Basic Information
Name | Nuclear control of ATPase protein 2 |
Uniprot ID | Q12374 |
Systematic gene name | YPR155C |
Standard gene name | NCA2 |
Gene names | NCA2 YPR155C |
Description from SGD | YPR155C NCA2 SGDID:S000006359, Chr XVI from 837413-835563, Genome Release 64-3-1, reverse complement, Verified ORF, "Protein that regulates expression of Fo-F1 ATP synthase subunits; involved in the regulation of mitochondrial expression of subunits 6 (Atp6p) and 8 (Atp8p) of the Fo-F1 ATP synthase; functions with Nca3p" |
Protein length | 616 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MIINRRILKS FEEISHSLEE SLREVAFDSQ QQLIQDVREE NEELSRLQDQ
LQLIRSIVEK ICISIKTDNI DSYCSVPFDL LYNICKDIAD PSSFEDGDLQ
YLVSQAIFEY IILLCYYSVT NECVQGLPAV YEAEQYYKTV SDSILKSFLY
CLQNSVSTIR LLSQTVLKDV NKKKLSHQKW SLKALSVDLL EKIRPRINKF
MVIRNFRFVG LPKKPIEIAS LVSDIPRGIV HERLDMVTQS SKYYTIKLGQ
LITEFDQQPE ENGMFTEVHL PNYERRLKSL QDFFGLAMSD SNLLDVIRCS
AKFHKDHPLR RFTKPSILTR YWPSILLCLL YGPSSVMSLW NSRYFIQDFI
KTNVVDFAKG LILNWLWAPL KQVWSTVKHD EGSAISVTSQ ETLNSDMDSL
TRMIVSFVVD NSDSTSNSPI DPILLSTKVE HGDLTEFMEI YETQLHHPIK
NIATGGLVRS LLIQLQKTKV DGSMALNGID KMLKSQQLVF GVVALSPALV
ILYSSIVALK RFVKLGNVWS NEKRYREQIS ISLNNVERVL NYSKQGADAD
EEHLNQGLLV IEVSNLYKLG SFLIPRSRKK EWFRDVEELV DTNLDSGAHI
NVVNRIYHVY GRFLIH
LQLIRSIVEK ICISIKTDNI DSYCSVPFDL LYNICKDIAD PSSFEDGDLQ
YLVSQAIFEY IILLCYYSVT NECVQGLPAV YEAEQYYKTV SDSILKSFLY
CLQNSVSTIR LLSQTVLKDV NKKKLSHQKW SLKALSVDLL EKIRPRINKF
MVIRNFRFVG LPKKPIEIAS LVSDIPRGIV HERLDMVTQS SKYYTIKLGQ
LITEFDQQPE ENGMFTEVHL PNYERRLKSL QDFFGLAMSD SNLLDVIRCS
AKFHKDHPLR RFTKPSILTR YWPSILLCLL YGPSSVMSLW NSRYFIQDFI
KTNVVDFAKG LILNWLWAPL KQVWSTVKHD EGSAISVTSQ ETLNSDMDSL
TRMIVSFVVD NSDSTSNSPI DPILLSTKVE HGDLTEFMEI YETQLHHPIK
NIATGGLVRS LLIQLQKTKV DGSMALNGID KMLKSQQLVF GVVALSPALV
ILYSSIVALK RFVKLGNVWS NEKRYREQIS ISLNNVERVL NYSKQGADAD
EEHLNQGLLV IEVSNLYKLG SFLIPRSRKK EWFRDVEELV DTNLDSGAHI
NVVNRIYHVY GRFLIH
Legend
- X Phoshorylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[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] | 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) |
[29, 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) |
[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] | Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications) |
[29, 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) |
[29, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[520, 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) |