUMAN	RELB	physical	21988832
TNNC1_HUMAN	TNNC1	physical	21988832
PAK6_HUMAN	PAK6	physical	21988832
MLKL_HUMAN	MLKL	physical	21988832
CDK1_HUMAN	CDK1	physical	23602568
CCNA2_HUMAN	CCNA2	physical	23602568
CDN1B_HUMAN	CDKN1B	physical	23602568
CKS1_HUMAN	CKS1B	physical	23602568
CCNB1_HUMAN	CCNB1	physical	23602568
CCNB2_HUMAN	CCNB2	physical	23602568
CKS2_HUMAN	CKS2	physical	23602568
PMYT1_HUMAN	PKMYT1	physical	23602568
CDN1A_HUMAN	CDKN1A	physical	23602568
ZRAB2_HUMAN	ZRANB2	physical	22863883
UBP16_HUMAN	USP16	physical	24013421
UIMC1_HUMAN	UIMC1	physical	23264621
HS90A_HUMAN	HSP90AA1	physical	17525741
CDC37_HUMAN	CDC37	physical	17525741
HSP74_HUMAN	HSPA4	physical	17525741
ABL1_HUMAN	ABL1	physical	2183353
SIR1_HUMAN	SIRT1	physical	19107194
H11_HUMAN	HIST1H1A	physical	19107194
FBW1A_HUMAN	BTRC	physical	25149538
CKS1_HUMAN	CKS1B	physical	25416956
SP1_HUMAN	SP1	physical	25398907
EP300_HUMAN	EP300	physical	24530506
NUCL_HUMAN	NCL	physical	24530506
H2B1B_HUMAN	HIST1H2BB	physical	22539978
H11_HUMAN	HIST1H1A	physical	22539978
CDC20_HUMAN	CDC20	physical	10799291
CCNB1_HUMAN	CCNB1	physical	12612082
CIP1_HUMAN	CCNB1IP1	physical	12612082
BARD1_HUMAN	BARD1	physical	15665273
CCNA2_HUMAN	CCNA2	physical	25852190
CCNB1_HUMAN	CCNB1	physical	25852190
CCNB2_HUMAN	CCNB2	physical	25852190
CKS1_HUMAN	CKS1B	physical	25852190
CKS2_HUMAN	CKS2	physical	25852190
PMYT1_HUMAN	PKMYT1	physical	25852190
CKS1_HUMAN	CKS1B	physical	26186194
CKS2_HUMAN	CKS2	physical	26186194
CDK3_HUMAN	CDK3	physical	26186194
CDT1_HUMAN	CDT1	physical	26186194
CCNB2_HUMAN	CCNB2	physical	26186194
CCNB1_HUMAN	CCNB1	physical	26186194
SKP2_HUMAN	SKP2	physical	26186194
CDN1B_HUMAN	CDKN1B	physical	26186194
ICK_HUMAN	ICK	physical	26186194
CDK17_HUMAN	CDK17	physical	26186194
CDN1C_HUMAN	CDKN1C	physical	26186194
GEMI_HUMAN	GMNN	physical	26186194
CDKN3_HUMAN	CDKN3	physical	26186194
PMYT1_HUMAN	PKMYT1	physical	26186194
CDN1A_HUMAN	CDKN1A	physical	26186194
CCNB1_HUMAN	CCNB1	physical	26344197
CCNB2_HUMAN	CCNB2	physical	26344197
CKS1_HUMAN	CKS1B	physical	26344197
PRDX2_HUMAN	PRDX2	physical	26344197
AT2A2_HUMAN	ATP2A2	physical	26496610
CCNB1_HUMAN	CCNB1	physical	26496610
CCND3_HUMAN	CCND3	physical	26496610
CHK1_HUMAN	CHEK1	physical	26496610
CKS1_HUMAN	CKS1B	physical	26496610
CKS2_HUMAN	CKS2	physical	26496610
MVD1_HUMAN	MVD	physical	26496610
SKP2_HUMAN	SKP2	physical	26496610
TCPA_HUMAN	TCP1	physical	26496610
CDK13_HUMAN	CDK13	physical	26496610
VA0D1_HUMAN	ATP6V0D1	physical	26496610
CCNB2_HUMAN	CCNB2	physical	26496610
DLG5_HUMAN	DLG5	physical	26496610
TCPH_HUMAN	CCT7	physical	26496610
TCPD_HUMAN	CCT4	physical	26496610
ASCC3_HUMAN	ASCC3	physical	26496610
TCPE_HUMAN	CCT5	physical	26496610
CUTA_HUMAN	CUTA	physical	26496610
TM165_HUMAN	TMEM165	physical	26496610
TIM29_HUMAN	C19orf52	physical	26496610
ESCO1_HUMAN	ESCO1	physical	26496610
MSI2H_HUMAN	MSI2	physical	26496610
GATA2_HUMAN	GATA2	physical	25670854
EZH2_HUMAN	EZH2	physical	25800736
TP53B_HUMAN	TP53BP1	physical	25607646
UBP16_HUMAN	USP16	physical	26323689
UBP22_HUMAN	USP22	physical	27030811
H11_HUMAN	HIST1H1A	physical	18695677
TREA_YEAST	NTH1	physical	27203179
PHSG_YEAST	GPH1	physical	27203179
CCNB2_HUMAN	CCNB2	physical	28514442
CCNB1_HUMAN	CCNB1	physical	28514442
PMYT1_HUMAN	PKMYT1	physical	28514442
CDN1A_HUMAN	CDKN1A	physical	28514442
CDK3_HUMAN	CDK3	physical	28514442
CDT1_HUMAN	CDT1	physical	28514442
CDN1B_HUMAN	CDKN1B	physical	28514442
CDN1C_HUMAN	CDKN1C	physical	28514442
CDK17_HUMAN	CDK17	physical	28514442
ICK_HUMAN	ICK	physical	28514442
DCD_HUMAN	DCD	physical	29128334
THOC4_HUMAN	ALYREF	physical	29128334
ERH_HUMAN	ERH	physical	29128334
PLAK_HUMAN	JUP	physical	29128334
THIO_HUMAN	TXN	physical	29128334
ADT2_HUMAN	SLC25A5	physical	29128334
DESP_HUMAN	DSP	physical	29128334
RMXL2_HUMAN	RBMXL2	physical	29128334
FBRL_HUMAN	FBL	physical	29128334
SAFB1_HUMAN	SAFB	physical	29128334
HORN_HUMAN	HRNR	physical	29128334
MOB2_HUMAN	MOB2	physical	29128334
LYSC_HUMAN	LYZ	physical	29128334
SCYL2_HUMAN	SCYL2	physical	29128334
FILA2_HUMAN	FLG2	physical	29128334
GFAP_HUMAN	GFAP	physical	29128334
RNPS1_HUMAN	RNPS1	physical	29128334
KPRP_HUMAN	KPRP	physical	29128334
BOLA2_HUMAN	BOLA2	physical	29128334
B2CL1_HUMAN	BCL2L1	physical	22617334
MDM4_HUMAN	MDM4	physical	15735705
RB_HUMAN	RB1	physical	11306463
CDC20_HUMAN	CDC20	physical	26912231
STK3_HUMAN	STK3	physical	27566175
ITB3_HUMAN	ITGB3	physical	10896934

Drug and Disease Associations

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

Regulatory Network of CDK1_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 MET-1 AND LYS-6, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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 TYR-4; THR-5; THR-14;TYR-15; TYR-19; SER-39; SER-46; THR-141; TYR-160; THR-161; SER-178;TYR-181; THR-222; SER-233 AND SER-248, AND MASS SPECTROMETRY.	19369195 [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 THR-5; THR-14; TYR-15;TYR-19; SER-39; TYR-77; THR-161 AND THR-222, AND MASS SPECTROMETRY.	18691976 [Abstract]
"Cdc25 phosphatases are required for timely assembly of CDK1-cyclin Bat the G2/M transition."; Timofeev O., Cizmecioglu O., Settele F., Kempf T., Hoffmann I.; J. Biol. Chem. 285:16978-16990(2010). Cited for: FUNCTION IN G2-M TRANSITION, DEPHOSPHORYLATION AT THR-14 AND TYR-15 BYCDC25, PHOSPHORYLATION AT THR-161 BY CDK7/CAK, AND INTERACTION WITHB-CYCLIN.	20360007 [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-14; TYR-15; TYR-19 ANDTHR-161, AND MASS 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-14; TYR-15 AND TYR-19,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 THR-14 AND TYR-15, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-160 AND THR-161, ANDMASS SPECTROMETRY.	18220336 [Abstract]
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry."; Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.; Mol. Cell. Proteomics 6:537-547(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; TYR-15 AND TYR-19,AND MASS SPECTROMETRY.	17192257 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, AND MASSSPECTROMETRY.	17924679 [Abstract]
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline."; Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; Electrophoresis 28:2027-2034(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14 AND TYR-15, AND MASSSPECTROMETRY.	17487921 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, AND MASSSPECTROMETRY.	16565220 [Abstract]
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14 AND TYR-15, AND MASSSPECTROMETRY.	16083285 [Abstract]
"Myt1: a membrane-associated inhibitory kinase that phosphorylatesCdc2 on both threonine-14 and tyrosine-15."; Mueller P.R., Coleman T.R., Kumagai A., Dunphy W.G.; Science 270:86-90(1995). Cited for: PHOSPHORYLATION AT THR-14 AND TYR-15 BY PKMYT1.	7569953 [Abstract]
"The protein kinase Cdelta catalytic fragment is critical formaintenance of the G2/M DNA damage checkpoint."; LaGory E.L., Sitailo L.A., Denning M.F.; J. Biol. Chem. 285:1879-1887(2010). Cited for: PHOSPHORYLATION AT TYR-15.	19917613 [Abstract]
"New Cdc2 Tyr 4 phosphorylation by dsRNA-activated protein kinasetriggers Cdc2 polyubiquitination and G2 arrest under genotoxicstresses."; Yoon C.-H., Miah M.A., Kim K.P., Bae Y.-S.; EMBO Rep. 11:393-399(2010). Cited for: FUNCTION IN G2 ARREST UPON DNA DAMAGE, PHOSPHORYLATION AT TYR-4 BYPKR/EIF2AK2, POLYUBIQUITINATION, AND MUTAGENESIS OF TYR-4.	20395957 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15 AND TYR-19, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15 AND TYR-19, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15 AND TYR-19, AND MASSSPECTROMETRY.	15592455 [Abstract]
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules."; Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.; Mol. Cell. Proteomics 4:1240-1250(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15, AND MASSSPECTROMETRY.	15951569 [Abstract]
Ubiquitylation
Reference	PubMed
"Proteomic analysis of ubiquitinated proteins in normal hepatocytecell line Chang liver cells."; Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E.,Wu J., Luo Y., Qiang B., Yuan J., Sun X., Peng X.; Proteomics 8:2885-2896(2008). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-89, AND MASSSPECTROMETRY.	18655026 [Abstract]

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