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P14635 (CCNB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
G2/mitotic-specific cyclin-B1
Gene names
Name:CCNB1
Synonyms:CCNB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length433 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential for the control of the cell cycle at the G2/M (mitosis) transition. Ref.18 Ref.19

Subunit structure

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. Ref.1 Ref.8 Ref.10 Ref.11

Subcellular location

Cytoplasm. Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome Ref.8 Ref.9 Ref.12 Ref.14.

Developmental stage

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

Post-translational modification

Ubiquitinated by the SCF(NIPA) complex during interphase, leading to its destruction. Not ubiquitinated during G2/M phases. Ref.13

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. Ref.9 Ref.12

Sequence similarities

Belongs to the cyclin family. Cyclin AB subfamily.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
   Molecular functionCyclin
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

G2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process

Traceable author statement. Source: Reactome

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to fatty acid

Inferred from electronic annotation. Source: Ensembl

cellular response to hypoxia

Inferred from electronic annotation. Source: Ensembl

cellular response to iron(III) ion

Inferred from electronic annotation. Source: Ensembl

cellular response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

digestive tract development

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic metaphase plate congression

Inferred from mutant phenotype PubMed 18195732. Source: BHF-UCL

mitotic nuclear envelope disassembly

Traceable author statement. Source: Reactome

mitotic spindle checkpoint

Inferred from mutant phenotype PubMed 18195732. Source: BHF-UCL

mitotic spindle stabilization

Inferred from mutant phenotype PubMed 18195732. Source: BHF-UCL

negative regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

oocyte maturation

Inferred from electronic annotation. Source: Ensembl

positive regulation of attachment of spindle microtubules to kinetochore

Inferred from mutant phenotype PubMed 18195732. Source: BHF-UCL

positive regulation of cardiac muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of histone phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of mRNA 3'-end processing

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitotic cell cycle

Inferred from mutant phenotype PubMed 18195732. Source: BHF-UCL

positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

protein complex assembly

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

regulation of cell cycle

Traceable author statement. Source: Reactome

regulation of chromosome condensation

Inferred from electronic annotation. Source: Ensembl

regulation of cyclin-dependent protein serine/threonine kinase activity

Inferred from electronic annotation. Source: InterPro

regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

response to DDT

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

tissue regeneration

Inferred from electronic annotation. Source: Ensembl

ventricular cardiac muscle cell development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcentrosome

Inferred from direct assay Ref.12. Source: UniProtKB

condensed nuclear chromosome outer kinetochore

Inferred from direct assay PubMed 18195732. Source: BHF-UCL

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

membrane

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from electronic annotation. Source: InterPro

spindle pole

Inferred from direct assay PubMed 18195732. Source: BHF-UCL

   Molecular_functionkinase activity

Inferred from electronic annotation. Source: Ensembl

patched binding

Inferred from physical interaction PubMed 11331587. Source: BHF-UCL

protein kinase binding

Inferred from physical interaction Ref.12. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P14635-1)

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.
Isoform 2 (identifier: P14635-2)

The sequence of this isoform differs from the canonical sequence as follows:
     362-398: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 433433G2/mitotic-specific cyclin-B1
PRO_0000080350

Regions

Region169 – 1779Interaction with CDK2
Region258 – 2614Interaction with CDK2
Compositional bias51 – 8535Lys-rich

Amino acid modifications

Modified residue731N6-acetyllysine Ref.16
Modified residue1261Phosphoserine; by CDK1 Ref.9 Ref.12
Modified residue1281Phosphoserine Ref.9
Modified residue1331Phosphoserine; by PLK1 Ref.9 Ref.12
Modified residue1471Phosphoserine Ref.9 Ref.12
Modified residue3211Phosphothreonine Ref.15

Natural variations

Alternative sequence362 – 39837Missing in isoform 2.
VSP_053892

Experimental info

Mutagenesis1331S → A: Strongly impairs phosphorylation by PLK1. Ref.9 Ref.12
Mutagenesis1471S → A: Does not affect phosphorylation by PLK1. Ref.12
Sequence conflict1081E → G in BAF82120. Ref.3
Sequence conflict1531V → A in BAF82120. Ref.3

Secondary structure

........................................... 433
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: E2C4767AE8A11EC0

FASTA43348,337
        10         20         30         40         50         60 
MALRVTRNSK INAENKAKIN MAGAKRVPTA PAATSKPGLR PRTALGDIGN KVSEQLQAKM 

        70         80         90        100        110        120 
PMKKEAKPSA TGKVIDKKLP KPLEKVPMLV PVPVSEPVPE PEPEPEPEPV KEEKLSPEPI 

       130        140        150        160        170        180 
LVDTASPSPM ETSGCAPAEE DLCQAFSDVI LAVNDVDAED GADPNLCSEY VKDIYAYLRQ 

       190        200        210        220        230        240 
LEEEQAVRPK YLLGREVTGN MRAILIDWLV QVQMKFRLLQ ETMYMTVSII DRFMQNNCVP 

       250        260        270        280        290        300 
KKMLQLVGVT AMFIASKYEE MYPPEIGDFA FVTDNTYTKH QIRQMEMKIL RALNFGLGRP 

       310        320        330        340        350        360 
LPLHFLRRAS KIGEVDVEQH TLAKYLMELT MLDYDMVHFP PSQIAAGAFC LALKILDNGE 

       370        380        390        400        410        420 
WTPTLQHYLS YTEESLLPVM QHLAKNVVMV NQGLTKHMTV KNKYATSKHA KISTLPQLNS 

       430 
ALVQDLAKAV AKV 

« Hide

Isoform 2 [UniParc].

Checksum: 1B7AFCE21614F6D5
Show »

FASTA39644,102

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA32992.
RefSeqNP_114172.1. NM_031966.3.
UniGeneHs.23960.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2B9RX-ray2.90A/B165-433[»]
2JGZX-ray2.90B167-426[»]
DisProtDP00223.
ProteinModelPortalP14635.
SMRP14635. Positions 167-426.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107332. 86 interactions.
DIPDIP-59N.
IntActP14635. 22 interactions.
MINTMINT-1202632.
STRING9606.ENSP00000256442.

Chemistry

BindingDBP14635.
ChEMBLCHEMBL1907602.

PTM databases

PhosphoSiteP14635.

Polymorphism databases

DMDM116176.

Proteomic databases

PaxDbP14635.
PRIDEP14635.

Protocols and materials databases

DNASU891.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000256442; ENSP00000256442; ENSG00000134057.
ENST00000505500; ENSP00000424588; ENSG00000134057.
GeneID891.
KEGGhsa:891.
UCSCuc003jvm.3. human. [P14635-1]

Organism-specific databases

CTD891.
GeneCardsGC05P068462.
HGNCHGNC:1579. CCNB1.
HPACAB000115.
CAB003804.
HPA030741.
MIM123836. gene.
neXtProtNX_P14635.
PharmGKBPA95.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5024.
HOGENOMHOG000167672.
HOVERGENHBG061650.
InParanoidP14635.
KOK05868.
OMAHMTVKNK.
OrthoDBEOG7ZGX3C.
PhylomeDBP14635.
TreeFamTF101001.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
SignaLinkP14635.

Gene expression databases

ArrayExpressP14635.
BgeeP14635.
CleanExHS_CCNB1.
GenevestigatorP14635.

Family and domain databases

Gene3D1.10.472.10. 2 hits.
InterProIPR013763. Cyclin-like.
IPR014400. Cyclin_A/B/D/E.
IPR004367. Cyclin_C-dom.
IPR006671. Cyclin_N.
[Graphical view]
PfamPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
PIRSFPIRSF001771. Cyclin_A_B_D_E. 1 hit.
SMARTSM00385. CYCLIN. 2 hits.
[Graphical view]
SUPFAMSSF47954. SSF47954. 2 hits.
PROSITEPS00292. CYCLINS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCCNB1. human.
EvolutionaryTraceP14635.
GeneWikiCyclin_B1.
GenomeRNAi891.
NextBio35463711.
PROP14635.
SOURCESearch...

Entry information

Entry nameCCNB1_HUMAN
AccessionPrimary (citable) accession number: P14635
Secondary accession number(s): A8K066, Q5TZP9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: April 16, 2014
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM