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Protein

G2/mitotic-specific cyclin-B1

Gene

CCNB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential for the control of the cell cycle at the G2/M (mitosis) transition.2 Publications

GO - Molecular functioni

  • histone kinase activity Source: Ensembl
  • patched binding Source: BHF-UCL
  • protein kinase binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiR-HSA-113507. E2F-enabled inhibition of pre-replication complex formation.
R-HSA-156711. Polo-like kinase mediated events.
R-HSA-162658. Golgi Cisternae Pericentriolar Stack Reorganization.
R-HSA-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-HSA-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-HSA-176412. Phosphorylation of the APC/C.
R-HSA-176417. Phosphorylation of Emi1.
R-HSA-2299718. Condensation of Prophase Chromosomes.
R-HSA-2465910. MASTL Facilitates Mitotic Progression.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-2514853. Condensation of Prometaphase Chromosomes.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-2980767. Activation of NIMA Kinases NEK9, NEK6, NEK7.
R-HSA-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-HSA-380320. Recruitment of NuMA to mitotic centrosomes.
R-HSA-4419969. Depolymerisation of the Nuclear Lamina.
R-HSA-69273. Cyclin A/B1 associated events during G2/M transition.
R-HSA-69478. G2/M DNA replication checkpoint.
R-HSA-75035. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
SignaLinkiP14635.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
G2/mitotic-specific cyclin-B1
Gene namesi
Name:CCNB1
Synonyms:CCNB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:1579. CCNB1.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • condensed nuclear chromosome outer kinetochore Source: BHF-UCL
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • membrane Source: Ensembl
  • nucleoplasm Source: Reactome
  • nucleus Source: BHF-UCL
  • spindle pole Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi133 – 1331S → A: Strongly impairs phosphorylation by PLK1. 2 Publications
Mutagenesisi147 – 1471S → A: Does not affect phosphorylation by PLK1. 1 Publication

Organism-specific databases

PharmGKBiPA95.

Chemistry

ChEMBLiCHEMBL1907602.

Polymorphism and mutation databases

BioMutaiCCNB1.
DMDMi116176.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 433433G2/mitotic-specific cyclin-B1PRO_0000080350Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei73 – 731N6-acetyllysineCombined sources
Modified residuei126 – 1261Phosphoserine; by CDK12 Publications
Modified residuei128 – 1281Phosphoserine1 Publication
Modified residuei133 – 1331Phosphoserine; by PLK12 Publications
Modified residuei147 – 1471Phosphoserine2 Publications
Modified residuei321 – 3211PhosphothreonineCombined sources

Post-translational modificationi

Ubiquitinated by the SCF(NIPA) complex during interphase, leading to its destruction. Not ubiquitinated during G2/M phases.1 Publication
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.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP14635.
MaxQBiP14635.
PaxDbiP14635.
PRIDEiP14635.

PTM databases

iPTMnetiP14635.
PhosphoSiteiP14635.

Expressioni

Developmental stagei

Accumulates steadily during G2 and is abruptly destroyed at mitosis.1 Publication

Gene expression databases

BgeeiP14635.
CleanExiHS_CCNB1.
ExpressionAtlasiP14635. baseline and differential.
GenevisibleiP14635. HS.

Organism-specific databases

HPAiCAB000115.
CAB003804.
HPA030741.

Interactioni

Subunit structurei

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).6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCNB1IP1Q9NPC32EBI-495332,EBI-745269
CDK1P0649310EBI-495332,EBI-444308
CDKN1AP389362EBI-495332,EBI-375077
CDKN1BP465272EBI-495332,EBI-519280
FOXO1Q127782EBI-495332,EBI-1108782
PKMYT1Q996405EBI-495332,EBI-495308
UBE2KP610862EBI-495332,EBI-473850
UHRF2Q96PU42EBI-495332,EBI-625304

GO - Molecular functioni

  • patched binding Source: BHF-UCL
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107332. 120 interactions.
DIPiDIP-59N.
IntActiP14635. 57 interactions.
MINTiMINT-1202632.
STRINGi9606.ENSP00000256442.

Chemistry

BindingDBiP14635.

Structurei

Secondary structure

1
433
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi171 – 18414Combined sources
Turni189 – 1946Combined sources
Beta strandi195 – 1973Combined sources
Helixi199 – 21517Combined sources
Helixi220 – 23516Combined sources
Helixi241 – 2433Combined sources
Helixi244 – 25916Combined sources
Helixi266 – 2727Combined sources
Turni273 – 2753Combined sources
Helixi279 – 29214Combined sources
Turni293 – 2953Combined sources
Helixi302 – 31211Combined sources
Helixi317 – 33014Combined sources
Helixi334 – 3363Combined sources
Beta strandi337 – 3393Combined sources
Helixi341 – 35515Combined sources
Helixi363 – 3697Combined sources
Helixi373 – 39119Combined sources
Helixi399 – 4035Combined sources
Helixi407 – 4093Combined sources
Helixi412 – 4143Combined sources
Helixi416 – 4194Combined sources
Helixi421 – 4288Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2B9RX-ray2.90A/B165-433[»]
2JGZX-ray2.90B167-426[»]
4Y72X-ray2.30B165-433[»]
5HQ0X-ray2.30B165-433[»]
DisProtiDP00223.
ProteinModelPortaliP14635.
SMRiP14635. Positions 167-426.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14635.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni169 – 1779Interaction with CDK2
Regioni258 – 2614Interaction with CDK2

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi51 – 8535Lys-richAdd
BLAST

Sequence similaritiesi

Belongs to the cyclin family. Cyclin AB subfamily.Curated

Phylogenomic databases

eggNOGiKOG0653. Eukaryota.
COG5024. LUCA.
GeneTreeiENSGT00760000118939.
HOGENOMiHOG000167672.
HOVERGENiHBG061650.
InParanoidiP14635.
KOiK05868.
OMAiHMTVKNK.
OrthoDBiEOG7ZGX3C.
PhylomeDBiP14635.
TreeFamiTF101001.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR004367. Cyclin_C-dom.
IPR006671. Cyclin_N.
[Graphical view]
PfamiPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 2 hits.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
PROSITEiPS00292. CYCLINS. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P14635-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MALRVTRNSK INAENKAKIN MAGAKRVPTA PAATSKPGLR PRTALGDIGN
60 70 80 90 100
KVSEQLQAKM PMKKEAKPSA TGKVIDKKLP KPLEKVPMLV PVPVSEPVPE
110 120 130 140 150
PEPEPEPEPV KEEKLSPEPI LVDTASPSPM ETSGCAPAEE DLCQAFSDVI
160 170 180 190 200
LAVNDVDAED GADPNLCSEY VKDIYAYLRQ LEEEQAVRPK YLLGREVTGN
210 220 230 240 250
MRAILIDWLV QVQMKFRLLQ ETMYMTVSII DRFMQNNCVP KKMLQLVGVT
260 270 280 290 300
AMFIASKYEE MYPPEIGDFA FVTDNTYTKH QIRQMEMKIL RALNFGLGRP
310 320 330 340 350
LPLHFLRRAS KIGEVDVEQH TLAKYLMELT MLDYDMVHFP PSQIAAGAFC
360 370 380 390 400
LALKILDNGE WTPTLQHYLS YTEESLLPVM QHLAKNVVMV NQGLTKHMTV
410 420 430
KNKYATSKHA KISTLPQLNS ALVQDLAKAV AKV
Length:433
Mass (Da):48,337
Last modified:April 1, 1990 - v1
Checksum:iE2C4767AE8A11EC0
GO
Isoform 2 (identifier: P14635-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     362-398: Missing.

Note: No experimental confirmation available.
Show »
Length:396
Mass (Da):44,102
Checksum:i1B7AFCE21614F6D5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti108 – 1081E → G in BAF82120 (PubMed:14702039).Curated
Sequence conflicti153 – 1531V → A in BAF82120 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei362 – 39837Missing in isoform 2. 1 PublicationVSP_053892Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25753 mRNA. No translation available.
AY338491 Genomic DNA. Translation: AAP88038.1.
AK289431 mRNA. Translation: BAF82120.1.
BT020128 mRNA. Translation: AAV38930.1.
AC010273 Genomic DNA. No translation available.
AC022107 Genomic DNA. No translation available.
BC006510 mRNA. Translation: AAH06510.1.
CCDSiCCDS3997.1. [P14635-1]
PIRiA32992.
RefSeqiNP_114172.1. NM_031966.3. [P14635-1]
UniGeneiHs.23960.

Genome annotation databases

EnsembliENST00000256442; ENSP00000256442; ENSG00000134057. [P14635-1]
ENST00000505500; ENSP00000424588; ENSG00000134057. [P14635-2]
GeneIDi891.
KEGGihsa:891.
UCSCiuc003jvm.4. human. [P14635-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25753 mRNA. No translation available.
AY338491 Genomic DNA. Translation: AAP88038.1.
AK289431 mRNA. Translation: BAF82120.1.
BT020128 mRNA. Translation: AAV38930.1.
AC010273 Genomic DNA. No translation available.
AC022107 Genomic DNA. No translation available.
BC006510 mRNA. Translation: AAH06510.1.
CCDSiCCDS3997.1. [P14635-1]
PIRiA32992.
RefSeqiNP_114172.1. NM_031966.3. [P14635-1]
UniGeneiHs.23960.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2B9RX-ray2.90A/B165-433[»]
2JGZX-ray2.90B167-426[»]
4Y72X-ray2.30B165-433[»]
5HQ0X-ray2.30B165-433[»]
DisProtiDP00223.
ProteinModelPortaliP14635.
SMRiP14635. Positions 167-426.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107332. 120 interactions.
DIPiDIP-59N.
IntActiP14635. 57 interactions.
MINTiMINT-1202632.
STRINGi9606.ENSP00000256442.

Chemistry

BindingDBiP14635.
ChEMBLiCHEMBL1907602.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

PTM databases

iPTMnetiP14635.
PhosphoSiteiP14635.

Polymorphism and mutation databases

BioMutaiCCNB1.
DMDMi116176.

Proteomic databases

EPDiP14635.
MaxQBiP14635.
PaxDbiP14635.
PRIDEiP14635.

Protocols and materials databases

DNASUi891.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000256442; ENSP00000256442; ENSG00000134057. [P14635-1]
ENST00000505500; ENSP00000424588; ENSG00000134057. [P14635-2]
GeneIDi891.
KEGGihsa:891.
UCSCiuc003jvm.4. human. [P14635-1]

Organism-specific databases

CTDi891.
GeneCardsiCCNB1.
HGNCiHGNC:1579. CCNB1.
HPAiCAB000115.
CAB003804.
HPA030741.
MIMi123836. gene.
neXtProtiNX_P14635.
PharmGKBiPA95.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0653. Eukaryota.
COG5024. LUCA.
GeneTreeiENSGT00760000118939.
HOGENOMiHOG000167672.
HOVERGENiHBG061650.
InParanoidiP14635.
KOiK05868.
OMAiHMTVKNK.
OrthoDBiEOG7ZGX3C.
PhylomeDBiP14635.
TreeFamiTF101001.

Enzyme and pathway databases

ReactomeiR-HSA-113507. E2F-enabled inhibition of pre-replication complex formation.
R-HSA-156711. Polo-like kinase mediated events.
R-HSA-162658. Golgi Cisternae Pericentriolar Stack Reorganization.
R-HSA-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-HSA-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-HSA-176412. Phosphorylation of the APC/C.
R-HSA-176417. Phosphorylation of Emi1.
R-HSA-2299718. Condensation of Prophase Chromosomes.
R-HSA-2465910. MASTL Facilitates Mitotic Progression.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-2514853. Condensation of Prometaphase Chromosomes.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-2980767. Activation of NIMA Kinases NEK9, NEK6, NEK7.
R-HSA-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-HSA-380320. Recruitment of NuMA to mitotic centrosomes.
R-HSA-4419969. Depolymerisation of the Nuclear Lamina.
R-HSA-69273. Cyclin A/B1 associated events during G2/M transition.
R-HSA-69478. G2/M DNA replication checkpoint.
R-HSA-75035. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
SignaLinkiP14635.

Miscellaneous databases

ChiTaRSiCCNB1. human.
EvolutionaryTraceiP14635.
GeneWikiiCyclin_B1.
GenomeRNAii891.
NextBioi35463711.
PROiP14635.
SOURCEiSearch...

Gene expression databases

BgeeiP14635.
CleanExiHS_CCNB1.
ExpressionAtlasiP14635. baseline and differential.
GenevisibleiP14635. HS.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR004367. Cyclin_C-dom.
IPR006671. Cyclin_N.
[Graphical view]
PfamiPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 2 hits.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
PROSITEiPS00292. CYCLINS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of a human cyclin cDNA: evidence for cyclin mRNA and protein regulation in the cell cycle and for interaction with p34cdc2."
    Pines J., Hunter T.
    Cell 58:833-846(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, SUBUNIT.
  2. NIEHS SNPs program
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    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.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  5. "The DNA sequence and comparative analysis of human chromosome 5."
    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.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Placenta.
  7. "Structure and growth-dependent regulation of the human cyclin B1 promoter."
    Piaggio G., Farina A., Perrotti D., Manni I., Fuschi P., Sacchi A., Gaetano C.
    Exp. Cell Res. 216:396-402(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
  8. "Cyclin F regulates the nuclear localization of cyclin B1 through a cyclin-cyclin interaction."
    Kong M., Barnes E.A., Ollendorff V., Donoghue D.J.
    EMBO J. 19:1378-1388(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CCNF.
  9. "Cooperative phosphorylation including the activity of polo-like kinase 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-126; SER-128; SER-133 AND SER-147, MUTAGENESIS OF SER-133.
  10. "RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to phosphorylate epsin during the switch off of endocytosis in mitosis."
    Rosse C., L'Hoste S., Offner N., Picard A., Camonis J.
    J. Biol. Chem. 278:30597-30604(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RALBP1.
  11. "A novel RING finger protein, human enhancer of invasion 10, alters mitotic progression through regulation of cyclin B levels."
    Toby G.G., Gherraby W., Coleman T.R., Golemis E.A.
    Mol. Cell. Biol. 23:2109-2122(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HEI10.
  12. "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) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-126; SER-133 AND SER-147, MUTAGENESIS OF SER-133 AND SER-147.
  13. "NIPA defines an SCF-type mammalian E3 ligase that regulates mitotic entry."
    Bassermann F., von Klitzing C., Munch S., Bai R.-Y., Kawaguchi H., Morris S.W., Peschel C., Duyster J.
    Cell 122:45-57(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  14. "p21-mediated nuclear retention of cyclin B1-Cdk1 in response to genotoxic stress."
    Baus Charrier-Savournin F., Chateau M.-T., Gire V., Sedivy J., Piette J., Dulic V.
    Mol. Biol. Cell 15:3965-3976(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  15. "Cdk5 activator-binding protein C53 regulates apoptosis induced by genotoxic stress via modulating the G2/M DNA damage checkpoint."
    Jiang H., Luo S., Li H.
    J. Biol. Chem. 280:20651-20659(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDK5RAP3.
  16. "Kinase-selective enrichment enables quantitative phosphoproteomics of the 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Cyclin B and cyclin A confer different substrate recognition properties on CDK2."
    Brown N.R., Lowe E.D., Petri E., Skamnaki V., Antrobus R., Johnson L.N.
    Cell Cycle 6:1350-1359(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 167-426 IN COMPLEX WITH PHOSPHORYLATED CDK2, FUNCTION.
  20. Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 165-433, FUNCTION.

Entry informationi

Entry nameiCCNB1_HUMAN
AccessioniPrimary (citable) accession number: P14635
Secondary accession number(s): A8K066, Q5TZP9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: April 13, 2016
This is version 171 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.