LEU3/YLR451W Protein Information Help

Standard Name Leu3p
Systematic Name Ylr451wp
ORF Classification Verified
Description Zinc-knuckle transcription factor, repressor and activator; regulates genes involved in branched chain amino acid biosynthesis and ammonia assimilation; acts as a repressor in leucine-replete conditions and as an activator in the presence of alpha-isopropylmalate, an intermediate in leucine biosynthesis that accumulates during leucine starvation (1, 2, 3, 4, 5)
Name Description LEUcine biosynthesis 6
Experimental Data
Molecules/cell 125 7
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 886
Molecular Weight (Da) 100,152
Isoelectric Point (pI) 5.99

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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 Leu3p (InterPro)
Physical Interactions There are 8 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI000012E5AE | P08638
MIPS: YLR451W
NCBI: 126217 | 171833 | 3873 | 398366339 | 717060 | 93279244 | 93279245 | 93279246 | 93279247 | 93279252 | 93279253 | 93279256 | 93279257 | NP_013556.3
GenBank/EMBL/DDBJ: DAA09751.1 | M17222 | U22382 | Y00360
Amino Acid Sequence (or in FASTA format)
       1  MEGRSDFVAT SQSGSEMSHS ETRNRTGMNA RKRKFACVEC RQQKSKCDAH
      51  ERAPEPCTKC AKKNVPCILK RDFRRTYKRA RNEAIEKRFK ELTRTLTNLT
     101  SDEILKKIEE EQEIVLDNSN FTKEKVKQLR KSAFETTEIE PRSYKTLRGE
     151  PISYSTNRRH TDSSPLTLLS SSTNFDPVHS TNVMTDDQLK CLPKSLGDVY
     201  LSSSDIAELF QEFATKYHQF LPVVDLSKGA ERIYHLSPCL FWVILLIGLR
     251  RKFGATDLMT RLSVLVKSVL SEITISPIIR YTPSDKDEPV LNVASVYSVQ
     301  AFLLYTFWPP LTSSLSADTS WNTIGTAMFQ ALRVGLNCAG FSKEYASANS
     351  ELVNEQIRTW ICCNVVSQTV ASSFGFPAYV SFDYLVISSI RVPNSKSQVD
     401  IPNELRQMAQ IARFENQIVN TMNSTPASVT GMVSQEEKQP LLHVLNQQLS
     451  QLEISLEENN LDDIRKFLLL VAKVHLLTYY FTDVTSQSAG KSNGNIYEGS
     501  YSIMELDTSF ETKRGLVKVY NAAVNFLIHA NSMWEHDPTI IKYFPGLFVL
     551  NIWQSACIIS KLIHSSLHSM LDVNSGKKAY NNAISLTFNA SVLKYDMAYR
     601  SSGIMRSIWS LFANMYDAWK NDQKEGGGRL NNDFNLGITI KSRMSVNVFF
     651  DCLYILKEKC GMAKLERETK VSTAYNVDEE EEEDEDEEGE EEEEEEELSS
     701  KVPENMDSQQ LRTRKFTNVR HPEKKARKII ETIPLDPNPI NAGSTSSGSS
     751  LTTPNSQVAN TISYRGILNK MSPREQLNHA NLDSSVSTDI KDTEAVNEPL
     801  PIGRNAEHPA NQPPLSITQM QENTLPATQA NSSLLETYPI VQSNPVTTTI
     851  KESPNSIMAG WDNWESDMVW RDVDILMNEF AFNPKV*              

external links for Leu3p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily Organelle DB
Ashbya (AGD) BOND GPMdb (Mass Spec.) YPL+
Aspergillus (AspGD) BioPIXIE MIPS YeastGFP
Candida (CGD) CYC2008 (complexes) Pfam domains YeastRC Public Image Repository
Candida (CandidaDB) Complexome YeastRC Structure Prediction (Seattle)
YGOB DIP

YOGY GeneMANIA

References cited on this page View Complete Literature Guide for Leu3p
1) Friden P and Schimmel P  (1988) LEU3 of Saccharomyces cerevisiae activates multiple genes for branched-chain amino acid biosynthesis by binding to a common decanucleotide core sequence. Mol Cell Biol 8(7):2690-7
2) Zhou K, et al.  (1987) Structure of yeast regulatory gene LEU3 and evidence that LEU3 itself is under general amino acid control. Nucleic Acids Res 15(13):5261-73
3) Zhou KM, et al.  (1990) Yeast regulatory protein LEU3: a structure-function analysis. Nucleic Acids Res 18(2):291-8
4) Friden P and Schimmel P  (1987) LEU3 of Saccharomyces cerevisiae encodes a factor for control of RNA levels of a group of leucine-specific genes. Mol Cell Biol 7(8):2708-17
5) Sze JY, et al.  (1992) In vitro transcriptional activation by a metabolic intermediate: activation by Leu3 depends on alpha-isopropylmalate. Science 258(5085):1143-5
6) Beltzer JP, et al.  (1988) Yeast LEU4 encodes mitochondrial and nonmitochondrial forms of alpha-isopropylmalate synthase. J Biol Chem 263(1):368-74
7) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41