Basic Information
Name | NGG1-interacting factor 3 |
Uniprot ID | P53081 |
Systematic gene name | YGL221C |
Standard gene name | NIF3 |
Gene names | NIF3 YGL221C |
Description from SGD | YGL221C NIF3 SGDID:S000003189, Chr VII from 82292-81426, Genome Release 64-3-1, reverse complement, Verified ORF, "Protein of unknown function; similar to Listeria monocytogenes major sigma factor (rpoD gene product); the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies" |
Protein length | 288 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MSRAITRAQL DKLVRSITKF YPQKYADKSW DNTGLLIDCS TAQVTTADAN
AKTKVLLTVD LTKSVAQEAV DANCNVIVAY HPFIFPSWNR LSPHTNPQHE
TAIKLIQYGI SVYCPHTAVD AARGGVNDWL VRGLNNGENV AKSYALETVS
GETDDLIGYG RFVEFNKDIS LEQIVKNVKR VLRVPYVQVA SLAAPSAWNQ
LKIKKVAVCA GSGSGVFKQL KEDVDLYYTG EMSHHEVLKW KEMGKTVIVC
NHSNTERGFL QDVMKGLLQD EGHEVVVSKM DCDPLTVA
AKTKVLLTVD LTKSVAQEAV DANCNVIVAY HPFIFPSWNR LSPHTNPQHE
TAIKLIQYGI SVYCPHTAVD AARGGVNDWL VRGLNNGENV AKSYALETVS
GETDDLIGYG RFVEFNKDIS LEQIVKNVKR VLRVPYVQVA SLAAPSAWNQ
LKIKKVAVCA GSGSGVFKQL KEDVDLYYTG EMSHHEVLKW KEMGKTVIVC
NHSNTERGFL QDVMKGLLQD EGHEVVVSKM DCDPLTVA
Legend
- X Phoshorylation
- X K-acetylation
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.
- Internet Explorer: sorry. IE doesn't support WebGL.
- Firefox (version 4 or later): try force enable WebGL.
- Chrome: try force enable WebGL.
- Safari: enable WebGL.
References
[18, 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) |
[18, 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) |
[18, 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) |
[18, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[92, 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) |
[95, 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) |
[176, 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) |
[212, 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) |
[214, 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) |
[218, 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) |