dbPTM

CCNE1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CCNE1_HUMAN
UniProt AC	P24864
Protein Name	G1/S-specific cyclin-E1
Gene Name	CCNE1
Organism	Homo sapiens (Human).
Sequence Length	410
Subcellular Localization	Nucleus .
Protein Description	Essential for the control of the cell cycle at the G1/S (start) transition..
Protein Sequence	MPRERRERDAKERDTMKEDGGAEFSARSRKRKANVTVFLQDPDEEMAKIDRTARDQCGSQPWDNNAVCADPCSLIPTPDKEDDDRVYPNSTCKPRIIAPSRGSPLPVLSWANREEVWKIMLNKEKTYLRDQHFLEQHPLLQPKMRAILLDWLMEVCEVYKLHRETFYLAQDFFDRYMATQENVVKTLLQLIGISSLFIAAKLEEIYPPKLHQFAYVTDGACSGDEILTMELMIMKALKWRLSPLTIVSWLNVYMQVAYLNDLHEVLLPQYPQQIFIQIAELLDLCVLDVDCLEFPYGILAASALYHFSSSELMQKVSGYQWCDIENCVKWMVPFAMVIRETGSSKLKHFRGVADEDAHNIQTHRDSLDLLDKARAKKAMLSEQNRASPLPSGLLTPPQSGKKQSSGPEMA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
59	Phosphorylation	TARDQCGSQPWDNNA HHHHHHCCCCCCCCC	40.47	17525332
73	Phosphorylation	AVCADPCSLIPTPDK CCCCCCCCCCCCCCC	34.42	14536078
77	Phosphorylation	DPCSLIPTPDKEDDD CCCCCCCCCCCCCCC	36.81	15364936
87	Phosphorylation	KEDDDRVYPNSTCKP CCCCCCCCCCCCCCC	9.52	24719451
90	Phosphorylation	DDRVYPNSTCKPRII CCCCCCCCCCCCEEE	30.58	22817900
91	Phosphorylation	DRVYPNSTCKPRIIA CCCCCCCCCCCEEEC	31.05	28634298
100	Phosphorylation	KPRIIAPSRGSPLPV CCEEECCCCCCCCCC	40.01	30266825
103	Phosphorylation	IIAPSRGSPLPVLSW EECCCCCCCCCCCEE	23.35	19664994
109	Phosphorylation	GSPLPVLSWANREEV CCCCCCCEECCHHHH	25.11	28152594
366	Phosphorylation	NIQTHRDSLDLLDKA HHHHCHHHHHHHHHH	24.60	18691976
381	Phosphorylation	RAKKAMLSEQNRASP HHHHHHHCCCCCCCC	24.85	23898821
387	Phosphorylation	LSEQNRASPLPSGLL HCCCCCCCCCCCCCC	24.59	30266825
391	Phosphorylation	NRASPLPSGLLTPPQ CCCCCCCCCCCCCCC	50.16	30266825
395	Phosphorylation	PLPSGLLTPPQSGKK CCCCCCCCCCCCCCC	37.66	19276368
399	Phosphorylation	GLLTPPQSGKKQSSG CCCCCCCCCCCCCCC	59.35	17192257

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
73	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
77	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
387	S	Phosphorylation	Kinase	CDK2	P24941	PSP
395	T	Phosphorylation	Kinase	CDK2	P24941	PSP
395	T	Phosphorylation	Kinase	GSK3A	P49840	PSP
395	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
395	T	Phosphorylation	Kinase	GSK-FAMILY	-	GPS
395	T	Phosphorylation	Kinase	GSK3	-	Uniprot
399	S	Phosphorylation	Kinase	CDK1	P06493	PSP
399	S	Phosphorylation	Kinase	CDK2	P24941	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:18851830
-	K	Ubiquitination	E3 ubiquitin ligase	UHRF2	Q96PU4	PMID:21952639
-	K	Ubiquitination	E3 ubiquitin ligase	RHOBTB3	O94955	PMID:24145166
-	K	Ubiquitination	E3 ubiquitin ligase	SKP2	Q13309	PMID:10790373
-	K	Ubiquitination	E3 ubiquitin ligase	PRKN	O60260	PMID:12628165
-	K	Ubiquitination	E3 ubiquitin ligase	FBXW7	Q969H0	PMID:11533444
-	K	Ubiquitination	E3 ubiquitin ligase	MDM2	Q00987	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	FBXW2	Q9UKT8	PMID:17298674
-	K	Ubiquitination	E3 ubiquitin ligase	SPOP	O43791	PMID:30237511

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
77	T	Phosphorylation	14536078
Phosphorylation at Thr-77 creates a low affinity degron also recognized by FBXW7.
395	T	Phosphorylation	8861947
Phosphorylation of both Thr-395 by GSK3 and Ser-399 by CDK2 creates a high affinity degron recognized by FBXW7, and accelerates degradation via the ubiquitin proteasome pathway.
395	T	ubiquitylation	8861947
Phosphorylation of both Thr-395 by GSK3 and Ser-399 by CDK2 creates a high affinity degron recognized by FBXW7, and accelerates degradation via the ubiquitin proteasome pathway.
399	S	Phosphorylation	14536078
Phosphorylation of both Thr-395 by GSK3 and Ser-399 by CDK2 creates a high affinity degron recognized by FBXW7, and accelerates degradation via the ubiquitin proteasome pathway.
399	S	ubiquitylation	14536078
Phosphorylation of both Thr-395 by GSK3 and Ser-399 by CDK2 creates a high affinity degron recognized by FBXW7, and accelerates degradation via the ubiquitin proteasome pathway.

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 CCNE1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CUL3_HUMAN	CUL3	physical	10500095
CDK2_HUMAN	CDK2	physical	12839982
CDN1A_HUMAN	CDKN1A	physical	12839982
SMCA4_HUMAN	SMARCA4	physical	11085541
SF3B1_HUMAN	SF3B1	physical	9891079
RBL2_HUMAN	RBL2	physical	9891079
RBL1_HUMAN	RBL1	physical	9891079
MPIP1_HUMAN	CDC25A	physical	9891079
E2F4_HUMAN	E2F4	physical	9891079
CDK2_HUMAN	CDK2	physical	9891079
CDN1B_HUMAN	CDKN1B	physical	9891079
SMRC1_HUMAN	SMARCC1	physical	9891079
CDK1_HUMAN	CDK1	physical	9891079
SMCA4_HUMAN	SMARCA4	physical	9891079
SNF5_HUMAN	SMARCB1	physical	9891079
SMCA2_HUMAN	SMARCA2	physical	9891079
CDK1_HUMAN	CDK1	physical	1388288
CDK2_HUMAN	CDK2	physical	1388288
HERC5_HUMAN	HERC5	physical	10581175
CDK2_HUMAN	CDK2	physical	15004009
RRN3_HUMAN	RRN3	physical	15004009
ANDR_HUMAN	AR	physical	10953010
SKP2_HUMAN	SKP2	physical	11237742
COIL_HUMAN	COIL	physical	10751146
CDK2_HUMAN	CDK2	physical	12529437
CDN1B_HUMAN	CDKN1B	physical	12529437
CUL3_HUMAN	CUL3	physical	17192413
FOXM1_HUMAN	FOXM1	physical	15024056
CDN1A_HUMAN	CDKN1A	physical	17293600
CDN1B_HUMAN	CDKN1B	physical	17293600
CDK2_HUMAN	CDK2	physical	20837141
CDN1B_HUMAN	CDKN1B	physical	20837141
UHRF2_HUMAN	UHRF2	physical	21952639
CDK2_HUMAN	CDK2	physical	16223725
PIN1_HUMAN	PIN1	physical	16223725
CDN1B_MOUSE	Cdkn1b	physical	15980415
CDK2_HUMAN	CDK2	physical	21372285
SKP2_MOUSE	Skp2	physical	10790373
CDK2_HUMAN	CDK2	physical	17970072
CDK2_HUMAN	CDK2	physical	17431037
CDK2_HUMAN	CDK2	physical	17361108
H10_HUMAN	H1F0	physical	17361108
H15_HUMAN	HIST1H1B	physical	15670215
NPAT_HUMAN	NPAT	physical	15555599
TBG1_HUMAN	TUBG1	physical	15514162
CETN1_HUMAN	CETN1	physical	15514162
CDK2_HUMAN	CDK2	physical	15514162
H15_HUMAN	HIST1H1B	physical	15514162
CDK2_HUMAN	CDK2	physical	14701826
CDK2_HUMAN	CDK2	physical	12800980
NBN_HUMAN	NBN	physical	12607005
MRE11_HUMAN	MRE11A	physical	12607005
RB_HUMAN	RB1	physical	10499802
CDN1B_HUMAN	CDKN1B	physical	10393546
CDN1B_MOUSE	Cdkn1b	physical	10393546
H11_HUMAN	HIST1H1A	physical	10393546
RB_HUMAN	RB1	physical	10359664
MARCS_HUMAN	MARCKS	physical	10359664
H11_HUMAN	HIST1H1A	physical	9840927
H11_HUMAN	HIST1H1A	physical	22158041
CDK2_HUMAN	CDK2	physical	9716181
CDK6_HUMAN	CDK6	physical	9716181
CDK4_HUMAN	CDK4	physical	9716181
CDN1A_HUMAN	CDKN1A	physical	9716181
CDN1B_HUMAN	CDKN1B	physical	9716181
CDN1A_HUMAN	CDKN1A	physical	9632134
CDN1B_HUMAN	CDKN1B	physical	9632134
H11_HUMAN	HIST1H1A	physical	9632134
CDN1A_HUMAN	CDKN1A	physical	9380407
H11_HUMAN	HIST1H1A	physical	9380407
CDN1A_HUMAN	CDKN1A	physical	9218599
CDN1B_HUMAN	CDKN1B	physical	9218599
CDK2_HUMAN	CDK2	physical	9192873
CDN1B_HUMAN	CDKN1B	physical	9192873
H11_HUMAN	HIST1H1A	physical	9053846
RB_HUMAN	RB1	physical	9053846
CDK1_HUMAN	CDK1	physical	9053846
H11_HUMAN	HIST1H1A	physical	8647086
RB_HUMAN	RB1	physical	8647086
CDN1B_HUMAN	CDKN1B	physical	8978686
CDK2_HUMAN	CDK2	physical	8978686
CDN1A_HUMAN	CDKN1A	physical	13678583
FBXW7_HUMAN	FBXW7	physical	15364936
H15_HUMAN	HIST1H1B	physical	19318554
CDK2_HUMAN	CDK2	physical	18559665
CUL4B_HUMAN	CUL4B	physical	16322693
CDK2_HUMAN	CDK2	physical	11940657
CDN1B_HUMAN	CDKN1B	physical	11940657
H11_HUMAN	HIST1H1A	physical	11940657
FBXW7_HUMAN	FBXW7	physical	11565034
PRC1_HUMAN	PRC1	physical	9885575
RB_HUMAN	RB1	physical	9885575
H11_HUMAN	HIST1H1A	physical	9885575
UBF1_HUMAN	UBTF	physical	10202152
DPOD1_HUMAN	POLD1	physical	9545286
CDK2_HUMAN	CDK2	physical	21092281
CDK2_HUMAN	CDK2	physical	17254967
CDN1B_HUMAN	CDKN1B	physical	17254967
RB_HUMAN	RB1	physical	9190208
CDN1A_HUMAN	CDKN1A	physical	8756624
CDN1B_HUMAN	CDKN1B	physical	8756624
E2F1_HUMAN	E2F1	physical	12096339
CDN1A_HUMAN	CDKN1A	physical	9660939
CDK2_HUMAN	CDK2	physical	9660939
CDN1B_HUMAN	CDKN1B	physical	9660939
H15_HUMAN	HIST1H1B	physical	8662825
CDK2_HUMAN	CDK2	physical	8662825
P73_HUMAN	TP73	physical	12676926
RB_HUMAN	RB1	physical	12676926
CDC6_HUMAN	CDC6	physical	10339564
H11_HUMAN	HIST1H1A	physical	9886493
NPAT_HUMAN	NPAT	physical	9472014
CDK2_HUMAN	CDK2	physical	9472014
FOXM1_HUMAN	FOXM1	physical	16504183
CDK2_HUMAN	CDK2	physical	19470470
CDN1B_HUMAN	CDKN1B	physical	19470470
CTNB1_HUMAN	CTNNB1	physical	14985333
RB_HUMAN	RB1	physical	9139732
MYBB_HUMAN	MYBL2	physical	10593981
CDN1B_HUMAN	CDKN1B	physical	17254966
RB_HUMAN	RB1	physical	10486249
CDN1A_HUMAN	CDKN1A	physical	21988832
RHBT3_HUMAN	RHOBTB3	physical	24145166
CDK2_HUMAN	CDK2	physical	15980415
CDK2_HUMAN	CDK2	physical	21241890
CDN1B_HUMAN	CDKN1B	physical	25241761
CDN1A_HUMAN	CDKN1A	physical	25241761
GSK3B_HUMAN	GSK3B	physical	25241761
KLF10_HUMAN	KLF10	physical	25728284
CDK2_HUMAN	CDK2	physical	25728284
FBXW7_HUMAN	FBXW7	physical	14739463
CUL3_HUMAN	CUL3	physical	27477274
H11_HUMAN	HIST1H1A	physical	11160398
CDK2_HUMAN	CDK2	physical	28137908

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 CCNE1_HUMAN

Related Literatures of Post-Translational Modification

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 SER-100; SER-103; SER-381;SER-387 AND THR-395, 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 SER-103; SER-387 ANDTHR-395, 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-59, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Multisite phosphorylation by Cdk2 and GSK3 controls cyclin Edegradation."; Welcker M., Singer J., Loeb K.R., Grim J., Bloecher A.,Gurien-West M., Clurman B.E., Roberts J.M.; Mol. Cell 12:381-392(2003). Cited for: PHOSPHORYLATION AT THR-77; SER-387; THR-395 AND SER-399.	14536078 [Abstract]
"Activation of cyclin E/CDK2 is coupled to site-specificautophosphorylation and ubiquitin-dependent degradation of cyclin E."; Won K.A., Reed S.I.; EMBO J. 15:4182-4193(1996). Cited for: PHOSPHORYLATION AT THR-395.	8861947 [Abstract]

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