Basic Information
Name | DOCK-like protein 1 |
Uniprot ID | Q06409 |
Systematic gene name | YLR422W |
Standard gene name | DCK1 |
Gene names | DCK1 YLR422W |
Description from SGD | YLR422W DCK1 SGDID:S000004414, Chr XII from 965897-971695, Genome Release 64-3-1, Verified ORF, "Dock family protein (Dedicator Of CytoKinesis), homolog of human DOCK1; upstream component for regulation through the small GTPase Rho5p; may form a complex with Lmo1p that acts as a GEF for Rho5p; interacts with Ino4p; cytoplasmic protein that relocates to mitochondria under oxidative stress; implicated in mitophagy; not an essential protein; DOCK proteins act as guanine nucleotide exchange factors" |
Protein length | 1932 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MSQQDSQRWL PTDRLIYGVL VKSFLPLQRY PELVYENSNY ANVYVGAEVY
VFEESVDKKW CRAYQCLRPF PEEFISNMNS ANDVLPDVKP KVVIFPRKYV
HFEAEKAVST MPFFKAPSAE DFKPLISKEC ESRSFCDSLY VSSTDDISTG
KPRKTPRPPF PFFRYQKRSF KDEMGPILSL ISSHVYSMYS IGEFSIYRKM
IKLYYDLDTI RFRLSMNLTT EAEKINLIRA ATSLRTKIAK FLSSTYRKNK
LIANSTPRNP DPYGFEGIFA RDIDTGELLS YEIDKLRTLV SSSMLCGLTN
NFPTVPVVES DDESSSNGLF GTVRSSILVN LKDLAWDPSI SDPKYQDLSI
CVYLRTKDEV LTESFTMTKS SNMESALDEI PAMLFKNILE TIVHKNKVYL
VVVLKETIAI TTETAPEISS YNISTEESSS HSPFSPFNSS TENKIDHVKK
GLAAGVINIS PVFKFYNGLS VANKAQRFNL YLYSSDSSDS QNFNSSKDAD
LGWGGLINKI IKDSSEGVSV NPRAVSLSVT VKEIIGKQEA EKVLSTSLVP
IRSIPTYFYD TMFSQAERIY LNLGRVSLYG LPAADTNIEN VTVQISCRNK
AVKFCKNKLE ERSGDWKFVS VRPNESIGES IRIEGVENMN EDETLRVLVY
LNGFLMAKSN IHIKKKNEII EYRKGTVFQI MSSKSVPLIH LELEASYFGR
RYNINPAITN FLVLQTKNVE FDQQLKEHYS VTLKQLNNVS FKDLLKHFDT
ILAHYLLLLE SVNEATDKKG PSSSLPNIVF SEFVKFLNLM LTHQENSRYW
FNRLYKKVMS KELECPNVAP ILIKHMTTIF DRSHSSWTRT GTAICRTILY
IIVLAIGSSH SDEMPNFSHF FRSLHKFLML ADEPIMADQI LLIESIPSML
ETMTNHCKVE DLVRFAIGLF ECCQEKEMNQ KMYSRPLSVR EEEYLNTKFN
CLLKLINKKV LQNYLTNTES VDKLRLQFLS KTLEWLLTPY TPGDDKCFHV
ESLRLVNSVF ITIIEDYKFD MLQRNLIRLL PYLCKSFVHL RRYCKKARLM
RPRRVFTMLF PREIPCNYIP VDSIVNDEVV VEVLLELAII ICEITKIASS
RFPSYQSFSE IINLCDKDTL FQSNFYSRQI TNENVYTITK TVFLFFKQDW
FPGMKWLGVS ALLGRSSLIL LSLCKDYIIE NNSPSPSKES EKRVDMRLWA
EYVKVILLVS NHKSASLTKL AITPRKAVYL ISGDLKKISA YILNECWDAL
ATGHYNITYA KKYGLGALSD CQFELFVHNQ FLIREIFIFA FHRHIDATRI
CCKILWGLGL NFWRIFGSLQ PAVNACIPEL FSAYQIGKLR LNDYELERFV
SCLFFMMHVP DSDTFFPACM DFLRDLLGFL HIVNEIYKIP NQEEFDDDRT
ARHIEMFEYL LEANRPELFH KMIYDLFIHF IQKKDFVQAA LSLELLAGTY
AWDSNDTLEA ISFPPLPEQS SFERKEYLLK ESARNFSRGQ KPEKALAVYK
DLIKAYDEIN YDLNGLAFVH DQIAGIYTRL QSIDRLVPTY FKVSFMGFGF
PKSLRNKSFV FEGLPFEHIT SMHDRLLRSY HGSNIVHSQE EVDMLLMNPP
MGKYIHVASV EPCLSISDNY NSSDKKSSIN NKVRMYIENR DLRTFSNSRR
LPGAKGVTDL WVEEYTYHTM NTFPTLMNRS EIVKVTKSKL SPLENAIRSL
QVKIQELYGL ENMCNKTLKD HGDVNDLFTE LSTNITGTIS APVNGGISQY
KAFLEPSTSK QFSTDDLGRL TLAFDELVAV LGRCLTLHAE LLPSKDLKPS
HDLLVRLFEE NFAEEIERYS RTLSEANRSR NNMITARIIS HKNPNKKASF
SGRDHHTSGS NHSQFVLEHS DSFGPNSLLF GKYLTRTLSH SSTTSSLDKS
GIVSGTSSTF LAGSQPNTNT DSQHKHDYSH SG
VFEESVDKKW CRAYQCLRPF PEEFISNMNS ANDVLPDVKP KVVIFPRKYV
HFEAEKAVST MPFFKAPSAE DFKPLISKEC ESRSFCDSLY VSSTDDISTG
KPRKTPRPPF PFFRYQKRSF KDEMGPILSL ISSHVYSMYS IGEFSIYRKM
IKLYYDLDTI RFRLSMNLTT EAEKINLIRA ATSLRTKIAK FLSSTYRKNK
LIANSTPRNP DPYGFEGIFA RDIDTGELLS YEIDKLRTLV SSSMLCGLTN
NFPTVPVVES DDESSSNGLF GTVRSSILVN LKDLAWDPSI SDPKYQDLSI
CVYLRTKDEV LTESFTMTKS SNMESALDEI PAMLFKNILE TIVHKNKVYL
VVVLKETIAI TTETAPEISS YNISTEESSS HSPFSPFNSS TENKIDHVKK
GLAAGVINIS PVFKFYNGLS VANKAQRFNL YLYSSDSSDS QNFNSSKDAD
LGWGGLINKI IKDSSEGVSV NPRAVSLSVT VKEIIGKQEA EKVLSTSLVP
IRSIPTYFYD TMFSQAERIY LNLGRVSLYG LPAADTNIEN VTVQISCRNK
AVKFCKNKLE ERSGDWKFVS VRPNESIGES IRIEGVENMN EDETLRVLVY
LNGFLMAKSN IHIKKKNEII EYRKGTVFQI MSSKSVPLIH LELEASYFGR
RYNINPAITN FLVLQTKNVE FDQQLKEHYS VTLKQLNNVS FKDLLKHFDT
ILAHYLLLLE SVNEATDKKG PSSSLPNIVF SEFVKFLNLM LTHQENSRYW
FNRLYKKVMS KELECPNVAP ILIKHMTTIF DRSHSSWTRT GTAICRTILY
IIVLAIGSSH SDEMPNFSHF FRSLHKFLML ADEPIMADQI LLIESIPSML
ETMTNHCKVE DLVRFAIGLF ECCQEKEMNQ KMYSRPLSVR EEEYLNTKFN
CLLKLINKKV LQNYLTNTES VDKLRLQFLS KTLEWLLTPY TPGDDKCFHV
ESLRLVNSVF ITIIEDYKFD MLQRNLIRLL PYLCKSFVHL RRYCKKARLM
RPRRVFTMLF PREIPCNYIP VDSIVNDEVV VEVLLELAII ICEITKIASS
RFPSYQSFSE IINLCDKDTL FQSNFYSRQI TNENVYTITK TVFLFFKQDW
FPGMKWLGVS ALLGRSSLIL LSLCKDYIIE NNSPSPSKES EKRVDMRLWA
EYVKVILLVS NHKSASLTKL AITPRKAVYL ISGDLKKISA YILNECWDAL
ATGHYNITYA KKYGLGALSD CQFELFVHNQ FLIREIFIFA FHRHIDATRI
CCKILWGLGL NFWRIFGSLQ PAVNACIPEL FSAYQIGKLR LNDYELERFV
SCLFFMMHVP DSDTFFPACM DFLRDLLGFL HIVNEIYKIP NQEEFDDDRT
ARHIEMFEYL LEANRPELFH KMIYDLFIHF IQKKDFVQAA LSLELLAGTY
AWDSNDTLEA ISFPPLPEQS SFERKEYLLK ESARNFSRGQ KPEKALAVYK
DLIKAYDEIN YDLNGLAFVH DQIAGIYTRL QSIDRLVPTY FKVSFMGFGF
PKSLRNKSFV FEGLPFEHIT SMHDRLLRSY HGSNIVHSQE EVDMLLMNPP
MGKYIHVASV EPCLSISDNY NSSDKKSSIN NKVRMYIENR DLRTFSNSRR
LPGAKGVTDL WVEEYTYHTM NTFPTLMNRS EIVKVTKSKL SPLENAIRSL
QVKIQELYGL ENMCNKTLKD HGDVNDLFTE LSTNITGTIS APVNGGISQY
KAFLEPSTSK QFSTDDLGRL TLAFDELVAV LGRCLTLHAE LLPSKDLKPS
HDLLVRLFEE NFAEEIERYS RTLSEANRSR NNMITARIIS HKNPNKKASF
SGRDHHTSGS NHSQFVLEHS DSFGPNSLLF GKYLTRTLSH SSTTSSLDKS
GIVSGTSSTF LAGSQPNTNT DSQHKHDYSH SG
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) |
[118, 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) |
[118, 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) |
[118, 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) |
[118, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[143, 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) |
[366, 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) |
[366, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[368, 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) |
[368, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[432, 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) |
[512, 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) |
[1824, 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) |
[1849, 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) |
[1849, 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) |
[1849, 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) |
[1849, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1851, 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) |
[1851, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1887, 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) |
[1887, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1889, 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) |
[1889, 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) |
[1889, 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) |
[1889, 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) |
[1889, 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) |
[1889, 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) |
[1889, 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) |
[1889, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1891, 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) |
[1891, 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) |
[1891, 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) |
[1891, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1892, 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) |
[1892, 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) |
[1892, 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) |
[1892, 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) |
[1892, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1893, 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) |
[1893, 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) |
[1893, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1894, 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) |
[1894, 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) |
[1894, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1895, 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) |
[1895, 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) |
[1895, 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) |
[1895, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1896, 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) |
[1896, 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) |
[1896, 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) |
[1896, 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) |
[1896, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1900, 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) |
[1904, 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) |
[1904, 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) |
[1904, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1906, 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) |
[1906, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1907, 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) |
[1907, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1908, 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) |
[1908, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1909, 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) |
[1909, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1931, 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) |