dbPTM

CCNB1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CCNB1_HUMAN
UniProt AC	P14635
Protein Name	G2/mitotic-specific cyclin-B1
Gene Name	CCNB1
Organism	Homo sapiens (Human).
Sequence Length	433
Subcellular Localization	Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Protein Description	Essential for the control of the cell cycle at the G2/M (mitosis) transition..
Protein Sequence	MALRVTRNSKINAENKAKINMAGAKRVPTAPAATSKPGLRPRTALGDIGNKVSEQLQAKMPMKKEAKPSATGKVIDKKLPKPLEKVPMLVPVPVSEPVPEPEPEPEPEPVKEEKLSPEPILVDTASPSPMETSGCAPAEEDLCQAFSDVILAVNDVDAEDGADPNLCSEYVKDIYAYLRQLEEEQAVRPKYLLGREVTGNMRAILIDWLVQVQMKFRLLQETMYMTVSIIDRFMQNNCVPKKMLQLVGVTAMFIASKYEEMYPPEIGDFAFVTDNTYTKHQIRQMEMKILRALNFGLGRPLPLHFLRRASKIGEVDVEQHTLAKYLMELTMLDYDMVHFPPSQIAAGAFCLALKILDNGEWTPTLQHYLSYTEESLLPVMQHLAKNVVMVNQGLTKHMTVKNKYATSKHAKISTLPQLNSALVQDLAKAVAKV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	ALRVTRNSKINAENK CCCCCCCCCCCHHHC	31.46	17192257
10	Acetylation	LRVTRNSKINAENKA CCCCCCCCCCHHHCH	43.45	25953088
25	Ubiquitination	KINMAGAKRVPTAPA HCCCCCCCCCCCCCC	53.67	-
25	Acetylation	KINMAGAKRVPTAPA HCCCCCCCCCCCCCC	53.67	25953088
29	Phosphorylation	AGAKRVPTAPAATSK CCCCCCCCCCCCCCC	42.28	21406692
34	Phosphorylation	VPTAPAATSKPGLRP CCCCCCCCCCCCCCC	39.11	21406692
35	Phosphorylation	PTAPAATSKPGLRPR CCCCCCCCCCCCCCC	31.93	17192257
36	Ubiquitination	TAPAATSKPGLRPRT CCCCCCCCCCCCCCC	38.46	32015554
51	Acetylation	ALGDIGNKVSEQLQA CHHHHHHHHHHHHHH	41.76	26051181
51	Ubiquitination	ALGDIGNKVSEQLQA CHHHHHHHHHHHHHH	41.76	-
53	Phosphorylation	GDIGNKVSEQLQAKM HHHHHHHHHHHHHHC	22.64	30576142
59	Acetylation	VSEQLQAKMPMKKEA HHHHHHHHCCCCCCC	30.49	25953088
59	Ubiquitination	VSEQLQAKMPMKKEA HHHHHHHHCCCCCCC	30.49	33845483
69	Phosphorylation	MKKEAKPSATGKVID CCCCCCCCCCCCCCC	37.44	17192257
73	Acetylation	AKPSATGKVIDKKLP CCCCCCCCCCCCCCC	31.49	19608861
73	Ubiquitination	AKPSATGKVIDKKLP CCCCCCCCCCCCCCC	31.49	33845483
95	Phosphorylation	MLVPVPVSEPVPEPE EEEEEECCCCCCCCC	30.07	-
111	Sumoylation	EPEPEPVKEEKLSPE CCCCCCCCCCCCCCC	71.51	-
111	Sumoylation	EPEPEPVKEEKLSPE CCCCCCCCCCCCCCC	71.51	-
116	Phosphorylation	PVKEEKLSPEPILVD CCCCCCCCCCCEEEE	37.98	20117088
126	Phosphorylation	PILVDTASPSPMETS CEEEECCCCCCCCCC	28.18	20117088
128	Phosphorylation	LVDTASPSPMETSGC EEECCCCCCCCCCCC	34.09	20117088
133	Phosphorylation	SPSPMETSGCAPAEE CCCCCCCCCCCCCCH	20.69	20117088
147	Phosphorylation	EDLCQAFSDVILAVN HHHHHHHHHHEEEEC	33.70	20117088
175	Phosphorylation	SEYVKDIYAYLRQLE HHHHHHHHHHHHHHH	10.18	27642862
177	Phosphorylation	YVKDIYAYLRQLEEE HHHHHHHHHHHHHHH	5.85	22817900
190	Ubiquitination	EEQAVRPKYLLGREV HHHCCCCHHHCCCCC	37.66	21890473
190	Ubiquitination	EEQAVRPKYLLGREV HHHCCCCHHHCCCCC	37.66	22817900
190	Ubiquitination	EEQAVRPKYLLGREV HHHCCCCHHHCCCCC	37.66	21890473
258	Ubiquitination	AMFIASKYEEMYPPE HHHHHHCHHHHCCCC	18.02	33845483
262	Phosphorylation	ASKYEEMYPPEIGDF HHCHHHHCCCCCCCE	20.93	22210691
273	Phosphorylation	IGDFAFVTDNTYTKH CCCEEEEECCCCCHH	19.65	22210691
278	Phosphorylation	FVTDNTYTKHQIRQM EEECCCCCHHHHHHH	21.73	22210691
279	Ubiquitination	VTDNTYTKHQIRQME EECCCCCHHHHHHHH	24.09	21906983
279	Ubiquitination	VTDNTYTKHQIRQME EECCCCCHHHHHHHH	24.09	-
310	Phosphorylation	LHFLRRASKIGEVDV HHHHHHHHHCCCCCH	24.01	23927012
311	Ubiquitination	HFLRRASKIGEVDVE HHHHHHHHCCCCCHH	54.46	33845483
311	Ubiquitination	HFLRRASKIGEVDVE HHHHHHHHCCCCCHH	54.46	-
311	Acetylation	HFLRRASKIGEVDVE HHHHHHHHCCCCCHH	54.46	25953088
321	Phosphorylation	EVDVEQHTLAKYLME CCCHHHHHHHHHHHH	28.27	17192257
362	Phosphorylation	ILDNGEWTPTLQHYL EHHCCCCCCCHHHHH	11.33	25159151
364	Phosphorylation	DNGEWTPTLQHYLSY HCCCCCCCHHHHHHC	31.51	25627689
370	Phosphorylation	PTLQHYLSYTEESLL CCHHHHHHCCHHHHH	23.89	25627689
372	Phosphorylation	LQHYLSYTEESLLPV HHHHHHCCHHHHHHH	29.87	25627689
389	Sulfoxidation	HLAKNVVMVNQGLTK HHHHCCEEECCCHHH	1.72	21406390
395	Phosphorylation	VMVNQGLTKHMTVKN EEECCCHHHCCHHCC	26.23	-
396	Ubiquitination	MVNQGLTKHMTVKNK EECCCHHHCCHHCCH	36.10	29967540
411	Ubiquitination	YATSKHAKISTLPQL HCCCCCCCCCCHHHH	36.59	29967540
413	Phosphorylation	TSKHAKISTLPQLNS CCCCCCCCCHHHHHH	24.16	21712546
428	Ubiquitination	ALVQDLAKAVAKV-- HHHHHHHHHHHCC--	51.17	-

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
126	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
126	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
126	S	Phosphorylation	Kinase	PLK1	P53350	PSP
126	S	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
126	S	Phosphorylation	Kinase	MAPK_GROUP	-	PhosphoELM
128	S	Phosphorylation	Kinase	CDK1	P06493	PSP
128	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
128	S	Phosphorylation	Kinase	PLK1	P53350	PSP
128	S	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
128	S	Phosphorylation	Kinase	MAPK_GROUP	-	PhosphoELM
133	S	Phosphorylation	Kinase	PLK1	P53350	Uniprot
133	S	Phosphorylation	Kinase	PLK3	Q9H4B4	PSP
147	S	Phosphorylation	Kinase	PLK1	P53350	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	FZR1	Q9UM11	PMID:22529100
-	K	Ubiquitination	E3 ubiquitin ligase	BRCA1	P38398	PMID:23246971
-	K	Ubiquitination	E3 ubiquitin ligase	PRKN	O60260	PMID:26387737
-	K	Ubiquitination	E3 ubiquitin ligase	CDC20	Q12834	PMID:11285280
-	K	Ubiquitination	E3 ubiquitin ligase	ZC3HC1	Q86WB0	PMID:16258267
-	K	Ubiquitination	E3 ubiquitin ligase	KLHL9	Q9P2J3	PMID:18075312
-	K	Ubiquitination	E3 ubiquitin ligase	KLHL10	Q6JEL2	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	KLHL11	Q9NVR0	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	KLHL12	Q53G59	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	KLHL13	Q9P2N7	PMID:18075312
-	K	Ubiquitination	E3 ubiquitin ligase	ANAPC11	Q9NYG5	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	RFPL4A	A6NLU0	PMID:12525704
-	K	Ubiquitination	E3 ubiquitin ligase	CCNB1IP1	Q9NPC3	PMID:12612082
-	K	Ubiquitination	E3 ubiquitin ligase	KLHL9#KLHL13	Q9P2J3#Q9P2N7	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
133	S	Phosphorylation	12447691
Phosphorylated by PLK1 at Ser-133 on centrosomes during prophase: phosphorylation by PLK1 does not cause nuclear import.
133	S	Phosphorylation	12447691
Phosphorylation at Ser-147 was also reported to be mediated by PLK1 but Ser-133 seems to be the primary phosphorylation site.
147	S	Phosphorylation	12447691
Phosphorylation at Ser-147 was also reported to be mediated by PLK1 but Ser-133 seems to be the primary phosphorylation site.

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 CCNB1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CDK2_HUMAN	CDK2	physical	9891079
CDK1_HUMAN	CDK1	physical	9891079
CDK1_HUMAN	CDK1	physical	2570636
CCNF_HUMAN	CCNF	physical	10716937
CDN1A_HUMAN	CDKN1A	physical	17679094
CDK1_HUMAN	CDK1	physical	17679094
CDK1_HUMAN	CDK1	physical	16784539
CC14A_HUMAN	CDC14A	physical	16784539
CDC27_HUMAN	CDC27	physical	16479161
TSYL2_HUMAN	TSPYL2	physical	18591933
CDK1_HUMAN	CDK1	physical	16159883
CDC27_HUMAN	CDC27	physical	12097298
FOXM1_HUMAN	FOXM1	physical	15024056
CDK1_HUMAN	CDK1	physical	20228808
UHRF2_HUMAN	UHRF2	physical	21952639
FZR1_HUMAN	FZR1	physical	14701726
CDC20_HUMAN	CDC20	physical	14701726
CDK2_HUMAN	CDK2	physical	20733051
PCNA_HUMAN	PCNA	physical	7903056
CDK1_HUMAN	CDK1	physical	17431037
H11_HUMAN	HIST1H1A	physical	10362260
H11_HUMAN	HIST1H1A	physical	22158041
LMNB1_RAT	Lmnb1	physical	9053846
RFA1_HUMAN	RPA1	physical	8397206
H11_HUMAN	HIST1H1A	physical	8397206
APC4_HUMAN	ANAPC4	physical	20733055
CDC20_HUMAN	CDC20	physical	20733055
CDK1_HUMAN	CDK1	physical	20733055
CDC27_HUMAN	CDC27	physical	20733055
CDK2_HUMAN	CDK2	physical	18471975
CKS1_HUMAN	CKS1B	physical	18471975
CKS2_HUMAN	CKS2	physical	18471975
H11_HUMAN	HIST1H1A	physical	11836499
CDC27_HUMAN	CDC27	physical	16921029
FZR1_HUMAN	FZR1	physical	16921029
CDK1_HUMAN	CDK1	physical	20956543
H15_HUMAN	HIST1H1B	physical	20956543
NDC80_HUMAN	NDC80	physical	22939629
SDHF2_HUMAN	SDHAF2	physical	22939629
PRC1_HUMAN	PRC1	physical	9885575
RB_HUMAN	RB1	physical	9885575
H11_HUMAN	HIST1H1A	physical	9885575
MFN1_HUMAN	MFN1	physical	23253261
H15_HUMAN	HIST1H1B	physical	8662825
CDK1_HUMAN	CDK1	physical	8662825
CDK1_HUMAN	CDK1	physical	8463339
P73_HUMAN	TP73	physical	12676926
CDC6_HUMAN	CDC6	physical	10339564
CDK7_HUMAN	CDK7	physical	11113184
RB_HUMAN	RB1	physical	9315635
TP53B_HUMAN	TP53BP1	physical	20126263
DPOLA_HUMAN	POLA1	physical	11259605
SQSTM_HUMAN	SQSTM1	physical	20974803
RHBT3_HUMAN	RHOBTB3	physical	24145166
EP300_HUMAN	EP300	physical	9560267
TF65_HUMAN	RELA	physical	9560267
CDK1_HUMAN	CDK1	physical	9560267
CCNB2_HUMAN	CCNB2	physical	26344197
DIAP3_HUMAN	DIAPH3	physical	26344197
HNRLL_HUMAN	HNRNPLL	physical	26344197
RNH2C_HUMAN	RNASEH2C	physical	26344197
CDK1_HUMAN	CDK1	physical	24508230
CDK1_HUMAN	CDK1	physical	26496610
CDN1B_HUMAN	CDKN1B	physical	26496610
CKS1_HUMAN	CKS1B	physical	26496610
CKS2_HUMAN	CKS2	physical	26496610
NCBP1_HUMAN	NCBP1	physical	26496610
PRDX1_HUMAN	PRDX1	physical	26496610
RS3_HUMAN	RPS3	physical	26496610
KAT6A_HUMAN	KAT6A	physical	26496610
FXR1_HUMAN	FXR1	physical	26496610
ARK72_HUMAN	AKR7A2	physical	26496610
PMYT1_HUMAN	PKMYT1	physical	26496610
KEAP1_HUMAN	KEAP1	physical	26496610
PDCD6_HUMAN	PDCD6	physical	26496610
PRDX3_HUMAN	PRDX3	physical	26496610
S27A2_HUMAN	SLC27A2	physical	26496610
ALKB8_HUMAN	ALKBH8	physical	26496610
SYTC2_HUMAN	TARSL2	physical	26496610
CDC27_HUMAN	CDC27	physical	25750436
APC4_HUMAN	ANAPC4	physical	25750436
CDK1_HUMAN	CDK1	physical	25750436
APC10_HUMAN	ANAPC10	physical	25750436
FOXO1_HUMAN	FOXO1	physical	25241761
FZR1_HUMAN	FZR1	physical	25241761
CDN1A_HUMAN	CDKN1A	physical	25241761
UBE3C_HUMAN	UBE3C	physical	26389696
PRKN_HUMAN	PARK2	physical	26387737
PRKDC_HUMAN	PRKDC	physical	26221070
TIF1B_HUMAN	TRIM28	physical	27030811
CCAR1_HUMAN	CCAR1	physical	27030811
CDK1_HUMAN	CDK1	physical	27030811
CDK3_HUMAN	CDK3	physical	27030811
BCLF1_HUMAN	BCLAF1	physical	27030811
STK38_HUMAN	STK38	physical	27030811
RS18_HUMAN	RPS18	physical	27030811
STAU1_HUMAN	STAU1	physical	27030811
GRWD1_HUMAN	GRWD1	physical	27030811
DNMT1_HUMAN	DNMT1	physical	27030811
HDAC1_HUMAN	HDAC1	physical	27030811
UBP22_HUMAN	USP22	physical	27030811
PTC1_HUMAN	PTCH1	physical	15592520

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 CCNB1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73, AND MASS SPECTROMETRY.	19608861 [Abstract]
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-9, AND MASSSPECTROMETRY.	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-9; SER-35; SER-69 ANDTHR-321, AND MASS SPECTROMETRY.	18691976 [Abstract]
"Active cyclin B1-Cdk1 first appears on centrosomes in prophase."; Jackman M., Lindon C., Nigg E.A., Pines J.; Nat. Cell Biol. 5:143-148(2003). Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-126; SER-133 AND SER-147,AND MUTAGENESIS OF SER-133 AND SER-147.	12524548 [Abstract]
"Cooperative phosphorylation including the activity of polo-likekinase 1 regulates the subcellular localization of cyclin B1."; Yuan J., Eckerdt F., Bereiter-Hahn J., Kurunci-Csacsko E.,Kaufmann M., Strebhardt K.; Oncogene 21:8282-8292(2002). Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-126; SER-128; SER-133 ANDSER-147, AND MUTAGENESIS OF SER-133.	12447691 [Abstract]

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