Basic Information
Name | Uncharacterized protein YKL187C |
Uniprot ID | P34231 |
Systematic gene name | YKL187C |
Standard gene name | FAT3 |
Gene names | FAT3 YKL187C |
Description from SGD | YKL187C FAT3 SGDID:S000001670, Chr XI from 91536-89284, Genome Release 64-3-1, reverse complement, Verified ORF, "Protein required for fatty acid uptake; protein abundance increases in cortical patches in response to oleate exposure; the authentic, non-tagged protein is detected in a phosphorylated state in highly purified mitochondria in high-throughput studies; FAT3 has a paralog, YLR413W, that arose from the whole genome duplication" |
Protein length | 750 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MRIEKHRTPL SKGIIWTILS VCLLFMFTTL ILVIVATAGS TANYKPLTNI
YIGEADIKHI NVSKVIPQIG PILTILGSAL TAPNSSLDDI FGAMKNIADT
PALTPLLTLL SNADNTTVTI ESLTELAPLA ISGNPASSTR QLTEINGLLK
YSDNATETLD GLSRLVSASL SSASSNSSSD STTLVLDLLK DSDNPQNSTD
ALLTLNNLTM SEKAQLLPVF RLFAFSTNQT ATMTALATLM NTTISSSLAQ
TLLTQLQNTI SNGGSLNNTF STLQPLVPQA SAPAFDAVEL LLNQTTSTNQ
TLSTLSDLLE QNLTQSSSAK KAFAALTQLM ENSDNSTMVV TSVQSLAAVT
NTTQSTQQLI GLDDVISSSS NTNETLSILS ELQSGLSGNS SSVQYIPYLF
SLLGASTDPK TTFSSLVTLT SWAQENPQTF LPILDILADA KSVQPISAEE
LNAMTPNILE YLKIPIYYRL SIFTLCHANL ENKILDCNSP HAVQNLDFRS
IIYDALVTSD FQPYLNALNI SANDLYLEGK LLHREHQYVP AVRSVLALNL
LAIIFSFFTM IFIILLYFNR YMFKQPLWLI ALALHVCVGV ATVLAAIIIS
VMIAIIKSGT ADDKYGVVFK AGPAYTGLIW TAFALSFIAT GLIIYTWWRN
RRSGRYMSGS VTNRKGEIYT YGDGSAISAD RFGDHNLGDD DDADFEKQVN
RNEITAIDNS SSANNTDVTG STSNRTELSH PDVTPKDSNG PVNNNAHLVA
YIGEADIKHI NVSKVIPQIG PILTILGSAL TAPNSSLDDI FGAMKNIADT
PALTPLLTLL SNADNTTVTI ESLTELAPLA ISGNPASSTR QLTEINGLLK
YSDNATETLD GLSRLVSASL SSASSNSSSD STTLVLDLLK DSDNPQNSTD
ALLTLNNLTM SEKAQLLPVF RLFAFSTNQT ATMTALATLM NTTISSSLAQ
TLLTQLQNTI SNGGSLNNTF STLQPLVPQA SAPAFDAVEL LLNQTTSTNQ
TLSTLSDLLE QNLTQSSSAK KAFAALTQLM ENSDNSTMVV TSVQSLAAVT
NTTQSTQQLI GLDDVISSSS NTNETLSILS ELQSGLSGNS SSVQYIPYLF
SLLGASTDPK TTFSSLVTLT SWAQENPQTF LPILDILADA KSVQPISAEE
LNAMTPNILE YLKIPIYYRL SIFTLCHANL ENKILDCNSP HAVQNLDFRS
IIYDALVTSD FQPYLNALNI SANDLYLEGK LLHREHQYVP AVRSVLALNL
LAIIFSFFTM IFIILLYFNR YMFKQPLWLI ALALHVCVGV ATVLAAIIIS
VMIAIIKSGT ADDKYGVVFK AGPAYTGLIW TAFALSFIAT GLIIYTWWRN
RRSGRYMSGS VTNRKGEIYT YGDGSAISAD RFGDHNLGDD DDADFEKQVN
RNEITAIDNS SSANNTDVTG STSNRTELSH PDVTPKDSNG PVNNNAHLVA
Legend
- X Phoshorylation
- X Ubiquitination
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[658, 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) |
[658, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[665, 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) |
[675, Phos] | Reinders J, Wagner K, Zahedit RP, et al (2007) Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase. Molecular and Cellular Proteomics 6:1896–1906. (Publication) (All modifications) |
[675, Phos] | Renvoisé M, Bonhomme L, Davanture M, et al (2014) Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae. Journal of Proteomics 106:140–150. (Publication) (All modifications) |
[675, 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) |
[675, 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) |
[675, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[678, 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) |
[678, Phos] | Reinders J, Wagner K, Zahedit RP, et al (2007) Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase. Molecular and Cellular Proteomics 6:1896–1906. (Publication) (All modifications) |
[678, Phos] | Renvoisé M, Bonhomme L, Davanture M, et al (2014) Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae. Journal of Proteomics 106:140–150. (Publication) (All modifications) |
[678, 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) |
[678, 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) |
[678, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[697, 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) |
[697, Ubi] | Peng, J., Schwartz, D., Elias, J.E., Thoreen, C.C., Cheng, D., Marsischky, G., Roelofs, J., Finley, D., Gygi, S.P. (2003). A proteomics approach to understanding protein ubiquitination. Nat Biotechnol 21: 921-926. (Publication) (All modifications) |
[710, 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) |
[711, 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) |
[712, 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) |
[729, 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) |
[738, 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) |