CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004240
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 G2/mitotic-specific cyclin-B1 
Protein Synonyms/Alias
  
Gene Name
 CCNB1 
Gene Synonyms/Alias
 CCNB 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
51ALGDIGNKVSEQLQAubiquitination[1]
73AKPSATGKVIDKKLPacetylation[2]
190EEQAVRPKYLLGREVubiquitination[1, 3, 4]
311HFLRRASKIGEVDVEubiquitination[1]
396MVNQGLTKHMTVKNKubiquitination[1]
411YATSKHAKISTLPQLubiquitination[1]
428ALVQDLAKAVAKV**ubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
 Essential for the control of the cell cycle at the G2/M (mitosis) transition. 
Sequence Annotation
 REGION 169 177 Interaction with CDK2.
 REGION 258 261 Interaction with CDK2.
 MOD_RES 73 73 N6-acetyllysine.
 MOD_RES 126 126 Phosphoserine; by CDK1.
 MOD_RES 128 128 Phosphoserine.
 MOD_RES 133 133 Phosphoserine; by PLK1.
 MOD_RES 147 147 Phosphoserine.
 MOD_RES 321 321 Phosphothreonine.  
Keyword
 3D-structure; Acetylation; Cell cycle; Cell division; Complete proteome; Cyclin; Cytoplasm; Cytoskeleton; Mitosis; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 433 AA 
Protein Sequence
MALRVTRNSK INAENKAKIN MAGAKRVPTA PAATSKPGLR PRTALGDIGN KVSEQLQAKM 60
PMKKEAKPSA TGKVIDKKLP KPLEKVPMLV PVPVSEPVPE PEPEPEPEPV KEEKLSPEPI 120
LVDTASPSPM ETSGCAPAEE DLCQAFSDVI LAVNDVDAED GADPNLCSEY VKDIYAYLRQ 180
LEEEQAVRPK YLLGREVTGN MRAILIDWLV QVQMKFRLLQ ETMYMTVSII DRFMQNNCVP 240
KKMLQLVGVT AMFIASKYEE MYPPEIGDFA FVTDNTYTKH QIRQMEMKIL RALNFGLGRP 300
LPLHFLRRAS KIGEVDVEQH TLAKYLMELT MLDYDMVHFP PSQIAAGAFC LALKILDNGE 360
WTPTLQHYLS YTEESLLPVM QHLAKNVVMV NQGLTKHMTV KNKYATSKHA KISTLPQLNS 420
ALVQDLAKAV AKV 433 
Gene Ontology
 GO:0005813; C:centrosome; IDA:UniProtKB.
 GO:0000942; C:condensed nuclear chromosome outer kinetochore; IDA:BHF-UCL.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0016020; C:membrane; IEA:Compara.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0000922; C:spindle pole; IDA:BHF-UCL.
 GO:0016301; F:kinase activity; IEA:Compara.
 GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0071398; P:cellular response to fatty acid; IEA:Compara.
 GO:0071456; P:cellular response to hypoxia; IEA:Compara.
 GO:0071283; P:cellular response to iron(III) ion; IEA:Compara.
 GO:0071407; P:cellular response to organic cyclic compound; IEA:Compara.
 GO:0048565; P:digestive tract development; IEA:Compara.
 GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
 GO:0000086; P:G2/M transition of mitotic cell cycle; NAS:UniProtKB.
 GO:0001701; P:in utero embryonic development; IEA:Compara.
 GO:0007080; P:mitotic metaphase plate congression; IMP:BHF-UCL.
 GO:0007077; P:mitotic nuclear envelope disassembly; TAS:Reactome.
 GO:0000236; P:mitotic prometaphase; IDA:BHF-UCL.
 GO:0071174; P:mitotic spindle checkpoint; IMP:BHF-UCL.
 GO:0043148; P:mitotic spindle stabilization; IMP:BHF-UCL.
 GO:0010629; P:negative regulation of gene expression; IEA:Compara.
 GO:0001933; P:negative regulation of protein phosphorylation; IEA:Compara.
 GO:0001556; P:oocyte maturation; IEA:Compara.
 GO:0051987; P:positive regulation of attachment of spindle microtubules to kinetochore; IMP:BHF-UCL.
 GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IEA:Compara.
 GO:0033129; P:positive regulation of histone phosphorylation; IEA:Compara.
 GO:0045931; P:positive regulation of mitotic cell cycle; IMP:BHF-UCL.
 GO:0031442; P:positive regulation of mRNA 3'-end processing; IEA:Compara.
 GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
 GO:0006461; P:protein complex assembly; IEA:Compara.
 GO:0006468; P:protein phosphorylation; IEA:Compara.
 GO:0060623; P:regulation of chromosome condensation; IEA:Compara.
 GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:InterPro.
 GO:0046680; P:response to DDT; IEA:Compara.
 GO:0042493; P:response to drug; IEA:Compara.
 GO:0009612; P:response to mechanical stimulus; IEA:Compara.
 GO:0007283; P:spermatogenesis; IEA:Compara.
 GO:0042246; P:tissue regeneration; IEA:Compara.
 GO:0055015; P:ventricular cardiac muscle cell development; IEA:Compara. 
Interpro
 IPR013763; Cyclin-like.
 IPR014400; Cyclin_A/B/D/E.
 IPR004367; Cyclin_C-dom.
 IPR006671; Cyclin_N. 
Pfam
 PF02984; Cyclin_C
 PF00134; Cyclin_N 
SMART
 SM00385; CYCLIN 
PROSITE
 PS00292; CYCLINS 
PRINTS