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Protein

Cell division control protein 2 homolog 1

Gene

CDC2

Organism
Pisum sativum (Garden pea)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Plays a key role in the control of the eukaryotic cell cycle. It is required in higher cells for entry into S-phase and mitosis. 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 inactivates the enzyme; while. Thr-145 phosphorylation is required for the catalytic activity of the enzyme (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei17ATPPROSITE-ProRule annotation1
Active sitei111Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi‹1 – 2ATPPROSITE-ProRule annotation›2

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processCell cycle, Cell division, Mitosis
LigandATP-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)
Alternative name(s):
p34
Gene namesi
Name:CDC2
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000085757‹1 – ›148Cell division control protein 2 homolog 1Add BLAST›148

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei145Phosphothreonine; by CAKBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP19026

Structurei

3D structure databases

ProteinModelPortaliP19026
SMRiP19026
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini‹1 – ›148Protein kinasePROSITE-ProRule annotationAdd BLAST›148

Sequence similaritiesi

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

Sequencei

Sequence statusi: Fragment.

P19026-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
VVYKARDRVT NETIALKKIR LEQEDEGVPS TAIREISLLK EMQHRNIVRL
60 70 80 90 100
QDVVHSEKRL YLVFEYLDLD LKKHMDSSPE FVKDPRQVKM FLYQMLCGIA
110 120 130 140
YCHSHRVLHR DLKPQNLLID RRTNCVKLAD FGLARAFGIP VRTFTHEV
Length:148
Mass (Da):17,445
Last modified:November 1, 1990 - v1
Checksum:i3B90EC6B2A2E74CA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Non-terminal residuei1481

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53035 mRNA Translation: CAA37207.1
PIRiA35778 A33109

Similar proteinsi

Entry informationi

Entry nameiCDC21_PEA
AccessioniPrimary (citable) accession number: P19026
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: May 23, 2018
This is version 101 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health