FPK1/YNR047W Protein Information Help

Standard Name Fpk1p 1
Systematic Name Ynr047wp
ORF Classification Verified
Description Ser/Thr protein kinase; regulates the putative phospholipid translocases Lem3p-Dnf1p/Dnf2p; phosphorylates and inhibits upstream inhibitory kinase, Ypk1p; localizes to the cytoplasm, early endosome/TGN compartments, and plasma membrane; FPK1 has a paralog, KIN82, that arose from the whole genome duplication (1, 2, 3, 4, 5)
Name Description FliPase Kinase 1 1
Experimental Data
Molecules/cell 752 6
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 893
Molecular Weight (Da) 100,546
Isoelectric Point (pI) 8

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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 Fpk1p (InterPro)
Physical Interactions There are 30 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI000012DF15 | P53739
MIPS: YNR047W
NCBI: 1302558 | 1730057 | 6324375 | NP_014445.1
GenBank/EMBL/DDBJ: DAA10588.1 | Z71662
External Classifications EC: 2.7.11.1 [Non-specific serine/threonine protein kinase]
Amino Acid Sequence (or in FASTA format)
 
       1  MAGHHHEHEQ ERDHEQEHEH DSLQRPTTGS ERTRSISFSK LLTRSWKRNA
      51  SSSNNMSVSS VNLYSDPENS RESDHNNSGS EGQSSRFSKL KSMFQSGNSS
     101  KNASAHNSSQ SSLEGDSASS SSKLRYVKPM TSVANASPAS PPLSPTIPET
     151  DVLQTPKMVH IDQHEHEREH SNCGSPIMLS SSSFSPTVAR TGTGRRRSPS
     201  TPIMPSQNSN NSSSTSAIRP NNYRHHSGSQ GFSSNNPFRE RAGTVRSSNP
     251  YFAYQGLPTH AMSSHDLDEG FQPYANGSGI HFLSTPTSKT NSLTNTKNLS
     301  NLSLNEIKEN EEVQEFNNED FFFHDIPKDL SLKDTLNGSP SRGSSKSPTI
     351  TQTFPSIIVG FDNEYEEDNN NDKHDEKEEQ QTTTDNKTRN LSPTKQNGKA
     401  THPRIKIPLR RAASEPNGLQ LASATSPTSS SARKTSGSSN INDKIPGQSV
     451  PPPNSFFPQE PSPKISDFPE PRRSRRLRTK SFSNKFQDIM VGPQSFEKIR
     501  LLGQGDVGKV FLVREKKTNR VYALKVLSKD EMIKRNKIKR VLTEQEILAT
     551  SNHPFIVTLY HSFQSEDYLY LCMEYCMGGE FFRALQTRKT KCICEDDARF
     601  YASEVTAALE YLHLLGFIYR DLKPENILLH QSGHIMLSDF DLSIQAKDSK
     651  VPVVKGSAQS TLVDTKICSD GFRTNSFVGT EEYIAPEVIR GNGHTAAVDW
     701  WTLGILIYEM LFGFTPFKGD NTNETFTNIL KNEVSFPNNN EISRTCKDLI
     751  KKLLTKNESK RLGCKMGAAD VKKHPFFKKV QWSLLRNQEP PLIPVLSEDG
     801  YDFAKLSSNK KRQTSQDSHK HLDEQEKNMF EERVEYDDEV SEDDPFHDFN
     851  SMSLMEQDNN SMIYGNTNSY GKIAYTPNSN RSRSNSHRTF FKR*

external links for Fpk1p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily YPL+
Ashbya (AGD) BOND GPMdb (Mass Spec.) YeastGFP
Candida (CGD) BioPIXIE MIPS YeastRC Public Image Repository
Candida (CandidaDB) CYC2008 (complexes) Pfam domains
YGOB Complexome YeastRC Structure Prediction (Seattle)
YOGY DIP


GeneMANIA

References cited on this page View Complete Literature Guide for Fpk1p
1) Nakano K, et al.  (2008) Protein kinases Fpk1p and Fpk2p are novel regulators of phospholipid asymmetry. Mol Biol Cell 19(4):1783-97
2) Burchett SA, et al.  (2001) Identification of novel pheromone-response regulators through systematic overexpression of 120 protein kinases in yeast. J Biol Chem 276(28):26472-8
3) Ubersax JA, et al.  (2003) Targets of the cyclin-dependent kinase Cdk1. Nature 425(6960):859-64
4) Byrne KP and Wolfe KH  (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
5) Roelants FM, et al.  (2010) A protein kinase network regulates the function of aminophospholipid flippases. Proc Natl Acad Sci U S A 107(1):34-9
6) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41