Basic Information

NameEndonuclease III homolog 1 (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase 1) (DNA glycosylase/AP lyase 1) (Endonuclease III-like glycosylase 1) (Redoxyendonuclease 1)
Uniprot IDP31378
Systematic gene nameYAL015C
Standard gene nameNTG1
Gene namesNTG1 OGG2 SCR1 YAL015C FUN33
Description from SGDYAL015C NTG1 SGDID:S000000013, Chr I from 128102-126903, Genome Release 64-3-1, reverse complement, Verified ORF, "DNA N-glycosylase and apurinic/apyrimidinic (AP) lyase; involved in base excision repair; acts in both nucleus and mitochondrion; creates a double-strand break at mtDNA origins that stimulates replication in response to oxidative stress; required for maintaining mitochondrial genome integrity; NTG1 has a paralog, NTG2, that arose from the whole genome duplication"
Protein length399
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MQKISKYSSM AILRKRPLVK TETGPESELL PEKRTKIKQE EVVPQPVDID
WVKSLPNKQY FEWIVVRNGN VPNRWATPLD PSILVTPAST KVPYKFQETY
ARMRVLRSKI LAPVDIIGGS SIPVTVASKC GISKEQISPR DYRLQVLLGV
MLSSQTKDEV TAMAMLNIMR YCIDELHSEE GMTLEAVLQI NETKLDELIH
SVGFHTRKAK YILSTCKILQ DQFSSDVPAT INELLGLPGV GPKMAYLTLQ
KAWGKIEGIC VDVHVDRLTK LWKWVDAQKC KTPDQTRTQL QNWLPKGLWT
EINGLLVGFG QIITKSRNLG DMLQFLPPDD PRSSLDWDLQ SQLYKEIQQN
IMSYPKWVKY LEGKRELNVE AEINVKHEEK TVEETMVKLE NDISVKVED

Legend

  • X SUMOylation
  • X Phoshorylation

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

[20, SUMO]Bhagwat, N.R., Owens, S.N., Ito, M., Boinapalli, J.V,, Poa, P., Ditzel, A., Kopparapu, S., Mahalawat, M., Davies, O.R., Collins, S.R., Johnson, J.R., Krogan, N.J., Hunter, N. (2021). SUMO is a pervasive regulator of meiosis. Elife 10:e57720. (Publication) (All modifications)
[20, SUMO]Swartzlander, D.B.,  McPherson, A.J.,  Powers, H.R.,  Limpose, K.L.,  Kuiper, E.G.,  Degtyareva, N.P.,  Corbett, A.H., Doetsch, P.W. (2016). Identification of SUMO modification sites in the base excision repair protein, Ntg1. DNA Repair (Amst) 48: 51-62. (Publication) (All modifications)
[23, 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)
[23, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[38, SUMO]Bhagwat, N.R., Owens, S.N., Ito, M., Boinapalli, J.V,, Poa, P., Ditzel, A., Kopparapu, S., Mahalawat, M., Davies, O.R., Collins, S.R., Johnson, J.R., Krogan, N.J., Hunter, N. (2021). SUMO is a pervasive regulator of meiosis. Elife 10:e57720. (Publication) (All modifications)
[38, SUMO]Swartzlander, D.B.,  McPherson, A.J.,  Powers, H.R.,  Limpose, K.L.,  Kuiper, E.G.,  Degtyareva, N.P.,  Corbett, A.H., Doetsch, P.W. (2016). Identification of SUMO modification sites in the base excision repair protein, Ntg1. DNA Repair (Amst) 48: 51-62. (Publication) (All modifications)
[341, 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)
[353, 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)
[364, SUMO]Griffiths, L.M., Swartzlander, D., Meadows, K.L,, Wilkinson, K.D., Corbett, A.H., Doetsch, P.W. (2009). Dynamic compartmentalization of base excision repair proteins in response to nuclear and mitochondrial oxidative stress. Mol Cell Biol 29(3):794-807 (Publication) (All modifications)
[376, SUMO]Bhagwat, N.R., Owens, S.N., Ito, M., Boinapalli, J.V,, Poa, P., Ditzel, A., Kopparapu, S., Mahalawat, M., Davies, O.R., Collins, S.R., Johnson, J.R., Krogan, N.J., Hunter, N. (2021). SUMO is a pervasive regulator of meiosis. Elife 10:e57720. (Publication) (All modifications)
[376, SUMO]Swartzlander, D.B.,  McPherson, A.J.,  Powers, H.R.,  Limpose, K.L.,  Kuiper, E.G.,  Degtyareva, N.P.,  Corbett, A.H., Doetsch, P.W. (2016). Identification of SUMO modification sites in the base excision repair protein, Ntg1. DNA Repair (Amst) 48: 51-62. (Publication) (All modifications)
[388, SUMO]Bhagwat, N.R., Owens, S.N., Ito, M., Boinapalli, J.V,, Poa, P., Ditzel, A., Kopparapu, S., Mahalawat, M., Davies, O.R., Collins, S.R., Johnson, J.R., Krogan, N.J., Hunter, N. (2021). SUMO is a pervasive regulator of meiosis. Elife 10:e57720. (Publication) (All modifications)
[388, SUMO]Swartzlander, D.B.,  McPherson, A.J.,  Powers, H.R.,  Limpose, K.L.,  Kuiper, E.G.,  Degtyareva, N.P.,  Corbett, A.H., Doetsch, P.W. (2016). Identification of SUMO modification sites in the base excision repair protein, Ntg1. DNA Repair (Amst) 48: 51-62. (Publication) (All modifications)
[396, SUMO]Swartzlander, D.B.,  McPherson, A.J.,  Powers, H.R.,  Limpose, K.L.,  Kuiper, E.G.,  Degtyareva, N.P.,  Corbett, A.H., Doetsch, P.W. (2016). Identification of SUMO modification sites in the base excision repair protein, Ntg1. DNA Repair (Amst) 48: 51-62. (Publication) (All modifications)