IPL1/YPL209C Protein Information Help

Standard Name Ipl1p 1
Systematic Name Ypl209cp
Alias Pac15p 2
ORF Classification Verified
Description Aurora kinase subunit of the conserved chromosomal passenger complex (CPC; Ipl1p-Sli15p-Bir1p-Nbl1p), involved in regulating kinetochore-microtubule attachments; helps maintain condensed chromosomes during anaphase and early telophase; required for SPB cohesion and prevention of multipolar spindle formation; localizes to nuclear foci that become diffuse upon DNA replication stress; required for inhibition of karyopherin/importin Pse1p (aka Kap121p) upon SAC arrest (3, 4, 5, 6, 7, 8, 9)
Name Description Increase in PLoidy 1
Experimental Data
Molecules/cell 149 10
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 367
Molecular Weight (Da) 42,946
Isoelectric Point (pI) 10.53

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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 Ipl1p (InterPro)
Physical Interactions There are 139 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI000012D7F6 | P38991
MIPS: YPL209C
NCBI: 1370434 | 460244 | 51013815 | 6325047 | 729855 | NP_015115.1
GenBank/EMBL/DDBJ: DAA11227.1 | AY693182 | U07163 | Z73565
External Classifications EC: 2.7.11.1 [Non-specific serine/threonine protein kinase]
Amino Acid Sequence (or in FASTA format)
       1  MQRNSLVNIK LNANSPSKKT TTRPNTSRIN KPWRISHSPQ QRNPNSKIPS
      51  PVREKLNRLP VNNKKFLDME SSKIPSPIRK ATSSKMIHEN KKLPKFKSLS
     101  LDDFELGKKL GKGKFGKVYC VRHRSTGYIC ALKVMEKEEI IKYNLQKQFR
     151  REVEIQTSLN HPNLTKSYGY FHDEKRVYLL MEYLVNGEMY KLLRLHGPFN
     201  DILASDYIYQ IANALDYMHK KNIIHRDIKP ENILIGFNNV IKLTDFGWSI
     251  INPPENRRKT VCGTIDYLSP EMVESREYDH TIDAWALGVL AFELLTGAPP
     301  FEEEMKDTTY KRIAALDIKM PSNISQDAQD LILKLLKYDP KDRMRLGDVK
     351  MHPWILRNKP FWENKRL*                                   

external links for Ipl1p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily Organelle DB
Ashbya (AGD) BOND GPMdb (Mass Spec.) YPL+
Candida (CGD) BioPIXIE MIPS YeastGFP
Candida (CandidaDB) CYC2008 (complexes) Pfam domains YeastRC Public Image Repository
YGOB Complexome YeastRC Structure Prediction (Seattle)
YOGY DIP


GeneMANIA


YeastRC Mass Spec (Seattle)


YeastRC Two-Hybrid (Seattle)

References cited on this page View Complete Literature Guide for Ipl1p
1) Chan CS and Botstein D  (1993) Isolation and characterization of chromosome-gain and increase-in-ploidy mutants in yeast. Genetics 135(3):677-91
2) Geiser JR, et al.  (1997) Saccharomyces cerevisiae genes required in the absence of the CIN8-encoded spindle motor act in functionally diverse mitotic pathways. Mol Biol Cell 8(6):1035-50
3) Kang Js JS, et al.  (2001) Functional cooperation of Dam1, Ipl1, and the inner centromere protein (INCENP)-related protein Sli15 during chromosome segregation. J Cell Biol 155(5):763-74
4) Cheeseman IM, et al.  (2002) Phospho-regulation of kinetochore-microtubule attachments by the Aurora kinase Ipl1p. Cell 111(2):163-72
5) Vas AC, et al.  (2007) In vivo analysis of chromosome condensation in Saccharomyces cerevisiae. Mol Biol Cell 18(2):557-68
6) Nakajima Y, et al.  (2009) Nbl1p: a Borealin/Dasra/CSC-1-like protein essential for Aurora/Ipl1 complex function and integrity in Saccharomyces cerevisiae. Mol Biol Cell 20(6):1772-84
7) Shirk K, et al.  (2011) The Aurora kinase Ipl1 is necessary for spindle pole body cohesion during budding yeast meiosis. J Cell Sci 124(Pt 17):2891-6
8) Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
9) Cairo LV, et al.  (2013) Mitosis-specific regulation of nuclear transport by the spindle assembly checkpoint protein Mad1p. Mol Cell 49(1):109-20
10) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41