dbPTM

CDC6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CDC6_HUMAN
UniProt AC	Q99741
Protein Name	Cell division control protein 6 homolog
Gene Name	CDC6
Organism	Homo sapiens (Human).
Sequence Length	560
Subcellular Localization	Nucleus . Cytoplasm . The protein is nuclear in G1 and cytoplasmic in S-phase cells (PubMed:9566895).
Protein Description	Involved in the initiation of DNA replication. Also participates in checkpoint controls that ensure DNA replication is completed before mitosis is initiated..
Protein Sequence	MPQTRSQAQATISFPKRKLSRALNKAKNSSDAKLEPTNVQTVTCSPRVKALPLSPRKRLGDDNLCNTPHLPPCSPPKQGKKENGPPHSHTLKGRRLVFDNQLTIKSPSKRELAKVHQNKILSSVRKSQEITTNSEQRCPLKKESACVRLFKQEGTCYQQAKLVLNTAVPDRLPAREREMDVIRNFLREHICGKKAGSLYLSGAPGTGKTACLSRILQDLKKELKGFKTIMLNCMSLRTAQAVFPAIAQEICQEEVSRPAGKDMMRKLEKHMTAEKGPMIVLVLDEMDQLDSKGQDVLYTLFEWPWLSNSHLVLIGIANTLDLTDRILPRLQAREKCKPQLLNFPPYTRNQIVTILQDRLNQVSRDQVLDNAAVQFCARKVSAVSGDVRKALDVCRRAIEIVESDVKSQTILKPLSECKSPSEPLIPKRVGLIHISQVISEVDGNRMTLSQEGAQDSFPLQQKILVCSLMLLIRQLKIKEVTLGKLYEAYSKVCRKQQVAAVDQSECLSLSGLLEARGILGLKRNKETRLTKVFFKIEEKEIEHALKDKALIGNILATGLP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
20	Phosphorylation	SFPKRKLSRALNKAK HCCHHHHHHHHHHHC	20.67	21406692
25	Ubiquitination	KLSRALNKAKNSSDA HHHHHHHHHCCCCCC	62.68	21906983
27	Ubiquitination	SRALNKAKNSSDAKL HHHHHHHCCCCCCCC	60.00	21906983
33	Ubiquitination	AKNSSDAKLEPTNVQ HCCCCCCCCCCCCCE	59.37	-
37	Phosphorylation	SDAKLEPTNVQTVTC CCCCCCCCCCEEEEC	38.35	23927012
41	Phosphorylation	LEPTNVQTVTCSPRV CCCCCCEEEECCCCC	17.31	29255136
43	Phosphorylation	PTNVQTVTCSPRVKA CCCCEEEECCCCCEE	15.62	23401153
45	Phosphorylation	NVQTVTCSPRVKALP CCEEEECCCCCEECC	13.33	29255136
49	Ubiquitination	VTCSPRVKALPLSPR EECCCCCEECCCCCC	45.55	-
54	Phosphorylation	RVKALPLSPRKRLGD CCEECCCCCCCCCCC	22.25	9889196
67	Phosphorylation	GDDNLCNTPHLPPCS CCCCCCCCCCCCCCC	15.87	25159151
74	Phosphorylation	TPHLPPCSPPKQGKK CCCCCCCCCCCCCCC	50.43	9889196
88	Phosphorylation	KENGPPHSHTLKGRR CCCCCCCCCCCCCCE	24.76	25159151
90	Phosphorylation	NGPPHSHTLKGRRLV CCCCCCCCCCCCEEE	32.93	20860994
92	Acetylation	PPHSHTLKGRRLVFD CCCCCCCCCCEEEEC	52.07	19343071
92	Ubiquitination	PPHSHTLKGRRLVFD CCCCCCCCCCEEEEC	52.07	-
103	Phosphorylation	LVFDNQLTIKSPSKR EEECCCEEECCCCHH	19.32	24732914
105	Acetylation	FDNQLTIKSPSKREL ECCCEEECCCCHHHH	51.59	19343071
106	Phosphorylation	DNQLTIKSPSKRELA CCCEEECCCCHHHHH	30.47	9889196
108	Phosphorylation	QLTIKSPSKRELAKV CEEECCCCHHHHHHH	51.97	24732914
109	Acetylation	LTIKSPSKRELAKVH EEECCCCHHHHHHHH	53.96	19343071
114	Ubiquitination	PSKRELAKVHQNKIL CCHHHHHHHHHHHHH	53.53	-
119	Ubiquitination	LAKVHQNKILSSVRK HHHHHHHHHHHHHHH	38.15	-
122	Phosphorylation	VHQNKILSSVRKSQE HHHHHHHHHHHHHHC	30.20	24732914
123	Phosphorylation	HQNKILSSVRKSQEI HHHHHHHHHHHHHCC	23.61	24732914
126	Ubiquitination	KILSSVRKSQEITTN HHHHHHHHHHCCCCC	55.10	-
127	Phosphorylation	ILSSVRKSQEITTNS HHHHHHHHHCCCCCC	23.60	25159151
131	Phosphorylation	VRKSQEITTNSEQRC HHHHHCCCCCCCCCC	21.12	24732914
132	Phosphorylation	RKSQEITTNSEQRCP HHHHCCCCCCCCCCC	42.27	24732914
134	Phosphorylation	SQEITTNSEQRCPLK HHCCCCCCCCCCCCC	32.77	21815630
151	Acetylation	SACVRLFKQEGTCYQ HHHHHHHHCCCCHHH	52.62	26051181
151	Sumoylation	SACVRLFKQEGTCYQ HHHHHHHHCCCCHHH	52.62	-
151	Sumoylation	SACVRLFKQEGTCYQ HHHHHHHHCCCCHHH	52.62	-
151	Ubiquitination	SACVRLFKQEGTCYQ HHHHHHHHCCCCHHH	52.62	-
166	Phosphorylation	QAKLVLNTAVPDRLP HHHHHHCCCCCCCCC	25.52	29632367
194	Ubiquitination	REHICGKKAGSLYLS HHHHCCCCCCCEEEC	43.17	-
199	Phosphorylation	GKKAGSLYLSGAPGT CCCCCCEEECCCCCC	10.66	29496907
208	Ubiquitination	SGAPGTGKTACLSRI CCCCCCCHHHHHHHH	32.55	-
220	Ubiquitination	SRILQDLKKELKGFK HHHHHHHHHHHCCCC	53.11	-
221	Ubiquitination	RILQDLKKELKGFKT HHHHHHHHHHCCCCH	75.48	-
235	Phosphorylation	TIMLNCMSLRTAQAV HHHHHHCCHHHHHHH	19.52	29083192
261	Ubiquitination	EVSRPAGKDMMRKLE HCCCHHHHHHHHHHH	44.55	-
379	Ubiquitination	AVQFCARKVSAVSGD HHHHHHHHHHHCCCH	23.24	-
381	Phosphorylation	QFCARKVSAVSGDVR HHHHHHHHHCCCHHH	26.45	20068231
384	Phosphorylation	ARKVSAVSGDVRKAL HHHHHHCCCHHHHHH	29.06	20068231
389	Ubiquitination	AVSGDVRKALDVCRR HCCCHHHHHHHHHHH	53.82	-
406	Ubiquitination	EIVESDVKSQTILKP HHHHCCCCCCCCCCC	41.66	-
407	Phosphorylation	IVESDVKSQTILKPL HHHCCCCCCCCCCCH	32.19	24732914
409	Phosphorylation	ESDVKSQTILKPLSE HCCCCCCCCCCCHHH	35.05	29214152
412	Ubiquitination	VKSQTILKPLSECKS CCCCCCCCCHHHCCC	39.81	-
415	Phosphorylation	QTILKPLSECKSPSE CCCCCCHHHCCCCCC	49.85	24732914
418	Ubiquitination	LKPLSECKSPSEPLI CCCHHHCCCCCCCCC	62.44	-
419	Phosphorylation	KPLSECKSPSEPLIP CCHHHCCCCCCCCCC	45.37	25159151
421	Phosphorylation	LSECKSPSEPLIPKR HHHCCCCCCCCCCCC	59.96	21815630
427	Ubiquitination	PSEPLIPKRVGLIHI CCCCCCCCCEEEEEH	53.36	-
478	Ubiquitination	LIRQLKIKEVTLGKL HHHHHCCCCCHHHHH	44.54	-
481	Phosphorylation	QLKIKEVTLGKLYEA HHCCCCCHHHHHHHH	30.77	-
484	Ubiquitination	IKEVTLGKLYEAYSK CCCCHHHHHHHHHHH	51.51	-
491	Ubiquitination	KLYEAYSKVCRKQQV HHHHHHHHHHHHHHC	32.45	-
495	Ubiquitination	AYSKVCRKQQVAAVD HHHHHHHHHHCEEEC	39.70	-
527	Phosphorylation	GLKRNKETRLTKVFF CCCCCCCCCCEEEEE	32.37	22210691
531	Ubiquitination	NKETRLTKVFFKIEE CCCCCCEEEEEEECH	41.45	-
535	Ubiquitination	RLTKVFFKIEEKEIE CCEEEEEEECHHHHH	37.43	-
539	Ubiquitination	VFFKIEEKEIEHALK EEEEECHHHHHHHHH	51.72	-
546	Ubiquitination	KEIEHALKDKALIGN HHHHHHHHCHHHHHH	58.95	-
548	Ubiquitination	IEHALKDKALIGNIL HHHHHHCHHHHHHHH	43.43	-

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
37	T	Phosphorylation	Kinase	PLK1	P53350	PSP
54	S	Phosphorylation	Kinase	CDK2	P24941	PSP
74	S	Phosphorylation	Kinase	CDK2	P24941	PSP
106	S	Phosphorylation	Kinase	CDK2	P24941	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	FZR1	Q9UM11	PMID:10995389
-	K	Ubiquitination	E3 ubiquitin ligase	CCNF	P41002	PMID:26818844
-	K	Ubiquitination	E3 ubiquitin ligase	HUWE1	Q7Z6Z7	PMID:18617514
-	K	Ubiquitination	E3 ubiquitin ligase	TOM1	O60784	PMID:23129771
-	K	Ubiquitination	E3 ubiquitin ligase	DTL	Q9NZJ0	PMID:24434580

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CDC6_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 CDC6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
P2R3B_HUMAN	PPP2R3B	physical	10629059
ORC2_HUMAN	ORC2	physical	12614612
ORC1_HUMAN	ORC1	physical	12614612
MCM7_HUMAN	MCM7	physical	12614612
KPSH1_HUMAN	PSKH1	physical	9889196
CCNA2_HUMAN	CCNA2	physical	9889196
MYC_HUMAN	MYC	physical	10899308
ORC1_HUMAN	ORC1	physical	9566895
CDK2_HUMAN	CDK2	physical	9566895
CCNA2_HUMAN	CCNA2	physical	9566895
MCM3_HUMAN	MCM3	physical	10464337
MCM7_HUMAN	MCM7	physical	10464337
MCM3_HUMAN	MCM3	physical	11046155
ORC2_HUMAN	ORC2	physical	11046155
P2R3A_HUMAN	PPP2R3A	physical	18397887
MCM8_HUMAN	MCM8	physical	15684404
HUWE1_HUMAN	HUWE1	physical	17567951
ATR_HUMAN	ATR	physical	20048340
ATM_HUMAN	ATM	physical	20048340
ATRIP_HUMAN	ATRIP	physical	20048340
ATR_XENLA	atr	physical	20048340
BMI1_HUMAN	BMI1	physical	19462008
CCL2_HUMAN	CCL2	physical	21383955
FZR1_HUMAN	FZR1	physical	14701726
CDC20_HUMAN	CDC20	physical	14701726
ORC1_HUMAN	ORC1	physical	15232106
ORC2_HUMAN	ORC2	physical	15232106
MCM10_HUMAN	MCM10	physical	15232106
MCM2_HUMAN	MCM2	physical	15232106
ORC3_HUMAN	ORC3	physical	15232106
CDN2A_HUMAN	CDKN2A	physical	15232106
ARF_HUMAN	CDKN2A	physical	15232106
CDN1A_HUMAN	CDKN1A	physical	15232106
MCM3_HUMAN	MCM3	physical	15232106
UBE2K_HUMAN	UBE2K	physical	21988832
DPOLA_HUMAN	POLA1	physical	26344197
CDN1A_HUMAN	CDKN1A	physical	25241761
CCNF_HUMAN	CCNF	physical	26818844
GRWD1_HUMAN	GRWD1	physical	25990725

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613805	Meier-Gorlin syndrome 5 (MGORS5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CDC6_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-45, AND MASSSPECTROMETRY.	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-45, 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-45 AND SER-54, AND MASSSPECTROMETRY.	18691976 [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-166, AND MASSSPECTROMETRY.	17924679 [Abstract]