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Protein

Cell division control protein 2 homolog 1

Gene

CDC2A

Organism
Medicago sativa (Alfalfa)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Plays a key role in the control of the eukaryotic cell cycle. Component of the kinase complex that phosphorylates the repetitive C-terminus of RNA polymerase II.

Catalytic activityi

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

Enzyme regulationi

Phosphorylation at Thr-11 or Tyr-12 inactivates the enzyme, while phosphorylation at Thr-158 activates it.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei30 – 301ATPPROSITE-ProRule annotation
Active sitei124 – 1241Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi7 – 159ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB-EC
  3. RNA polymerase II carboxy-terminal domain kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell division Source: UniProtKB-KW
  2. mitotic nuclear division Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division control protein 2 homolog 1 (EC:2.7.11.22, EC:2.7.11.23)
Gene namesi
Name:CDC2A
OrganismiMedicago sativa (Alfalfa)
Taxonomic identifieri3879 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeMedicago

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 291›291Cell division control protein 2 homolog 1PRO_0000085753Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei11 – 111PhosphothreonineBy similarity
Modified residuei12 – 121PhosphotyrosineBy similarity
Modified residuei158 – 1581Phosphothreonine; by CAKBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP24923.

Expressioni

Tissue specificityi

Found in most organs including root, young leaf, stem, vegetative meristem and flower bud.

Structurei

3D structure databases

ProteinModelPortaliP24923.
SMRiP24923. Positions 2-287.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 284284Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

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: Fragment.

P24923-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
GENVEKIGEG TYGVVYKARD RVTNETIALK KIRLEQEDEG VPSTAIREIS
60 70 80 90 100
LLKEMQHRNI VRLQDVVHSD KRLYLVFEYL DLDLKKHMDS SPEFIKDPRQ
110 120 130 140 150
VKMFLYQMLC GIAYCHSHRV LHRDLKPQNL LIDRRTNSLK LADFGLARAF
160 170 180 190 200
GIPVRTFTHE VVTLWYRAPE ILLGSRHYST PVDVWSVGCI FAEMANRRPL
210 220 230 240 250
SPGDSEIDEL FKIFRILGTP NEDTWPGVTS LPDFKSTFPR WPSKDLATVV
260 270 280 290
PNLEPAGLDL LNSMLCLDPT KRITARSAVE HEYFKDIKFV P
Length:291
Mass (Da):33,481
Last modified:March 1, 1992 - v1
Checksum:iE5D4F43E592D22B5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58365 mRNA. Translation: AAB41817.1.
PIRiA39107.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58365 mRNA. Translation: AAB41817.1.
PIRiA39107.

3D structure databases

ProteinModelPortaliP24923.
SMRiP24923. Positions 2-287.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP24923.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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

  1. "Complementation of a yeast cell cycle mutant by an alfalfa cDNA encoding a protein kinase homologous to p34cdc2."
    Hirt H., Pay A., Gyoergyey J., Bako L., Nemeth K., Boegre L., Schweyen R.J., Heberle-Bors E., Dudits D.
    Proc. Natl. Acad. Sci. U.S.A. 88:1636-1640(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiCDC21_MEDSA
AccessioniPrimary (citable) accession number: P24923
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: February 4, 2015
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. 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.