P53036

Name	SIT4-associating protein SAP4
Uniprot ID	P53036
Systematic gene name	YGL229C
Standard gene name	SAP4
Gene names	SAP4 YGL229C
Description from SGD	YGL229C SAP4 SGDID:S000003198, Chr VII from 66959-64503, Genome Release 64-3-1, reverse complement, Verified ORF, "Protein required for function of the Sit4p protein phosphatase; member of a family of similar proteins that form complexes with Sit4p, including Sap155p, Sap185p, and Sap190p; SAP4 has a paralog, SAP155, that arose from the whole genome duplication"
Protein length	818
Download	sequence (fasta, from Uniprot), modifications (csv format)
Database links	Uniprot, SGD, TheCellVision.org, FungiDB

MSLWPFGETL SHSGIDSILE EYYLIFRSLE GNETSSTDDK KNEPSMESES
EFGTESRDRS DLNQSFIDRI LLETALLDEL NGAANDRLVD FICLGYFYDD
RSQQVRHMDY LVDMLMAYLK DIDRTGYRTP FLLENSFHQT GEYEDQDDED
PMLYVNIISS IFCSKSAPIV EALVQNTPFL SSLFEVFQFE NIEAENCPIL
AVFLKINETL LFEQTSSYLE FFKSQPNIVD KFLYHIEVSP LVEFLIKIML
TDQVESPTNI IDFLYHQDLI PKCLNLLENS KYSPGIQNSS GELLKALISI
STNFKLDTLW IGPNRLTRQL ASPQYVDQLI NIILFQRGHA MGVAVSIIIE
LIRKNNSDYD EVDLLSTTIV DNPPSQRDPV YLGHLLYELT MHMEDFYALL
IKLENDDDDD HDTASKALPS VKHHLLENQL HESFRPLGFE RVKITELISE
MLHCSNMGLM NSKRGEKIAR TRDKCRDTLD QNSLEKAMKN LNINDNTITS
NTLEDKCNNN DSNDSNDNQK QKKNIKKKFH DNELYSTFDT SDDNIDDDDD
MSFEIPYVSE TQNLKIRKNP TIGDLFKIKL HDLGFFPKFL QLFLRYPWNN
FWHNIVFDII QQIFNGRMDF SYNSFLVYSL FDFKKSTRFI PKPLYGSNQK
LPVKDFHIIS DFILQGHKDS FEFYEKEKTN LGYMGQLVLI AEEIAKYSKI
YKTDLIAPDI YAFLQDEVWM SYSSDILNET RTMCSIILGG GQFCAESDEN
TNQDFLEKAD MSKPAHPSTM DENEIVHEED VKLHDKVAEL IDELGQLTEL
DIHDKIKDVI VDHHSDLN

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[35, 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)
[36, 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)
[36, 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)
[36, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[37, 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)
[37, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[136, 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)
[815, 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)
[815, 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)
[815, 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)
[815, Phos]	MacGilvray, M.E., Shishkova, E., Place, M., Wagner, E.R., Coon, J.J., Gasch, A.P. (2020). Phosphoproteome response to dithiothreitol reveals unique versus shared features of Saccharomyces cerevisiae stress responses. Journal of Proteome Research 19(8): 3405-3417. (Publication) (All modifications)
[815, 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)
[815, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)