EKS-SAC-00101
Eukaryotic Protein Kinase & Protein Phosphatase Database
TagContent
EKPD IDEKS-SAC-00101
Classification
Group/FamilyScoreE-ValueStartEndDomain Length
CMGC/MAPK399.03.5E-12014309296
StatusReviewed
Ensembl ProteinYBL016W
UniProt AccessionP16892; D6VPY4;
Protein NameMitogen-activated protein kinase FUS3
Protein Synonyms/Alias MAP kinase FUS3;
Gene NameFUS3
Gene Synonyms/Alias FUS3; DAC2; YBL016W; YBL03.21, YBL0303;
Ensembl Information
Ensembl Gene IDEnsembl Protein IDEnsembl Transcript ID
YBL016WYBL016WYBL016W
OrganismSaccharomyces cerevisiae
Functional DescriptionTogether with closely related KSS1, FUS3 is the finalkinase in the signal transduction cascade regulating activation/repression of the mating and filamentation pathways, induced by pheromone and nitrogen/carbon limitation, respectively. Phosphorylated FUS3 activates the mating but suppresses the filamentation pathway, whereas activated KSS1 activates both pathways. Pheromone-activated FUS3 functions by inhibiting the binding of the transcriptional activator STE12 to filamentation specific genes while inducing its binding to and activity at mating specific genes. Non-activated FUS3 has a repressive effect on STE12 transcriptional activity. KSS1 can partially compensate for the lack of FUS3 but mating efficiency is reduced and the filamentation program is partially activated upon pheromone signaling. FUS3 phosphorylates STE7, STE5, FAR1, DIG1, DIG2 and STE12.
Protein Length353
Protein Sequence
(FASTA)
MPKRIVYNIS SDFQLKSLLG EGAYGVVCSA THKPTGEIVA IKKIEPFDKP LFALRTLREI 60
KILKHFKHEN IITIFNIQRP DSFENFNEVY IIQELMQTDL HRVISTQMLS DDHIQYFIYQ 120
TLRAVKVLHG SNVIHRDLKP SNLLINSNCD LKVCDFGLAR IIDESAADNS EPTGQQSGMT 180
EYVATRWYRA PEVMLTSAKY SRAMDVWSCG CILAELFLRR PIFPGRDYRH QLLLIFGIIG 240
TPHSDNDLRC IESPRAREYI KSLPMYPAAP LEKMFPRVNP KGIDLLQRML VFDPAKRITA 300
KEALEHPYLQ TYHDPNDEPE GEPIPPSFFE FDHYKEALTT KDLKKLIWNE IFS 353
Nucleotide Sequence
(FASTA)
ATGCCAAAGA GAATTGTATA CAATATATCC AGTGACTTCC AGTTGAAGTC GTTACTGGGA 60
GAGGGTGCAT ACGGTGTGGT ATGTTCTGCA ACGCATAAGC CCACGGGAGA AATCGTGGCA 120
ATAAAAAAGA TCGAACCATT CGATAAGCCT TTGTTCGCAT TACGTACGCT GCGTGAAATA 180
AAGATCCTGA AGCACTTCAA GCACGAAAAT ATCATAACAA TCTTCAACAT TCAACGCCCT 240
GACTCGTTCG AAAACTTCAA TGAGGTCTAC ATAATTCAAG AGCTAATGCA GACAGATTTA 300
CACCGTGTAA TCTCCACCCA GATGCTGAGT GACGATCATA TACAATATTT TATATACCAA 360
ACCTTGAGAG CAGTGAAAGT GCTGCATGGT TCGAACGTCA TCCATCGTGA TTTAAAGCCC 420
TCCAACCTTC TCATAAACTC CAACTGTGAC TTGAAAGTAT GTGATTTCGG TTTAGCAAGA 480
ATCATTGACG AGTCAGCCGC GGACAATTCA GAGCCCACAG GTCAGCAAAG CGGCATGACC 540
GAGTATGTGG CCACACGTTG GTACAGGGCG CCAGAGGTGA TGTTAACCTC TGCCAAATAC 600
TCAAGGGCCA TGGACGTGTG GTCCTGCGGA TGTATTCTCG CTGAACTTTT CTTAAGACGG 660
CCAATCTTCC CTGGCAGAGA TTATCGCCAT CAACTACTAC TGATATTCGG TATCATCGGT 720
ACACCTCACT CAGATAATGA TTTGCGGTGT ATAGAGTCAC CCAGGGCTAG AGAGTACATA 780
AAGTCGCTTC CCATGTACCC TGCCGCGCCA CTGGAGAAGA TGTTCCCTCG AGTCAACCCG 840
AAAGGCATAG ATCTTTTACA GCGTATGCTT GTTTTTGACC CTGCGAAGAG GATTACTGCT 900
AAGGAGGCAC TGGAGCATCC GTATTTGCAA ACATACCACG ATCCAAACGA CGAACCTGAA 960
GGCGAACCCA TCCCACCCAG CTTCTTCGAG TTTGATCACT ACAAGGAGGC ACTAACGACG 1020
AAAGACCTCA AGAAACTCAT TTGGAACGAA ATATTTAGTT AG 1062
Domain Profile
S: 2     eslkplgeGaygvvvsavdkrteervaikklsrpfqketsakrtlRElkllkelkheNii  61
         + ++ lgeGaygvv+sa++k t+e vaikk+  pf+k   a rtlRE+k+lk++kheNii
Q: 14    QLKSLLGEGAYGVVCSATHKPTGEIVAIKKIE-PFDKPLFALRTLREIKILKHFKHENII  72
         667889*************************9.***************************
S: 62    klldvftpeeeleelkdvYlvtelmetdLkkviksqklsdehiklllyqilrglkylHsa  121
         +++++ +p++ +e++++vY+++elm+tdL++vi++q lsd+hi++++yq lr++k lH +
Q: 73    TIFNIQRPDS-FENFNEVYIIQELMQTDLHRVISTQMLSDDHIQYFIYQTLRAVKVLHGS  131
         *********9.*************************************************
S: 122   nviHrDlKPsNllvnedcelkildFGlarsadkekekk.........lteyvatrwYraP  172
         nviHrDlKPsNll+n++c+lk++dFGlar+ d++   +         +teyvatrwYraP
Q: 132   NVIHRDLKPSNLLINSNCDLKVCDFGLARIIDESAADNseptgqqsgMTEYVATRWYRAP  191
         ******************************88776655678999****************
S: 173   eillslkeytkavDiWsvGCIlaElltgkplfpgkdeidqlekilevlgtp.seeflkki  231
         e++l++ +y++a+D+Ws+GCIlaEl+ ++p+fpg+d+ +ql +i+ ++gtp s+++l++i
Q: 192   EVMLTSAKYSRAMDVWSCGCILAELFLRRPIFPGRDYRHQLLLIFGIIGTPhSDNDLRCI  251
         ***************************************************44689****
S: 232   eseearnyikslpkkkkkdfeelfpkaseealdLleklLvldpdkRisveeaLehpYl  289
         es +ar+yikslp+++++++e++fp+ +++ +dLl+++Lv+dp kRi+++eaLehpYl
Q: 252   ESPRAREYIKSLPMYPAAPLEKMFPRVNPKGIDLLQRMLVFDPAKRITAKEALEHPYL  309
         *********************************************************7
Domain Sequence
(FASTA)
QLKSLLGEGA YGVVCSATHK PTGEIVAIKK IEPFDKPLFA LRTLREIKIL KHFKHENIIT 60
IFNIQRPDSF ENFNEVYIIQ ELMQTDLHRV ISTQMLSDDH IQYFIYQTLR AVKVLHGSNV 120
IHRDLKPSNL LINSNCDLKV CDFGLARIID ESAADNSEPT GQQSGMTEYV ATRWYRAPEV 180
MLTSAKYSRA MDVWSCGCIL AELFLRRPIF PGRDYRHQLL LIFGIIGTPH SDNDLRCIES 240
PRAREYIKSL PMYPAAPLEK MFPRVNPKGI DLLQRMLVFD PAKRITAKEA LEHPYL 296
Keyword3D-structure; ATP-binding; Cell cycle; Cell division; Complete proteome; Conjugation; Cytoplasm; Kinase; Mitosis; Nucleotide-binding; Nucleus; Periplasm; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; Transferase.
Sequence SourceEnsembl
Orthology
Ortholog group
Ailuropoda melanoleuca"; ?>Anolis carolinensis"; ?>Bos taurus"; ?>Caenorhabditis elegans"; ?>Cavia porcellus"; ?>Dasypus novemcinctus"; ?>Dipodomys ordii"; ?>Drosophila melanogaster"; ?>Equus caballus"; ?>Erinaceus europaeus"; ?>Gadus morhua"; ?>Gallus gallus"; ?>Gasterosteus aculeatus"; ?>Ictidomys tridecemlineatus"; ?>Latimeria chalumnae"; ?>Loxodonta africana"; ?>Macropus eugenii"; ?>Meleagris gallopavo"; ?>Mustela putorius furo"; ?>Myotis lucifugus"; ?>Nomascus leucogenys"; ?>Oreochromis niloticus"; ?>Oryzias latipes"; ?>Pelodiscus sinensis"; ?>Petromyzon marinus"; ?>Pongo abelii"; ?>Sarcophilus harrisii"; ?>Sus scrofa"; ?>Taeniopygia guttata"; ?>Takifugu rubripes"; ?>Tetraodon nigroviridis"; ?>Tursiops truncatus"; ?>Xenopus tropicalis"; ?>Xiphophorus maculatus"; ?>
EKS-AIM-00435
EKS-ANC-00449
EKS-BOT-00462
EKS-CAE-00385
EKS-CAP-00493
EKS-DAN-00034
EKS-DIO-00097
EKS-DRM-00222
EKS-EQC-00449
EKS-ERE-00049
EKS-GAM-00267
EKS-GAG-00389
EKS-GAA-00558
EKS-ICT-00441
EKS-LAC-00473
EKS-LOA-00471
EKS-MAE-00072
EKS-MEG-00382
EKS-MUP-00452
EKS-MYL-00457
EKS-NOL-00423
EKS-ORN-00582
EKS-ORL-00529
EKS-PES-00410
EKS-PEM-00252
EKS-POA-00449
EKS-SAH-00430
EKS-SUS-00410
EKS-TAG-00529
EKS-TAR-00571
EKS-TEN-00572
EKS-TUT-00168
EKS-XET-00610
EKS-XIM-00572
Gene Ontology
GO:0043332; C:mating projection tip
GO:0005739; C:mitochondrion
GO:0005634; C:nucleus
GO:0042597; C:periplasmic space
GO:0005524; F:ATP binding
GO:0004707; F:MAP kinase activity
GO:0007050; P:cell cycle arrest
GO:0051301; P:cell division
GO:0001403; P:invasive growth in response to glucose limitation
GO:0007067; P:mitosis
GO:0043409; P:negative regulation of MAPK cascade
GO:0010526; P:negative regulation of transposition, RNA-mediated
GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion
KEGG
sce:YBL016W;
InterPros
IPR011009; Kinase-like_dom.
IPR003527; MAP_kinase_CS.
IPR000719; Prot_kinase_cat_dom.
IPR017441; Protein_kinase_ATP_BS.
IPR002290; Ser/Thr_dual-sp_kinase_dom.
IPR008271; Ser/Thr_kinase_AS.
Pfam
PF00069; Pkinase; 1.
SMARTs
SM00220; S_TKc; 1.
Prosites
PS01351; MAPK; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
Prints
Created Date20-Feb-2013