Basic Information

NameNucleoporin NUP116/NSP116 (Nuclear pore protein NUP116/NSP116)
Uniprot IDQ02630
Systematic gene nameYMR047C
Standard gene nameNUP116
Gene namesNUP116 NSP116 YMR047C YM9532.12C
Description from SGDYMR047C NUP116 SGDID:S000004650, Chr XIII from 366705-363364, Genome Release 64-3-1, reverse complement, Verified ORF, "FG-nucleoporin component of central core of the nuclear pore complex; contributes directly to nucleocytoplasmic transport and maintenance of the nuclear pore complex (NPC) permeability barrier; forms a stable association with Nup82p, Gle2p and two other FG-nucleoporins (Nsp1p and Nup159p); NUP116 has a paralog, NUP100, that arose from the whole genome duplication"
Protein length1113
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MFGVSRGAFP SATTQPFGST GSTFGGQQQQ QQPVANTSAF GLSQQTNTTQ
APAFGNFGNQ TSNSPFGMSG STTANGTPFG QSQLTNNNAS GSIFGGMGNN
TALSAGSASV VPNSTAGTSI KPFTTFEEKD PTTGVINVFQ SITCMPEYRN
FSFEELRFQD YQAGRKFGTS QNGTGTTFNN PQGTTNTGFG IMGNNNSTTS
ATTGGLFGQK PATGMFGTGT GSGGGFGSGA TNSTGLFGSS TNLSGNSAFG
ANKPATSGGL FGNTTNNPTN GTNNTGLFGQ QNSNTNGGLF GQQQNSFGAN
NVSNGGAFGQ VNRGAFPQQQ TQQGSGGIFG QSNANANGGA FGQQQGTGAL
FGAKPASGGL FGQSAGSKAF GMNTNPTGTT GGLFGQTNQQ QSGGGLFGQQ
QNSNAGGLFG QNNQSQNQSG LFGQQNSSNA FGQPQQQGGL FGSKPAGGLF
GQQQGASTFA SGNAQNNSIF GQNNQQQQST GGLFGQQNNQ SQSQPGGLFG
QTNQNNNQPF GQNGLQQPQQ NNSLFGAKPT GFGNTSLFSN STTNQSNGIS
GNNLQQQSGG LFQNKQQPAS GGLFGSKPSN TVGGGLFGNN QVANQNNPAS
TSGGLFGSKP ATGSLFGGTN STAPNASSGG IFGSNNASNT AATTNSTGLF
GNKPVGAGAS TSAGGLFGNN NNSSLNNSNG STGLFGSNNT SQSTNAGGLF
QNNTSTNTSG GGLFSQPSQS MAQSQNALQQ QQQQQRLQIQ NNNPYGTNEL
FSKATVTNTV SYPIQPSATK IKADERKKAS LTNAYKMIPK TLFTAKLKTN
NSVMDKAQIK VDPKLSISID KKNNQIAISN QQEENLDESI LKASELLFNP
DKRSFKNLIN NRKMLIASEE KNNGSQNNDM NFKSKSEEQE TILGKPKMDE
KETANGGERM VLSSKNDGED SATKHHSRNM DEENKENVAD LQKQEYSEDD
KKAVFADVAE KDASFINENY YISPSLDTLS SYSLLQLRKV PHLVVGHKSY
GKIEFLEPVD LAGIPLTSLG GVIITFEPKT CIIYANLPNR PKRGEGINVR
ARITCFNCYP VDKSTRKPIK DPNHQLVKRH IERLKKNPNS KFESYDADSG
TYVFIVNHAA EQT

Legend

  • X Phoshorylation
  • X K-benzoylation

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

[152, 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)
[152, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[241, Phos]Studer RA, Rodriguez-Mias RA, Haas KM, et al (2016) Evolution of protein phosphorylation across 18 fungal species. Science 354:229–232. (Publication) (All modifications)
[241, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[816, 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)
[816, 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)
[816, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[818, 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)
[886, 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)
[886, 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)
[886, 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)
[886, 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)
[886, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[895, K-bz]Wang, D., Yan, F., Wu, P., Ge, K., Li, M., Li, T., Gao, Y., Peng, C., Chen, Y. (2022). Global profiling of regulatory elements in the histone benzoylation pathway. Nature Communications 13(1):1369 (Publication) (All modifications)
[921, 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)
[921, 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)
[921, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[947, 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)
[947, 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)
[947, 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)
[947, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)