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P14635

- CCNB1_HUMAN

UniProt

P14635 - CCNB1_HUMAN

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Protein

G2/mitotic-specific cyclin-B1

Gene

CCNB1

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. kinase activity Source: Ensembl
  2. patched binding Source: BHF-UCL
  3. protein kinase binding Source: UniProtKB

GO - Biological processi

  1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  2. cellular response to fatty acid Source: Ensembl
  3. cellular response to hypoxia Source: Ensembl
  4. cellular response to iron(III) ion Source: Ensembl
  5. cellular response to organic cyclic compound Source: Ensembl
  6. digestive tract development Source: Ensembl
  7. G1/S transition of mitotic cell cycle Source: Reactome
  8. G2/M transition of mitotic cell cycle Source: Reactome
  9. in utero embryonic development Source: Ensembl
  10. mitotic cell cycle Source: Reactome
  11. mitotic metaphase plate congression Source: BHF-UCL
  12. mitotic nuclear envelope disassembly Source: Reactome
  13. mitotic spindle checkpoint Source: BHF-UCL
  14. mitotic spindle stabilization Source: BHF-UCL
  15. negative regulation of gene expression Source: Ensembl
  16. negative regulation of protein phosphorylation Source: Ensembl
  17. oocyte maturation Source: Ensembl
  18. positive regulation of attachment of spindle microtubules to kinetochore Source: BHF-UCL
  19. positive regulation of cardiac muscle cell proliferation Source: Ensembl
  20. positive regulation of histone phosphorylation Source: Ensembl
  21. positive regulation of mitotic cell cycle Source: BHF-UCL
  22. positive regulation of mRNA 3'-end processing Source: Ensembl
  23. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  24. protein complex assembly Source: Ensembl
  25. protein phosphorylation Source: Ensembl
  26. regulation of cell cycle Source: Reactome
  27. regulation of chromosome condensation Source: Ensembl
  28. regulation of cyclin-dependent protein serine/threonine kinase activity Source: InterPro
  29. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  30. response to DDT Source: Ensembl
  31. response to drug Source: Ensembl
  32. response to mechanical stimulus Source: Ensembl
  33. spermatogenesis Source: Ensembl
  34. tissue regeneration Source: Ensembl
  35. ventricular cardiac muscle cell development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiREACT_1006. Polo-like kinase mediated events.
REACT_1100. Golgi Cisternae Pericentriolar Stack Reorganization.
REACT_1321. E2F-enabled inhibition of pre-replication complex formation.
REACT_150182. MASTL Facilitates Mitotic Progression.
REACT_150260. Condensation of Prometaphase Chromosomes.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_15510. Recruitment of NuMA to mitotic centrosomes.
REACT_160122. Activation of NIMA Kinases NEK9, NEK6, NEK7.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_163931. Nuclear Pore Complex (NPC) Disassembly.
REACT_172744. Condensation of Prophase Chromosomes.
REACT_1846. G2/M DNA replication checkpoint.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_200828. Depolymerisation of the Nuclear Lamina.
REACT_407. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
REACT_6875. Phosphorylation of Emi1.
REACT_6904. Phosphorylation of the APC/C.
SignaLinkiP14635.

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
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:1579. CCNB1.

Subcellular locationi

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. condensed nuclear chromosome outer kinetochore Source: BHF-UCL
  3. cytoplasm Source: UniProtKB
  4. cytosol Source: Reactome
  5. membrane Source: Ensembl
  6. nucleoplasm Source: Reactome
  7. nucleus Source: BHF-UCL
  8. 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.

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-acetyllysine1 Publication
Modified residuei126 – 1261Phosphoserine; by CDK12 Publications
Modified residuei128 – 1281Phosphoserine1 Publication
Modified residuei133 – 1331Phosphoserine; by PLK12 Publications
Modified residuei147 – 1471Phosphoserine2 Publications
Modified residuei321 – 3211Phosphothreonine1 Publication

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.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP14635.
PaxDbiP14635.
PRIDEiP14635.

PTM databases

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.
GenevestigatoriP14635.

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.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCNB1IP1Q9NPC32EBI-495332,EBI-745269
CDK1P064936EBI-495332,EBI-444308
FOXO1Q127782EBI-495332,EBI-1108782
PKMYT1Q996404EBI-495332,EBI-495308
UBE2KP610862EBI-495332,EBI-473850
UHRF2Q96PU42EBI-495332,EBI-625304

Protein-protein interaction databases

BioGridi107332. 88 interactions.
DIPiDIP-59N.
IntActiP14635. 24 interactions.
MINTiMINT-1202632.
STRINGi9606.ENSP00000256442.

Structurei

Secondary structure

1
433
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni173 – 1775Combined sources
Helixi178 – 1836Combined sources
Turni189 – 1924Combined sources
Beta strandi193 – 1975Combined sources
Helixi199 – 21517Combined sources
Helixi220 – 23415Combined sources
Helixi241 – 2433Combined sources
Helixi244 – 25916Combined sources
Helixi266 – 2727Combined sources
Beta strandi275 – 2773Combined sources
Helixi279 – 29214Combined sources
Helixi302 – 31110Combined sources
Helixi317 – 32913Combined sources
Helixi330 – 3323Combined sources
Helixi334 – 3363Combined sources
Beta strandi337 – 3393Combined sources
Helixi343 – 35614Combined sources
Helixi365 – 3684Combined sources
Turni375 – 3784Combined sources
Helixi379 – 38911Combined sources
Helixi399 – 4035Combined sources
Helixi407 – 4093Combined sources
Helixi412 – 4143Combined sources
Helixi420 – 4223Combined 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[»]
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

eggNOGiCOG5024.
GeneTreeiENSGT00760000118939.
HOGENOMiHOG000167672.
HOVERGENiHBG061650.
InParanoidiP14635.
KOiK05868.
OMAiHMTVKNK.
OrthoDBiEOG7ZGX3C.
PhylomeDBiP14635.
TreeFamiTF101001.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR014400. Cyclin_A/B/D/E/F.
IPR004367. Cyclin_C-dom.
IPR006671. Cyclin_N.
[Graphical view]
PfamiPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001771. Cyclin_A_B_D_E. 1 hit.
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. Align

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.3. human. [P14635-1]

Polymorphism databases

DMDMi116176.

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 .
CCDSi CCDS3997.1. [P14635-1 ]
PIRi A32992.
RefSeqi NP_114172.1. NM_031966.3. [P14635-1 ]
UniGenei Hs.23960.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2B9R X-ray 2.90 A/B 165-433 [» ]
2JGZ X-ray 2.90 B 167-426 [» ]
DisProti DP00223.
ProteinModelPortali P14635.
SMRi P14635. Positions 167-426.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107332. 88 interactions.
DIPi DIP-59N.
IntActi P14635. 24 interactions.
MINTi MINT-1202632.
STRINGi 9606.ENSP00000256442.

Chemistry

BindingDBi P14635.
ChEMBLi CHEMBL1907602.

PTM databases

PhosphoSitei P14635.

Polymorphism databases

DMDMi 116176.

Proteomic databases

MaxQBi P14635.
PaxDbi P14635.
PRIDEi P14635.

Protocols and materials databases

DNASUi 891.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000256442 ; ENSP00000256442 ; ENSG00000134057 . [P14635-1 ]
ENST00000505500 ; ENSP00000424588 ; ENSG00000134057 . [P14635-2 ]
GeneIDi 891.
KEGGi hsa:891.
UCSCi uc003jvm.3. human. [P14635-1 ]

Organism-specific databases

CTDi 891.
GeneCardsi GC05P068462.
HGNCi HGNC:1579. CCNB1.
HPAi CAB000115.
CAB003804.
HPA030741.
MIMi 123836. gene.
neXtProti NX_P14635.
PharmGKBi PA95.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5024.
GeneTreei ENSGT00760000118939.
HOGENOMi HOG000167672.
HOVERGENi HBG061650.
InParanoidi P14635.
KOi K05868.
OMAi HMTVKNK.
OrthoDBi EOG7ZGX3C.
PhylomeDBi P14635.
TreeFami TF101001.

Enzyme and pathway databases

Reactomei REACT_1006. Polo-like kinase mediated events.
REACT_1100. Golgi Cisternae Pericentriolar Stack Reorganization.
REACT_1321. E2F-enabled inhibition of pre-replication complex formation.
REACT_150182. MASTL Facilitates Mitotic Progression.
REACT_150260. Condensation of Prometaphase Chromosomes.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_15510. Recruitment of NuMA to mitotic centrosomes.
REACT_160122. Activation of NIMA Kinases NEK9, NEK6, NEK7.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_163931. Nuclear Pore Complex (NPC) Disassembly.
REACT_172744. Condensation of Prophase Chromosomes.
REACT_1846. G2/M DNA replication checkpoint.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_200828. Depolymerisation of the Nuclear Lamina.
REACT_407. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
REACT_6875. Phosphorylation of Emi1.
REACT_6904. Phosphorylation of the APC/C.
SignaLinki P14635.

Miscellaneous databases

ChiTaRSi CCNB1. human.
EvolutionaryTracei P14635.
GeneWikii Cyclin_B1.
GenomeRNAii 891.
NextBioi 35463711.
PROi P14635.
SOURCEi Search...

Gene expression databases

Bgeei P14635.
CleanExi HS_CCNB1.
ExpressionAtlasi P14635. baseline and differential.
Genevestigatori P14635.

Family and domain databases

Gene3Di 1.10.472.10. 2 hits.
InterProi IPR013763. Cyclin-like.
IPR014400. Cyclin_A/B/D/E/F.
IPR004367. Cyclin_C-dom.
IPR006671. Cyclin_N.
[Graphical view ]
Pfami PF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF001771. Cyclin_A_B_D_E. 1 hit.
SMARTi SM00385. CYCLIN. 2 hits.
[Graphical view ]
SUPFAMi SSF47954. SSF47954. 2 hits.
PROSITEi PS00292. CYCLINS. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "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.
  16. "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].
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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.
  19. "The crystal structure of human cyclin B."
    Petri E.T., Errico A., Escobedo L., Hunt T., Basavappa R.
    Cell Cycle 6:1342-1349(2007) [PubMed] [Europe PMC] [Abstract]
    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: November 26, 2014
This is version 155 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

External Data

Dasty 3