Basic Information

NameLong-chain-fatty-acid--CoA ligase 2 (EC 6.2.1.3) (Fatty acid activator 2) (Long-chain acyl-CoA synthetase 2)
Uniprot IDP39518
Systematic gene nameYER015W
Standard gene nameFAA2
Gene namesFAA2 FAM1 YER015W
Description from SGDYER015W FAA2 SGDID:S000000817, Chr V from 184541-186775, Genome Release 64-3-1, Verified ORF, "Medium chain fatty acyl-CoA synthetase; activates imported fatty acids; accepts a wide range of fatty acid chain lengths with a preference for medium chains, C9:0-C13:0; localized to the peroxisome; comparative analysis suggests that a mitochondrially targeted form may result from translation starting at a non-canonical codon upstream of the annotated start codon"
Protein length744
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MAAPDYALTD LIESDPRFES LKTRLAGYTK GSDEYIEELY SQLPLTSYPR
YKTFLKKQAV AISNPDNEAG FSSIYRSSLS SENLVSCVDK NLRTAYDHFM
FSARRWPQRD CLGSRPIDKA TGTWEETFRF ESYSTVSKRC HNIGSGILSL
VNTKRKRPLE ANDFVVAILS HNNPEWILTD LACQAYSLTN TALYETLGPN
TSEYILNLTE APILIFAKSN MYHVLKMVPD MKFVNTLVCM DELTHDELRM
LNESLLPVKC NSLNEKITFF SLEQVEQVGC FNKIPAIPPT PDSLYTISFT
SGTTGLPKGV EMSHRNIASG IAFAFSTFRI PPDKRNQQLY DMCFLPLAHI
FERMVIAYDL AIGFGIGFLH KPDPTVLVED LKILKPYAVA LVPRILTRFE
AGIKNALDKS TVQRNVANTI LDSKSARFTA RGGPDKSIMN FLVYHRVLID
KIRDSLGLSN NSFIITGSAP ISKDTLLFLR SALDIGIRQG YGLTETFAGV
CLSEPFEKDV GSCGAIGISA ECRLKSVPEM GYHADKDLKG ELQIRGPQVF
ERYFKNPNET SKAVDQDGWF STGDVAFIDG KGRISVIDRV KNFFKLAHGE
YIAPEKIENI YLSSCPYITQ IFVFGDPLKT FLVGIVGVDV DAAQPILAAK
HPEVKTWTKE VLVENLNRNK KLRKEFLNKI NKCTDGLQGF EKLHNIKVGL
EPLTLEDDVV TPTFKIKRAK ASKFFKDTLD QLYAEGSLVK TEKL

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

[32, 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)
[32, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[35, 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)
[35, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[41, 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)
[41, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[46, 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)
[46, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[47, 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)
[47, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[226, 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)
[259, 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)
[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)
[711, 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)
[711, Phos]Albuquerque, C.P., Smolka, M.B., Payne, S.H., Bafna, V., Eng, J., Zhou, H. (2008). A multidimensional chromatography technology for in-depth phosphoproteome analysis. Molecular and Cellular Proteomics 7(7):1389-1396. (Publication) (All modifications)
[711, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)