Basic Information
Name | Uncharacterized ATP-dependent helicase IRC20 (EC 3.6.1.-) (Increased recombination centers protein 20) |
Uniprot ID | Q06554 |
Systematic gene name | YLR247C |
Standard gene name | IRC20 |
Gene names | IRC20 YLR247C |
Description from SGD | YLR247C IRC20 SGDID:S000004237, Chr XII from 633354-628684, Genome Release 64-3-1, reverse complement, Verified ORF, "E3 ubiquitin ligase and putative helicase; involved in synthesis-dependent strand annealing-mediated homologous recombination; ensures precise end-joining along with Srs2p in the Yku70p/Yku80p/Lig4p-dependent NHEJ pathway; controls 2-um plasmid copy number by regulating the levels of the Flp1p recombinase; localizes to both the mitochondrion and the nucleus; contains a Snf2/Swi2 family ATPase/helicase and a RING finger domain; null mutant displays increased levels of spontaneous Rad52p foci" |
Protein length | 1556 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MSAVGALLAR EYNVTAEKCD FFLENGSFDS VIAALPALNQ EQETVTQKVS
KNGKELINVA SVNIEIPERI SLSNNGRQLF KFIVDIEILP CENDNEATLV
VSSDSVSLFQ IGFKMENNSK IAVDKQLPLI LDICAHKNQE RALRNQLENR
KSLERKPSRK RRKKNSNVND PEKLLKSRIH ELSLSYKDFE CSPVVFRYND
SSLTWVLSFN LKLKFLNNKF NRFSVEANQI LDLTFSNRDE NEFERYHKHS
HIHSNFIQKQ FISQILEYSK DRLSKIKPFL PQSIPDLKVN LLPFQRESVE
WMLIKEGHGN SLSDTPTVID EVGLIDFMNE YYAYGYELIA RSPDEVGPSL
LWNKLTGYIL TTEDAAHLYN QYRKERLSGD YPVCAKGVLA EEMGLGKTIE
ILSLILLNRR KLKDSEATFI DDENRTITKT KTTLIICPNA ILKQWLEEIE
LHANSLKWYT YRGYNEIMKD CKTVDEAVQQ LCQYDIIVTS YNIIATEVHH
AEFNRSIRSR RLKSPKYDYS SPLALMQFYR IILDEVQMLR SSSTYSAKCT
SLLHRIHTWG VSGTPIQNIY NFRMIMSYLK LHPFCDEVDF IRTLQEEIKL
RNEAKDYTSN DFVCQLKGVR FSIKDCMNIF YRYDLCIRHS KANVASQIHI
PRQHNFIIPL EFAPIEWDNY LNLWNNFLEL SGYNSDGSGS PRVSNAFLNE
WLSRLRYICC HALFPEILST RQKRLHGHLS RISNIDDILI SMRMDAFDSL
IGYYRERFHL SIKQAQYELE ISNTPAKALE SFIKIRDDLM IHIRQKFNVE
DPFDKSLNLS EDEDEHMDER FGEKETSSGD ESDREINGAK NHDNHNNDGM
LSNHLKKKGL RAMMNLLHDC YFFLGSVYYN LGTRKLEEAD DKHRKEKTEE
VVYSDVFPKN ELEEIEENRL LEQENYANAE ILRKSILSSE ARKVDMTIKM
ARTKFAPMTS NIPLRLINIE FDHKNDYSSN LAVSRCFKSL SKLIEGLNEQ
TKNFNELLDE LLIIIYEPVH RTEDDDSTNK IIGNEEYSTS IDSQDKIFSL
LGCLEIILQN RDNILTSESE VKIPKHLVPE GSIISKYQKQ LLNSLRLISG
TPLRTVFDEL KNSRIVRRIS SSNESESTIQ NFEDYLLQYE VESKSLFKYN
KQVRESLKIL GSIYNAKTEY YSQLQRISDS LVSLHSLSAP QLSHLIRTIN
KSLGGTLDAK INNIESRLIY LKNLSRLKDT LNDNQILSCS ICLGEVEIGA
IIKCGHYFCK SCILTWLRAH SKCPICKGFC SISEVYNFKF KNSTEKREKE
IQEPRREGAD SSQDNSNENS IISNMSEVEK LFGNKYEQFH QINEVHQIHI
KESFGAKIDF VIKLISYLRL KSEQENADPP QVILYSQKTE YLKVIGKVLK
LYHIEHLACL SNTANVGETI NNFKRQPSVT CLLLNVKTLG AGLNLINAKH
IFLLDPILNN SDELQAMGRN NRIGQDEETF VWNFMIRNTV EENILRYKCI
LEERKRKEKS KKGDKYDEAQ DETDNEESDD AKFEISVVDQ EVSNEHLWNC
FFHGSD
KNGKELINVA SVNIEIPERI SLSNNGRQLF KFIVDIEILP CENDNEATLV
VSSDSVSLFQ IGFKMENNSK IAVDKQLPLI LDICAHKNQE RALRNQLENR
KSLERKPSRK RRKKNSNVND PEKLLKSRIH ELSLSYKDFE CSPVVFRYND
SSLTWVLSFN LKLKFLNNKF NRFSVEANQI LDLTFSNRDE NEFERYHKHS
HIHSNFIQKQ FISQILEYSK DRLSKIKPFL PQSIPDLKVN LLPFQRESVE
WMLIKEGHGN SLSDTPTVID EVGLIDFMNE YYAYGYELIA RSPDEVGPSL
LWNKLTGYIL TTEDAAHLYN QYRKERLSGD YPVCAKGVLA EEMGLGKTIE
ILSLILLNRR KLKDSEATFI DDENRTITKT KTTLIICPNA ILKQWLEEIE
LHANSLKWYT YRGYNEIMKD CKTVDEAVQQ LCQYDIIVTS YNIIATEVHH
AEFNRSIRSR RLKSPKYDYS SPLALMQFYR IILDEVQMLR SSSTYSAKCT
SLLHRIHTWG VSGTPIQNIY NFRMIMSYLK LHPFCDEVDF IRTLQEEIKL
RNEAKDYTSN DFVCQLKGVR FSIKDCMNIF YRYDLCIRHS KANVASQIHI
PRQHNFIIPL EFAPIEWDNY LNLWNNFLEL SGYNSDGSGS PRVSNAFLNE
WLSRLRYICC HALFPEILST RQKRLHGHLS RISNIDDILI SMRMDAFDSL
IGYYRERFHL SIKQAQYELE ISNTPAKALE SFIKIRDDLM IHIRQKFNVE
DPFDKSLNLS EDEDEHMDER FGEKETSSGD ESDREINGAK NHDNHNNDGM
LSNHLKKKGL RAMMNLLHDC YFFLGSVYYN LGTRKLEEAD DKHRKEKTEE
VVYSDVFPKN ELEEIEENRL LEQENYANAE ILRKSILSSE ARKVDMTIKM
ARTKFAPMTS NIPLRLINIE FDHKNDYSSN LAVSRCFKSL SKLIEGLNEQ
TKNFNELLDE LLIIIYEPVH RTEDDDSTNK IIGNEEYSTS IDSQDKIFSL
LGCLEIILQN RDNILTSESE VKIPKHLVPE GSIISKYQKQ LLNSLRLISG
TPLRTVFDEL KNSRIVRRIS SSNESESTIQ NFEDYLLQYE VESKSLFKYN
KQVRESLKIL GSIYNAKTEY YSQLQRISDS LVSLHSLSAP QLSHLIRTIN
KSLGGTLDAK INNIESRLIY LKNLSRLKDT LNDNQILSCS ICLGEVEIGA
IIKCGHYFCK SCILTWLRAH SKCPICKGFC SISEVYNFKF KNSTEKREKE
IQEPRREGAD SSQDNSNENS IISNMSEVEK LFGNKYEQFH QINEVHQIHI
KESFGAKIDF VIKLISYLRL KSEQENADPP QVILYSQKTE YLKVIGKVLK
LYHIEHLACL SNTANVGETI NNFKRQPSVT CLLLNVKTLG AGLNLINAKH
IFLLDPILNN SDELQAMGRN NRIGQDEETF VWNFMIRNTV EENILRYKCI
LEERKRKEKS KKGDKYDEAQ DETDNEESDD AKFEISVVDQ EVSNEHLWNC
FFHGSD
Legend
- X Phoshorylation
- X Ubiquitination
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
[2, 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) |
[73, 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) |
[593, 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) |
[605, Ubi] | 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) |
[810, 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) |
[810, 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) |
[810, 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) |
[810, 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) |
[810, 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) |
[810, 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) |
[810, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[826, 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) |
[827, 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) |
[828, 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) |
[832, 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) |
[832, 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) |
[832, 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) |
[938, 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) |
[939, 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) |
[1311, 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) |
[1312, 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) |
[1312, 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) |
[1312, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1316, 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) |
[1316, 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) |
[1320, 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) |
[1428, 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) |
[1430, 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) |
[1523, 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) |
[1523, 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) |
[1523, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |