Basic Information
Name | Midasin (Dynein-related AAA-ATPase REA1) (MIDAS-containing protein) (Ribosome export/assembly protein 1) |
Uniprot ID | Q12019 |
Systematic gene name | YLR106C |
Standard gene name | REA1 |
Gene names | REA1 MDN1 YLR106C L2901 L8004.13 |
Description from SGD | YLR106C REA1 SGDID:S000004096, Chr XII from 363738-349006, Genome Release 64-3-1, reverse complement, Verified ORF, "Huge dynein-related AAA-type ATPase (midasin); forms extended pre-60S particle with the Rix1 complex; involved with interaction partners Rsa4p and Ytm1p, in the ATP-dependent remodeling of the pre-60S particle at successive maturation steps during ribosomal biogenesis; involved in the removal of biogenesis factors including GTPase Nog2p prior to nuclear export; contains a hexameric AAA-motor head domain and a long flexible tail with a MIDAS (metal ion-dependent adhesion site) domain" |
Protein length | 4910 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MSQDRILLDL DVVNQRLILF NSAFPSDAIE APFHFSNKES TSENLDNLAG
TILHSRSITG HVFLYKHIFL EIVARWIKDS KKKDYVLVIE KLASIITIFP
VAMPLIEDYL DKENDHFITI LQNPSTQKDS DMFKILLAYY RLLYHNKEVF
ARFIQPDILY QLVDLLTKEQ ENQVVIFLAL KVLSLYLDMG EKTLNDMLDT
YIKSRDSLLG HFEGDSGIDY SFLELNEAKR CANFSKLPSV PECFTIEKKS
SYFIIEPQDL STKVASICGV IVPKVHTIHD KVFYPLTFVP THKTVSSLRQ
LGRKIQNSTP IMLIGKAGSG KTFLINELSK YMGCHDSIVK IHLGEQTDAK
LLIGTYTSGD KPGTFEWRAG VLATAVKEGR WVLIEDIDKA PTDVLSILLS
LLEKRELTIP SRGETVKAAN GFQLISTVRI NEDHQKDSSN KIYNLNMIGM
RIWNVIELEE PSEEDLTHIL AQKFPILTNL IPKLIDSYKN VKSIYMNTKF
ISLNKGAHTR VVSVRDLIKL CERLDILFKN NGINKPDQLI QSSVYDSIFS
EAADCFAGAI GEFKALEPII QAIGESLDIA SSRISLFLTQ HVPTLENLDD
SIKIGRAVLL KEKLNIQKKS MNSTLFAFTN HSLRLMEQIS VCIQMTEPVL
LVGETGTGKT TVVQQLAKML AKKLTVINVS QQTETGDLLG GYKPVNSKTV
AVPIQENFET LFNATFSLKK NEKFHKMLHR CFNKNQWKNV VKLWNEAYKM
AQSILKITNT ENENENAKKK KRRLNTHEKK LLLDKWADFN DSVKKFEAQS
SSIENSFVFN FVEGSLVKTI RAGEWLLLDE VNLATADTLE SISDLLTEPD
SRSILLSEKG DAEPIKAHPD FRIFACMNPA TDVGKRDLPM GIRSRFTEIY
VHSPERDITD LLSIIDKYIG KYSVSDEWVG NDIAELYLEA KKLSDNNTIV
DGSNQKPHFS IRTLTRTLLY VTDIIHIYGL RRSLYDGFCM SFLTLLDQKS
EAILKPVIEK FTLGRLKNVK SIMSQTPPSP GPDYVQFKHY WMKKGPNTIQ
EQAHYIITPF VEKNMMNLVR ATSGKRFPVL IQGPTSSGKT SMIKYLADIT
GHKFVRINNH EHTDLQEYLG TYVTDDTGKL SFKEGVLVEA LRKGYWIVLD
ELNLAPTDVL EALNRLLDDN RELFIPETQE VVHPHPDFLL FATQNPPGIY
GGRKILSRAF RNRFLELHFD DIPQDELEII LRERCQIAPS YAKKIVEVYR
QLSIERSASR LFEQKNSFAT LRDLFRWALR DAVGYEQLAA SGYMLLAERC
RTPQEKVTVK KTLEKVMKVK LDMDQYYASL EDKSLEAIGS VTWTKGMRRL
SVLVSSCLKN KEPVLLVGET GCGKTTICQL LAQFMGRELI TLNAHQNTET
GDILGAQRPV RNRSEIQYKL IKSLKTALNI ANDQDVDLKE LLQLYSKSDN
KNIAEDVQLE IQKLRDSLNV LFEWSDGPLI QAMRTGNFFL LDEISLADDS
VLERLNSVLE PERSLLLAEQ GSSDSLVTAS ENFQFFATMN PGGDYGKKEL
SPALRNRFTE IWVPSMEDFN DVNMIVSSRL LEDLKDLANP IVKFSEWFGK
KLGGGNATSG VISLRDILAW VEFINKVFPK IQNKSTALIQ GASMVFIDAL
GTNNTAYLAE NENDLKSLRT ECIIQLLKLC GDDLELQQIE TNEIIVTQDE
LQVGMFKIPR FPDAQSSSFN LTAPTTASNL VRVVRAMQVH KPILLEGSPG
VGKTSLITAL ANITGNKLTR INLSEQTDLV DLFGADAPGE RSGEFLWHDA
PFLRAMKKGE WVLLDEMNLA SQSVLEGLNA CLDHRGEAYI PELDISFSCH
PNFLVFAAQN PQYQGGGRKG LPKSFVNRFS VVFIDMLTSD DLLLIAKHLY
PSIEPDIIAK MIKLMSTLED QVCKRKLWGN SGSPWEFNLR DTLRWLKLLN
QYSICEDVDV FDFVDIIVKQ RFRTISDKNK AQLLIEDIFG KFSTKENFFK
LTEDYVQINN EVALRNPHYR YPITQNLFPL ECNVAVYESV LKAINNNWPL
VLVGPSNSGK TETIRFLASI LGPRVDVFSM NSDIDSMDIL GGYEQVDLTR
QISYITEELT NIVREIISMN MKLSPNATAI MEGLNLLKYL LNNIVTPEKF
QDFRNRFNRF FSHLEGHPLL KTMSMNIEKM TEIITKEASV KFEWFDGMLV
KAVEKGHWLI LDNANLCSPS VLDRLNSLLE IDGSLLINEC SQEDGQPRVL
KPHPNFRLFL TMDPKYGELS RAMRNRGVEI YIDELHSRST AFDRLTLGFE
LGENIDFVSI DDGIKKIKLN EPDMSIPLKH YVPSYLSRPC IFAQVHDILL
LSDEEPIEES LAAVIPISHL GEVGKWANNV LNCTEYSEKK IAERLYVFIT
FLTDMGVLEK INNLYKPANL KFQKALGLHD KQLTEETVSL TLNEYVLPTV
SKYSDKIKSP ESLYLLSSLR LLLNSLNALK LINEKSTHGK IDELTYIELS
AAAFNGRHLK NIPRIPIFCI LYNILTVMSE NLKTESLFCG SNQYQYYWDL
LVIVIAALET AVTKDEARLR VYKELIDSWI ASVKSKSDIE ITPFLNINLE
FTDVLQLSRG HSITLLWDIF RKNYPTTSNS WLAFEKLINL SEKFDKVRLL
QFSESYNSIK DLMDVFRLLN DDVLNNKLSE FNLLLSKLED GINELELISN
KFLNKRKHYF ADEFDNLIRY TFSVDTAELI KELAPASSLA TQKLTKLITN
KYNYPPIFDV LWTEKNAKLT SFTSTIFSSQ FLEDVVRKSN NLKSFSGNQI
KQSISDAELL LSSTIKCSPN LLKSQMEYYK NMLLSWLRKV IDIHVGGDCL
KLTLKELCSL IEEKTASETR VTFAEYIFPA LDLAESSKSL EELGEAWITF
GTGLLLLFVP DSPYDPAIHD YVLYDLFLKT KTFSQNLMKS WRNVRKVISG
DEEIFTEKLI NTISDDDAPQ SPRVYRTGMS IDSLFDEWMA FLSSTMSSRQ
IKELVSSYKC NSDQSDRRLE MLQQNSAHFL NRLESGYSKF ADLNDILAGY
IYSINFGFDL LKLQKSKDRA SFQISPLWSM DPINISCAEN VLSAYHELSR
FFKKGDMEDT SIEKVLMYFL TLFKFHKRDT NLLEIFEAAL YTLYSRWSVR
RFRQEQEENE KSNMFKFNDN SDDYEADFRK LFPDYEDTAL VTNEKDISSP
ENLDDIYFKL ADTYISVFDK DHDANFSSEL KSGAIITTIL SEDLKNTRIE
ELKSGSLSAV INTLDAETQS FKNTEVFGNI DFYHDFSIPE FQKAGDIIET
VLKSVLKLLK QWPEHATLKE LYRVSQEFLN YPIKTPLARQ LQKIEQIYTY
LAEWEKYASS EVSLNNTVKL ITDLIVSWRK LELRTWKGLF NSEDAKTRKS
IGKWWFYLYE SIVISNFVSE KKETAPNATL LVSSLNLFFS KSTLGEFNAR
LDLVKAFYKH IQLIGLRSSK IAGLLHNTIK FYYQFKPLID ERITNGKKSL
EKEIDDIILL ASWKDVNVDA LKQSSRKSHN NLYKIVRKYR DLLNGDAKTI
IEAGLLYSNE NKLKLPTLKQ HFYEDPNLEA SKNLVKEIST WSMRAAPLRN
IDTVASNMDS YLEKISSQEF PNFADLASDF YAEAERLRKE TPNVYTKENK
KRLAYLKTQK SKLLGDALKE LRRIGLKVNF REDIQKVQSS TTTILANIAP
FNNEYLNSSD AFFFKILDLL PKLRSAASNP SDDIPVAAIE RGMALAQSLM
FSLITVRHPL SEFTNDYCKI NGMMLDLEHF TCLKGDIVHS SLKANVDNVR
LFEKWLPSLL DYAAQTLSVI SKYSATSEQQ KILLDAKSTL SSFFVHFNSS
RIFDSSFIES YSRFELFINE LLKKLENAKE TGNAFVFDII IEWIKANKGG
PIKKEQKRGP SVEDVEQAFR RTFTSIILSF QKVIGDGIES ISETDDNWLS
ASFKKVMVNV KLLRSSVVSK NIETALSLLK DFDFTTTESI YVKSVISFTL
PVITRYYNAM TVVLERSRIY YTNTSRGMYI LSTILHSLAK NGFCSPQPPS
EEVDDKNLQE GTGLGDGEGA QNNNKDVEQD EDLTEDAQNE NKEQQDKDER
DDENEDDAVE MEGDMAGELE DLSNGEENDD EDTDSEEEEL DEEIDDLNED
DPNAIDDKMW DDKASDNSKE KDTDQNLDGK NQEEDVQAAE NDEQQRDNKE
GGDEDPNAPE DGDEEIENDE NAEEENDVGE QEDEVKDEEG EDLEANVPEI
ETLDLPEDMN LDSEHEESDE DVDMSDGMPD DLNKEEVGNE DEEVKQESGI
ESDNENDEPG PEEDAGETET ALDEEEGAEE DVDMTNDEGK EDEENGPEEQ
AMSDEEELKQ DAAMEENKEK GGEQNTEGLD GVEEKADTED IDQEAAVQQD
SGSKGAGADA TDTQEQDDVG GSGTTQNTYE EDQEDVTKNN EESREEATAA
LKQLGDSMKE YHRRRQDIKE AQTNGEEDEN LEKNNERPDE FEHVEGANTE
TDTQALGSAT QDQLQTIDED MAIDDDREEQ EVDQKELVED ADDEKMDIDE
EEMLSDIDAH DANNDVDSKK SGFIGKRKSE EDFENELSNE HFSADQEDDS
EIQSLIENIE DNPPDASASL TPERSLEESR ELWHKSEIST ADLVSRLGEQ
LRLILEPTLA TKLKGDYKTG KRLNMKRIIP YIASQFRKDK IWLRRTKPSK
RQYQIMIALD DSKSMSESKC VKLAFDSLCL VSKTLTQLEA GGLSIVKFGE
NIKEVHSFDQ QFSNESGARA FQWFGFQETK TDVKKLVAES TKIFERARAM
VHNDQWQLEI VISDGICEDH ETIQKLVRRA RENKIMLVFV IIDGITSNES
ILDMSQVNYI PDQYGNPQLK ITKYLDTFPF EFYVVVHDIS ELPEMLSLIL
RQYFTDLASS
TILHSRSITG HVFLYKHIFL EIVARWIKDS KKKDYVLVIE KLASIITIFP
VAMPLIEDYL DKENDHFITI LQNPSTQKDS DMFKILLAYY RLLYHNKEVF
ARFIQPDILY QLVDLLTKEQ ENQVVIFLAL KVLSLYLDMG EKTLNDMLDT
YIKSRDSLLG HFEGDSGIDY SFLELNEAKR CANFSKLPSV PECFTIEKKS
SYFIIEPQDL STKVASICGV IVPKVHTIHD KVFYPLTFVP THKTVSSLRQ
LGRKIQNSTP IMLIGKAGSG KTFLINELSK YMGCHDSIVK IHLGEQTDAK
LLIGTYTSGD KPGTFEWRAG VLATAVKEGR WVLIEDIDKA PTDVLSILLS
LLEKRELTIP SRGETVKAAN GFQLISTVRI NEDHQKDSSN KIYNLNMIGM
RIWNVIELEE PSEEDLTHIL AQKFPILTNL IPKLIDSYKN VKSIYMNTKF
ISLNKGAHTR VVSVRDLIKL CERLDILFKN NGINKPDQLI QSSVYDSIFS
EAADCFAGAI GEFKALEPII QAIGESLDIA SSRISLFLTQ HVPTLENLDD
SIKIGRAVLL KEKLNIQKKS MNSTLFAFTN HSLRLMEQIS VCIQMTEPVL
LVGETGTGKT TVVQQLAKML AKKLTVINVS QQTETGDLLG GYKPVNSKTV
AVPIQENFET LFNATFSLKK NEKFHKMLHR CFNKNQWKNV VKLWNEAYKM
AQSILKITNT ENENENAKKK KRRLNTHEKK LLLDKWADFN DSVKKFEAQS
SSIENSFVFN FVEGSLVKTI RAGEWLLLDE VNLATADTLE SISDLLTEPD
SRSILLSEKG DAEPIKAHPD FRIFACMNPA TDVGKRDLPM GIRSRFTEIY
VHSPERDITD LLSIIDKYIG KYSVSDEWVG NDIAELYLEA KKLSDNNTIV
DGSNQKPHFS IRTLTRTLLY VTDIIHIYGL RRSLYDGFCM SFLTLLDQKS
EAILKPVIEK FTLGRLKNVK SIMSQTPPSP GPDYVQFKHY WMKKGPNTIQ
EQAHYIITPF VEKNMMNLVR ATSGKRFPVL IQGPTSSGKT SMIKYLADIT
GHKFVRINNH EHTDLQEYLG TYVTDDTGKL SFKEGVLVEA LRKGYWIVLD
ELNLAPTDVL EALNRLLDDN RELFIPETQE VVHPHPDFLL FATQNPPGIY
GGRKILSRAF RNRFLELHFD DIPQDELEII LRERCQIAPS YAKKIVEVYR
QLSIERSASR LFEQKNSFAT LRDLFRWALR DAVGYEQLAA SGYMLLAERC
RTPQEKVTVK KTLEKVMKVK LDMDQYYASL EDKSLEAIGS VTWTKGMRRL
SVLVSSCLKN KEPVLLVGET GCGKTTICQL LAQFMGRELI TLNAHQNTET
GDILGAQRPV RNRSEIQYKL IKSLKTALNI ANDQDVDLKE LLQLYSKSDN
KNIAEDVQLE IQKLRDSLNV LFEWSDGPLI QAMRTGNFFL LDEISLADDS
VLERLNSVLE PERSLLLAEQ GSSDSLVTAS ENFQFFATMN PGGDYGKKEL
SPALRNRFTE IWVPSMEDFN DVNMIVSSRL LEDLKDLANP IVKFSEWFGK
KLGGGNATSG VISLRDILAW VEFINKVFPK IQNKSTALIQ GASMVFIDAL
GTNNTAYLAE NENDLKSLRT ECIIQLLKLC GDDLELQQIE TNEIIVTQDE
LQVGMFKIPR FPDAQSSSFN LTAPTTASNL VRVVRAMQVH KPILLEGSPG
VGKTSLITAL ANITGNKLTR INLSEQTDLV DLFGADAPGE RSGEFLWHDA
PFLRAMKKGE WVLLDEMNLA SQSVLEGLNA CLDHRGEAYI PELDISFSCH
PNFLVFAAQN PQYQGGGRKG LPKSFVNRFS VVFIDMLTSD DLLLIAKHLY
PSIEPDIIAK MIKLMSTLED QVCKRKLWGN SGSPWEFNLR DTLRWLKLLN
QYSICEDVDV FDFVDIIVKQ RFRTISDKNK AQLLIEDIFG KFSTKENFFK
LTEDYVQINN EVALRNPHYR YPITQNLFPL ECNVAVYESV LKAINNNWPL
VLVGPSNSGK TETIRFLASI LGPRVDVFSM NSDIDSMDIL GGYEQVDLTR
QISYITEELT NIVREIISMN MKLSPNATAI MEGLNLLKYL LNNIVTPEKF
QDFRNRFNRF FSHLEGHPLL KTMSMNIEKM TEIITKEASV KFEWFDGMLV
KAVEKGHWLI LDNANLCSPS VLDRLNSLLE IDGSLLINEC SQEDGQPRVL
KPHPNFRLFL TMDPKYGELS RAMRNRGVEI YIDELHSRST AFDRLTLGFE
LGENIDFVSI DDGIKKIKLN EPDMSIPLKH YVPSYLSRPC IFAQVHDILL
LSDEEPIEES LAAVIPISHL GEVGKWANNV LNCTEYSEKK IAERLYVFIT
FLTDMGVLEK INNLYKPANL KFQKALGLHD KQLTEETVSL TLNEYVLPTV
SKYSDKIKSP ESLYLLSSLR LLLNSLNALK LINEKSTHGK IDELTYIELS
AAAFNGRHLK NIPRIPIFCI LYNILTVMSE NLKTESLFCG SNQYQYYWDL
LVIVIAALET AVTKDEARLR VYKELIDSWI ASVKSKSDIE ITPFLNINLE
FTDVLQLSRG HSITLLWDIF RKNYPTTSNS WLAFEKLINL SEKFDKVRLL
QFSESYNSIK DLMDVFRLLN DDVLNNKLSE FNLLLSKLED GINELELISN
KFLNKRKHYF ADEFDNLIRY TFSVDTAELI KELAPASSLA TQKLTKLITN
KYNYPPIFDV LWTEKNAKLT SFTSTIFSSQ FLEDVVRKSN NLKSFSGNQI
KQSISDAELL LSSTIKCSPN LLKSQMEYYK NMLLSWLRKV IDIHVGGDCL
KLTLKELCSL IEEKTASETR VTFAEYIFPA LDLAESSKSL EELGEAWITF
GTGLLLLFVP DSPYDPAIHD YVLYDLFLKT KTFSQNLMKS WRNVRKVISG
DEEIFTEKLI NTISDDDAPQ SPRVYRTGMS IDSLFDEWMA FLSSTMSSRQ
IKELVSSYKC NSDQSDRRLE MLQQNSAHFL NRLESGYSKF ADLNDILAGY
IYSINFGFDL LKLQKSKDRA SFQISPLWSM DPINISCAEN VLSAYHELSR
FFKKGDMEDT SIEKVLMYFL TLFKFHKRDT NLLEIFEAAL YTLYSRWSVR
RFRQEQEENE KSNMFKFNDN SDDYEADFRK LFPDYEDTAL VTNEKDISSP
ENLDDIYFKL ADTYISVFDK DHDANFSSEL KSGAIITTIL SEDLKNTRIE
ELKSGSLSAV INTLDAETQS FKNTEVFGNI DFYHDFSIPE FQKAGDIIET
VLKSVLKLLK QWPEHATLKE LYRVSQEFLN YPIKTPLARQ LQKIEQIYTY
LAEWEKYASS EVSLNNTVKL ITDLIVSWRK LELRTWKGLF NSEDAKTRKS
IGKWWFYLYE SIVISNFVSE KKETAPNATL LVSSLNLFFS KSTLGEFNAR
LDLVKAFYKH IQLIGLRSSK IAGLLHNTIK FYYQFKPLID ERITNGKKSL
EKEIDDIILL ASWKDVNVDA LKQSSRKSHN NLYKIVRKYR DLLNGDAKTI
IEAGLLYSNE NKLKLPTLKQ HFYEDPNLEA SKNLVKEIST WSMRAAPLRN
IDTVASNMDS YLEKISSQEF PNFADLASDF YAEAERLRKE TPNVYTKENK
KRLAYLKTQK SKLLGDALKE LRRIGLKVNF REDIQKVQSS TTTILANIAP
FNNEYLNSSD AFFFKILDLL PKLRSAASNP SDDIPVAAIE RGMALAQSLM
FSLITVRHPL SEFTNDYCKI NGMMLDLEHF TCLKGDIVHS SLKANVDNVR
LFEKWLPSLL DYAAQTLSVI SKYSATSEQQ KILLDAKSTL SSFFVHFNSS
RIFDSSFIES YSRFELFINE LLKKLENAKE TGNAFVFDII IEWIKANKGG
PIKKEQKRGP SVEDVEQAFR RTFTSIILSF QKVIGDGIES ISETDDNWLS
ASFKKVMVNV KLLRSSVVSK NIETALSLLK DFDFTTTESI YVKSVISFTL
PVITRYYNAM TVVLERSRIY YTNTSRGMYI LSTILHSLAK NGFCSPQPPS
EEVDDKNLQE GTGLGDGEGA QNNNKDVEQD EDLTEDAQNE NKEQQDKDER
DDENEDDAVE MEGDMAGELE DLSNGEENDD EDTDSEEEEL DEEIDDLNED
DPNAIDDKMW DDKASDNSKE KDTDQNLDGK NQEEDVQAAE NDEQQRDNKE
GGDEDPNAPE DGDEEIENDE NAEEENDVGE QEDEVKDEEG EDLEANVPEI
ETLDLPEDMN LDSEHEESDE DVDMSDGMPD DLNKEEVGNE DEEVKQESGI
ESDNENDEPG PEEDAGETET ALDEEEGAEE DVDMTNDEGK EDEENGPEEQ
AMSDEEELKQ DAAMEENKEK GGEQNTEGLD GVEEKADTED IDQEAAVQQD
SGSKGAGADA TDTQEQDDVG GSGTTQNTYE EDQEDVTKNN EESREEATAA
LKQLGDSMKE YHRRRQDIKE AQTNGEEDEN LEKNNERPDE FEHVEGANTE
TDTQALGSAT QDQLQTIDED MAIDDDREEQ EVDQKELVED ADDEKMDIDE
EEMLSDIDAH DANNDVDSKK SGFIGKRKSE EDFENELSNE HFSADQEDDS
EIQSLIENIE DNPPDASASL TPERSLEESR ELWHKSEIST ADLVSRLGEQ
LRLILEPTLA TKLKGDYKTG KRLNMKRIIP YIASQFRKDK IWLRRTKPSK
RQYQIMIALD DSKSMSESKC VKLAFDSLCL VSKTLTQLEA GGLSIVKFGE
NIKEVHSFDQ QFSNESGARA FQWFGFQETK TDVKKLVAES TKIFERARAM
VHNDQWQLEI VISDGICEDH ETIQKLVRRA RENKIMLVFV IIDGITSNES
ILDMSQVNYI PDQYGNPQLK ITKYLDTFPF EFYVVVHDIS ELPEMLSLIL
RQYFTDLASS
Legend
- X Phoshorylation
- X Ubiquitination
- X K-benzoylation
Structure
No 3d structure was found in the AlphaFold Protein Structure Database.
References
[478, 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) |
[478, 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) |
[478, 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) |
[478, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[623, 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) |
[623, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[851, 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) |
[1026, 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) |
[1026, 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) |
[1026, 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) |
[1026, 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) |
[1026, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1029, 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) |
[1551, 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) |
[1754, 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) |
[1754, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1924, 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) |
[1978, 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) |
[1995, 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) |
[2325, 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) |
[2325, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[2931, 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) |
[2962, 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) |
[2962, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[2964, 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) |
[2964, Phos] | Guo X, Niemi NM, Hutchins PD, et al (2017b) Ptc7p dephosphorylates select mitochondrial proteins to enhance metabolic function. Cell Reports 18:307–313. (Publication) (All modifications) |
[2964, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[2971, 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) |
[2971, 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) |
[2971, Phos] | Guo X, Niemi NM, Coon JJ, Pagliarini DJ (2017a) Integrative proteomics and biochemical analyses define Ptc6p as the Saccharomyces cerevisiae pyruvate dehydrogenase phosphatase. J Biol Chem 292:11751–11759. (Publication) (All modifications) |
[2971, Phos] | Guo X, Niemi NM, Hutchins PD, et al (2017b) Ptc7p dephosphorylates select mitochondrial proteins to enhance metabolic function. Cell Reports 18:307–313. (Publication) (All modifications) |
[2971, 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) |
[2971, 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) |
[2971, 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) |
[2971, 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) |
[2971, 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) |
[2971, 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) |
[2971, 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) |
[2971, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[3171, 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) |
[3171, 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) |
[3171, 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) |
[3171, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[3357, 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) |
[3357, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[3363, 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) |
[3363, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[3645, 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) |
[4084, 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) |
[4084, 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) |
[4084, 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) |
[4084, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[4165, 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) |
[4165, 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) |
[4353, 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) |
[4353, 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) |
[4353, 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) |
[4353, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[4376, 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) |
[4388, 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) |
[4388, 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) |
[4388, Phos] | Guo X, Niemi NM, Hutchins PD, et al (2017b) Ptc7p dephosphorylates select mitochondrial proteins to enhance metabolic function. Cell Reports 18:307–313. (Publication) (All modifications) |
[4388, 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) |
[4388, 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) |
[4388, 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) |
[4388, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[4401, 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) |
[4401, 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) |
[4401, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[4403, 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) |
[4403, 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) |
[4403, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[4411, 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) |
[4411, 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) |
[4413, 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) |
[4413, 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) |
[4413, 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) |
[4413, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[4422, 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) |
[4425, 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) |
[4425, 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) |
[4428, 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) |
[4443, 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) |
[4443, 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) |
[4443, 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) |
[4443, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[4457, 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) |
[4473, 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) |
[4499, 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) |
[4555, 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) |
[4555, 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) |
[4555, Phos] | Guo X, Niemi NM, Coon JJ, Pagliarini DJ (2017a) Integrative proteomics and biochemical analyses define Ptc6p as the Saccharomyces cerevisiae pyruvate dehydrogenase phosphatase. J Biol Chem 292:11751–11759. (Publication) (All modifications) |
[4555, 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) |
[4555, 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) |
[4555, 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) |
[4555, Phos] | Pultz, D., Bennetzen, M.V., Rødkær, S.V., Zimmermann, C., Enserink, J.M., Andersen, J.S., Færgeman, N.J. (2012). Global mapping of protein phosphorylation events identifies Ste20, Sch9 and the cell-cycle regulatory kinases Cdc28/Pho85 as mediators of fatty acid starvation responses in Saccharomyces cerevisiae. Mol Biosyst 8: 796-803. (Publication) (All modifications) |
[4555, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[4568, 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) |
[4568, 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) |
[4568, 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) |
[4568, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[4571, 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) |
[4571, 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) |
[4571, Phos] | Guo X, Niemi NM, Coon JJ, Pagliarini DJ (2017a) Integrative proteomics and biochemical analyses define Ptc6p as the Saccharomyces cerevisiae pyruvate dehydrogenase phosphatase. J Biol Chem 292:11751–11759. (Publication) (All modifications) |
[4571, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[4579, 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) |
[4588, 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) |
[4600, 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) |
[4625, 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) |
[4636, 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) |
[4636, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[4639, 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) |
[4639, 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) |
[4639, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[4640, 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) |
[4640, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[4645, 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) |
[4661, Phos] | Guo X, Niemi NM, Coon JJ, Pagliarini DJ (2017a) Integrative proteomics and biochemical analyses define Ptc6p as the Saccharomyces cerevisiae pyruvate dehydrogenase phosphatase. J Biol Chem 292:11751–11759. (Publication) (All modifications) |
[4661, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |