MGA2/YIR033W Protein Information Help

Standard Name Mga2p
Systematic Name Yir033wp
ORF Classification Verified
Description ER membrane protein involved in regulation of OLE1 transcription; inactive ER form dimerizes and one subunit is then activated by ubiquitin/proteasome-dependent processing followed by nuclear targeting; MGA2 has a paralog, SPT23, that arose from the whole genome duplication (1, 2, 3)
Name Description Multicopy suppressor of GAm1 (snf2) 4
Experimental Data
Molecules/cell 300 5
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 1,113
Molecular Weight (Da) 127,053
Isoelectric Point (pI) 4.89

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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 Mga2p (InterPro)
Transmembrane Domains There are 1 total predicted transmembrane domains (TMHMM)
Physical Interactions There are 41 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0000053083 | P40578
MIPS: YIR033W
NCBI: 557839 | 6322224 | 731921 | NP_012299.1
GenBank/EMBL/DDBJ: DAA08580.1 | Z38061
Amino Acid Sequence (or in FASTA format)
       1  MQQNSEFLTE TPGSDPHISQ LHANSVMESQ LLDDFLLNGS PMYQDDSMAH
      51  INIDEGANFQ NFIKTDEGDS PNLLSFEGIG NNTHVNQNVS TPLEEEMESN
     101  RALKEEEEDE HENKVFNEKN IGNPAHDEIV FGRKETIQSV YINPLDYLKV
     151  NAAQLPLDVE VSGLPQVSRV ENQLKLKVKI TSETPLNQSM LYLPSDSISR
     201  EKFYLKKNIE DFSEDFKKNL LYINAFVLCA VSNRTTNVCT KCVKREQRRA
     251  ARRKSGIADN LLWCNNINRR LVVFNNKQVF PIMKTFDNVK EFELTTRLVC
     301  YCRHHKANNG FVILFTITDW QNRLLGKFTT TPIMITDRKP ANMDTTKFNN
     351  TTTSSRRQLT EEESTTEYYS TDNNQLSKDE NMPFQYTYQH NPYDNDSQMN
     401  NIPLKDKNVP FPYSISQQTD LLQNNNLSLN LSLPNQHIPS PTSMSEEGSE
     451  SFNYHHRDND NPVRTISLTN IEQQSQLNQR KRARNNLEND IGKPLFKHSF
     501  SNSISATNTM NPALHSMQDF SMKNNNNNLP SINRVIPSQG PINGGIEVTL
     551  LGCNFKDGLS VKFGSNLALS TQCWSETTIV TYLPPAAYAG QVFVSITDTN
     601  NENNNDDLPQ EIEINDNKKA IFTYVDDTDR QLIELALQIV GLKMNGKLED
     651  ARNIAKRIVG NDSPDSGTNG NSCSKSTGPS PNQHSMNLNT SVLYSDEVLI
     701  QKVIKSLNIN SNISICDSLG RTLLHLACLK NYSSLVYTLI KKGARVNDID
     751  SFGLTPLHFA CISGDPKIIK MLLNCKVNYS LRSHNGLTAR EVFIANHIHS
     801  KEIDKKQDNR DNHKFVHNDT YISEVLSLFE EFQNGTKFTD SVETDSNYSI
     851  SRKYSQSSFN SSLLDNESLN ENLFESQSMI NPTSMEIQHP TLQLFENSSY
     901  SEYDQSDFEE DGDEDLFVTD EVEKPGVACR EEQSELLDIG SSANEPEEDN
     951  GSTSLWNRVL HRINDDLPKY EDLFPLSWGK DDKLKTTNQD SIVEQSASNI
    1001  ENSENSEEED YEEEEEFLKK QFNRFFQNKQ NFRNDKMLIF FWIPLTLLLL
    1051  TWFIMYKFGN QDSSINHISE LISEYLRIAL AKFLLGNERM KTAFRSKLSN
    1101  LQTTRMLNDL IVS*                                       

external links for Mga2p
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
Candida (CandidaDB) CYC2008 (complexes) Pfam domains
YGOB Complexome YeastRC Structure Prediction (Seattle)
YOGY DIP


GeneMANIA


YeastRC Two-Hybrid (Seattle)

References cited on this page View Complete Literature Guide for Mga2p
1) Chellappa R, et al.  (2001) The membrane proteins, Spt23p and Mga2p, play distinct roles in the activation of Saccharomyces cerevisiae OLE1 gene expression. Fatty acid-mediated regulation of Mga2p activity is independent of its proteolytic processing into a soluble transcription activator. J Biol Chem 276(47):43548-56
2) Shcherbik N, et al.  (2003) Rsp5p is required for ER bound Mga2p120 polyubiquitination and release of the processed/tethered transactivator Mga2p90. Curr Biol 13(14):1227-33
3) 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
4) Zhang S, et al.  (1997) Genetic redundancy between SPT23 and MGA2: regulators of Ty-induced mutations and Ty1 transcription in Saccharomyces cerevisiae. Mol Cell Biol 17(8):4718-29
5) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41