MKT1_YEAST - dbPTM
MKT1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MKT1_YEAST
UniProt AC P40850
Protein Name Protein MKT1
Gene Name MKT1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 830
Subcellular Localization
Protein Description Required for propagation of M2 dsRNA satellite at temperature above 30 degrees Celsius if an L-A RNA virus carrying NEX (N) is present in the cells..
Protein Sequence MAIKSLESFLFERGLVGSYAIEALNNCTLDIDVNHYVSRLLTNKREQYLDAIGGFPTSLKMYLESDLKIFKDFNITPIFVFNGGLTYNQLEASGHFTAASASASISSTTTSSSGTNATTRSNTESVLLQRSRGWTQWNNLISSNQNSYIDQPIQPQEPFRHNTTIDSKAYQNDLIAYFIEHGYMYQVAPYSSWFQLAYLLNSAYIDAIYGPTDCLMLDCVDRFILGMEFPNKEFRFIDRSRVMKDLGCTHEEFIDIAMAVGNDLQPTTLPPLQIYPVPQLFDIALEMVLNTGTNFYAYQLSTTLQNDSKENIQNYQRGISALRYMPVLKDTGKVELFVQEIVVSEEDSEKNNKDGKKSNLSSPSSASSSASPATTVTKNASEKLTYEKSSTKEVRKPRDIPNDVHDFIGQMLPHEYYFYRSIGLVTGKLFDAIVTGVYPEEPPLGGGSSTSYKKLVSKSVEIFKNKEINLLTQPINRYYQIKQIKQVKWYAANEPTTLTNRMSPSMFETINHLIVKTETSDEKEFSISEFITTINGSSNMAKDFISEKVIFPNSVPIESKLNSPFNLLSTNFLRLLVLLEFFTFDFKEKLLEPTRWGEVFLKLNELNIDSKYHESVIIFLVFLKCDVLKLDEEVQPPAPSALSQATLRSYPEESLYVLLITRVLTLFQVDQKPSNYHGPIDKKTLIFRDHLSFIKENLNELFEAVLISSLTSGEFNRLSLDNFGWARKIVRYLPFKLDSPNTIMAMMWEFFLQKYLHNGNAKNDALSLVATEFNTYKSTPNLDEQFVESHRFLLEISKVMQELNAAKLIDENVFKLFTKAVEFTTTALSS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
4Ubiquitination----MAIKSLESFLF
----CCCCCHHHHHH		39.1823793018
5Phosphorylation---MAIKSLESFLFE
---CCCCCHHHHHHH		31.1229688323
8PhosphorylationMAIKSLESFLFERGL
CCCCCHHHHHHHCCC		32.3222369663
60UbiquitinationGGFPTSLKMYLESDL
CCCCCHHHHHHHHCC		25.8517644757
121PhosphorylationGTNATTRSNTESVLL
CCCCCCCCCCHHHEE		46.1130377154
123PhosphorylationNATTRSNTESVLLQR
CCCCCCCCHHHEEEC		30.7730377154
329UbiquitinationLRYMPVLKDTGKVEL
HHCCCEECCCCCEEE		54.1823749301
353UbiquitinationEDSEKNNKDGKKSNL
HHHHHCCCCCCCCCC		76.7922817900
356UbiquitinationEKNNKDGKKSNLSSP
HHCCCCCCCCCCCCC		64.2622817900
357UbiquitinationKNNKDGKKSNLSSPS
HCCCCCCCCCCCCCC		50.5423749301
358PhosphorylationNNKDGKKSNLSSPSS
CCCCCCCCCCCCCCH		46.6322369663
361PhosphorylationDGKKSNLSSPSSASS
CCCCCCCCCCCHHCC		44.4422369663
362PhosphorylationGKKSNLSSPSSASSS
CCCCCCCCCCHHCCC		31.7822369663
364PhosphorylationKSNLSSPSSASSSAS
CCCCCCCCHHCCCCC		40.2522369663
365PhosphorylationSNLSSPSSASSSASP
CCCCCCCHHCCCCCC		35.2422369663
367PhosphorylationLSSPSSASSSASPAT
CCCCCHHCCCCCCCC		27.1222369663
368PhosphorylationSSPSSASSSASPATT
CCCCHHCCCCCCCCC		29.6422369663
369PhosphorylationSPSSASSSASPATTV
CCCHHCCCCCCCCCC		30.2120377248
371PhosphorylationSSASSSASPATTVTK
CHHCCCCCCCCCCCC		19.6022369663
374PhosphorylationSSSASPATTVTKNAS
CCCCCCCCCCCCCHH		25.7822369663
375PhosphorylationSSASPATTVTKNASE
CCCCCCCCCCCCHHH		28.4322369663
377PhosphorylationASPATTVTKNASEKL
CCCCCCCCCCHHHCC		19.2522369663
378UbiquitinationSPATTVTKNASEKLT
CCCCCCCCCHHHCCE		46.2917644757
383UbiquitinationVTKNASEKLTYEKSS
CCCCHHHCCEECCCC		43.5723749301
386PhosphorylationNASEKLTYEKSSTKE
CHHHCCEECCCCCCC		31.6227017623
389PhosphorylationEKLTYEKSSTKEVRK
HCCEECCCCCCCCCC		31.1627017623
391PhosphorylationLTYEKSSTKEVRKPR
CEECCCCCCCCCCCC		38.0127017623
464UbiquitinationSKSVEIFKNKEINLL
HCCCHHHCCCCCCCC		73.1617644757
466UbiquitinationSVEIFKNKEINLLTQ
CCHHHCCCCCCCCCC		61.6423749301
466AcetylationSVEIFKNKEINLLTQ
CCHHHCCCCCCCCCC		61.6424489116
488UbiquitinationIKQIKQVKWYAANEP
HHCCEEEEEEECCCC		31.8023749301
505PhosphorylationLTNRMSPSMFETINH
CCCCCCHHHHHHHCE		28.8819779198
517PhosphorylationINHLIVKTETSDEKE
HCEEEEECCCCCCCE		33.3319779198
532PhosphorylationFSISEFITTINGSSN
EEHHHHHHEECCCCC		27.2619779198
548UbiquitinationAKDFISEKVIFPNSV
HHHHHCCCEECCCCC		33.5617644757
548AcetylationAKDFISEKVIFPNSV
HHHHHCCCEECCCCC		33.5624489116
560UbiquitinationNSVPIESKLNSPFNL
CCCCCHHHCCCCCHH		38.6117644757
672UbiquitinationTLFQVDQKPSNYHGP
HHCCCCCCCCCCCCC		46.0517644757
676PhosphorylationVDQKPSNYHGPIDKK
CCCCCCCCCCCCCCC		16.7030377154
682UbiquitinationNYHGPIDKKTLIFRD
CCCCCCCCCEEEEHH		48.6717644757
683UbiquitinationYHGPIDKKTLIFRDH
CCCCCCCCEEEEHHH		44.8317644757
728UbiquitinationDNFGWARKIVRYLPF
CCCHHHHHHHHHCCC		37.4917644757
807UbiquitinationMQELNAAKLIDENVF
HHHHHHHHCCCHHHH		43.4917644757
815AcetylationLIDENVFKLFTKAVE
CCCHHHHHHHHHHHH		38.1124489116
815UbiquitinationLIDENVFKLFTKAVE
CCCHHHHHHHHHHHH		38.1117644757
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of MKT1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MKT1_YEAST !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of MKT1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PBP1_YEASTPBP1physical
15082763
MKS1_YEASTMKS1genetic
6371496
SKI2_YEASTSKI2genetic
6371496
SKI3_YEASTSKI3genetic
6371496
CSL4_YEASTCSL4genetic
6371496
RRP41_YEASTSKI6genetic
6371496
SKI7_YEASTSKI7genetic
6371496
IF5A1_YEASTHYP2physical
16554755
HSP60_YEASTHSP60physical
16554755
HSP60_YEASTHSP60physical
16429126
RGP1_YEASTRGP1genetic
17314980
TAF13_YEASTTAF13genetic
17314980
SSN8_YEASTSSN8genetic
17314980
FAB1_YEASTFAB1genetic
17314980
SWD3_YEASTSWD3genetic
19547744
CDC24_YEASTCDC24genetic
27708008
PSB6_YEASTPRE7genetic
27708008
MED22_YEASTSRB6genetic
27708008
TECR_YEASTTSC13genetic
27708008
NOP14_YEASTNOP14genetic
27708008
SEC1_YEASTSEC1genetic
27708008
MOB2_YEASTMOB2genetic
27708008
GPI10_YEASTGPI10genetic
27708008
SMD1_YEASTSMD1genetic
27708008
MED6_YEASTMED6genetic
27708008
KTHY_YEASTCDC8genetic
27708008
FNTA_YEASTRAM2genetic
27708008
PRP19_YEASTPRP19genetic
27708008
SSL1_YEASTSSL1genetic
27708008
NUF2_YEASTNUF2genetic
27708008
ESA1_YEASTESA1genetic
27708008
TBF1_YEASTTBF1genetic
27708008
HRR25_YEASTHRR25genetic
27708008
DIB1_YEASTDIB1genetic
27708008
EF1A_YEASTTEF2genetic
27708008
GOSR1_YEASTGOS1genetic
27708008
CWP2_YEASTCWP2genetic
27708008
KTI12_YEASTKTI12genetic
27708008
RL40A_YEASTRPL40Bgenetic
27708008
RL40B_YEASTRPL40Bgenetic
27708008
RT109_YEASTRTT109genetic
27708008
RL22A_YEASTRPL22Agenetic
27708008
YM16A_YEASTYMR316C-Agenetic
27708008
SIN3_YEASTSIN3genetic
27708008
AP1G1_YEASTAPL4genetic
27708008
FCY1_YEASTFCY1genetic
27708008
OPT2_YEASTOPT2genetic
27708008
PMP1_YEASTPMP1physical
26404137
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MKT1_YEAST

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; SER-362 ANDSER-371, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory