CCNB2_HUMAN - dbPTM
CCNB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CCNB2_HUMAN
UniProt AC O95067
Protein Name G2/mitotic-specific cyclin-B2
Gene Name CCNB2
Organism Homo sapiens (Human).
Sequence Length 398
Subcellular Localization
Protein Description Essential for the control of the cell cycle at the G2/M (mitosis) transition..
Protein Sequence MALLRRPTVSSDLENIDTGVNSKVKSHVTIRRTVLEEIGNRVTTRAAQVAKKAQNTKVPVQPTKTTNVNKQLKPTASVKPVQMEKLAPKGPSPTPEDVSMKEENLCQAFSDALLCKIEDIDNEDWENPQLCSDYVKDIYQYLRQLEVLQSINPHFLDGRDINGRMRAILVDWLVQVHSKFRLLQETLYMCVGIMDRFLQVQPVSRKKLQLVGITALLLASKYEEMFSPNIEDFVYITDNAYTSSQIREMETLILKELKFELGRPLPLHFLRRASKAGEVDVEQHTLAKYLMELTLIDYDMVHYHPSKVAAAASCLSQKVLGQGKWNLKQQYYTGYTENEVLEVMQHMAKNVVKVNENLTKFIAIKNKYASSKLLKISMIPQLNSKAVKDLASPLIGRS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
8PhosphorylationMALLRRPTVSSDLEN
CCCCCCCCCCHHHHC		31.0721712546
10PhosphorylationLLRRPTVSSDLENID
CCCCCCCCHHHHCCC		22.1730576142
11PhosphorylationLRRPTVSSDLENIDT
CCCCCCCHHHHCCCC		41.7130576142
18PhosphorylationSDLENIDTGVNSKVK
HHHHCCCCCCCHHHH		38.9529255136
22PhosphorylationNIDTGVNSKVKSHVT
CCCCCCCHHHHHHCE		36.1029255136
23AcetylationIDTGVNSKVKSHVTI
CCCCCCHHHHHHCEE		48.7725953088
23UbiquitinationIDTGVNSKVKSHVTI
CCCCCCHHHHHHCEE		48.7732015554
25UbiquitinationTGVNSKVKSHVTIRR
CCCCHHHHHHCEEHH		38.2829967540
33PhosphorylationSHVTIRRTVLEEIGN
HHCEEHHHHHHHHHH		21.4228555341
43PhosphorylationEEIGNRVTTRAAQVA
HHHHHHHHHHHHHHH		13.8228555341
44PhosphorylationEIGNRVTTRAAQVAK
HHHHHHHHHHHHHHH		18.5628555341
57UbiquitinationAKKAQNTKVPVQPTK
HHHHCCCCCCCCCCC		52.6827667366
64UbiquitinationKVPVQPTKTTNVNKQ
CCCCCCCCCCCCCCC		61.1032015554
70UbiquitinationTKTTNVNKQLKPTAS
CCCCCCCCCCCCCCC		53.3729967540
73UbiquitinationTNVNKQLKPTASVKP
CCCCCCCCCCCCCCC		37.5229967540
75PhosphorylationVNKQLKPTASVKPVQ
CCCCCCCCCCCCCEE		29.9429978859
77PhosphorylationKQLKPTASVKPVQME
CCCCCCCCCCCEEHH		32.9029978859
79UbiquitinationLKPTASVKPVQMEKL
CCCCCCCCCEEHHHH		36.6629967540
85UbiquitinationVKPVQMEKLAPKGPS
CCCEEHHHHCCCCCC		44.6029967540
92PhosphorylationKLAPKGPSPTPEDVS
HHCCCCCCCCHHHCC		50.5019664994
94PhosphorylationAPKGPSPTPEDVSMK
CCCCCCCCHHHCCCC		43.5830266825
99PhosphorylationSPTPEDVSMKEENLC
CCCHHHCCCCHHHHH		36.1423927012
101UbiquitinationTPEDVSMKEENLCQA
CHHHCCCCHHHHHHH		55.1329967540
110PhosphorylationENLCQAFSDALLCKI
HHHHHHHHHHHEEEH		25.6224732914
204PhosphorylationFLQVQPVSRKKLQLV
HHHCCCCCHHHHHHH		45.1017192257
220PhosphorylationITALLLASKYEEMFS
HHHHHHHHHHHHHHC		35.42-
258UbiquitinationTLILKELKFELGRPL
HHHHHHHHHHHCCCC		37.5729967540
274PhosphorylationLHFLRRASKAGEVDV
HHHHHHHHHCCCCCH		22.6423882029
275UbiquitinationHFLRRASKAGEVDVE
HHHHHHHHCCCCCHH		60.4729967540
285PhosphorylationEVDVEQHTLAKYLME
CCCHHHHHHHHHHHH		28.2718691976
289PhosphorylationEQHTLAKYLMELTLI
HHHHHHHHHHHHHCC		12.9823663014
294PhosphorylationAKYLMELTLIDYDMV
HHHHHHHHCCCCCCC		14.3623663014
298PhosphorylationMELTLIDYDMVHYHP
HHHHCCCCCCCCCCH		10.0323663014
303PhosphorylationIDYDMVHYHPSKVAA
CCCCCCCCCHHHHHH		12.1923663014
306PhosphorylationDMVHYHPSKVAAAAS
CCCCCCHHHHHHHHH		26.8423663014
318UbiquitinationAASCLSQKVLGQGKW
HHHHHHHHHHCCCCC		35.7329967540
324UbiquitinationQKVLGQGKWNLKQQY
HHHHCCCCCCCHHHE		25.6429967540
328UbiquitinationGQGKWNLKQQYYTGY
CCCCCCCHHHEECCC		31.9429967540
349UbiquitinationEVMQHMAKNVVKVNE
HHHHHHHHCCCCCCC		42.5829967540
353UbiquitinationHMAKNVVKVNENLTK
HHHHCCCCCCCCHHH		34.7529967540
359PhosphorylationVKVNENLTKFIAIKN
CCCCCCHHHHHHHCH		35.1822817900
360UbiquitinationKVNENLTKFIAIKNK
CCCCCHHHHHHHCHH		37.6322817900
365UbiquitinationLTKFIAIKNKYASSK
HHHHHHHCHHHHCCH		38.0622817900
367UbiquitinationKFIAIKNKYASSKLL
HHHHHCHHHHCCHHH		36.8721890473
368PhosphorylationFIAIKNKYASSKLLK
HHHHCHHHHCCHHHH		22.5525219547
370PhosphorylationAIKNKYASSKLLKIS
HHCHHHHCCHHHHHH		25.5625219547
371PhosphorylationIKNKYASSKLLKISM
HCHHHHCCHHHHHHC		21.1025219547
372UbiquitinationKNKYASSKLLKISMI
CHHHHCCHHHHHHCC		56.1729967540
372AcetylationKNKYASSKLLKISMI
CHHHHCCHHHHHHCC		56.1725953088
375UbiquitinationYASSKLLKISMIPQL
HHCCHHHHHHCCHHH		43.0727667366
377PhosphorylationSSKLLKISMIPQLNS
CCHHHHHHCCHHHCC		14.7425219547
378SulfoxidationSKLLKISMIPQLNSK
CHHHHHHCCHHHCCH		6.2021406390
385UbiquitinationMIPQLNSKAVKDLAS
CCHHHCCHHHHHHHH		57.0132015554
388UbiquitinationQLNSKAVKDLASPLI
HHCCHHHHHHHHHHC		52.4629967540
392PhosphorylationKAVKDLASPLIGRS-
HHHHHHHHHHCCCC-		27.7725159151
398PhosphorylationASPLIGRS-------
HHHHCCCC-------		39.0825159151
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

Oops, there are no upstream regulatory protein records of CCNB2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CCNB2_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 CCNB2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TGFR2_HUMANTGFBR2physical
9926943
TSYL2_HUMANTSPYL2physical
18591933
MCM2_HUMANMCM2physical
15232106
CDN1A_HUMANCDKN1Aphysical
15232106
CDK2_HUMANCDK2physical
15232106
CDK7_HUMANCDK7physical
26344197
DIAP3_HUMANDIAPH3physical
26344197
RNH2C_HUMANRNASEH2Cphysical
26344197
CDK1_HUMANCDK1physical
26496610
PMYT1_HUMANPKMYT1physical
26496610
PAXI1_HUMANPAXIP1physical
26496610
PDS5A_HUMANPDS5Aphysical
26496610
SFR15_HUMANSCAF4physical
26496610
K2C73_HUMANKRT73physical
26496610
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 CCNB2_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-398, AND MASSSPECTROMETRY.
"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-8; SER-92; THR-94;SER-392 AND SER-398, AND MASS SPECTROMETRY.
"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-92; SER-99 AND SER-398,AND MASS SPECTROMETRY.
"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-92; THR-94; SER-99;SER-204; SER-392 AND SER-398, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND MASSSPECTROMETRY.
"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 THR-94, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory