P40508

Name	PUP1 protein homolog
Uniprot ID	P40508
Systematic gene name	YIL077C
Standard gene name	RCI37
Gene names	RCI37 YIL077C
Description from SGD	YIL077C RCI37 SGDID:S000001339, Chr IX from 215953-214991, Genome Release 64-3-1, reverse complement, Uncharacterized ORF, "Protein that associates with the large mitoribosomal subunit; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies; deletion confers sensitivity to 4-(N-(S-glutathionylacetyl)amino) phenylarsenoxide (GSAO)"
Protein length	320
Download	sequence (fasta, from Uniprot), modifications (csv format)
Database links	Uniprot, SGD, TheCellVision.org, FungiDB

MLGKEEEQQY GQNGKGMENE LPFMKRPWFK KAYENAIEFH EKDELLDARD
RLELSKAYRS IAKAEMWGGW LGFSAVFLTP FAYRYYKTKA IKGVKVPRNF
VLGVMALFFA TNFAGRSMYT RQLNERDPTG VLKDNYSNKY GDNDFGAFQH
DQTKEIPRNQ RQYNMMRLLD SGSPSRWSMY FYITYQNPER RLPDPKVKLQ
QMKKGGVFNG SPFMNQRDPI GLYRNKGRKS PDPIEGEQND SPVLSSWEKI
RNGDNSSSSS WENIRNTSRD QSQESDASVD HESDIFISGF SDDGNATDNS
SSDDKYQRLL QSGRYGGNRS

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[230, Phos]	Vlastaridis P, Kyriakidou P, Chaliotis A, et al (2017) Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes. GigaScience 6:1–11. (Publication) (All modifications)
[230, Phos]	Guo X, Niemi NM, Coon JJ, Pagliarini DJ (2017a) Integrative proteomics and biochemical analyses define Ptc6p as the Saccharomyces cerevisiae pyruvate dehydrogenase phosphatase. J Biol Chem 292:11751–11759. (Publication) (All modifications)
[230, Phos]	Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications)
[230, Phos]	Holt, L.J.,  Tuch, B.B.,  Villén, J.,  Johnson, A.D.,  Gygi, S.P.,  Morgan, D.O. (2009). Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution. Science 325(5948): 1682-1686. (Publication) (All modifications)
[230, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[295, Glyc]	Cao, L.,  Yu, L.,  Guo, Z.,  Shen, A.,  Guo, Y.,  Liang, X. (2014). N-Glycosylation site analysis of proteins from Saccharomyces cerevisiae by using hydrophilic interaction liquid chromatography-based enrichment, parallel deglycosylation, and mass spectrometry. J Proteome Res 13: 1485-1493. (Publication) (All modifications)
[299, Glyc]	Cao, L.,  Yu, L.,  Guo, Z.,  Shen, A.,  Guo, Y.,  Liang, X. (2014). N-Glycosylation site analysis of proteins from Saccharomyces cerevisiae by using hydrophilic interaction liquid chromatography-based enrichment, parallel deglycosylation, and mass spectrometry. J Proteome Res 13: 1485-1493. (Publication) (All modifications)