Basic Information
Name | Inhibitory regulator protein IRA1 |
Uniprot ID | P18963 |
Systematic gene name | YBR140C |
Standard gene name | IRA1 |
Gene names | IRA1 GLC1 PPD1 YBR140C YBR1016 |
Description from SGD | YBR140C IRA1 SGDID:S000000344, Chr II from 526628-517350, Genome Release 64-3-1, reverse complement, Verified ORF, "GTPase-activating protein; negatively regulates RAS by converting it from GTP- to the GDP-bound inactive form, required for reducing cAMP levels under nutrient limiting conditions, mediates membrane association of adenylate cyclase; mutations cause catalase T deficiency, defective glycogen synthesis and defective trehalose accumulation; IRA1 has a paralog, IRA2, that arose from the whole genome duplication; defects in human homolog NF1 are associated with neurofibromatosis" |
Protein length | 3092 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MNQSDPQDKK NFPMEYSLTK HLFFDRLLLV LPIESNLKTY ADVEADSVFN
SCRSIILNIA ITKDLNPIIE NTLGLIDLIV QDEEITSDNI TDDIAHSILV
LLRLLSDVFE YYWDQNNDFK KIRNDNYKPG FSSHRPNFHT SRPKHTRINP
ALATMLLCKI SKLKFNTRTL KVLQNMSHHL SGSATISKSS ILPDSQEFLQ
KRNYPAYTEK IDLTIDYIQR FISASNHVEF TKCVKTKVVA PLLISHTSTE
LGVVNHLDLF GCEYLTDKNL LAYLDILQHL SSYMKRTIFH SLLLYYASKA
FLFWIMARPK EYVKIYNNLI SSDYNSPSSS SDNGGSNNSD KTSISQLVSL
LFDDVYSTFS VSSLLTNVNN DHHYHLHHSS SSSKTTNTNS PNSISKTSIK
QSSVNASGNV SPSQFSTGND ASPTSPMASL SSPLNTNILG YPLSPITSTL
GQANTSTSTT AATTKTDADT PSTMNTNNNN NNNNSANLNN IPQRIFSLDD
ISSFNSSRKS LNLDDSNSLF LWDTSQHSNA SMTNTNMHAG VNNSQSQNDQ
SSLNYMENIM ELYSNYTGSE LSSHTAILRF LVVLTLLDSE VYDEMNSNSY
RKISEPIMNI NPKDSNTSSW GSASKNPSIR HLTHGLKKLT LQQGRKRNVK
FLTYLIRNLN GGQFVSDVSL IDSIRSILFL MTMTSSISQI DSNIASVIFS
KRFYNLLGQN LEVGTNWNSA TANTFISHCV ERNPLTHRRL QLEFFASGLQ
LDSDLFLRHL QLEKELNHID LPKISLYTEG FRVFFHLVST KKLHEDIAEK
TSSVLKRLFC IIADILLKAT PYFDDNVTKI IASILDGHIL DQFDAARTLS
NDDHVSFDAA TSVYTEPTEI IHNSSDASLV SSLSQSPLSI NSGSNITNTR
TWDIQSILPT LSNRSSASDL SLSNILTNPL EAQQNNNANL LAHRLSGVPT
TKRYASPNDS ERSRQSPYSS PPQLQQSDLP SPLSVLSSSA GFSSNHSITA
TPTILKNIKS PKPNKTKKIA DDKQLKQPSY SRVILSDNDE ARKIMMNIFS
IFKRMTNWFI RPDANTEFPK TFTDIIKPLF VSILDSNQRL QVTARAFIEI
PLSYIATFED IDNDLDPRVL NDHYLLCTYA VTLFASSLFD LKLENAKREM
LLDIIVKFQR VRSYLSNLAE KHNLVQAIIT TERLTLPLLV GAVGSGIFIS
LYCSRGNTPR LIKISCCEFL RSLRFYQKYV GALDQYSIYN IDFIDAMAQD
NFTASGSVAL QRRLRNNILT YIKGSDSILL DSMDVIYKKW FYFSCSKSVT
QEELVDFRSL AGILASMSGI LSDMQELEKS KSAPDNEGDS LSFESRNPAY
EVHKSLKLEL TKKMNFFISK QCQWLNNPNL LTRENSRDIL SIELHPLSFN
LLFNNLGLKI DELMSIDLSK SHEDSSFVLL EQIIIIIRTI LKRDDDEKIM
LLFSTDLLDA VDKLIEIVEK ISIKSSKYYK GIIQMSKMFR AFEHSEKNLG
ISNHFHLKNK WLKLVIGWFK LSINKDYDFE NLSRPLREMD LQKRDEDFLY
IDTSIESAKA LAYLTHNVPL EIPPSSSKED WNRSSTVSFG NHFTILLKGL
EKSADLNQFP VSLRHKISIL NENVIIALTN LSNANVNVSL KFTLPMGYSP
NKDIRIAFLR VFIDIVTNYP VNPEKHEMDK MLAIDDFLKY IIKNPILAFF
GSLACSPADV DLYAGGFLNA FDTRNASHIL VTELLKQEIK RAARSDDILR
RNSCATRALS LYTRSRGNKY LIKTLRPVLQ GIVDNKESFE IDKMKPGSEN
SEKMLDLFEK YMTRLIDAIT SSIDDFPIEL VDICKTIYNA ASVNFPEYAY
IAVGSFVFLR FIGPALVSPD SENIIIVTHA HDRKPFITLA KVIQSLANGR
ENIFKKDILV SKEEFLKTCS DKIFNFLSEL CKIPTNNFTV NVREDPTPIS
FDYSFLHKFF YLNEFTIRKE IINESKLPGE FSFLKNTVML NDKILGVLGQ
PSMEIKNEIP PFVVENREKY PSLYEFMSRY AFKKVDMKEE EEDNAPFVHE
AMTLDGIQII VVTFTNCEYN NFVMDSLVYK VLQIYARMWC SKHYVVIDCT
TFYGGKANFQ KLTTLFFSLI PEQASSNCMG CYYFNVNKSF MDQWASSYTV
ENPYLVTTIP RCFINSNTDQ SLIKSLGLSG RSLEVLKDVR VTLHDITLYD
KEKKKFCPVS LKIGNKYFQV LHEIPQLYKV TVSNRTFSIK FNNVYKISNL
ISVDVSNTTG VSSEFTLSLD NEEKLVFCSP KYLEIVKMFY YAQLKMEEDF
GTDFSNDISF STSSSAVNAS YCNVKEVGEI ISHLSLVILV GLFNEDDLVK
NISYNLLVAT QEAFNLDFGT RLHKSPETYV PDDTTTFLAL IFKAFSESST
ELTPYIWKYM LDGLENDVIP QEHIPTVVCS LSYWVPNLYE HVYLANDEEG
PEAISRIIYS LIRLTVKEPN FTTAYLQQIW FLLALDGRLT NVIVEEIVSH
ALDRDSENRD WMKAVSILTS FPTTEIACQV IEKLINMIKS FLPSLAVEAS
AHSWSELTIL SKISVSIFFE SPLLSQMYLP EILFAVSLLI DVGPSEIRVS
LYELLMNVCH SLTNNESLPE RNRKNLDIVC ATFARQKLNF ISGFSQEKGR
VLPNFAASSF SSKFGTLDLF TKNIMLLMEY GSISEGAQWE AKYKKYLMDA
IFGHRSFFSA RAMMILGIMS KSHTSLFLCK ELLVETMKVF AEPVVDDEQM
FIIIAHVFTY SKIVEGLDPS SELMKELFWL ATICVESPHP LLFEGGLLFM
VNCLKRLYTV HLQLGFDGKS LAKKLMESRN FAATLLAKLE SYNGCIWNED
NFPHIILGFI ANGLSIPVVK GAALDCLQAL FKNTYYERKS NPKSSDYLCY
LFLLHLVLSP EQLSTLLLEV GFEDELVPLN NTLKVPLTLI NWLSSDSDKS
NIVLYQGALL FSCVMSDEPC KFRFALLMRY LLKVNPICVF RFYTLTRKEF
RRLSTLEQSS EAVAVSFELI GMLVTHSEFN YLEEFNDEMV ELLKKRGLSV
VKPLDIFDQE HIEKLKGEGE HQVAIYERKR LATMILARMS CS
SCRSIILNIA ITKDLNPIIE NTLGLIDLIV QDEEITSDNI TDDIAHSILV
LLRLLSDVFE YYWDQNNDFK KIRNDNYKPG FSSHRPNFHT SRPKHTRINP
ALATMLLCKI SKLKFNTRTL KVLQNMSHHL SGSATISKSS ILPDSQEFLQ
KRNYPAYTEK IDLTIDYIQR FISASNHVEF TKCVKTKVVA PLLISHTSTE
LGVVNHLDLF GCEYLTDKNL LAYLDILQHL SSYMKRTIFH SLLLYYASKA
FLFWIMARPK EYVKIYNNLI SSDYNSPSSS SDNGGSNNSD KTSISQLVSL
LFDDVYSTFS VSSLLTNVNN DHHYHLHHSS SSSKTTNTNS PNSISKTSIK
QSSVNASGNV SPSQFSTGND ASPTSPMASL SSPLNTNILG YPLSPITSTL
GQANTSTSTT AATTKTDADT PSTMNTNNNN NNNNSANLNN IPQRIFSLDD
ISSFNSSRKS LNLDDSNSLF LWDTSQHSNA SMTNTNMHAG VNNSQSQNDQ
SSLNYMENIM ELYSNYTGSE LSSHTAILRF LVVLTLLDSE VYDEMNSNSY
RKISEPIMNI NPKDSNTSSW GSASKNPSIR HLTHGLKKLT LQQGRKRNVK
FLTYLIRNLN GGQFVSDVSL IDSIRSILFL MTMTSSISQI DSNIASVIFS
KRFYNLLGQN LEVGTNWNSA TANTFISHCV ERNPLTHRRL QLEFFASGLQ
LDSDLFLRHL QLEKELNHID LPKISLYTEG FRVFFHLVST KKLHEDIAEK
TSSVLKRLFC IIADILLKAT PYFDDNVTKI IASILDGHIL DQFDAARTLS
NDDHVSFDAA TSVYTEPTEI IHNSSDASLV SSLSQSPLSI NSGSNITNTR
TWDIQSILPT LSNRSSASDL SLSNILTNPL EAQQNNNANL LAHRLSGVPT
TKRYASPNDS ERSRQSPYSS PPQLQQSDLP SPLSVLSSSA GFSSNHSITA
TPTILKNIKS PKPNKTKKIA DDKQLKQPSY SRVILSDNDE ARKIMMNIFS
IFKRMTNWFI RPDANTEFPK TFTDIIKPLF VSILDSNQRL QVTARAFIEI
PLSYIATFED IDNDLDPRVL NDHYLLCTYA VTLFASSLFD LKLENAKREM
LLDIIVKFQR VRSYLSNLAE KHNLVQAIIT TERLTLPLLV GAVGSGIFIS
LYCSRGNTPR LIKISCCEFL RSLRFYQKYV GALDQYSIYN IDFIDAMAQD
NFTASGSVAL QRRLRNNILT YIKGSDSILL DSMDVIYKKW FYFSCSKSVT
QEELVDFRSL AGILASMSGI LSDMQELEKS KSAPDNEGDS LSFESRNPAY
EVHKSLKLEL TKKMNFFISK QCQWLNNPNL LTRENSRDIL SIELHPLSFN
LLFNNLGLKI DELMSIDLSK SHEDSSFVLL EQIIIIIRTI LKRDDDEKIM
LLFSTDLLDA VDKLIEIVEK ISIKSSKYYK GIIQMSKMFR AFEHSEKNLG
ISNHFHLKNK WLKLVIGWFK LSINKDYDFE NLSRPLREMD LQKRDEDFLY
IDTSIESAKA LAYLTHNVPL EIPPSSSKED WNRSSTVSFG NHFTILLKGL
EKSADLNQFP VSLRHKISIL NENVIIALTN LSNANVNVSL KFTLPMGYSP
NKDIRIAFLR VFIDIVTNYP VNPEKHEMDK MLAIDDFLKY IIKNPILAFF
GSLACSPADV DLYAGGFLNA FDTRNASHIL VTELLKQEIK RAARSDDILR
RNSCATRALS LYTRSRGNKY LIKTLRPVLQ GIVDNKESFE IDKMKPGSEN
SEKMLDLFEK YMTRLIDAIT SSIDDFPIEL VDICKTIYNA ASVNFPEYAY
IAVGSFVFLR FIGPALVSPD SENIIIVTHA HDRKPFITLA KVIQSLANGR
ENIFKKDILV SKEEFLKTCS DKIFNFLSEL CKIPTNNFTV NVREDPTPIS
FDYSFLHKFF YLNEFTIRKE IINESKLPGE FSFLKNTVML NDKILGVLGQ
PSMEIKNEIP PFVVENREKY PSLYEFMSRY AFKKVDMKEE EEDNAPFVHE
AMTLDGIQII VVTFTNCEYN NFVMDSLVYK VLQIYARMWC SKHYVVIDCT
TFYGGKANFQ KLTTLFFSLI PEQASSNCMG CYYFNVNKSF MDQWASSYTV
ENPYLVTTIP RCFINSNTDQ SLIKSLGLSG RSLEVLKDVR VTLHDITLYD
KEKKKFCPVS LKIGNKYFQV LHEIPQLYKV TVSNRTFSIK FNNVYKISNL
ISVDVSNTTG VSSEFTLSLD NEEKLVFCSP KYLEIVKMFY YAQLKMEEDF
GTDFSNDISF STSSSAVNAS YCNVKEVGEI ISHLSLVILV GLFNEDDLVK
NISYNLLVAT QEAFNLDFGT RLHKSPETYV PDDTTTFLAL IFKAFSESST
ELTPYIWKYM LDGLENDVIP QEHIPTVVCS LSYWVPNLYE HVYLANDEEG
PEAISRIIYS LIRLTVKEPN FTTAYLQQIW FLLALDGRLT NVIVEEIVSH
ALDRDSENRD WMKAVSILTS FPTTEIACQV IEKLINMIKS FLPSLAVEAS
AHSWSELTIL SKISVSIFFE SPLLSQMYLP EILFAVSLLI DVGPSEIRVS
LYELLMNVCH SLTNNESLPE RNRKNLDIVC ATFARQKLNF ISGFSQEKGR
VLPNFAASSF SSKFGTLDLF TKNIMLLMEY GSISEGAQWE AKYKKYLMDA
IFGHRSFFSA RAMMILGIMS KSHTSLFLCK ELLVETMKVF AEPVVDDEQM
FIIIAHVFTY SKIVEGLDPS SELMKELFWL ATICVESPHP LLFEGGLLFM
VNCLKRLYTV HLQLGFDGKS LAKKLMESRN FAATLLAKLE SYNGCIWNED
NFPHIILGFI ANGLSIPVVK GAALDCLQAL FKNTYYERKS NPKSSDYLCY
LFLLHLVLSP EQLSTLLLEV GFEDELVPLN NTLKVPLTLI NWLSSDSDKS
NIVLYQGALL FSCVMSDEPC KFRFALLMRY LLKVNPICVF RFYTLTRKEF
RRLSTLEQSS EAVAVSFELI GMLVTHSEFN YLEEFNDEMV ELLKKRGLSV
VKPLDIFDQE HIEKLKGEGE HQVAIYERKR LATMILARMS CS
Legend
- X Phoshorylation
- X K-benzoylation
Structure
No 3d structure was found in the AlphaFold Protein Structure Database.
References
[4, 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) |
[62, 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) |
[62, 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) |
[62, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[207, 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) |
[207, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[331, 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) |
[385, 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) |
[385, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[388, 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) |
[390, 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) |
[390, 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) |
[390, 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) |
[390, 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) |
[390, 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) |
[390, 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) |
[390, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[393, 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) |
[393, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[395, 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) |
[395, 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) |
[395, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[497, 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) |
[497, 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) |
[497, 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) |
[497, 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) |
[497, 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) |
[497, 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) |
[497, 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) |
[497, 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) |
[497, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[506, 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) |
[507, 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) |
[615, 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) |
[615, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[617, 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) |
[617, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[618, 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) |
[618, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[619, 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) |
[619, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[622, 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) |
[622, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[624, 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) |
[624, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[628, 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) |
[654, 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) |
[654, 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) |
[654, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[676, 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) |
[676, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[688, 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) |
[688, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[692, 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) |
[692, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[874, 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) |
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[950, 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) |
[950, 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) |
[951, 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) |
[956, 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) |
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[2179, 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) |
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[3076, 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) |
[3076, 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) |
[3076, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |