STE5/YDR103W Protein Information Help

Standard Name Ste5p 1
Systematic Name Ydr103wp
Alias Hmd3p 2 , Nul3p 3
ORF Classification Verified
Description Pheromone-responsive MAPK scaffold protein; couples activation of the G-protein-coupled pheromone receptor to MAPK activation; intramolecular interaction of PH and VWA domains blocks activation of assembled signaling cascade components (Ste11p, Ste7p and Fus3p) under basal conditions; Gbeta-gamma (Ste4p-Ste18p)-dependent docking at the plasma membrane and binding of PI(4,5)P2 by the PH domain relieves autoinhibition, resulting in pheromone-dependent pathway activation (10, 11, 12, 4, 5, 6, 7, 8, 9)
Name Description STErile 1
Experimental Data
Molecules/cell 1900 13
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 917
Molecular Weight (Da) 102,726
Isoelectric Point (pI) 5.19

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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 Ste5p (InterPro)
Physical Interactions There are 109 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0000036C34 | P32917
MIPS: YDR103W
NCBI: 218496 | 226192697 | 291190975 | 310689636 | 311115 | 311161 | 393289 | 401871549 | 464816 | 6320308 | 633639 | NP_010388.1
GenBank/EMBL/DDBJ: DAA11949.1 | D12917 | L01620 | L07865 | L23856 | Z47746
Amino Acid Sequence (or in FASTA format)
 
       1  MMETPTDNIV SPFHNFGSST QYSGTLSRTP NQIIELEKPS TLSPLSRGKK
      51  WTEKLARFQR SSAKKKRFSP SPISSSTFSF SPKSRVTSSN SSGNEDGNLM
     101  NTPSTVSTDY LPQHPHRTSS LPRPNSNLFH ASNSNLSRAN EPPRAENLSD
     151  NIPPKVAPFG YPIQRTSIKK SFLNASCTLC DEPISNRRKG EKIIELACGH
     201  LSHQECLIIS FGTTSKADVR ALFPFCTKCK KDTNKAVQCI PENDELKDIL
     251  ISDFLIHKIP DSELSITPQS RFPPYSPLLP PFGLSYTPVE RQTIYSQAPS
     301  LNPNLILAAP PKERNQIPQK KSNYTFLHSP LGHRRIPSGA NSILADTSVA
     351  LSANDSISAV SNSVRAKDDE TKTTLPLLRS YFIQILLNNF QEELQDWRID
     401  GDYGLLRLVD KLMISKDGQR YIQCWCFLFE DAFVIAEVDN DVDVLEIRLK
     451  NLEVFTPIAN LRMTTLEASV LKCTLNKQHC ADLSDLYIVQ NINSDESTTV
     501  QKWISGILNQ DFVFNEDNIT STLPILPIIK NFSKDVGNGR HETSTFLGLI
     551  NPNKVVEVGN VHDNDTVIIR RGFTLNSGEC SRQSTVDSIQ SVLTTISSIL
     601  SLKREKPDNL AIILQIDFTK LKEEDSLIVV YNSLKALTIK FARLQFCFVD
     651  RNNYVLDYGS VLHKIDSLDS ISNLKSKSSS TQFSPIWLKN TLYPENIHEH
     701  LGIVAVSNSN MEAKKSILFQ DYRCFTSFGR RRPNELKIKV GYLNVDYSDK
     751  IDELVEASSW TFVLETLCYS FGLSFDEHDD DDEEDNDDST DNELDNSSGS
     801  LSDAESTTTI HIDSPFDNEN ATANMVNDRN LLTEGEHSNI ENLETVASSV
     851  QPALIPNIRF SLHSEEEGTN ENENENDMPV LLLSDMDKGI DGITRRSSFS
     901  SLIESGNNNC PLHMDYI*

external links for Ste5p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily YPL+
Ashbya (AGD) BOND GPMdb (Mass Spec.) YeastGFP
YGOB BioPIXIE MIPS YeastRC Public Image Repository
YOGY CYC2008 (complexes) Pfam domains

Complexome


DIP


GeneMANIA

References cited on this page View Complete Literature Guide for Ste5p
1) Liao H and Thorner J  (1980) Yeast mating pheromone alpha factor inhibits adenylate cyclase. Proc Natl Acad Sci U S A 77(4):1898-902
2) Sugimoto K, et al.  (1995) Dosage suppressors of the dominant G1 cyclin mutant CLN3-2: identification of a yeast gene encoding a putative RNA/ssDNA binding protein. Mol Gen Genet 248(6):712-8
3) Mortimer RK and Hawthorne DC  (1973) Genetic Mapping in Saccharomyces IV. Mapping of Temperature-Sensitive Genes and Use of Disomic Strains in Localizing Genes. Genetics 74(1):33-54
4) Choi KY, et al.  (1999) Characterization of Fus3 localization: active Fus3 localizes in complexes of varying size and specific activity. Mol Biol Cell 10(5):1553-68
5) Printen JA and Sprague GF Jr  (1994) Protein-protein interactions in the yeast pheromone response pathway: Ste5p interacts with all members of the MAP kinase cascade. Genetics 138(3):609-19
6) Kranz JE, et al.  (1994) The MAP kinase Fus3 associates with and phosphorylates the upstream signaling component Ste5. Genes Dev 8(3):313-27
7) Winters MJ, et al.  (2005) A membrane binding domain in the ste5 scaffold synergizes with gbetagamma binding to control localization and signaling in pheromone response. Mol Cell 20(1):21-32
8) Garrenton LS, et al.  (2006) Function of the MAPK scaffold protein, Ste5, requires a cryptic PH domain. Genes Dev 20(14):1946-58
9) Hao N, et al.  (2008) Regulation of cell signaling dynamics by the protein kinase-scaffold Ste5. Mol Cell 30(5):649-56
10) Good M, et al.  (2009) The Ste5 scaffold directs mating signaling by catalytically unlocking the Fus3 MAP kinase for activation. Cell 136(6):1085-97
11) Malleshaiah MK, et al.  (2010) The scaffold protein Ste5 directly controls a switch-like mating decision in yeast. Nature 465(7294):101-5
12) Zalatan JG, et al.  (2012) Conformational control of the Ste5 scaffold protein insulates against MAP kinase misactivation. Science 337(6099):1218-22
13) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41