P53907

Name	Uncharacterized protein YNL144C
Uniprot ID	P53907
Systematic gene name	YNL144C
Standard gene name	YNL144C
Gene names	YNL144C N1205 N1790
Description from SGD	YNL144C YNL144C SGDID:S000005088, Chr XIV from 355042-352820, Genome Release 64-3-1, reverse complement, Uncharacterized ORF, "Putative protein of unknown function; non-tagged protein is detected in highly purified mitochondria in high-throughput studies; contains a PH domain and binds phosphatidylinositols and phosphatidylethanolamine in a large-scale study; YNL144C has a paralog, YHR131C, that arose from the whole genome duplication"
Protein length	740
Download	sequence (fasta, from Uniprot), modifications (csv format)
Database links	Uniprot, SGD, TheCellVision.org, FungiDB

MSSSIFEMTI DHDGMDSTGL KLSQTASSIS MGDEFLCSST TSNSILDSPL
PKVTFNHIDS ITDINTNIMN EIVEPQSGVD VDVADKNVLY CIDPYPVEPP
CYDFANPSKV IRYPIYEHCR PCLTSVKPPS YTPSVEHYTV VSMKMEKLSP
FENASSRLWN NFILQINSTQ INFYSIDDSL TRHIKNYRGG DMFDHSHHSK
TASDRHHSAR SLLNAFTTKS TYQFDKYDKE RICGEIARDE HKFLSDERLF
KSYSLQCAKV GLPIDYSSRD FVLRMRCEGQ QFLVQFSHVD ELIYWAMYLN
MGISLSLDLE LREMPTYRSV PRRRHPRARR FKQHNKNKNK NKSRQNSDRN
DSRSHSLLLR RSHTSSVVTK VATGNERPTN KSRSRSLSLL PPSVSDASHD
SNGPNDSGSL AGESSQTDFC GLFTSKLRNF FKTDSSSRKN SNMDIGQKMR
SKELNSVQEE IDDNGSTTNT NTSVLSSTFS PTAHSVLTAQ TSIHENFRSR
SNSNPIDPLR CDRSVLKINN FEPVYEGTGR STISNSAERT NREEKLNRGN
EDVNGDEDDD EDEDDANYEE DDEDGYVEDD DINRLVYLDE RESRYENADV
EYGTIFSTKS FSVTGCLNHD FPKKLSLKCG NKNQSSNDSK WAPATQLVSR
KRYIKDSLRC IKPLTEDHPW VGKIIFKPAL PPAFETNNPP IRVYSGEDST
DLMHVKNHYL KPYIVGSCGF LKTGSKLFHF YDRTNDLTNL

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[441, Phos]	Swaney, D.L.,  Beltrao, P.,  Starita, L.,  Guo, A.,  Rush, J.,  Fields, S.,  Krogan, N.J.,  Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications)
[501, Phos]	Swaney, D.L.,  Beltrao, P.,  Starita, L.,  Guo, A.,  Rush, J.,  Fields, S.,  Krogan, N.J.,  Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications)
[503, Phos]	Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[503, 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)
[503, 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)
[503, Phos]	Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications)
[503, 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)
[503, Phos]	Swaney, D.L.,  Beltrao, P.,  Starita, L.,  Guo, A.,  Rush, J.,  Fields, S.,  Krogan, N.J.,  Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications)
[503, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[517, Ubi]	Swaney, D.L.,  Beltrao, P.,  Starita, L.,  Guo, A.,  Rush, J.,  Fields, S.,  Krogan, N.J.,  Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications)
[640, Ubi]	Swaney, D.L.,  Beltrao, P.,  Starita, L.,  Guo, A.,  Rush, J.,  Fields, S.,  Krogan, N.J.,  Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications)