MOT3/YMR070W Protein Information Help

Standard Name Mot3p 1
Systematic Name Ymr070wp
Alias Rox7p
ORF Classification Verified
Description Transcriptional repressor and activator with two C2-H2 zinc fingers; involved in repression of a subset of hypoxic genes by Rox1p, repression of several DAN/TIR genes during aerobic growth, and repression of ergosterol biosynthetic genes in response to hyperosmotic stress; contributes to recruitment of the Tup1p-Cyc8p general repressor to promoters; involved in positive transcriptional regulation of CWP2 and other genes; can form the [MOT3+] prion (2, 3, 4, 5, 6, 7, 8) Also known as: [MOT3+] 9 , [MOT3]
Name Description Modifier of Transcription 1
Experimental Data
Molecules/cell 1690 10
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 490
Molecular Weight (Da) 54,382
Isoelectric Point (pI) 9.2

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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 Mot3p (InterPro)
Physical Interactions There are 18 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI000012F3CA | P54785
MIPS: YMR070W
NCBI: 1708268 | 51013869 | 6323715 | 763017 | 805130 | NP_013786.1
GenBank/EMBL/DDBJ: DAA09968.1 | AY693209 | U25279 | Z48952
Amino Acid Sequence (or in FASTA format)
       1  MNADHHLQQQ QQQRQQHQQQ QHQQQQHQHQ HQQQQHTILQ NVSNTNNIGS
      51  DSLASQPFNT TTVSSNKDDV MVNSGARELP MPLHQQQYIY PYYQYTSNNS
     101  NNNNVTAGNN MSASPIVHNN SNNSNNSNIS ASDYTVANNS TSNNNNNNNN
     151  NNNNNNNIHP NQFTAAANMN SNAAAAAYYS FPTANMPIPQ QDQQYMFNPA
     201  SYISHYYSAV NSNNNGNNAA NNGSNNSSHS APAPAPGPPH HHHHHSNTHN
     251  NLNNGGAVNT NNAPQHHPTI ITDQFQFQLQ QNPSPNLNLN INPAQPLHLP
     301  PGWKINTMPQ PRPTTAPNHP PAPVPSSNPV ASNLVPAPSS DHKYIHQCQF
     351  CEKSFKRKSW LKRHLLSHSQ QRHFLCPWCL SRQKRKDNLL QHMKLKHTNY
     401  LLDELKKNNI IFNYNNSSSS NNNNDNNNNN NSNSASGSGG AGAAAAAATA
     451  PENEDGNGYD TNIKTLINDG VLNKDDVKRV LNNLIVSHNK *         

external links for Mot3p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily Organelle DB
Ashbya (AGD) BOND GPMdb (Mass Spec.) YPL+
YGOB BioPIXIE MIPS YeastGFP
YOGY CYC2008 (complexes) Pfam domains YeastRC Public Image Repository

Complexome YeastRC Structure Prediction (Seattle)

GeneMANIA

References cited on this page View Complete Literature Guide for Mot3p
1) Madison JM, et al.  (1998) Identification and analysis of Mot3, a zinc finger protein that binds to the retrotransposon Ty long terminal repeat (delta) in Saccharomyces cerevisiae. Mol Cell Biol 18(4):1879-90
2) Grishin AV, et al.  (1998) Mot3, a Zn finger transcription factor that modulates gene expression and attenuates mating pheromone signaling in Saccharomyces cerevisiae. Genetics 149(2):879-92
3) Kastaniotis AJ, et al.  (2000) Roles of transcription factor Mot3 and chromatin in repression of the hypoxic gene ANB1 in yeast. Mol Cell Biol 20(19):7088-98
4) Abramova N, et al.  (2001) Reciprocal regulation of anaerobic and aerobic cell wall mannoprotein gene expression in Saccharomyces cerevisiae. J Bacteriol 183(9):2881-7
5) Hongay C, et al.  (2002) Mot3 is a transcriptional repressor of ergosterol biosynthetic genes and is required for normal vacuolar function in Saccharomyces cerevisiae. EMBO J 21(15):4114-24
6) Sertil O, et al.  (2003) Synergistic repression of anaerobic genes by Mot3 and Rox1 in Saccharomyces cerevisiae. Nucleic Acids Res 31(20):5831-7
7) Mennella TA, et al.  (2003) Recruitment of Tup1-Ssn6 by yeast hypoxic genes and chromatin-independent exclusion of TATA binding protein. Eukaryot Cell 2(6):1288-303
8) Montanes FM, et al.  (2011) Repression of ergosterol biosynthesis is essential for stress resistance and is mediated by the Hog1 MAP kinase and the Mot3 and Rox1 transcription factors. Mol Microbiol 79(4):1008-23
9) Alberti S, et al.  (2009) A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 137(1):146-58
10) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41