HUMAN:CDK2

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	CDK2 (synonyms: CDKN2)
Protein Name(s)	Cyclin-dependent kinase 2 Cell division protein kinase 2 p33 protein kinase
External Links
UniProt	P24941
EMBL	X61622 X62071 M68520 AB012305 BT006821 AF512553 AK291941 AC025162 AC034102 CH471054 BC003065
CCDS	CCDS8898.1 CCDS8899.1
PIR	A41227
RefSeq	NP_001277159.1 NP_001789.2 NP_439892.2
UniGene	Hs.19192 Hs.689624
PDB	1AQ1 1B38 1B39 1BUH 1CKP 1DI8 1DM2 1E1V 1E1X 1E9H 1F5Q 1FIN 1FQ1 1FVT 1FVV 1G5S 1GIH 1GII 1GIJ 1GY3 1GZ8 1H00 1H01 1H07 1H08 1H0V 1H0W 1H1P 1H1Q 1H1R 1H1S 1H24 1H25 1H26 1H27 1H28 1HCK 1HCL 1JST 1JSU 1JSV 1JVP 1KE5 1KE6 1KE7 1KE8 1KE9 1OGU 1OI9 1OIQ 1OIR 1OIT 1OIU 1OIY 1OKV 1OKW 1OL1 1OL2 1P2A 1P5E 1PF8 1PKD 1PW2 1PXI 1PXJ 1PXK 1PXL 1PXM 1PXN 1PXO 1PXP 1PYE 1QMZ 1R78 1URC 1URW 1V1K 1VYW 1VYZ 1W0X 1W8C 1W98 1WCC 1Y8Y 1Y91 1YKR 2A0C 2A4L 2B52 2B53 2B54 2B55 2BHE 2BHH 2BKZ 2BPM 2BTR 2BTS 2C4G 2C5N 2C5O 2C5V 2C5X 2C5Y 2C68 2C69 2C6I 2C6K 2C6L 2C6M 2C6O 2C6T 2CCH 2CCI 2CJM 2CLX 2DS1 2DUV 2EXM 2FVD 2G9X 2HIC 2I40 2IW6 2IW8 2IW9 2J9M 2JGZ 2R3F 2R3G 2R3H 2R3I 2R3J 2R3K 2R3L 2R3M 2R3N 2R3O 2R3P 2R3Q 2R3R 2R64 2UUE 2UZB 2UZD 2UZE 2UZL 2UZN 2UZO 2V0D 2V22 2VTA 2VTH 2VTI 2VTJ 2VTL 2VTM 2VTN 2VTO 2VTP 2VTQ 2VTR 2VTS 2VTT 2VU3 2VV9 2W05 2W06 2W17 2W1H 2WEV 2WFY 2WHB 2WIH 2WIP 2WMA 2WMB 2WPA 2WXV 2X1N 2XMY 2XNB 3BHT 3BHU 3BHV 3DDP 3DDQ 3DOG 3EID 3EJ1 3EOC 3EZR 3EZV 3F5X 3FZ1 3IG7 3IGG 3LE6 3LFN 3LFQ 3LFS 3MY5 3NS9 3PJ8 3PXF 3PXQ 3PXR 3PXY 3PXZ 3PY0 3PY1 3QHR 3QHW 3QL8 3QQF 3QQG 3QQH 3QQJ 3QQK 3QQL 3QRT 3QRU 3QTQ 3QTR 3QTS 3QTU 3QTW 3QTX 3QTZ 3QU0 3QWJ 3QWK 3QX2 3QX4 3QXO 3QXP 3QZF 3QZG 3QZH 3QZI 3R1Q 3R1S 3R1Y 3R28 3R6X 3R71 3R73 3R7E 3R7I 3R7U 3R7V 3R7Y 3R83 3R8L 3R8M 3R8P 3R8U 3R8V 3R8Z 3R9D 3R9H 3R9N 3R9O 3RAH 3RAI 3RAK 3RAL 3RJC 3RK5 3RK7 3RK9 3RKB 3RM6 3RM7 3RMF 3RNI 3ROY 3RPO 3RPR 3RPV 3RPY 3RZB 3S00 3S0O 3S1H 3S2P 3SQQ 3SW4 3SW7 3TI1 3TIY 3TIZ 3TNW 3ULI 3UNJ 3UNK 3WBL 4ACM 4BCK 4BCM 4BCN 4BCO 4BCP 4BCQ 4BGH 4BZD 4CFN 4CFW 4EK3 4EK4 4EK5 4EK6 4EK8 4EOI 4EOJ 4EOK 4EOL 4EOM 4EON 4EOO 4EOP 4EOQ 4EOR 4EOS 4ERW 4EZ3 4EZ7 4FKG 4FKI 4FKJ 4FKL 4FKO 4FKP 4FKQ 4FKR 4FKS 4FKT 4FKU 4FKV 4FKW 4FX3 4GCJ 4I3Z 4II5 4KD1 4LYN 4NJ3
PDBsum	1AQ1 1B38 1B39 1BUH 1CKP 1DI8 1DM2 1E1V 1E1X 1E9H 1F5Q 1FIN 1FQ1 1FVT 1FVV 1G5S 1GIH 1GII 1GIJ 1GY3 1GZ8 1H00 1H01 1H07 1H08 1H0V 1H0W 1H1P 1H1Q 1H1R 1H1S 1H24 1H25 1H26 1H27 1H28 1HCK 1HCL 1JST 1JSU 1JSV 1JVP 1KE5 1KE6 1KE7 1KE8 1KE9 1OGU 1OI9 1OIQ 1OIR 1OIT 1OIU 1OIY 1OKV 1OKW 1OL1 1OL2 1P2A 1P5E 1PF8 1PKD 1PW2 1PXI 1PXJ 1PXK 1PXL 1PXM 1PXN 1PXO 1PXP 1PYE 1QMZ 1R78 1URC 1URW 1V1K 1VYW 1VYZ 1W0X 1W8C 1W98 1WCC 1Y8Y 1Y91 1YKR 2A0C 2A4L 2B52 2B53 2B54 2B55 2BHE 2BHH 2BKZ 2BPM 2BTR 2BTS 2C4G 2C5N 2C5O 2C5V 2C5X 2C5Y 2C68 2C69 2C6I 2C6K 2C6L 2C6M 2C6O 2C6T 2CCH 2CCI 2CJM 2CLX 2DS1 2DUV 2EXM 2FVD 2G9X 2HIC 2I40 2IW6 2IW8 2IW9 2J9M 2JGZ 2R3F 2R3G 2R3H 2R3I 2R3J 2R3K 2R3L 2R3M 2R3N 2R3O 2R3P 2R3Q 2R3R 2R64 2UUE 2UZB 2UZD 2UZE 2UZL 2UZN 2UZO 2V0D 2V22 2VTA 2VTH 2VTI 2VTJ 2VTL 2VTM 2VTN 2VTO 2VTP 2VTQ 2VTR 2VTS 2VTT 2VU3 2VV9 2W05 2W06 2W17 2W1H 2WEV 2WFY 2WHB 2WIH 2WIP 2WMA 2WMB 2WPA 2WXV 2X1N 2XMY 2XNB 3BHT 3BHU 3BHV 3DDP 3DDQ 3DOG 3EID 3EJ1 3EOC 3EZR 3EZV 3F5X 3FZ1 3IG7 3IGG 3LE6 3LFN 3LFQ 3LFS 3MY5 3NS9 3PJ8 3PXF 3PXQ 3PXR 3PXY 3PXZ 3PY0 3PY1 3QHR 3QHW 3QL8 3QQF 3QQG 3QQH 3QQJ 3QQK 3QQL 3QRT 3QRU 3QTQ 3QTR 3QTS 3QTU 3QTW 3QTX 3QTZ 3QU0 3QWJ 3QWK 3QX2 3QX4 3QXO 3QXP 3QZF 3QZG 3QZH 3QZI 3R1Q 3R1S 3R1Y 3R28 3R6X 3R71 3R73 3R7E 3R7I 3R7U 3R7V 3R7Y 3R83 3R8L 3R8M 3R8P 3R8U 3R8V 3R8Z 3R9D 3R9H 3R9N 3R9O 3RAH 3RAI 3RAK 3RAL 3RJC 3RK5 3RK7 3RK9 3RKB 3RM6 3RM7 3RMF 3RNI 3ROY 3RPO 3RPR 3RPV 3RPY 3RZB 3S00 3S0O 3S1H 3S2P 3SQQ 3SW4 3SW7 3TI1 3TIY 3TIZ 3TNW 3ULI 3UNJ 3UNK 3WBL 4ACM 4BCK 4BCM 4BCN 4BCO 4BCP 4BCQ 4BGH 4BZD 4CFN 4CFW 4EK3 4EK4 4EK5 4EK6 4EK8 4EOI 4EOJ 4EOK 4EOL 4EOM 4EON 4EOO 4EOP 4EOQ 4EOR 4EOS 4ERW 4EZ3 4EZ7 4FKG 4FKI 4FKJ 4FKL 4FKO 4FKP 4FKQ 4FKR 4FKS 4FKT 4FKU 4FKV 4FKW 4FX3 4GCJ 4I3Z 4II5 4KD1 4LYN 4NJ3
ProteinModelPortal	P24941
SMR	P24941
BioGrid	107452
DIP	DIP-161N
IntAct	P24941
MINT	MINT-96328
STRING	9606.ENSP00000266970
BindingDB	P24941
ChEMBL	CHEMBL3038470
DrugBank	DB06616
GuidetoPHARMACOLOGY	1973
PhosphoSite	P24941
DMDM	116051
MaxQB	P24941
PaxDb	P24941
PRIDE	P24941
DNASU	1017
Ensembl	ENST00000266970 ENST00000354056
GeneID	1017
KEGG	hsa:1017
UCSC	uc001sit.4 uc001siu.4
CTD	1017
GeneCards	GC12P056360
HGNC	HGNC:1771
HPA	CAB013115
MIM	116953
neXtProt	NX_P24941
PharmGKB	PA101
eggNOG	COG0515
GeneTree	ENSGT00760000119154
HOGENOM	HOG000233024
HOVERGEN	HBG014652
InParanoid	P24941
KO	K02206
OrthoDB	EOG7966H8
PhylomeDB	P24941
TreeFam	TF101021
BRENDA	2.7.11.22
Reactome	REACT_1095 REACT_111214 REACT_1156 REACT_1221 REACT_1625 REACT_169168 REACT_169185 REACT_1857 REACT_1915 REACT_24970 REACT_27271 REACT_308 REACT_6769 REACT_6837 REACT_9003 REACT_9029
SignaLink	P24941
ChiTaRS	CDK2
EvolutionaryTrace	P24941
GeneWiki	Cyclin-dependent_kinase_2
GenomeRNAi	1017
NextBio	4273
PRO	PR:P24941
Proteomes	UP000005640
Bgee	P24941
CleanEx	HS_CDK2
ExpressionAtlas	P24941
Genevestigator	P24941
GO	GO:0015030 GO:0005813 GO:0000781 GO:0000793 GO:0000307 GO:0005737 GO:0005829 GO:0005768 GO:0005654 GO:0005634 GO:0005667 GO:0000805 GO:0000806 GO:0005524 GO:0030332 GO:0004693 GO:0046872 GO:0031145 GO:0007596 GO:0071732 GO:0051298 GO:0006977 GO:0006281 GO:0006260 GO:0000082 GO:0000086 GO:0016572 GO:0007126 GO:0000278 GO:0031571 GO:0007067 GO:0008284 GO:0032298 GO:0045893 GO:0006813 GO:0007265 GO:0060968 GO:0051439
InterPro	IPR011009 IPR000719 IPR017441 IPR002290 IPR008271
Pfam	PF00069
SMART	SM00220
SUPFAM	SSF56112
PROSITE	PS00107 PS50011 PS00108

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0016310	phosphorylation	PMID:23140174^[1]	ECO:0000314			P		Figure 1 (A-D)	complete CACAO 5859
	GO:0004674	protein serine/threonine kinase activity	PMID:23479742^[2]	ECO:0000314			F		Figure 5	complete CACAO 9198
part_of	GO:0097124	cyclin A2-CDK2 complex	PMID:8684460^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:26996940^[4]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P51943	F	has_input:(UniProtKB:P10636)	Seeded From UniProt	complete
part_of	GO:0097135	cyclin E2-CDK2 complex	PMID:18305109^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0097134	cyclin E1-CDK2 complex	PMID:18305109^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0097123	cyclin A1-CDK2 complex	PMID:18305109^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0019904	protein domain specific binding	PMID:8876165^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P38936	F		Seeded From UniProt	complete
enables	GO:0019904	protein domain specific binding	PMID:15024385^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P46527	F		Seeded From UniProt	complete
enables	GO:0030332	cyclin binding	PMID:15024385^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P20248	F		Seeded From UniProt	complete
part_of	GO:0097124	cyclin A2-CDK2 complex	PMID:8876165^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0097124	cyclin A2-CDK2 complex	PMID:15024385^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0000307	cyclin-dependent protein kinase holoenzyme complex	PMID:1312467^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0030332	cyclin binding	PMID:1312467^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P20248	F		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	PMID:8245034^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0097472	cyclin-dependent protein kinase activity	PMID:1312467^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:28666995^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0097472	cyclin-dependent protein kinase activity	PMID:28666995^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0016572	histone phosphorylation	PMID:11746698^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0097124	cyclin A2-CDK2 complex	PMID:11746698^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0030332	cyclin binding	PMID:23781148^[12]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:12944431^[13]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007099	centriole replication	PMID:26297806^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0018105	peptidyl-serine phosphorylation	PMID:23184662^[15]	ECO:0000314	direct assay evidence used in manual assertion		P	has_direct_input:(UniProtKB:P13639)\|causally_upstream_of(GO:0010801) has_direct_input:(UniProtKB:P13639)	Seeded From UniProt	complete
part_of	GO:0097124	cyclin A2-CDK2 complex	PMID:1312467^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0007265	Ras protein signal transduction	PMID:9054499^[16]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0060968	regulation of gene silencing	PMID:20935635^[17]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
contributes_to	GO:0035173	histone kinase activity	PMID:8692841^[18]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0030332	cyclin binding	PMID:1653904^[19]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0015030	Cajal body	PMID:10995387^[20]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0008284	positive regulation of cell population proliferation	PMID:10767298^[21]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005768	endosome	PMID:21262353^[22]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:10767298^[21]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:10767298^[21]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004693	cyclin-dependent protein serine/threonine kinase activity	PMID:21596315^[23]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0000307	cyclin-dependent protein kinase holoenzyme complex	PMID:8692841^[18]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0000086	G2/M transition of mitotic cell cycle	PMID:1653904^[19]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0030332	cyclin binding	PMID:21873635^[24]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104772 PANTHER:PTN000623979 RGD:70486 UniProtKB:P24941	F		Seeded From UniProt	complete
involved_in	GO:0010389	regulation of G2/M transition of mitotic cell cycle	PMID:21873635^[24]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000623979 PomBase:SPBC11B10.09	P		Seeded From UniProt	complete
involved_in	GO:0008284	positive regulation of cell population proliferation	PMID:21873635^[24]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104772 PANTHER:PTN000623979 TAIR:locus:2099478 UniProtKB:P24941	P		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:21873635^[24]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0004106 FB:FBgn0005640 FB:FBgn0013435 FB:FBgn0013762 FB:FBgn0015618 FB:FBgn0263237 MGI:MGI:101765 MGI:MGI:104772 MGI:MGI:88351 MGI:MGI:88357 PANTHER:PTN000623091 RGD:621124 RGD:70514 SGD:S000001622 SGD:S000001865 SGD:S000005488 SGD:S000005952 SGD:S000005963 SGD:S000006365 TAIR:locus:2119961 UniProtKB:P06493 UniProtKB:P11802 UniProtKB:P21127 UniProtKB:P24941 UniProtKB:P50750 UniProtKB:Q00534 UniProtKB:Q00646 UniProtKB:Q9UQ88 WB:WBGene00000405 WB:WBGene00000407 WB:WBGene00019362 ZFIN:ZDB-GENE-040808-34 dictyBase:DDB_G0267442 dictyBase:DDB_G0272813 dictyBase:DDB_G0288677	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[24]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000623979 PomBase:SPBC11B10.09 SGD:S000000364 TAIR:locus:2099478 UniProtKB:P24941	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21873635^[24]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0015618 FB:FBgn0019949 FB:FBgn0263237 MGI:MGI:101765 MGI:MGI:102956 MGI:MGI:104772 MGI:MGI:1328368 MGI:MGI:88353 MGI:MGI:88357 MGI:MGI:894318 PANTHER:PTN000623091 PomBase:SPAC2F3.15 PomBase:SPBC11B10.09 PomBase:SPBC32H8.10 RGD:1305435 RGD:1359638 RGD:2319 RGD:619874 RGD:621120 RGD:621124 RGD:70486 RGD:70514 SGD:S000000364 SGD:S000001622 SGD:S000002266 SGD:S000005952 TAIR:locus:2008595 TAIR:locus:2027819 TAIR:locus:2033349 TAIR:locus:2080290 TAIR:locus:2084086 TAIR:locus:2099478 TAIR:locus:2119961 TAIR:locus:2158554 TAIR:locus:2194045 UniProtKB:O76039 UniProtKB:O94921 UniProtKB:P06493 UniProtKB:P11802 UniProtKB:P21127 UniProtKB:P24941 UniProtKB:P49336 UniProtKB:P50613 UniProtKB:P61075 UniProtKB:P79432 UniProtKB:Q00534 UniProtKB:Q00535 UniProtKB:Q00646 UniProtKB:Q5B3E4 UniProtKB:Q8IDW1 UniProtKB:Q8IIL5 UniProtKB:Q8IJQ1 UniProtKB:Q8RWN3 UniProtKB:Q8W4P1 UniProtKB:Q92772 UniProtKB:Q96VK3 UniProtKB:Q9NYV4 UniProtKB:Q9UQ88 WB:WBGene00000405 dictyBase:DDB_G0267442 dictyBase:DDB_G0288677	C		Seeded From UniProt	complete
enables	GO:0004693	cyclin-dependent protein serine/threonine kinase activity	PMID:21873635^[24]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0004106 FB:FBgn0005640 FB:FBgn0013762 FB:FBgn0019949 FB:FBgn0263237 MGI:MGI:104772 MGI:MGI:88351 MGI:MGI:88357 PANTHER:PTN000623091 PomBase:SPAC23H4.17c PomBase:SPAC2F3.15 PomBase:SPBC11B10.09 PomBase:SPBC19F8.07 PomBase:SPBC32H8.10 RGD:2319 RGD:621120 RGD:621124 RGD:70486 RGD:70514 SGD:S000000364 SGD:S000001622 SGD:S000005952 SGD:S000005963 SGD:S000006365 TAIR:locus:2011761 UniProtKB:A0A1D8PDA6 UniProtKB:C9K505 UniProtKB:O94921 UniProtKB:P06493 UniProtKB:P11802 UniProtKB:P24941 UniProtKB:P50750 UniProtKB:P61075 UniProtKB:Q00534 UniProtKB:Q00646 UniProtKB:Q8IJQ1 WB:WBGene00000405 ZFIN:ZDB-GENE-010131-2 dictyBase:DDB_G0272813 dictyBase:DDB_G0288677	F		Seeded From UniProt	complete
part_of	GO:0000307	cyclin-dependent protein kinase holoenzyme complex	PMID:21873635^[24]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104772 PANTHER:PTN000623979 PomBase:SPBC11B10.09 SGD:S000000364 UniProtKB:P24941	C		Seeded From UniProt	complete
involved_in	GO:0000082	G1/S transition of mitotic cell cycle	PMID:21873635^[24]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104772 PANTHER:PTN000623979 PomBase:SPBC11B10.09	P		Seeded From UniProt	complete
part_of	GO:0005813	centrosome	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0097135	cyclin E2-CDK2 complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P97377 ensembl:ENSMUSP00000026416	C		Seeded From UniProt	complete
part_of	GO:0097134	cyclin E1-CDK2 complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P97377 ensembl:ENSMUSP00000026416	C		Seeded From UniProt	complete
part_of	GO:0097124	cyclin A2-CDK2 complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P97377 ensembl:ENSMUSP00000026416	C		Seeded From UniProt	complete
part_of	GO:0097123	cyclin A1-CDK2 complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P97377 ensembl:ENSMUSP00000026416	C		Seeded From UniProt	complete
involved_in	GO:0045893	positive regulation of transcription, DNA-templated	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P97377 ensembl:ENSMUSP00000026416	P		Seeded From UniProt	complete
involved_in	GO:0032298	positive regulation of DNA-dependent DNA replication initiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P97377 ensembl:ENSMUSP00000026416	P		Seeded From UniProt	complete
enables	GO:0030332	cyclin binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P97377 ensembl:ENSMUSP00000026416	F		Seeded From UniProt	complete
involved_in	GO:0018105	peptidyl-serine phosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P97377 ensembl:ENSMUSP00000026416	P		Seeded From UniProt	complete
enables	GO:0016301	kinase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P97377 ensembl:ENSMUSP00000026416	F		Seeded From UniProt	complete
involved_in	GO:0008284	positive regulation of cell population proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P97377 ensembl:ENSMUSP00000026416	P		Seeded From UniProt	complete
involved_in	GO:0006813	potassium ion transport	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P97377 ensembl:ENSMUSP00000026416	P		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P97377 ensembl:ENSMUSP00000026416	P		Seeded From UniProt	complete
part_of	GO:0005667	transcription factor complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P97377 ensembl:ENSMUSP00000026416	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P97377 ensembl:ENSMUSP00000026416	C		Seeded From UniProt	complete
enables	GO:0004693	cyclin-dependent protein serine/threonine kinase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P97377 ensembl:ENSMUSP00000026416	F		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P97377 ensembl:ENSMUSP00000026416	F		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P97377 ensembl:ENSMUSP00000026416	F		Seeded From UniProt	complete
part_of	GO:0000806	Y chromosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P97377 ensembl:ENSMUSP00000026416	C		Seeded From UniProt	complete
part_of	GO:0000805	X chromosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P97377 ensembl:ENSMUSP00000026416	C		Seeded From UniProt	complete
part_of	GO:0000793	condensed chromosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P97377 ensembl:ENSMUSP00000026416	C		Seeded From UniProt	complete
part_of	GO:0000781	chromosome, telomeric region	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P97377 ensembl:ENSMUSP00000026416	C		Seeded From UniProt	complete
part_of	GO:0000307	cyclin-dependent protein kinase holoenzyme complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P97377 ensembl:ENSMUSP00000026416	C		Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P97377 ensembl:ENSMUSP00000026416	F		Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P97377 ensembl:ENSMUSP00000026416	P		Seeded From UniProt	complete
involved_in	GO:0000082	G1/S transition of mitotic cell cycle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P97377 ensembl:ENSMUSP00000026416	P		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR008271	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR017441	F		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR008271	P		Seeded From UniProt	complete
enables	GO:0004693	cyclin-dependent protein serine/threonine kinase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.7.11.22	F		Seeded From UniProt	complete
involved_in	GO:0071732	cellular response to nitric oxide	PMID:20079829^[25]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051298	centrosome duplication	PMID:19238148^[26]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031571	mitotic G1 DNA damage checkpoint	PMID:21319273^[27]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051321	meiotic cell cycle	PMID:19238148^[26]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006260	DNA replication	PMID:19238148^[26] Reactome:R-HSA-176318	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005813	centrosome	PMID:19238148^[26]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1901796	regulation of signal transduction by p53 class mediator	Reactome:R-HSA-5633007	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031145	anaphase-promoting complex-dependent catabolic process	Reactome:R-HSA-174143	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006977	DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest	Reactome:R-HSA-69563 Reactome:R-HSA-6791312	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-69191 Reactome:R-HSA-174273 Reactome:R-HSA-174054 Reactome:R-HSA-157906	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-HSA-69562 Reactome:R-HSA-69199 Reactome:R-HSA-69195 Reactome:R-HSA-69005 Reactome:R-HSA-68944 Reactome:R-HSA-68918 Reactome:R-HSA-68917 Reactome:R-HSA-68916 Reactome:R-HSA-6805109 Reactome:R-HSA-6793661 Reactome:R-HSA-5684096 Reactome:R-HSA-5684081 Reactome:R-HSA-4088024 Reactome:R-HSA-3788708 Reactome:R-HSA-3788705 Reactome:R-HSA-188390 Reactome:R-HSA-188386 Reactome:R-HSA-188371 Reactome:R-HSA-188350 Reactome:R-HSA-187959 Reactome:R-HSA-187949 Reactome:R-HSA-187948 Reactome:R-HSA-187937 Reactome:R-HSA-187934 Reactome:R-HSA-187916 Reactome:R-HSA-187575 Reactome:R-HSA-187574 Reactome:R-HSA-187552 Reactome:R-HSA-187520 Reactome:R-HSA-176318 Reactome:R-HSA-176298 Reactome:R-HSA-174273 Reactome:R-HSA-174164 Reactome:R-HSA-174110 Reactome:R-HSA-174079 Reactome:R-HSA-157906 Reactome:R-HSA-1363314 Reactome:R-HSA-1363311 Reactome:R-HSA-1363306 Reactome:R-HSA-1363303	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004693	cyclin-dependent protein serine/threonine kinase activity	Reactome:R-HSA-3788705 Reactome:R-HSA-188390 Reactome:R-HSA-187959 Reactome:R-HSA-187520 Reactome:R-HSA-174079	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0000086	G2/M transition of mitotic cell cycle	Reactome:R-HSA-69275	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000082	G1/S transition of mitotic cell cycle	Reactome:R-HSA-69206	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0206	C		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
enables	GO:0016301	kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539	C		Seeded From UniProt	complete
involved_in	GO:0007049	cell cycle	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0131	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0227	P		Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F		Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0234	P		Seeded From UniProt	complete
part_of	GO:0005768	endosome	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0967 UniProtKB-SubCell:SL-0101	C		Seeded From UniProt	complete
involved_in	GO:0051301	cell division	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0132	P		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
involved_in	GO:0051321	meiotic cell cycle	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0469	P		Seeded From UniProt	complete
involved_in	GO:0016310	phosphorylation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	P		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0723	F		Seeded From UniProt	complete
part_of	GO:0005815	microtubule organizing center	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0048	C		Seeded From UniProt	complete
part_of	GO:0015030	Cajal body	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0031	C		Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ Breuer, D et al. (2012) CDK2 regulates HIV-1 transcription by phosphorylation of CDK9 on serine 90. Retrovirology 9 94 PubMed GONUTS page
↑ Zou, Y et al. (2013) CUL4B promotes replication licensing by up-regulating the CDK2-CDC6 cascade. J. Cell Biol. 200 743-56 PubMed GONUTS page
↑ Russo, AA et al. (1996) Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex. Nature 382 325-31 PubMed GONUTS page
↑ Kutter, S et al. (2016) Regulation of Microtubule Assembly by Tau and not by Pin1. J. Mol. Biol. 428 1742-59 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 Wang, C et al. (2008) A novel endogenous human CaMKII inhibitory protein suppresses tumor growth by inducing cell cycle arrest via p27 stabilization. J. Biol. Chem. 283 11565-74 PubMed GONUTS page
↑ ^6.0 ^6.1 Kriwacki, RW et al. (1996) Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity. Proc. Natl. Acad. Sci. U.S.A. 93 11504-9 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 Lacy, ER et al. (2004) p27 binds cyclin-CDK complexes through a sequential mechanism involving binding-induced protein folding. Nat. Struct. Mol. Biol. 11 358-64 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 Pagano, M et al. (1992) Cyclin A is required at two points in the human cell cycle. EMBO J. 11 961-71 PubMed GONUTS page
↑ Pahel, G et al. (1993) Structural and functional characterization of the HPV16 E7 protein expressed in bacteria. J. Biol. Chem. 268 26018-25 PubMed GONUTS page
↑ ^10.0 ^10.1 McGrath, DA et al. (2017) Structural basis of divergent cyclin-dependent kinase activation by Spy1/RINGO proteins. EMBO J. 36 2251-2262 PubMed GONUTS page
↑ ^11.0 ^11.1 Adkins, JN & Lumb, KJ (2002) Intrinsic structural disorder and sequence features of the cell cycle inhibitor p57Kip2. Proteins 46 1-7 PubMed GONUTS page
↑ Liu, Q et al. (2013) Overexpression of DOC-1R inhibits cell cycle G1/S transition by repressing CDK2 expression and activation. Int. J. Biol. Sci. 9 541-9 PubMed GONUTS page
↑ Terret, ME et al. (2003) DOC1R: a MAP kinase substrate that control microtubule organization of metaphase II mouse oocytes. Development 130 5169-77 PubMed GONUTS page
↑ Kodani, A et al. (2015) Centriolar satellites assemble centrosomal microcephaly proteins to recruit CDK2 and promote centriole duplication. Elife 4 PubMed GONUTS page
↑ Hizli, AA et al. (2013) Phosphorylation of eukaryotic elongation factor 2 (eEF2) by cyclin A-cyclin-dependent kinase 2 regulates its inhibition by eEF2 kinase. Mol. Cell. Biol. 33 596-604 PubMed GONUTS page
↑ Serrano, M et al. (1997) Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a. Cell 88 593-602 PubMed GONUTS page
↑ Chen, S et al. (2010) Cyclin-dependent kinases regulate epigenetic gene silencing through phosphorylation of EZH2. Nat. Cell Biol. 12 1108-14 PubMed GONUTS page
↑ ^18.0 ^18.1 Reardon, JT et al. (1996) Isolation and characterization of two human transcription factor IIH (TFIIH)-related complexes: ERCC2/CAK and TFIIH. Proc. Natl. Acad. Sci. U.S.A. 93 6482-7 PubMed GONUTS page
↑ ^19.0 ^19.1 Tsai, LH et al. (1991) Isolation of the human cdk2 gene that encodes the cyclin A- and adenovirus E1A-associated p33 kinase. Nature 353 174-7 PubMed GONUTS page
↑ Ma, T et al. (2000) Cell cycle-regulated phosphorylation of p220(NPAT) by cyclin E/Cdk2 in Cajal bodies promotes histone gene transcription. Genes Dev. 14 2298-313 PubMed GONUTS page
↑ ^21.0 ^21.1 ^21.2 Laronga, C et al. (2000) Association of the cyclin-dependent kinases and 14-3-3 sigma negatively regulates cell cycle progression. J. Biol. Chem. 275 23106-12 PubMed GONUTS page
↑ Fiset, A et al. (2011) Compartmentalized CDK2 is connected with SHP-1 and β-catenin and regulates insulin internalization. Cell. Signal. 23 911-9 PubMed GONUTS page
↑ Huang, X et al. (2011) Deubiquitinase USP37 is activated by CDK2 to antagonize APC(CDH1) and promote S phase entry. Mol. Cell 42 511-23 PubMed GONUTS page
↑ ^24.0 ^24.1 ^24.2 ^24.3 ^24.4 ^24.5 ^24.6 ^24.7 ^24.8 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Kumar, S et al. (2010) Cdk2 nitrosylation and loss of mitochondrial potential mediate NO-dependent biphasic effect on HL-60 cell cycle. Free Radic. Biol. Med. 48 851-61 PubMed GONUTS page
↑ ^26.0 ^26.1 ^26.2 ^26.3 Malumbres, M & Barbacid, M (2009) Cell cycle, CDKs and cancer: a changing paradigm. Nat. Rev. Cancer 9 153-66 PubMed GONUTS page
↑ Neganova, I et al. (2011) An important role for CDK2 in G1 to S checkpoint activation and DNA damage response in human embryonic stem cells. Stem Cells 29 651-9 PubMed GONUTS page

[PMID:23140174-1] Breuer, D et al. (2012) CDK2 regulates HIV-1 transcription by phosphorylation of CDK9 on serine 90. Retrovirology 9 94 PubMed GONUTS page

[PMID:23479742-2] Zou, Y et al. (2013) CUL4B promotes replication licensing by up-regulating the CDK2-CDC6 cascade. J. Cell Biol. 200 743-56 PubMed GONUTS page

[PMID:8684460-3] Russo, AA et al. (1996) Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex. Nature 382 325-31 PubMed GONUTS page

[PMID:26996940-4] Kutter, S et al. (2016) Regulation of Microtubule Assembly by Tau and not by Pin1. J. Mol. Biol. 428 1742-59 PubMed GONUTS page

[PMID:18305109-5] 5.0 ^5.1 ^5.2 Wang, C et al. (2008) A novel endogenous human CaMKII inhibitory protein suppresses tumor growth by inducing cell cycle arrest via p27 stabilization. J. Biol. Chem. 283 11565-74 PubMed GONUTS page

[PMID:8876165-6] 6.0 ^6.1 Kriwacki, RW et al. (1996) Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity. Proc. Natl. Acad. Sci. U.S.A. 93 11504-9 PubMed GONUTS page

[PMID:15024385-7] 7.0 ^7.1 ^7.2 Lacy, ER et al. (2004) p27 binds cyclin-CDK complexes through a sequential mechanism involving binding-induced protein folding. Nat. Struct. Mol. Biol. 11 358-64 PubMed GONUTS page

[PMID:1312467-8] 8.0 ^8.1 ^8.2 ^8.3 Pagano, M et al. (1992) Cyclin A is required at two points in the human cell cycle. EMBO J. 11 961-71 PubMed GONUTS page

[PMID:8245034-9] Pahel, G et al. (1993) Structural and functional characterization of the HPV16 E7 protein expressed in bacteria. J. Biol. Chem. 268 26018-25 PubMed GONUTS page

[PMID:28666995-10] 10.0 ^10.1 McGrath, DA et al. (2017) Structural basis of divergent cyclin-dependent kinase activation by Spy1/RINGO proteins. EMBO J. 36 2251-2262 PubMed GONUTS page

[PMID:11746698-11] 11.0 ^11.1 Adkins, JN & Lumb, KJ (2002) Intrinsic structural disorder and sequence features of the cell cycle inhibitor p57Kip2. Proteins 46 1-7 PubMed GONUTS page

[PMID:23781148-12] Liu, Q et al. (2013) Overexpression of DOC-1R inhibits cell cycle G1/S transition by repressing CDK2 expression and activation. Int. J. Biol. Sci. 9 541-9 PubMed GONUTS page

[PMID:12944431-13] Terret, ME et al. (2003) DOC1R: a MAP kinase substrate that control microtubule organization of metaphase II mouse oocytes. Development 130 5169-77 PubMed GONUTS page

[PMID:26297806-14] Kodani, A et al. (2015) Centriolar satellites assemble centrosomal microcephaly proteins to recruit CDK2 and promote centriole duplication. Elife 4 PubMed GONUTS page

[PMID:23184662-15] Hizli, AA et al. (2013) Phosphorylation of eukaryotic elongation factor 2 (eEF2) by cyclin A-cyclin-dependent kinase 2 regulates its inhibition by eEF2 kinase. Mol. Cell. Biol. 33 596-604 PubMed GONUTS page

[PMID:9054499-16] Serrano, M et al. (1997) Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a. Cell 88 593-602 PubMed GONUTS page

[PMID:20935635-17] Chen, S et al. (2010) Cyclin-dependent kinases regulate epigenetic gene silencing through phosphorylation of EZH2. Nat. Cell Biol. 12 1108-14 PubMed GONUTS page

[PMID:8692841-18] 18.0 ^18.1 Reardon, JT et al. (1996) Isolation and characterization of two human transcription factor IIH (TFIIH)-related complexes: ERCC2/CAK and TFIIH. Proc. Natl. Acad. Sci. U.S.A. 93 6482-7 PubMed GONUTS page

[PMID:1653904-19] 19.0 ^19.1 Tsai, LH et al. (1991) Isolation of the human cdk2 gene that encodes the cyclin A- and adenovirus E1A-associated p33 kinase. Nature 353 174-7 PubMed GONUTS page

[PMID:10995387-20] Ma, T et al. (2000) Cell cycle-regulated phosphorylation of p220(NPAT) by cyclin E/Cdk2 in Cajal bodies promotes histone gene transcription. Genes Dev. 14 2298-313 PubMed GONUTS page

[PMID:10767298-21] 21.0 ^21.1 ^21.2 Laronga, C et al. (2000) Association of the cyclin-dependent kinases and 14-3-3 sigma negatively regulates cell cycle progression. J. Biol. Chem. 275 23106-12 PubMed GONUTS page

[PMID:21262353-22] Fiset, A et al. (2011) Compartmentalized CDK2 is connected with SHP-1 and β-catenin and regulates insulin internalization. Cell. Signal. 23 911-9 PubMed GONUTS page

[PMID:21596315-23] Huang, X et al. (2011) Deubiquitinase USP37 is activated by CDK2 to antagonize APC(CDH1) and promote S phase entry. Mol. Cell 42 511-23 PubMed GONUTS page

[PMID:21873635-24] 24.0 ^24.1 ^24.2 ^24.3 ^24.4 ^24.5 ^24.6 ^24.7 ^24.8 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:20079829-25] Kumar, S et al. (2010) Cdk2 nitrosylation and loss of mitochondrial potential mediate NO-dependent biphasic effect on HL-60 cell cycle. Free Radic. Biol. Med. 48 851-61 PubMed GONUTS page

[PMID:19238148-26] 26.0 ^26.1 ^26.2 ^26.3 Malumbres, M & Barbacid, M (2009) Cell cycle, CDKs and cancer: a changing paradigm. Nat. Rev. Cancer 9 153-66 PubMed GONUTS page

[PMID:21319273-27] Neganova, I et al. (2011) An important role for CDK2 in G1 to S checkpoint activation and DNA damage response in human embryonic stem cells. Stem Cells 29 651-9 PubMed GONUTS page

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HUMAN:CDK2

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