CCNB1_HUMAN
ID CCNB1_HUMAN Reviewed; 433 AA.
AC P14635; A8K066; Q5TZP9;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=G2/mitotic-specific cyclin-B1;
GN Name=CCNB1; Synonyms=CCNB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, AND SUBUNIT.
RX PubMed=2570636; DOI=10.1016/0092-8674(89)90936-7;
RA Pines J., Hunter T.;
RT "Isolation of a human cyclin cDNA: evidence for cyclin mRNA and protein
RT regulation in the cell cycle and for interaction with p34cdc2.";
RL Cell 58:833-846(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
RX PubMed=7843284; DOI=10.1006/excr.1995.1050;
RA Piaggio G., Farina A., Perrotti D., Manni I., Fuschi P., Sacchi A.,
RA Gaetano C.;
RT "Structure and growth-dependent regulation of the human cyclin B1
RT promoter.";
RL Exp. Cell Res. 216:396-402(1995).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CCNF.
RX PubMed=10716937; DOI=10.1093/emboj/19.6.1378;
RA Kong M., Barnes E.A., Ollendorff V., Donoghue D.J.;
RT "Cyclin F regulates the nuclear localization of cyclin B1 through a cyclin-
RT cyclin interaction.";
RL EMBO J. 19:1378-1388(2000).
RN [9]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-126; SER-128; SER-133 AND
RP SER-147, AND MUTAGENESIS OF SER-133.
RX PubMed=12447691; DOI=10.1038/sj.onc.1206011;
RA Yuan J., Eckerdt F., Bereiter-Hahn J., Kurunci-Csacsko E., Kaufmann M.,
RA Strebhardt K.;
RT "Cooperative phosphorylation including the activity of polo-like kinase 1
RT regulates the subcellular localization of cyclin B1.";
RL Oncogene 21:8282-8292(2002).
RN [10]
RP INTERACTION WITH RALBP1.
RX PubMed=12775724; DOI=10.1074/jbc.m302191200;
RA Rosse C., L'Hoste S., Offner N., Picard A., Camonis J.;
RT "RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to
RT phosphorylate epsin during the switch off of endocytosis in mitosis.";
RL J. Biol. Chem. 278:30597-30604(2003).
RN [11]
RP INTERACTION WITH HEI10.
RX PubMed=12612082; DOI=10.1128/mcb.23.6.2109-2122.2003;
RA Toby G.G., Gherraby W., Coleman T.R., Golemis E.A.;
RT "A novel RING finger protein, human enhancer of invasion 10, alters mitotic
RT progression through regulation of cyclin B levels.";
RL Mol. Cell. Biol. 23:2109-2122(2003).
RN [12]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-126; SER-133 AND SER-147, AND
RP MUTAGENESIS OF SER-133 AND SER-147.
RX PubMed=12524548; DOI=10.1038/ncb918;
RA Jackman M., Lindon C., Nigg E.A., Pines J.;
RT "Active cyclin B1-Cdk1 first appears on centrosomes in prophase.";
RL Nat. Cell Biol. 5:143-148(2003).
RN [13]
RP UBIQUITINATION.
RX PubMed=16009132; DOI=10.1016/j.cell.2005.04.034;
RA Bassermann F., von Klitzing C., Munch S., Bai R.-Y., Kawaguchi H.,
RA Morris S.W., Peschel C., Duyster J.;
RT "NIPA defines an SCF-type mammalian E3 ligase that regulates mitotic
RT entry.";
RL Cell 122:45-57(2005).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=15181148; DOI=10.1091/mbc.e03-12-0871;
RA Baus Charrier-Savournin F., Chateau M.-T., Gire V., Sedivy J., Piette J.,
RA Dulic V.;
RT "p21-mediated nuclear retention of cyclin B1-Cdk1 in response to genotoxic
RT stress.";
RL Mol. Biol. Cell 15:3965-3976(2004).
RN [15]
RP INTERACTION WITH CDK5RAP3.
RX PubMed=15790566; DOI=10.1074/jbc.m413431200;
RA Jiang H., Luo S., Li H.;
RT "Cdk5 activator-binding protein C53 regulates apoptosis induced by
RT genotoxic stress via modulating the G2/M DNA damage checkpoint.";
RL J. Biol. Chem. 280:20651-20659(2005).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-321, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP INTERACTION WITH INCA1.
RX PubMed=21540187; DOI=10.1074/jbc.m110.203471;
RA Baeumer N., Tickenbrock L., Tschanter P., Lohmeyer L., Diederichs S.,
RA Baeumer S., Skryabin B.V., Zhang F., Agrawal-Singh S., Koehler G.,
RA Berdel W.E., Serve H., Koschmieder S., Mueller-Tidow C.;
RT "Inhibitor of cyclin-dependent kinase (CDK) interacting with cyclin A1
RT (INCA1) regulates proliferation and is repressed by oncogenic signaling.";
RL J. Biol. Chem. 286:28210-28222(2011).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 167-426 IN COMPLEX WITH
RP PHOSPHORYLATED CDK2, AND FUNCTION.
RX PubMed=17495531; DOI=10.4161/cc.6.11.4278;
RA Brown N.R., Lowe E.D., Petri E., Skamnaki V., Antrobus R., Johnson L.N.;
RT "Cyclin B and cyclin A confer different substrate recognition properties on
RT CDK2.";
RL Cell Cycle 6:1350-1359(2007).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 165-433, AND FUNCTION.
RX PubMed=17495533; DOI=10.4161/cc.6.11.4297;
RA Petri E.T., Errico A., Escobedo L., Hunt T., Basavappa R.;
RT "The crystal structure of human cyclin B.";
RL Cell Cycle 6:1342-1349(2007).
CC -!- FUNCTION: Essential for the control of the cell cycle at the G2/M
CC (mitosis) transition. {ECO:0000269|PubMed:17495531,
CC ECO:0000269|PubMed:17495533}.
CC -!- SUBUNIT: Interacts with the CDC2 protein kinase to form a
CC serine/threonine kinase holoenzyme complex also known as maturation
CC promoting factor (MPF). The cyclin subunit imparts substrate
CC specificity to the complex. Binds HEI10. Interacts with catalytically
CC active RALBP1 and CDC2 during mitosis to form an endocytotic complex
CC during interphase. Interacts with CCNF; interaction is required for
CC nuclear localization. Interacts with CDK5RAP3 (PubMed:15790566).
CC Interacts with RFPL4A and UBE2A (By similarity). Interacts with INCA1
CC (PubMed:21540187). {ECO:0000250|UniProtKB:P24860,
CC ECO:0000269|PubMed:10716937, ECO:0000269|PubMed:12612082,
CC ECO:0000269|PubMed:12775724, ECO:0000269|PubMed:15790566,
CC ECO:0000269|PubMed:17495531, ECO:0000269|PubMed:21540187,
CC ECO:0000269|PubMed:2570636}.
CC -!- INTERACTION:
CC P14635; Q9NPC3: CCNB1IP1; NbExp=2; IntAct=EBI-495332, EBI-745269;
CC P14635; P06493: CDK1; NbExp=24; IntAct=EBI-495332, EBI-444308;
CC P14635; P46527: CDKN1B; NbExp=2; IntAct=EBI-495332, EBI-519280;
CC P14635; O75618-1: DEDD; NbExp=3; IntAct=EBI-495332, EBI-15621191;
CC P14635; Q99640: PKMYT1; NbExp=6; IntAct=EBI-495332, EBI-495308;
CC P14635; Q13635: PTCH1; NbExp=2; IntAct=EBI-495332, EBI-8775406;
CC P14635; P61086: UBE2K; NbExp=2; IntAct=EBI-495332, EBI-473850;
CC P14635; Q96PU4: UHRF2; NbExp=2; IntAct=EBI-495332, EBI-625304;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P14635-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P14635-2; Sequence=VSP_053892;
CC -!- DEVELOPMENTAL STAGE: Accumulates steadily during G2 and is abruptly
CC destroyed at mitosis. {ECO:0000269|PubMed:2570636}.
CC -!- PTM: Ubiquitinated by the SCF(NIPA) complex during interphase, leading
CC to its destruction. Not ubiquitinated during G2/M phases.
CC {ECO:0000269|PubMed:16009132}.
CC -!- PTM: Phosphorylated by PLK1 at Ser-133 on centrosomes during prophase:
CC phosphorylation by PLK1 does not cause nuclear import. Phosphorylation
CC at Ser-147 was also reported to be mediated by PLK1 but Ser-133 seems
CC to be the primary phosphorylation site. {ECO:0000269|PubMed:12447691,
CC ECO:0000269|PubMed:12524548}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CCNB1ID951ch5q13.html";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ccnb1/";
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DR EMBL; M25753; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY338491; AAP88038.1; -; Genomic_DNA.
DR EMBL; AK289431; BAF82120.1; -; mRNA.
DR EMBL; BT020128; AAV38930.1; -; mRNA.
DR EMBL; AC010273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022107; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006510; AAH06510.1; -; mRNA.
DR CCDS; CCDS3997.1; -. [P14635-1]
DR PIR; A32992; A32992.
DR RefSeq; NP_114172.1; NM_031966.3. [P14635-1]
DR PDB; 2B9R; X-ray; 2.90 A; A/B=165-433.
DR PDB; 2JGZ; X-ray; 2.90 A; B=167-426.
DR PDB; 4Y72; X-ray; 2.30 A; B=165-433.
DR PDB; 4YC3; X-ray; 2.70 A; B=165-433.
DR PDB; 5HQ0; X-ray; 2.30 A; B=165-433.
DR PDB; 5LQF; X-ray; 2.06 A; B/E=165-433.
DR PDB; 6GU2; X-ray; 2.00 A; B=165-433.
DR PDB; 6GU3; X-ray; 2.65 A; B=165-433.
DR PDB; 6GU4; X-ray; 2.73 A; B=165-433.
DR PDB; 7NJ0; EM; 3.60 A; C=1-433.
DR PDBsum; 2B9R; -.
DR PDBsum; 2JGZ; -.
DR PDBsum; 4Y72; -.
DR PDBsum; 4YC3; -.
DR PDBsum; 5HQ0; -.
DR PDBsum; 5LQF; -.
DR PDBsum; 6GU2; -.
DR PDBsum; 6GU3; -.
DR PDBsum; 6GU4; -.
DR PDBsum; 7NJ0; -.
DR AlphaFoldDB; P14635; -.
DR SMR; P14635; -.
DR BioGRID; 107332; 199.
DR ComplexPortal; CPX-2007; Cyclin B1-CDK1 complex.
DR CORUM; P14635; -.
DR DIP; DIP-59N; -.
DR ELM; P14635; -.
DR IntAct; P14635; 78.
DR MINT; P14635; -.
DR STRING; 9606.ENSP00000256442; -.
DR BindingDB; P14635; -.
DR ChEMBL; CHEMBL2412; -.
DR DrugCentral; P14635; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; P14635; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P14635; -.
DR MetOSite; P14635; -.
DR PhosphoSitePlus; P14635; -.
DR SwissPalm; P14635; -.
DR BioMuta; CCNB1; -.
DR DMDM; 116176; -.
DR CPTAC; CPTAC-1236; -.
DR EPD; P14635; -.
DR jPOST; P14635; -.
DR MassIVE; P14635; -.
DR MaxQB; P14635; -.
DR PaxDb; P14635; -.
DR PeptideAtlas; P14635; -.
DR PRIDE; P14635; -.
DR ProteomicsDB; 53068; -. [P14635-1]
DR ProteomicsDB; 65222; -.
DR Antibodypedia; 3537; 1897 antibodies from 46 providers.
DR DNASU; 891; -.
DR Ensembl; ENST00000256442.10; ENSP00000256442.5; ENSG00000134057.15. [P14635-1]
DR Ensembl; ENST00000505500.5; ENSP00000424588.1; ENSG00000134057.15. [P14635-2]
DR GeneID; 891; -.
DR KEGG; hsa:891; -.
DR MANE-Select; ENST00000256442.10; ENSP00000256442.5; NM_031966.4; NP_114172.1.
DR UCSC; uc003jvm.4; human. [P14635-1]
DR CTD; 891; -.
DR DisGeNET; 891; -.
DR GeneCards; CCNB1; -.
DR HGNC; HGNC:1579; CCNB1.
DR HPA; ENSG00000134057; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 123836; gene.
DR neXtProt; NX_P14635; -.
DR OpenTargets; ENSG00000134057; -.
DR PharmGKB; PA95; -.
DR VEuPathDB; HostDB:ENSG00000134057; -.
DR eggNOG; KOG0653; Eukaryota.
DR GeneTree; ENSGT00940000154586; -.
DR HOGENOM; CLU_020695_2_1_1; -.
DR InParanoid; P14635; -.
DR OMA; CAEENCQ; -.
DR OrthoDB; 993640at2759; -.
DR PhylomeDB; P14635; -.
DR TreeFam; TF101001; -.
DR PathwayCommons; P14635; -.
DR Reactome; R-HSA-113507; E2F-enabled inhibition of pre-replication complex formation.
DR Reactome; R-HSA-156711; Polo-like kinase mediated events.
DR Reactome; R-HSA-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-HSA-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-HSA-176412; Phosphorylation of the APC/C.
DR Reactome; R-HSA-176417; Phosphorylation of Emi1.
DR Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-HSA-2465910; MASTL Facilitates Mitotic Progression.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-2514853; Condensation of Prometaphase Chromosomes.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-2980767; Activation of NIMA Kinases NEK9, NEK6, NEK7.
DR Reactome; R-HSA-2995383; Initiation of Nuclear Envelope (NE) Reformation.
DR Reactome; R-HSA-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-HSA-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-HSA-68875; Mitotic Prophase.
DR Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-HSA-69478; G2/M DNA replication checkpoint.
DR Reactome; R-HSA-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-HSA-8878166; Transcriptional regulation by RUNX2.
DR SignaLink; P14635; -.
DR SIGNOR; P14635; -.
DR BioGRID-ORCS; 891; 511 hits in 1103 CRISPR screens.
DR ChiTaRS; CCNB1; human.
DR EvolutionaryTrace; P14635; -.
DR GeneWiki; Cyclin_B1; -.
DR GenomeRNAi; 891; -.
DR Pharos; P14635; Tchem.
DR PRO; PR:P14635; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P14635; protein.
DR Bgee; ENSG00000134057; Expressed in secondary oocyte and 140 other tissues.
DR ExpressionAtlas; P14635; baseline and differential.
DR Genevisible; P14635; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0097125; C:cyclin B1-CDK1 complex; IDA:CAFA.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000940; C:outer kinetochore; IDA:BHF-UCL.
DR GO; GO:0000922; C:spindle pole; IDA:BHF-UCL.
DR GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; IDA:CAFA.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0005113; F:patched binding; IPI:BHF-UCL.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IPI:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IMP:BHF-UCL.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:BHF-UCL.
DR GO; GO:0051987; P:positive regulation of attachment of spindle microtubules to kinetochore; IMP:BHF-UCL.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IDA:CAFA.
DR GO; GO:1905448; P:positive regulation of mitochondrial ATP synthesis coupled electron transport; IDA:CAFA.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:BHF-UCL.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0090266; P:regulation of mitotic cell cycle spindle assembly checkpoint; IMP:BHF-UCL.
DR CDD; cd00043; CYCLIN; 2.
DR DisProt; DP00223; -.
DR IDEAL; IID00141; -.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10177; PTHR10177; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR PIRSF; PIRSF001771; Cyclin_A_B_D_E; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SMART; SM01332; Cyclin_C; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
DR PROSITE; PS00292; CYCLINS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Cyclin; Cytoplasm; Cytoskeleton; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..433
FT /note="G2/mitotic-specific cyclin-B1"
FT /id="PRO_0000080350"
FT REGION 19..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..177
FT /note="Interaction with CDK2"
FT REGION 258..261
FT /note="Interaction with CDK2"
FT MOD_RES 73
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 126
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:12447691,
FT ECO:0000269|PubMed:12524548"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12447691"
FT MOD_RES 133
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000269|PubMed:12447691,
FT ECO:0000269|PubMed:12524548"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12447691,
FT ECO:0000269|PubMed:12524548"
FT MOD_RES 321
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT VAR_SEQ 362..398
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_053892"
FT MUTAGEN 133
FT /note="S->A: Strongly impairs phosphorylation by PLK1."
FT /evidence="ECO:0000269|PubMed:12447691,
FT ECO:0000269|PubMed:12524548"
FT MUTAGEN 147
FT /note="S->A: Does not affect phosphorylation by PLK1."
FT /evidence="ECO:0000269|PubMed:12524548"
FT CONFLICT 108
FT /note="E -> G (in Ref. 3; BAF82120)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="V -> A (in Ref. 3; BAF82120)"
FT /evidence="ECO:0000305"
FT HELIX 171..184
FT /evidence="ECO:0007829|PDB:6GU2"
FT TURN 189..194
FT /evidence="ECO:0007829|PDB:6GU2"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:6GU2"
FT HELIX 199..216
FT /evidence="ECO:0007829|PDB:6GU2"
FT HELIX 220..236
FT /evidence="ECO:0007829|PDB:6GU2"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:6GU2"
FT HELIX 244..259
FT /evidence="ECO:0007829|PDB:6GU2"
FT HELIX 266..272
FT /evidence="ECO:0007829|PDB:6GU2"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:6GU2"
FT HELIX 279..292
FT /evidence="ECO:0007829|PDB:6GU2"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:6GU2"
FT HELIX 302..312
FT /evidence="ECO:0007829|PDB:6GU2"
FT HELIX 317..329
FT /evidence="ECO:0007829|PDB:6GU2"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:6GU2"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:6GU2"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:2B9R"
FT HELIX 341..356
FT /evidence="ECO:0007829|PDB:6GU2"
FT HELIX 363..366
FT /evidence="ECO:0007829|PDB:6GU2"
FT HELIX 373..391
FT /evidence="ECO:0007829|PDB:6GU2"
FT HELIX 399..403
FT /evidence="ECO:0007829|PDB:6GU2"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:6GU2"
FT HELIX 412..414
FT /evidence="ECO:0007829|PDB:6GU2"
FT HELIX 416..419
FT /evidence="ECO:0007829|PDB:6GU2"
FT HELIX 421..428
FT /evidence="ECO:0007829|PDB:6GU2"
SQ 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
