CDC5/YMR001C Protein Information Help

Standard Name Cdc5p 1
Systematic Name Ymr001cp
Alias Msd2p 2 , Pkx2p
ORF Classification Verified
Description Polo-like kinase; controls targeting and activation of Rho1p at cell division site via Rholp guanine nucleotide exchange factors; regulates Spc72p; also functions in adaptation to DNA damage during meiosis; has similarity to Xenopus Plx1 and S. pombe Plo1p; possible Cdc28p substrate (3, 4, 5, 6, 7, 8)
Name Description Cell Division Cycle 9
Experimental Data
Molecules/cell 1480 10
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 705
Molecular Weight (Da) 81,030
Isoelectric Point (pI) 9.64

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Cdc5p (InterPro)
Physical Interactions There are 183 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0000127258 | P32562
MIPS: YMR001C
NCBI: 172187 | 416768 | 6323643 | 728648 | NP_013714.1 | NM_001182497.1
GenBank/EMBL/DDBJ: AAA02576.1 | CAA88516.1 | DAA09899.1 | M84220 | Z48613
External Classifications EC: 2.7.11.21 [Polo kinase]
Amino Acid Sequence (or in FASTA format)
       1  MSLGPLKAIN DKQLNTRSKL VHTPIKGNTA DLVGKENHFK QTKRLDPNND
      51  HHHQPAQKKK REKLSALCKT PPSLIKTRGK DYHRGHFLGE GGFARCFQIK
     101  DDSGEIFAAK TVAKASIKSE KTRKKLLSEI QIHKSMSHPN IVQFIDCFED
     151  DSNVYILLEI CPNGSLMELL KRRKVLTEPE VRFFTTQICG AIKYMHSRRV
     201  IHRDLKLGNI FFDSNYNLKI GDFGLAAVLA NESERKYTIC GTPNYIAPEV
     251  LMGKHSGHSF EVDIWSLGVM LYALLIGKPP FQARDVNTIY ERIKCRDFSF
     301  PRDKPISDEG KILIRDILSL DPIERPSLTE IMDYVWFRGT FPPSIPSTVM
     351  SEAPNFEDIP EEQSLVNFKD CMEKSLLLES MSSDKIQRQK RDYISSIKSS
     401  IDKLEEYHQN RPFLPHSLSP GGTKQKYKEV VDIEAQRRLN DLAREARIRR
     451  AQQAVLRKEL IATSTNVIKS EISLRILASE CHLTLNGIVE AEAQYKMGGL
     501  PKSRLPKIKH PMIVTKWVDY SNKHGFSYQL STEDIGVLFN NGTTVLRLAD
     551  AEEFWYISYD DREGWVASHY LLSEKPRELS RHLEVVDFFA KYMKANLSRV
     601  STFGREEYHK DDVFLRRYTR YKPFVMFELS DGTFQFNFKD HHKMAISDGG
     651  KLVTYISPSH ESTTYPLVEV LKYGEIPGYP ESNFREKLTL IKEGLKQKST
     701  IVTVD*                                                

external links for Cdc5p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily LoQate
Ashbya (AGD) BOND GPMdb (Mass Spec.) YPL+
Candida (CGD) CYC2008 (complexes) MIPS YeastGFP
YGOB Complexome Pfam domains YeastRC Public Image Repository
YOGY DIP YeastRC Structure Prediction (Seattle)

GeneMANIA


IMP

References cited on this page View Complete Literature Guide for Cdc5p
1) Hartwell LH, et al.  (1973) Genetic Control of the Cell Division Cycle in Yeast: V. Genetic Analysis of cdc Mutants. Genetics 74(2):267-286
2) Kitada K, et al.  (1993) A multicopy suppressor gene of the Saccharomyces cerevisiae G1 cell cycle mutant gene dbf4 encodes a protein kinase and is identified as CDC5. Mol Cell Biol 13(7):4445-57
3) Hu F and Elledge SJ  (2002) Bub2 is a cell cycle regulated phospho-protein controlled by multiple checkpoints. Cell Cycle 1(5):351-5
4) Ubersax JA, et al.  (2003) Targets of the cyclin-dependent kinase Cdk1. Nature 425(6960):859-64
5) Alexandru G, et al.  (2001) Phosphorylation of the cohesin subunit Scc1 by Polo/Cdc5 kinase regulates sister chromatid separation in yeast. Cell 105(4):459-72
6) Yoshida S, et al.  (2006) Polo-like kinase Cdc5 controls the local activation of Rho1 to promote cytokinesis. Science 313(5783):108-11
7) Snead JL, et al.  (2007) A Coupled Chemical-Genetic and Bioinformatic Approach to Polo-like Kinase Pathway Exploration. Chem Biol 14(11):1261-72
8) Iacovella MG, et al.  (2010) Analysis of Polo-like kinase Cdc5 in the meiosis recombination checkpoint. Cell Cycle 9(6):1182-93
9) Hartwell LH, et al.  (1970) Genetic control of the cell-division cycle in yeast. I. Detection of mutants. Proc Natl Acad Sci U S A 66(2):352-9
10) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41