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Protein

Cyclin-dependent kinase B2-1

Gene

CDKB2-1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.
ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei43 – 431ATPPROSITE-ProRule annotation
Active sitei145 – 1451Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi20 – 289ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • G2/M transition of mitotic cell cycle Source: TAIR
  • histone phosphorylation Source: TAIR
  • hormone-mediated signaling pathway Source: TAIR
  • regulation of G2/M transition of mitotic cell cycle Source: TAIR
  • regulation of meristem structural organization Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT1G76540-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-dependent kinase B2-1 (EC:2.7.11.22, EC:2.7.11.23)
Short name:
CDKB2;1
Gene namesi
Name:CDKB2-1
Ordered Locus Names:At1g76540
ORF Names:F14G6.14
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G76540.

Subcellular locationi

GO - Cellular componenti

  • cyclin-dependent protein kinase holoenzyme complex Source: TAIR
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 313313Cyclin-dependent kinase B2-1PRO_0000293115Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei25 – 251PhosphotyrosineBy similarity
Modified residuei179 – 1791PhosphothreonineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ8LF80.
PRIDEiQ8LF80.

Expressioni

Tissue specificityi

Expressed in root tips, shoot apical meristem, leaf primordia vascular tissues and tapetum of anthers.3 Publications

Developmental stagei

Expressed from early G2 phase and increases to reach a peak at mitosis.1 Publication

Interactioni

Subunit structurei

Interacts with CYCD4-1 and CKS1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CKS1O232495EBI-1253579,EBI-1253127
CYCD1-1P427512EBI-1253579,EBI-2025690
CYCD4-1Q8LGA14EBI-1253579,EBI-1253202

Protein-protein interaction databases

BioGridi29206. 35 interactions.
IntActiQ8LF80. 12 interactions.
STRINGi3702.AT1G76540.1.

Structurei

3D structure databases

ProteinModelPortaliQ8LF80.
SMRiQ8LF80. Positions 10-307.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 304291Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233024.
InParanoidiQ8LF80.
KOiK07760.
OMAiISAKMAM.
PhylomeDBiQ8LF80.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8LF80-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDEGVIAVSA MDAFEKLEKV GEGTYGKVYR AREKATGKIV ALKKTRLHED
60 70 80 90 100
EEGVPSTTLR EISILRMLAR DPHVVRLMDV KQGLSKEGKT VLYLVFEYMD
110 120 130 140 150
TDVKKFIRSF RSTGKNIPTQ TIKSLMYQLC KGMAFCHGHG ILHRDLKPHN
160 170 180 190 200
LLMDPKTMRL KIADLGLARA FTLPMKKYTH EILTLWYRAP EVLLGATHYS
210 220 230 240 250
TAVDMWSVGC IFAELVTNQA IFQGDSELQQ LLHIFKLFGT PNEEMWPGVS
260 270 280 290 300
TLKNWHEYPQ WKPSTLSSAV PNLDEAGVDL LSKMLQYEPA KRISAKMAME
310
HPYFDDLPEK SSL
Length:313
Mass (Da):35,593
Last modified:July 10, 2007 - v2
Checksum:i7E0EBD7A553DB9C9
GO

Sequence cautioni

The sequence AAM61558.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti250 – 2501S → G in AAK63856 (PubMed:14593172).Curated
Sequence conflicti250 – 2501S → G in AAN28798 (PubMed:14593172).Curated
Sequence conflicti267 – 2671S → F in AAK63856 (PubMed:14593172).Curated
Sequence conflicti267 – 2671S → F in AAN28798 (PubMed:14593172).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ297936 mRNA. Translation: CAC34052.1.
AB047279 mRNA. Translation: BAB62068.1.
AC015450 Genomic DNA. Translation: AAG51960.1.
CP002684 Genomic DNA. Translation: AEE35857.1.
AF389283 mRNA. Translation: AAK63856.1.
AY143859 mRNA. Translation: AAN28798.1.
AY085000 mRNA. Translation: AAM61558.1. Different initiation.
PIRiD96793.
RefSeqiNP_177780.1. NM_106304.2.
UniGeneiAt.10322.

Genome annotation databases

EnsemblPlantsiAT1G76540.1; AT1G76540.1; AT1G76540.
GeneIDi843987.
KEGGiath:AT1G76540.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ297936 mRNA. Translation: CAC34052.1.
AB047279 mRNA. Translation: BAB62068.1.
AC015450 Genomic DNA. Translation: AAG51960.1.
CP002684 Genomic DNA. Translation: AEE35857.1.
AF389283 mRNA. Translation: AAK63856.1.
AY143859 mRNA. Translation: AAN28798.1.
AY085000 mRNA. Translation: AAM61558.1. Different initiation.
PIRiD96793.
RefSeqiNP_177780.1. NM_106304.2.
UniGeneiAt.10322.

3D structure databases

ProteinModelPortaliQ8LF80.
SMRiQ8LF80. Positions 10-307.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi29206. 35 interactions.
IntActiQ8LF80. 12 interactions.
STRINGi3702.AT1G76540.1.

Proteomic databases

PaxDbiQ8LF80.
PRIDEiQ8LF80.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G76540.1; AT1G76540.1; AT1G76540.
GeneIDi843987.
KEGGiath:AT1G76540.

Organism-specific databases

GeneFarmi3281. 107.
TAIRiAT1G76540.

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233024.
InParanoidiQ8LF80.
KOiK07760.
OMAiISAKMAM.
PhylomeDBiQ8LF80.

Enzyme and pathway databases

BioCyciARA:AT1G76540-MONOMER.

Miscellaneous databases

PROiQ8LF80.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of novel cyclin-dependent kinases interacting with the CKS1 protein of Arabidopsis."
    Boudolf V., Rombauts S., Naudts M., Inze D., de Veylder L.
    J. Exp. Bot. 52:1381-1382(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH CKS1.
  2. "Arabidopsis D-type cyclin CYCD4;1 is a novel cyclin partner of B2-type cyclin-dependent kinase."
    Kono A., Umeda-Hara C., Lee J., Ito M., Uchimiya H., Umeda M.
    Plant Physiol. 132:1315-1321(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH CYCD4-1.
  3. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "Genome-wide analysis of core cell cycle genes in Arabidopsis."
    Vandepoele K., Raes J., de Veylder L., Rouze P., Rombauts S., Inze D.
    Plant Cell 14:903-916(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  8. "Cell cycle regulation in plant development."
    Inze D., de Veylder L.
    Annu. Rev. Genet. 40:77-105(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  9. "Expression of B2-type cyclin-dependent kinase is controlled by protein degradation in Arabidopsis thaliana."
    Adachi S., Uchimiya H., Umeda M.
    Plant Cell Physiol. 47:1683-1686(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  10. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCKB21_ARATH
AccessioniPrimary (citable) accession number: Q8LF80
Secondary accession number(s): Q94EX2, Q9C527
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: July 10, 2007
Last modified: June 24, 2015
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Protein abundance may be regulated through proteasome-mediated protein degradation.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.