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G2/mitotic-specific cyclin-B1

 CCNB1_HUMAN             Reviewed;         433 AA.
P14635; A8K066; Q5TZP9;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
25-OCT-2017, entry version 185.
RecName: Full=G2/mitotic-specific cyclin-B1;
Name=CCNB1; Synonyms=CCNB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, AND
SUBUNIT.
PubMed=2570636; DOI=10.1016/0092-8674(89)90936-7;
Pines J., Hunter T.;
"Isolation of a human cyclin cDNA: evidence for cyclin mRNA and
protein regulation in the cell cycle and for interaction with
p34cdc2.";
Cell 58:833-846(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
PubMed=7843284; DOI=10.1006/excr.1995.1050;
Piaggio G., Farina A., Perrotti D., Manni I., Fuschi P., Sacchi A.,
Gaetano C.;
"Structure and growth-dependent regulation of the human cyclin B1
promoter.";
Exp. Cell Res. 216:396-402(1995).
[8]
SUBCELLULAR LOCATION, AND INTERACTION WITH CCNF.
PubMed=10716937; DOI=10.1093/emboj/19.6.1378;
Kong M., Barnes E.A., Ollendorff V., Donoghue D.J.;
"Cyclin F regulates the nuclear localization of cyclin B1 through a
cyclin-cyclin interaction.";
EMBO J. 19:1378-1388(2000).
[9]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-126; SER-128; SER-133 AND
SER-147, AND MUTAGENESIS OF SER-133.
PubMed=12447691; DOI=10.1038/sj.onc.1206011;
Yuan J., Eckerdt F., Bereiter-Hahn J., Kurunci-Csacsko E.,
Kaufmann M., Strebhardt K.;
"Cooperative phosphorylation including the activity of polo-like
kinase 1 regulates the subcellular localization of cyclin B1.";
Oncogene 21:8282-8292(2002).
[10]
INTERACTION WITH RALBP1.
PubMed=12775724; DOI=10.1074/jbc.M302191200;
Rosse C., L'Hoste S., Offner N., Picard A., Camonis J.;
"RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to
phosphorylate epsin during the switch off of endocytosis in mitosis.";
J. Biol. Chem. 278:30597-30604(2003).
[11]
INTERACTION WITH HEI10.
PubMed=12612082; DOI=10.1128/MCB.23.6.2109-2122.2003;
Toby G.G., Gherraby W., Coleman T.R., Golemis E.A.;
"A novel RING finger protein, human enhancer of invasion 10, alters
mitotic progression through regulation of cyclin B levels.";
Mol. Cell. Biol. 23:2109-2122(2003).
[12]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-126; SER-133 AND SER-147,
AND MUTAGENESIS OF SER-133 AND SER-147.
PubMed=12524548; DOI=10.1038/ncb918;
Jackman M., Lindon C., Nigg E.A., Pines J.;
"Active cyclin B1-Cdk1 first appears on centrosomes in prophase.";
Nat. Cell Biol. 5:143-148(2003).
[13]
UBIQUITINATION.
PubMed=16009132; DOI=10.1016/j.cell.2005.04.034;
Bassermann F., von Klitzing C., Munch S., Bai R.-Y., Kawaguchi H.,
Morris S.W., Peschel C., Duyster J.;
"NIPA defines an SCF-type mammalian E3 ligase that regulates mitotic
entry.";
Cell 122:45-57(2005).
[14]
SUBCELLULAR LOCATION.
PubMed=15181148; DOI=10.1091/mbc.E03-12-0871;
Baus Charrier-Savournin F., Chateau M.-T., Gire V., Sedivy J.,
Piette J., Dulic V.;
"p21-mediated nuclear retention of cyclin B1-Cdk1 in response to
genotoxic stress.";
Mol. Biol. Cell 15:3965-3976(2004).
[15]
INTERACTION WITH CDK5RAP3.
PubMed=15790566; DOI=10.1074/jbc.M413431200;
Jiang H., Luo S., Li H.;
"Cdk5 activator-binding protein C53 regulates apoptosis induced by
genotoxic stress via modulating the G2/M DNA damage checkpoint.";
J. Biol. Chem. 280:20651-20659(2005).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-321, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 167-426 IN COMPLEX WITH
PHOSPHORYLATED CDK2, AND FUNCTION.
PubMed=17495531; DOI=10.4161/cc.6.11.4278;
Brown N.R., Lowe E.D., Petri E., Skamnaki V., Antrobus R.,
Johnson L.N.;
"Cyclin B and cyclin A confer different substrate recognition
properties on CDK2.";
Cell Cycle 6:1350-1359(2007).
[20]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 165-433, AND FUNCTION.
PubMed=17495533; DOI=10.4161/cc.6.11.4297;
Petri E.T., Errico A., Escobedo L., Hunt T., Basavappa R.;
"The crystal structure of human cyclin B.";
Cell Cycle 6:1342-1349(2007).
-!- FUNCTION: Essential for the control of the cell cycle at the G2/M
(mitosis) transition. {ECO:0000269|PubMed:17495531,
ECO:0000269|PubMed:17495533}.
-!- SUBUNIT: Interacts with the CDC2 protein kinase to form a
serine/threonine kinase holoenzyme complex also known as
maturation promoting factor (MPF). The cyclin subunit imparts
substrate specificity to the complex. Binds HEI10. Interacts with
catalytically active RALBP1 and CDC2 during mitosis to form an
endocytotic complex during interphase. Interacts with CCNF;
interaction is required for nuclear localization. Interacts with
CDK5RAP3 (PubMed:15790566). {ECO:0000269|PubMed:10716937,
ECO:0000269|PubMed:12612082, ECO:0000269|PubMed:12775724,
ECO:0000269|PubMed:15790566, ECO:0000269|PubMed:17495531,
ECO:0000269|PubMed:2570636}.
-!- INTERACTION:
Q9NPC3:CCNB1IP1; NbExp=2; IntAct=EBI-495332, EBI-745269;
P06493:CDK1; NbExp=17; IntAct=EBI-495332, EBI-444308;
P46527:CDKN1B; NbExp=2; IntAct=EBI-495332, EBI-519280;
O75618-1:DEDD; NbExp=3; IntAct=EBI-495332, EBI-15621191;
Q12778:FOXO1; NbExp=2; IntAct=EBI-495332, EBI-1108782;
Q99640:PKMYT1; NbExp=5; IntAct=EBI-495332, EBI-495308;
Q13635:PTCH1; NbExp=2; IntAct=EBI-495332, EBI-8775406;
P61086:UBE2K; NbExp=2; IntAct=EBI-495332, EBI-473850;
Q96PU4:UHRF2; NbExp=2; IntAct=EBI-495332, EBI-625304;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P14635-1; Sequence=Displayed;
Name=2;
IsoId=P14635-2; Sequence=VSP_053892;
Note=No experimental confirmation available.;
-!- DEVELOPMENTAL STAGE: Accumulates steadily during G2 and is
abruptly destroyed at mitosis. {ECO:0000269|PubMed:2570636}.
-!- PTM: Ubiquitinated by the SCF(NIPA) complex during interphase,
leading to its destruction. Not ubiquitinated during G2/M phases.
{ECO:0000269|PubMed:16009132}.
-!- PTM: Phosphorylated by PLK1 at Ser-133 on centrosomes during
prophase: phosphorylation by PLK1 does not cause nuclear import.
Phosphorylation at Ser-147 was also reported to be mediated by
PLK1 but Ser-133 seems to be the primary phosphorylation site.
{ECO:0000269|PubMed:12447691, ECO:0000269|PubMed:12524548}.
-!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CCNB1ID951ch5q13.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/ccnb1/";
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EMBL; M25753; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AY338491; AAP88038.1; -; Genomic_DNA.
EMBL; AK289431; BAF82120.1; -; mRNA.
EMBL; BT020128; AAV38930.1; -; mRNA.
EMBL; AC010273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC022107; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC006510; AAH06510.1; -; mRNA.
CCDS; CCDS3997.1; -. [P14635-1]
PIR; A32992; A32992.
RefSeq; NP_114172.1; NM_031966.3. [P14635-1]
UniGene; Hs.23960; -.
PDB; 2B9R; X-ray; 2.90 A; A/B=165-433.
PDB; 2JGZ; X-ray; 2.90 A; B=167-426.
PDB; 4Y72; X-ray; 2.30 A; B=165-433.
PDB; 4YC3; X-ray; 2.70 A; B=165-433.
PDB; 5HQ0; X-ray; 2.30 A; B=165-433.
PDB; 5LQF; X-ray; 2.06 A; B/E=165-433.
PDBsum; 2B9R; -.
PDBsum; 2JGZ; -.
PDBsum; 4Y72; -.
PDBsum; 4YC3; -.
PDBsum; 5HQ0; -.
PDBsum; 5LQF; -.
DisProt; DP00223; -.
ProteinModelPortal; P14635; -.
SMR; P14635; -.
BioGrid; 107332; 147.
CORUM; P14635; -.
DIP; DIP-59N; -.
ELM; P14635; -.
IntAct; P14635; 61.
MINT; MINT-1202632; -.
STRING; 9606.ENSP00000256442; -.
BindingDB; P14635; -.
ChEMBL; CHEMBL2412; -.
TCDB; 1.I.1.1.3; the eukaryotic nuclear pore complex (e-npc) family.
iPTMnet; P14635; -.
PhosphoSitePlus; P14635; -.
BioMuta; CCNB1; -.
DMDM; 116176; -.
EPD; P14635; -.
MaxQB; P14635; -.
PaxDb; P14635; -.
PeptideAtlas; P14635; -.
PRIDE; P14635; -.
DNASU; 891; -.
Ensembl; ENST00000256442; ENSP00000256442; ENSG00000134057. [P14635-1]
Ensembl; ENST00000505500; ENSP00000424588; ENSG00000134057. [P14635-2]
GeneID; 891; -.
KEGG; hsa:891; -.
UCSC; uc003jvm.4; human. [P14635-1]
CTD; 891; -.
DisGeNET; 891; -.
EuPathDB; HostDB:ENSG00000134057.14; -.
GeneCards; CCNB1; -.
HGNC; HGNC:1579; CCNB1.
HPA; CAB000115; -.
HPA; CAB003804; -.
HPA; HPA030741; -.
HPA; HPA061448; -.
MIM; 123836; gene.
neXtProt; NX_P14635; -.
OpenTargets; ENSG00000134057; -.
PharmGKB; PA95; -.
eggNOG; KOG0653; Eukaryota.
eggNOG; COG5024; LUCA.
GeneTree; ENSGT00760000118939; -.
HOGENOM; HOG000167672; -.
HOVERGEN; HBG061650; -.
InParanoid; P14635; -.
KO; K05868; -.
OMA; HMTVKNK; -.
OrthoDB; EOG091G0E9B; -.
PhylomeDB; P14635; -.
TreeFam; TF101001; -.
Reactome; R-HSA-113507; E2F-enabled inhibition of pre-replication complex formation.
Reactome; R-HSA-156711; Polo-like kinase mediated events.
Reactome; R-HSA-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
Reactome; R-HSA-176408; Regulation of APC/C activators between G1/S and early anaphase.
Reactome; R-HSA-176412; Phosphorylation of the APC/C.
Reactome; R-HSA-176417; Phosphorylation of Emi1.
Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes.
Reactome; R-HSA-2465910; MASTL Facilitates Mitotic Progression.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-2514853; Condensation of Prometaphase Chromosomes.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-2980767; Activation of NIMA Kinases NEK9, NEK6, NEK7.
Reactome; R-HSA-3301854; Nuclear Pore Complex (NPC) Disassembly.
Reactome; R-HSA-4419969; Depolymerisation of the Nuclear Lamina.
Reactome; R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
Reactome; R-HSA-68875; Mitotic Prophase.
Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
Reactome; R-HSA-69478; G2/M DNA replication checkpoint.
Reactome; R-HSA-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
SignaLink; P14635; -.
SIGNOR; P14635; -.
ChiTaRS; CCNB1; human.
EvolutionaryTrace; P14635; -.
GeneWiki; Cyclin_B1; -.
GenomeRNAi; 891; -.
PRO; PR:P14635; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000134057; -.
CleanEx; HS_CCNB1; -.
ExpressionAtlas; P14635; baseline and differential.
Genevisible; P14635; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0000942; C:condensed nuclear chromosome outer kinetochore; IDA:BHF-UCL.
GO; GO:0097125; C:cyclin B1-CDK1 complex; IDA:CAFA.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016020; C:membrane; IEA:Ensembl.
GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0000922; C:spindle pole; IDA:BHF-UCL.
GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; IDA:CAFA.
GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; TAS:Reactome.
GO; GO:0035173; F:histone kinase activity; IEA:Ensembl.
GO; GO:0005113; F:patched binding; IPI:BHF-UCL.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0044389; F:ubiquitin-like protein ligase binding; IPI:UniProtKB.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0071398; P:cellular response to fatty acid; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0071283; P:cellular response to iron(III) ion; IEA:Ensembl.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:2000775; P:histone H3-S10 phosphorylation involved in chromosome condensation; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0007080; P:mitotic metaphase plate congression; IMP:BHF-UCL.
GO; GO:0007077; P:mitotic nuclear envelope disassembly; TAS:Reactome.
GO; GO:0007052; P:mitotic spindle organization; IMP:BHF-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO; GO:0001556; P:oocyte maturation; IEA:Ensembl.
GO; GO:0051987; P:positive regulation of attachment of spindle microtubules to kinetochore; IMP:BHF-UCL.
GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IEA:Ensembl.
GO; GO:0031662; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G2/M transition of mitotic cell cycle; IDA:CAFA.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
GO; GO:0033129; P:positive regulation of histone phosphorylation; IEA:Ensembl.
GO; GO:1905448; P:positive regulation of mitochondrial ATP synthesis coupled electron transport; IDA:CAFA.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:BHF-UCL.
GO; GO:0031442; P:positive regulation of mRNA 3'-end processing; IEA:Ensembl.
GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition; TAS:Reactome.
GO; GO:0006461; P:protein complex assembly; IEA:Ensembl.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0051726; P:regulation of cell cycle; TAS:Reactome.
GO; GO:0060623; P:regulation of chromosome condensation; IEA:Ensembl.
GO; GO:0090266; P:regulation of mitotic cell cycle spindle assembly checkpoint; IMP:BHF-UCL.
GO; GO:0051439; P:regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO; GO:0046680; P:response to DDT; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0042246; P:tissue regeneration; IEA:Ensembl.
GO; GO:0055015; P:ventricular cardiac muscle cell development; IEA:Ensembl.
CDD; cd00043; CYCLIN; 2.
Gene3D; 1.10.472.10; -; 2.
InterPro; IPR013763; Cyclin-like.
InterPro; IPR036915; Cyclin-like_sf.
InterPro; IPR004367; Cyclin_C-dom.
InterPro; IPR006671; Cyclin_N.
Pfam; PF02984; Cyclin_C; 1.
Pfam; PF00134; Cyclin_N; 1.
SMART; SM00385; CYCLIN; 2.
SMART; SM01332; Cyclin_C; 1.
SUPFAM; SSF47954; SSF47954; 2.
PROSITE; PS00292; CYCLINS; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell cycle;
Cell division; Complete proteome; Cyclin; Cytoplasm; Cytoskeleton;
Mitosis; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
CHAIN 1 433 G2/mitotic-specific cyclin-B1.
/FTId=PRO_0000080350.
REGION 169 177 Interaction with CDK2.
REGION 258 261 Interaction with CDK2.
COMPBIAS 51 85 Lys-rich.
MOD_RES 73 73 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 126 126 Phosphoserine; by CDK1.
{ECO:0000269|PubMed:12447691,
ECO:0000269|PubMed:12524548}.
MOD_RES 128 128 Phosphoserine.
{ECO:0000269|PubMed:12447691}.
MOD_RES 133 133 Phosphoserine; by PLK1.
{ECO:0000269|PubMed:12447691,
ECO:0000269|PubMed:12524548}.
MOD_RES 147 147 Phosphoserine.
{ECO:0000269|PubMed:12447691,
ECO:0000269|PubMed:12524548}.
MOD_RES 321 321 Phosphothreonine.
{ECO:0000244|PubMed:18691976}.
VAR_SEQ 362 398 Missing (in isoform 2).
{ECO:0000303|Ref.4}.
/FTId=VSP_053892.
MUTAGEN 133 133 S->A: Strongly impairs phosphorylation by
PLK1. {ECO:0000269|PubMed:12447691,
ECO:0000269|PubMed:12524548}.
MUTAGEN 147 147 S->A: Does not affect phosphorylation by
PLK1. {ECO:0000269|PubMed:12524548}.
CONFLICT 108 108 E -> G (in Ref. 3; BAF82120).
{ECO:0000305}.
CONFLICT 153 153 V -> A (in Ref. 3; BAF82120).
{ECO:0000305}.
HELIX 171 184 {ECO:0000244|PDB:5LQF}.
TURN 189 194 {ECO:0000244|PDB:5LQF}.
STRAND 195 197 {ECO:0000244|PDB:4YC3}.
HELIX 199 216 {ECO:0000244|PDB:5LQF}.
HELIX 220 234 {ECO:0000244|PDB:5LQF}.
HELIX 241 243 {ECO:0000244|PDB:5LQF}.
HELIX 244 259 {ECO:0000244|PDB:5LQF}.
HELIX 266 272 {ECO:0000244|PDB:5LQF}.
STRAND 275 277 {ECO:0000244|PDB:5LQF}.
HELIX 279 292 {ECO:0000244|PDB:5LQF}.
TURN 293 295 {ECO:0000244|PDB:5LQF}.
HELIX 302 312 {ECO:0000244|PDB:5LQF}.
HELIX 317 330 {ECO:0000244|PDB:5LQF}.
HELIX 334 336 {ECO:0000244|PDB:5LQF}.
STRAND 337 339 {ECO:0000244|PDB:2B9R}.
HELIX 341 356 {ECO:0000244|PDB:5LQF}.
HELIX 363 369 {ECO:0000244|PDB:5LQF}.
HELIX 373 391 {ECO:0000244|PDB:5LQF}.
HELIX 399 403 {ECO:0000244|PDB:5LQF}.
HELIX 407 409 {ECO:0000244|PDB:5LQF}.
HELIX 412 414 {ECO:0000244|PDB:5LQF}.
HELIX 416 419 {ECO:0000244|PDB:5LQF}.
HELIX 421 428 {ECO:0000244|PDB:5LQF}.
SEQUENCE 433 AA; 48337 MW; E2C4767AE8A11EC0 CRC64;
MALRVTRNSK INAENKAKIN MAGAKRVPTA PAATSKPGLR PRTALGDIGN KVSEQLQAKM
PMKKEAKPSA TGKVIDKKLP KPLEKVPMLV PVPVSEPVPE PEPEPEPEPV KEEKLSPEPI
LVDTASPSPM ETSGCAPAEE DLCQAFSDVI LAVNDVDAED GADPNLCSEY VKDIYAYLRQ
LEEEQAVRPK YLLGREVTGN MRAILIDWLV QVQMKFRLLQ ETMYMTVSII DRFMQNNCVP
KKMLQLVGVT AMFIASKYEE MYPPEIGDFA FVTDNTYTKH QIRQMEMKIL RALNFGLGRP
LPLHFLRRAS KIGEVDVEQH TLAKYLMELT MLDYDMVHFP PSQIAAGAFC LALKILDNGE
WTPTLQHYLS YTEESLLPVM QHLAKNVVMV NQGLTKHMTV KNKYATSKHA KISTLPQLNS
ALVQDLAKAV AKV


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