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Protein

Cell division control protein 15

Gene

CDC15

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protein kinase of the mitotic exit network (MEN) essential for late nuclear division in the mitotic cycle. Promotes mitotic exit by phosphorylating DBF2 and directly switching on DBF2 kinase activity. Involved in the localization of DBF2 and DBF20 to the neck which is necessary to undergo cytokinesis. Plays a role in segregation of chromosomes during recovery from spindle checkpoint activation. Required for spindle pole localization of CDK1 and inactivation of CDC2 kinase activity at the end of mitosis. Required for spindle disassembly after meiosis II and plays a role in spore morphogenesis.23 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Kinase activity is inhibited by phosphorylation and activated by dephosphorylation by CDC14.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei54ATPPROSITE-ProRule annotation1
Active sitei146Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi31 – 39ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

  • actin cytoskeleton organization Source: GO_Central
  • meiotic spindle disassembly Source: SGD
  • mitotic cytokinesis Source: SGD
  • mitotic nuclear division Source: UniProtKB-KW
  • protein phosphorylation Source: SGD
  • regulation of exit from mitosis Source: SGD
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

Enzyme and pathway databases

BioCyciYEAST:G3O-28875-MONOMER.
BRENDAi2.7.11.1. 984.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division control protein 15 (EC:2.7.11.1)
Gene namesi
Name:CDC15
Synonyms:LYT1
Ordered Locus Names:YAR019C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:YAR019C.
SGDiS000000072. CDC15.

Subcellular locationi

  • Cytoplasmcytoskeletonspindle pole
  • Bud neck

  • Note: Localizes to the spindle pole bodies at late anaphase and translocates to the cytoplasm upon DNA replication stress. Localization to SPBs depends on CDC5 and TEM1 and is inhibited by BUB2. Accumulates at the daughter SPB after anaphase onset when the daughter SPB begins to penetrate the bud neck. Not found in the mother SPD during early anaphase. As anaphase proceeds, continues to accumulate on the daughter SPB and also localizes to the mother SPB. At the end of telophase, a portion of CDC15 localizes at the mother-bud neck.

GO - Cellular componenti

  • cellular bud neck Source: SGD
  • cytoplasm Source: UniProtKB-KW
  • spindle pole body Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000857171 – 974Cell division control protein 15Add BLAST974

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei561Phosphoserine1 Publication1
Modified residuei567PhosphoserineCombined sources1 Publication1
Modified residuei870Phosphothreonine1 Publication1

Post-translational modificationi

Phosphorylation by CDK1 reduces the binding to the mother spindle pole body. The extent of phosphorylation gradually increases during cell-cycle progression until some point during late anaphase/telophase when it is rapidly dephosphorylated by CDC14. Phosphorylation inhibits kinase activity and dephosphorylation by CDC14 activates CDC15.5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP27636.
PRIDEiP27636.
TopDownProteomicsiP27636.

PTM databases

iPTMnetiP27636.

Expressioni

Inductioni

Constitutively expressed.1 Publication

Interactioni

Subunit structurei

Homodimer. Interacts with TEM1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TEM1P389872EBI-4200,EBI-19113

Protein-protein interaction databases

BioGridi31801. 104 interactors.
DIPiDIP-5728N.
IntActiP27636. 6 interactors.
MINTiMINT-683916.

Structurei

3D structure databases

ProteinModelPortaliP27636.
SMRiP27636.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 272Protein kinasePROSITE-ProRule annotationAdd BLAST248

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni360 – 702Self association domainAdd BLAST343
Regioni751 – 974Auto-inhibitory domainAdd BLAST224

Domaini

The region between residues 360 and 702 is essential for function and is required for self-association and for binding to spindle pole bodies.1 Publication
The region between residues 751 and 974 is an auto-inhibitory domain which inhibits MEN signaling.1 Publication

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00860000133956.
HOGENOMiHOG000141997.
InParanoidiP27636.
KOiK06683.
OMAiVKYHGFI.
OrthoDBiEOG092C0D2J.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P27636-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSMADTDRV NLTPIQRASE KSVQYHLKQV IGRGSYGVVY KAINKHTDQV
60 70 80 90 100
VAIKEVVYEN DEELNDIMAE ISLLKNLNHN NIVKYHGFIR KSYELYILLE
110 120 130 140 150
YCANGSLRRL ISRSSTGLSE NESKTYVTQT LLGLKYLHGE GVIHRDIKAA
160 170 180 190 200
NILLSADNTV KLADFGVSTI VNSSALTLAG TLNWMAPEIL GNRGASTLSD
210 220 230 240 250
IWSLGATVVE MLTKNPPYHN LTDANIYYAV ENDTYYPPSS FSEPLKDFLS
260 270 280 290 300
KCFVKNMYKR PTADQLLKHV WINSTENVKV DKLNKFKEDF TDADYHWDAD
310 320 330 340 350
FQEEKLNISP SKFSLAAAPA AWAENNQELD LMPPTESQLL SQLKSSSKPL
360 370 380 390 400
TDLHVLFSVC SLENIADTII ECLSRTTVDK RLITAFGSIF VYDTQHNHSR
410 420 430 440 450
LRLKFIAMGG IPLIIKFEHL AKEFVIDYPQ TLIECGIMYP PNFASLKTPK
460 470 480 490 500
YILELVYRFY DLTSTAFWCR WCFKHLDISL LLNNIHERRA QSILLKLSSY
510 520 530 540 550
APWSFEKILP SLIDSKLKKK ILISPQITYV VFKSINYMIT TNDDKIHKSA
560 570 580 590 600
IPSSSSLPLS SSPTRNSPVN SVQSPSRSPV HSLMATRPSS PMRHKSISNF
610 620 630 640 650
PHLTISSKSR LLIELPEGFF TWLTSFFVDM AQIKDLSVLK YFTKLCYLTV
660 670 680 690 700
HINSTFLNDL LDNDAFFAFI RNIDTIIPFI DDAKTAAFIW KQITAICVEM
710 720 730 740 750
SLDMDQMSAS LFSTAMNFIR KKNNTSISGL EIILNCLHFT LRNVNDDVAP
760 770 780 790 800
TVGSSESHSV FLIKVNNDAA IELPIDQLVD LFYALNDDDV NLSKLISIFT
810 820 830 840 850
KICSLPGFEN LTINIIFHPN FYEKIVSFFD TYFNSLLIQI DLLKFIKLIF
860 870 880 890 900
SKSLLKLYDY TGQPDPIKQT EPNRRNKATV FKLRAILVQI TEFLNNNWNK
910 920 930 940 950
DVPKRNSNQV GGDSVLICQL CEDIRSLSKK GSLQKVSSVT AAIGSSPTKD
960 970
ERSNLRSSKD KSDGFSVPIT TFQT
Length:974
Mass (Da):110,242
Last modified:July 27, 2011 - v3
Checksum:i99383BD871A4A726
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti316A → R in CAA43041 (PubMed:1495480).Curated1
Sequence conflicti316A → R in CAA36906 (PubMed:1882551).Curated1
Sequence conflicti316A → R (PubMed:7941740).Curated1
Sequence conflicti316A → R in AAC04965 (PubMed:7731988).Curated1
Sequence conflicti321A → P in CAA43041 (PubMed:1495480).Curated1
Sequence conflicti321A → P in CAA36906 (PubMed:1882551).Curated1
Sequence conflicti321A → P (PubMed:7941740).Curated1
Sequence conflicti321A → P in AAC04965 (PubMed:7731988).Curated1
Sequence conflicti900 – 902KDV → NGC no nucleotide entry (PubMed:7941740).Curated3
Sequence conflicti900 – 902KDV → NGC in AAC04965 (PubMed:7731988).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60549 Genomic DNA. Translation: CAA43041.1.
X52683 Genomic DNA. Translation: CAA36906.1.
L22015 Genomic DNA. Translation: AAC04965.1.
M67445 Genomic DNA. Translation: AAA34400.1.
BK006935 Genomic DNA. Translation: DAA06996.2.
PIRiS15038.
RefSeqiNP_009411.2. NM_001178218.2.

Genome annotation databases

EnsemblFungiiYAR019C; YAR019C; YAR019C.
GeneIDi851274.
KEGGisce:YAR019C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60549 Genomic DNA. Translation: CAA43041.1.
X52683 Genomic DNA. Translation: CAA36906.1.
L22015 Genomic DNA. Translation: AAC04965.1.
M67445 Genomic DNA. Translation: AAA34400.1.
BK006935 Genomic DNA. Translation: DAA06996.2.
PIRiS15038.
RefSeqiNP_009411.2. NM_001178218.2.

3D structure databases

ProteinModelPortaliP27636.
SMRiP27636.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31801. 104 interactors.
DIPiDIP-5728N.
IntActiP27636. 6 interactors.
MINTiMINT-683916.

PTM databases

iPTMnetiP27636.

Proteomic databases

MaxQBiP27636.
PRIDEiP27636.
TopDownProteomicsiP27636.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYAR019C; YAR019C; YAR019C.
GeneIDi851274.
KEGGisce:YAR019C.

Organism-specific databases

EuPathDBiFungiDB:YAR019C.
SGDiS000000072. CDC15.

Phylogenomic databases

GeneTreeiENSGT00860000133956.
HOGENOMiHOG000141997.
InParanoidiP27636.
KOiK06683.
OMAiVKYHGFI.
OrthoDBiEOG092C0D2J.

Enzyme and pathway databases

BioCyciYEAST:G3O-28875-MONOMER.
BRENDAi2.7.11.1. 984.

Miscellaneous databases

PROiP27636.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCDC15_YEAST
AccessioniPrimary (citable) accession number: P27636
Secondary accession number(s): D6VPM6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 165 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 238 molecules/cell in log phase SD medium.1 Publication

Caution

It is uncertain whether Met-1 or Met-4 is the initiator.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome I
    Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names

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 one 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.