Basic Information

NameGlycine dehydrogenase (decarboxylating), mitochondrial (EC 1.4.4.2) (Glycine cleavage system P protein) (Glycine decarboxylase) (Glycine decarboxylase complex subunit P) (Glycine dehydrogenase (aminomethyl-transferring))
Uniprot IDP49095
Systematic gene nameYMR189W
Standard gene nameGCV2
Gene namesGCV2 GSD2 YMR189W YM9646.01
Description from SGDYMR189W GCV2 SGDID:S000004801, Chr XIII from 637500-640604, Genome Release 64-3-1, Verified ORF, "P subunit of the mitochondrial glycine decarboxylase complex; glycine decarboxylase is required for the catabolism of glycine to 5,10-methylene-THF; expression is regulated by levels of 5,10-methylene-THF in the cytoplasm"
Protein length1034
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MLRTRVTALL CRATVRSSTN YVSLARTRSF HSQSILLKTA ATDITSTQYS
RIFNPDLKNI DRPLDTFARR HLGPSPSDVK KMLKTMGYSD LNAFIEELVP
PNILKRRPLK LEAPSKGFCE QEMLQHLEKI ANKNHYKVKN FIGKGYYGTI
LPPVIQRNLL ESPEWYTSYT PYQPEISQGR LEALLNFQTV VSDLTGLPVA
NASLLDEGTA AGEAMLLSFN ISRKKKLKYV IDKKLHQQTK SVLHTRAKPF
NIEIIEVDCS DIKKAVDVLK NPDVSGCLVQ YPATDGSILP PDSMKQLSDA
LHSHKSLLSV ASDLMALTLL KPPAHYGADI VLGSSQRFGV PMGYGGPHAA
FFAVIDKLNR KIPGRIVGIS KDRLGKTALR LALQTREQHI KRDKATSNIC
TAQALLANVA SSYCVYHGPK GLQNISRRIF SLTSILANAI ENDSCPHELI
NKTWFDTLTI KLGNGISSEQ LLDKALKEFN INLFAVDTTT ISLALDETTT
KADVENLLKV FDIENSSQFL SEDYSNSFPR EFQRTDEILR NEVFHMHHSE
TAMLRYLHRL QSRDLSLANS MIPLGSCTMK LNSTVEMMPI TWPQFSNIHP
FQPSNQVQGY KELITSLEKD LCSITGFDGI SLQPNSGAQG EYTGLRVIRS
YLESKGENHR NVCLIPVSAH GTNPASAAMA GLKVVPVNCL QDGSLDLVDL
KNKAEQHSKE LAAVMITYPS TYGLFEPGIQ HAIDIVHSFG GQVYLDGANM
NAQVGLTSPG DLGADVCHLN LHKTFSIPHG GGGPAGAPIC VKSHLIPHLP
KHDVVDMITG IGGSKSIDSV SSAPYGNALV LPISYAYIKM MGNEGLPFSS
VIAMLNSNYM MTRLKDHYKI LFVNEMSTLK HCAHEFIVDL REYKAKGVEA
IDVAKRLQDY GFHAPTLAFP VPGTLMIEPT ESENLEELDR FCDAMISIKE
EINALVAGQP KGQILKNAPH SLEDLITSSN WDTRGYTREE AAYPLPFLRY
NKFWPTVARL DDTYGDMNLI CTCPSVEEIA NETE

Legend

  • X Phoshorylation
  • X K-Succinylation
  • X Multiple modifications

Structure

Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.


Use imported representation

Loading structure from server... It may take a while.

If you believe something went wrong, please make sure PDB ID is correct.
Please also make sure that WebGL is enabled in your browser.

References

[27, 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)
[29, 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)
[29, 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)
[29, 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)
[29, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[32, 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)
[49, 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)
[50, 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)
[58, K-succ]Frankovsky, J., Keresztesová, B., Bellová, J., et al. (2021). The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids. Journal of Biological Chemistry, 297(4): 101155. (Publication) (All modifications)
[80, K-succ]Frankovsky, J., Keresztesová, B., Bellová, J., et al. (2021). The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids. Journal of Biological Chemistry, 297(4): 101155. (Publication) (All modifications)
[80, K-acetyl]Henriksen, P., Wagner, S. A., Weinert, B. T., et al. (2012). Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Molecular & Cellular Proteomics, 11(11), 1510-1522. (Publication) (All modifications)
[708, 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)
[708, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[776, 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)
[776, 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)