dbPTM

CDT1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CDT1_HUMAN
UniProt AC	Q9H211
Protein Name	DNA replication factor Cdt1
Gene Name	CDT1 {ECO:0000312\|EMBL:AAG45181.1}
Organism	Homo sapiens (Human).
Sequence Length	546
Subcellular Localization	Nucleus . Chromosome, centromere, kinetochore . Transiently localizes to kinetochores during prometaphase and metaphase.
Protein Description	Required for both DNA replication and mitosis. [PubMed: 11125146]
Protein Sequence	MEQRRVTDFFARRRPGPPRIAPPKLACRTPSPARPALRAPASATSGSRKRARPPAAPGRDQARPPARRRLRLSVDEVSSPSTPEAPDIPACPSPGQKIKKSTPAAGQPPHLTSAQDQDTISELASCLQRARELGARVRALKASAQDAGESCTPEAEGRPEEPCGEKAPAYQRFHALAQPGLPGLVLPYKYQVLAEMFRSMDTIVGMLHNRSETPTFAKVQRGVQDMMRRRFEECNVGQIKTVYPASYRFRQERSVPTFKDGTRRSDYQLTIEPLLEQEADGAAPQLTASRLLQRRQIFSQKLVEHVKEHHKAFLASLSPAMVVPEDQLTRWHPRFNVDEVPDIEPAALPQPPATEKLTTAQEVLARARNLISPRMEKALSQLALRSAAPSSPGSPRPALPATPPATPPAASPSALKGVSQDLLERIRAKEAQKQLAQMTRCPEQEQRLQRLERLPELARVLRSVFVSERKPALSMEVACARMVGSCCTIMSPGEMEKHLLLLSELLPDWLSLHRIRTDTYVKLDKAADLAHITARLAHQTRAEEGL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MEQRRVTDFFARRR -CCCCHHHHHHHHCC	25.85	28555341
24	Ubiquitination	PPRIAPPKLACRTPS CCCCCCCCCCCCCCC	47.89	27667366
24	Acetylation	PPRIAPPKLACRTPS CCCCCCCCCCCCCCC	47.89	19276081
29	Phosphorylation	PPKLACRTPSPARPA CCCCCCCCCCCCCCH	28.18	30266825
31	Phosphorylation	KLACRTPSPARPALR CCCCCCCCCCCCHHH	30.49	30266825
42	Phosphorylation	PALRAPASATSGSRK CHHHCCCCCCCCCCC	30.90	26074081
44	Phosphorylation	LRAPASATSGSRKRA HHCCCCCCCCCCCCC	31.00	26074081
45	Phosphorylation	RAPASATSGSRKRAR HCCCCCCCCCCCCCC	34.19	26074081
47	Phosphorylation	PASATSGSRKRARPP CCCCCCCCCCCCCCC	34.10	26074081
49	Acetylation	SATSGSRKRARPPAA CCCCCCCCCCCCCCC	52.70	19276081
73	Phosphorylation	ARRRLRLSVDEVSSP HHHHHCEECCCCCCC	22.53	23401153
78	Phosphorylation	RLSVDEVSSPSTPEA CEECCCCCCCCCCCC	34.19	28450419
79	Phosphorylation	LSVDEVSSPSTPEAP EECCCCCCCCCCCCC	28.22	28464451
81	Phosphorylation	VDEVSSPSTPEAPDI CCCCCCCCCCCCCCC	59.55	28450419
82	Phosphorylation	DEVSSPSTPEAPDIP CCCCCCCCCCCCCCC	28.65	28450419
93	Phosphorylation	PDIPACPSPGQKIKK CCCCCCCCCCCCCCC	41.36	21856198
101	Phosphorylation	PGQKIKKSTPAAGQP CCCCCCCCCCCCCCC	34.32	26074081
102	Phosphorylation	GQKIKKSTPAAGQPP CCCCCCCCCCCCCCC	26.31	22199227
112	Phosphorylation	AGQPPHLTSAQDQDT CCCCCCCCCCCCHHH	20.98	26074081
113	Phosphorylation	GQPPHLTSAQDQDTI CCCCCCCCCCCHHHH	30.23	26074081
141	Sumoylation	GARVRALKASAQDAG HHHHHHHHHHHHHHH	39.03	-
141	Ubiquitination	GARVRALKASAQDAG HHHHHHHHHHHHHHH	39.03	21963094
141	Sumoylation	GARVRALKASAQDAG HHHHHHHHHHHHHHH	39.03	-
143	Phosphorylation	RVRALKASAQDAGES HHHHHHHHHHHHHHC	25.52	-
150	Phosphorylation	SAQDAGESCTPEAEG HHHHHHHCCCCCCCC	23.52	28450419
152	Phosphorylation	QDAGESCTPEAEGRP HHHHHCCCCCCCCCC	33.18	28450419
166	Ubiquitination	PEEPCGEKAPAYQRF CCCCCCCCCCHHHHH	44.98	21963094
189	Ubiquitination	PGLVLPYKYQVLAEM CCCCCCHHHHHHHHH	27.54	23503661
211	Phosphorylation	VGMLHNRSETPTFAK HHHHCCCCCCCHHHH	51.65	24719451
213	Phosphorylation	MLHNRSETPTFAKVQ HHCCCCCCCHHHHHH	28.95	28674419
218	Ubiquitination	SETPTFAKVQRGVQD CCCCHHHHHHHHHHH	34.41	33845483
240	Ubiquitination	ECNVGQIKTVYPASY HCCCCCEEEEEECCH	24.85	21890473
259	Sumoylation	ERSVPTFKDGTRRSD CCCCCCCCCCCCCCC	58.70	-
259	Sumoylation	ERSVPTFKDGTRRSD CCCCCCCCCCCCCCC	58.70	-
259	Ubiquitination	ERSVPTFKDGTRRSD CCCCCCCCCCCCCCC	58.70	32015554
301	Ubiquitination	RRQIFSQKLVEHVKE HHHHHHHHHHHHHHH	53.99	29967540
307	Ubiquitination	QKLVEHVKEHHKAFL HHHHHHHHHHHHHHH	53.92	21906983
311	Ubiquitination	EHVKEHHKAFLASLS HHHHHHHHHHHHHCC	42.62	22817900
316	Phosphorylation	HHKAFLASLSPAMVV HHHHHHHHCCCCEEC	31.37	29255136
318	Phosphorylation	KAFLASLSPAMVVPE HHHHHHCCCCEECCH	14.23	29255136
329	Phosphorylation	VVPEDQLTRWHPRFN ECCHHHHHHCCCCCC	26.53	29396449
356	Ubiquitination	PQPPATEKLTTAQEV CCCCCCCCCCHHHHH	46.94	21906983
358	Phosphorylation	PPATEKLTTAQEVLA CCCCCCCCHHHHHHH	31.02	28509920
359	Phosphorylation	PATEKLTTAQEVLAR CCCCCCCHHHHHHHH	36.46	28509920
372	Phosphorylation	ARARNLISPRMEKAL HHHHHHCCHHHHHHH	15.04	29496963
377	Sumoylation	LISPRMEKALSQLAL HCCHHHHHHHHHHHH	45.33	-
377	Sumoylation	LISPRMEKALSQLAL HCCHHHHHHHHHHHH	45.33	-
377	Ubiquitination	LISPRMEKALSQLAL HCCHHHHHHHHHHHH	45.33	21906983
380	Phosphorylation	PRMEKALSQLALRSA HHHHHHHHHHHHHHH	28.18	23312004
386	Phosphorylation	LSQLALRSAAPSSPG HHHHHHHHHCCCCCC	29.63	28450419
390	Phosphorylation	ALRSAAPSSPGSPRP HHHHHCCCCCCCCCC	44.42	25159151
391	Phosphorylation	LRSAAPSSPGSPRPA HHHHCCCCCCCCCCC	32.02	25159151
394	Phosphorylation	AAPSSPGSPRPALPA HCCCCCCCCCCCCCC	22.56	25159151
396	Methylation	PSSPGSPRPALPATP CCCCCCCCCCCCCCC	30.71	-
402	Phosphorylation	PRPALPATPPATPPA CCCCCCCCCCCCCCC	28.06	25159151
406	Phosphorylation	LPATPPATPPAASPS CCCCCCCCCCCCCHH	35.26	25159151
411	Phosphorylation	PATPPAASPSALKGV CCCCCCCCHHHHCCC	22.84	29209046
413	Phosphorylation	TPPAASPSALKGVSQ CCCCCCHHHHCCCCH	43.68	23312004
416	Ubiquitination	AASPSALKGVSQDLL CCCHHHHCCCCHHHH	57.91	21906983
419	Phosphorylation	PSALKGVSQDLLERI HHHHCCCCHHHHHHH	27.01	21815630
429	Ubiquitination	LLERIRAKEAQKQLA HHHHHHHHHHHHHHH	43.67	22817900
433	Sumoylation	IRAKEAQKQLAQMTR HHHHHHHHHHHHHHC	55.09	-
433	Ubiquitination	IRAKEAQKQLAQMTR HHHHHHHHHHHHHHC	55.09	21906983
433	Sumoylation	IRAKEAQKQLAQMTR HHHHHHHHHHHHHHC	55.09	-
463	Phosphorylation	ELARVLRSVFVSERK HHHHHHHHHHHCCCC	18.75	24719451
470	Ubiquitination	SVFVSERKPALSMEV HHHHCCCCCCCCHHH	30.50	-
474	Phosphorylation	SERKPALSMEVACAR CCCCCCCCHHHHHHH	18.27	22210691
491	Phosphorylation	GSCCTIMSPGEMEKH HHCCCCCCCCHHHHH	26.38	21815630
522	Ubiquitination	IRTDTYVKLDKAADL CCCCCCEEHHHHHHH	40.32	22817900
525	Ubiquitination	DTYVKLDKAADLAHI CCCEEHHHHHHHHHH	56.78	22817900
533	Phosphorylation	AADLAHITARLAHQT HHHHHHHHHHHHHHH	8.89	18767875

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
7	T	Phosphorylation	Kinase	AURB	Q96GD4	PSP
29	T	Phosphorylation	Kinase	CDK2	P24941	PSP
29	T	Phosphorylation	Kinase	JNK1	P45983	PSP
31	S	Phosphorylation	Kinase	CDK2	P24941	PSP
93	S	Phosphorylation	Kinase	MAPK8	P45983	Uniprot
102	T	Phosphorylation	Kinase	AURB	Q96GD4	PSP
143	S	Phosphorylation	Kinase	AURB	Q96GD4	PSP
318	S	Phosphorylation	Kinase	MAPK8	P45983	Uniprot
358	T	Phosphorylation	Kinase	AURB	Q96GD4	PSP
391	S	Phosphorylation	Kinase	JNK1	P45983	PSP
391	S	Phosphorylation	Kinase	P38A	Q16539	PSP
402	T	Phosphorylation	Kinase	JNK1	P45983	PSP
402	T	Phosphorylation	Kinase	P38A	Q16539	PSP
406	T	Phosphorylation	Kinase	JNK1	P45983	PSP
406	T	Phosphorylation	Kinase	P38A	Q16539	PSP
411	S	Phosphorylation	Kinase	JNK1	P45983	PSP
411	S	Phosphorylation	Kinase	P38A	Q16539	PSP
491	S	Phosphorylation	Kinase	JNK1	P45983	PSP
491	S	Phosphorylation	Kinase	P38A	Q16539	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	FBXO31	Q5XUX0	PMID:24828503
-	K	Ubiquitination	E3 ubiquitin ligase	SKP2	Q13309	PMID:10790373
-	K	Ubiquitination	E3 ubiquitin ligase	DTL	Q9NZJ0	PMID:16861906
-	K	Ubiquitination	E3 ubiquitin ligase	TRIM21	P19474	PMID:16407252

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
29	T	Phosphorylation	21856198
Phosphorylated at Thr-29 by MAPK8/JNK1, which blocks replication licensing in response to stress.
29	T	Phosphorylation	21856198
Phosphorylation at Thr-29 by CDK2 targets CDT1 for ubiquitination by SCF(SKP2) E3 ubiquitin ligase and subsequent degradation.
29	T	Phosphorylation	21856198
Phosphorylation by cyclin A-dependent kinases at Thr-29 targets CDT1 for ubiquitynation by SCF(SKP2) E3 ubiquitin ligase and subsequent degradation.
29	T	ubiquitylation	21856198
Phosphorylation at Thr-29 by CDK2 targets CDT1 for ubiquitination by SCF(SKP2) E3 ubiquitin ligase and subsequent degradation.
29	T	ubiquitylation	21856198
Phosphorylation by cyclin A-dependent kinases at Thr-29 targets CDT1 for ubiquitynation by SCF(SKP2) E3 ubiquitin ligase and subsequent degradation.

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 CDT1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CUL1_HUMAN	CUL1	physical	12840033
SKP2_HUMAN	SKP2	physical	12840033
CDC23_HUMAN	CDC23	physical	18162579
APC5_HUMAN	ANAPC5	physical	18162579
SMCA5_HUMAN	SMARCA5	physical	18162579
BAZ1B_HUMAN	BAZ1B	physical	18162579
PCNA_HUMAN	PCNA	physical	18162579
MCM4_HUMAN	MCM4	physical	18162579
MCM6_HUMAN	MCM6	physical	18162579
GRWD1_HUMAN	GRWD1	physical	18162579
NPM_HUMAN	NPM1	physical	18162579
IMA1_HUMAN	KPNA2	physical	18162579
IMB1_HUMAN	KPNB1	physical	18162579
TOP1_HUMAN	TOP1	physical	18162579
APC7_HUMAN	ANAPC7	physical	18162579
SKP2_HUMAN	SKP2	physical	18162579
CDC6_HUMAN	CDC6	physical	18162579
GEMI_HUMAN	GMNN	physical	18162579
TOP2A_HUMAN	TOP2A	physical	18162579
CDC20_HUMAN	CDC20	physical	18162579
FZR1_HUMAN	FZR1	physical	18162579
PCNA_HUMAN	PCNA	physical	16407242
HDA11_HUMAN	HDAC11	physical	19276081
KAT7_HUMAN	KAT7	physical	18832067
DDB1_HUMAN	DDB1	physical	15448697
DDB2_HUMAN	DDB2	physical	15448697
GEMI_HUMAN	GMNN	physical	15138268
CCNA1_HUMAN	CCNA1	physical	15138268
SKP2_HUMAN	SKP2	physical	15004027
CCNE1_HUMAN	CCNE1	physical	15004027
CCNA1_HUMAN	CCNA1	physical	15004027
CDK2_HUMAN	CDK2	physical	15004027
CDK4_HUMAN	CDK4	physical	15004027
PCNA_HUMAN	PCNA	physical	16362051
MCM6_HUMAN	MCM6	physical	18184650
GEMI_HUMAN	GMNN	physical	18184650
CCNA2_HUMAN	CCNA2	physical	18184650
HDA11_HUMAN	HDAC11	physical	20980834
GEMI_HUMAN	GMNN	physical	20980834
KAT7_HUMAN	KAT7	physical	20980834
MCM6_HUMAN	MCM6	physical	22140117
SMCA5_HUMAN	SMARCA5	physical	21937426
PCNA_HUMAN	PCNA	physical	16482215
FOXO3_HUMAN	FOXO3	physical	22451935
DDB1_HUMAN	DDB1	physical	22451935
GEMI_HUMAN	GMNN	physical	14993212
CDK1_HUMAN	CDK1	physical	14993212
CCNA2_HUMAN	CCNA2	physical	14993212
CDK2_HUMAN	CDK2	physical	14993212
CCNB1_HUMAN	CCNB1	physical	14993212
SKP2_HUMAN	SKP2	physical	14993212
SKP2_HUMAN	SKP2	physical	15855168
GEMI_HUMAN	GMNN	physical	15855168
DGCR8_HUMAN	DGCR8	physical	22939629
GEMI_HUMAN	GMNN	physical	15232106
ORC1_HUMAN	ORC1	physical	15232106
CDC5L_HUMAN	CDC5L	physical	15232106
CDC6_HUMAN	CDC6	physical	15232106
ORC2_HUMAN	ORC2	physical	15232106
PCNA_HUMAN	PCNA	physical	24423875
FBX31_HUMAN	FBXO31	physical	24828503
GEMI_HUMAN	GMNN	physical	14578910
MK09_HUMAN	MAPK9	physical	21930785
MK14_HUMAN	MAPK14	physical	21930785
MCM2_HUMAN	MCM2	physical	21930785
PCNA_HUMAN	PCNA	physical	21930785
DTL_HUMAN	DTL	physical	21930785
CCNA2_HUMAN	CCNA2	physical	26496610
CDK2_HUMAN	CDK2	physical	26496610
TIM8A_HUMAN	TIMM8A	physical	26496610
MCM6_HUMAN	MCM6	physical	26496610
SKP2_HUMAN	SKP2	physical	26496610
TFDP1_HUMAN	TFDP1	physical	26496610
TRIP4_HUMAN	TRIP4	physical	26496610
BZW1_HUMAN	BZW1	physical	26496610
TIM13_HUMAN	TIMM13	physical	26496610
GEMI_HUMAN	GMNN	physical	26496610
ANKH1_HUMAN	ANKHD1	physical	26496610
TPC13_HUMAN	TRAPPC13	physical	26496610
DTL_HUMAN	DTL	physical	26272819
PCNA_HUMAN	PCNA	physical	26272819
GRWD1_HUMAN	GRWD1	physical	25990725
CDC6_HUMAN	CDC6	physical	25990725

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613804	Meier-Gorlin syndrome 4 (MGORS4)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CDT1_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-318, AND MASSSPECTROMETRY.	19690332 [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-29; SER-31; SER-372 ANDSER-394, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318, AND MASSSPECTROMETRY.	15302935 [Abstract]
"JNK1 phosphorylation of Cdt1 inhibits recruitment of HBO1 histoneacetylase and blocks replication licensing in response to stress."; Miotto B., Struhl K.; Mol. Cell 44:62-71(2011). Cited for: PHOSPHORYLATION AT THR-29 BY MAPK8/JNK1, AND FUNCTION.	21856198 [Abstract]

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