dbPTM

CCNE2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CCNE2_HUMAN
UniProt AC	O96020
Protein Name	G1/S-specific cyclin-E2
Gene Name	CCNE2
Organism	Homo sapiens (Human).
Sequence Length	404
Subcellular Localization	Nucleus .
Protein Description	Essential for the control of the cell cycle at the late G1 and early S phase..
Protein Sequence	MSRRSSRLQAKQQPQPSQTESPQEAQIIQAKKRKTTQDVKKRREEVTKKHQYEIRNCWPPVLSGGISPCIIIETPHKEIGTSDFSRFTNYRFKNLFINPSPLPDLSWGCSKEVWLNMLKKESRYVHDKHFEVLHSDLEPQMRSILLDWLLEVCEVYTLHRETFYLAQDFFDRFMLTQKDINKNMLQLIGITSLFIASKLEEIYAPKLQEFAYVTDGACSEEDILRMELIILKALKWELCPVTIISWLNLFLQVDALKDAPKVLLPQYSQETFIQIAQLLDLCILAIDSLEFQYRILTAAALCHFTSIEVVKKASGLEWDSISECVDWMVPFVNVVKSTSPVKLKTFKKIPMEDRHNIQTHTNYLAMLEEVNYINTFRKGGQLSPVCNGGIMTPPKSTEKPPGKH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
17	Phosphorylation	AKQQPQPSQTESPQE HHCCCCCCCCCCHHH	44.48	29255136
19	Phosphorylation	QQPQPSQTESPQEAQ CCCCCCCCCCHHHHH	42.65	30266825
21	Phosphorylation	PQPSQTESPQEAQII CCCCCCCCHHHHHHH	34.96	29255136
31 (in isoform 2)	Ubiquitination	-	36.41	21906983
31 (in isoform 1)	Ubiquitination	-	36.41	21906983
31	Ubiquitination	EAQIIQAKKRKTTQD HHHHHHHHHCCCHHH	36.41	2190698
35	O-linked_Glycosylation	IQAKKRKTTQDVKKR HHHHHCCCHHHHHHH	33.45	30620550
36	O-linked_Glycosylation	QAKKRKTTQDVKKRR HHHHCCCHHHHHHHH	26.30	30620550
49	Ubiquitination	RREEVTKKHQYEIRN HHHHHHHHHHHHHHH	26.95	-
63	Phosphorylation	NCWPPVLSGGISPCI HCCCCCCCCCCCCEE	34.90	18691976
67	Phosphorylation	PVLSGGISPCIIIET CCCCCCCCCEEEEEC	19.59	28464451
74	Phosphorylation	SPCIIIETPHKEIGT CCEEEEECCCCCCCC	21.93	22817900
81	Phosphorylation	TPHKEIGTSDFSRFT CCCCCCCCCCCHHHH	30.68	28122231
82	Phosphorylation	PHKEIGTSDFSRFTN CCCCCCCCCCHHHHC	31.29	28122231
297	Phosphorylation	EFQYRILTAAALCHF HHHHHHHHHHHHHHH	16.33	28787133
337	Phosphorylation	PFVNVVKSTSPVKLK HHHEECCCCCCCCCC	23.62	26074081
338	Phosphorylation	FVNVVKSTSPVKLKT HHEECCCCCCCCCCE	31.19	26074081
339	Phosphorylation	VNVVKSTSPVKLKTF HEECCCCCCCCCCEE	34.48	26074081
359	Phosphorylation	EDRHNIQTHTNYLAM HHCCCCCHHHHHHHH	27.20	27067055
372	Phosphorylation	AMLEEVNYINTFRKG HHHHHHCCHHCCCCC	10.75	27067055
375	Phosphorylation	EEVNYINTFRKGGQL HHHCCHHCCCCCCCC	18.43	27067055
383	Phosphorylation	FRKGGQLSPVCNGGI CCCCCCCCCCCCCCC	13.85	25159151
392	Phosphorylation	VCNGGIMTPPKSTEK CCCCCCCCCCCCCCC	34.22	25159151
396	Phosphorylation	GIMTPPKSTEKPPGK CCCCCCCCCCCCCCC	47.80	18691976
397	Phosphorylation	IMTPPKSTEKPPGKH CCCCCCCCCCCCCCC	54.90	26074081

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
-	K	Ubiquitination	E3 ubiquitin ligase	FBXW7	Q969H0	PMID:19084516
-	K	Ubiquitination	E3 ubiquitin ligase	PRKN	O60260	PMID:12628165
-	K	Ubiquitination	E3 ubiquitin ligase	FBXW2	Q9UKT8	PMID:17298674

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CCNE2_HUMAN !!

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 CCNE2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CDK2_HUMAN	CDK2	physical	9858585
FBXW7_HUMAN	FBXW7	physical	19084516
H11_HUMAN	HIST1H1A	physical	9840927
CDK2_HUMAN	CDK2	physical	9840927
CDN1B_HUMAN	CDKN1B	physical	9840927
CDN1A_HUMAN	CDKN1A	physical	9840927
A4_HUMAN	APP	physical	21832049
CDK2_HUMAN	CDK2	physical	9840943
ORC3_HUMAN	ORC3	physical	15232106
CDK2_HUMAN	CDK2	physical	15232106
CDN1A_HUMAN	CDKN1A	physical	15232106
CDN1A_HUMAN	CDKN1A	physical	26186194
CDN1A_HUMAN	CDKN1A	physical	28514442

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 CCNE2_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-21, AND MASSSPECTROMETRY.	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-19 AND SER-21, AND MASSSPECTROMETRY.	19369195 [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-21, AND MASSSPECTROMETRY.	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-21; SER-383 AND THR-392,AND MASS SPECTROMETRY.	18691976 [Abstract]