MUK1_YEAST - dbPTM
MUK1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MUK1_YEAST
UniProt AC Q02866
Protein Name Protein MUK1
Gene Name MUK1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 612
Subcellular Localization Cytoplasm .
Protein Description Putative GTPase-activating protein..
Protein Sequence MARQLFTPPITNPRFDPNQSIRESYKNTTGGMQFQQNLHEDQNDNERSSCDGDENSTTGERLENNKSPILTKQEIDEALNTVTNLPPELSKLIDIFIDDLKQPKYVRPLSVLQLSSLFQSFYIKFDKASFQHVSSANNNGYYFSGGGSSSFLAAKETLSSGLSGIFGRSRSSSGNSLMRPRRSSSLFSNESISNSTNATQMLSPEEIKKQLKINELNNMKIEKYMELCERDVFKKILIVGTSVSSPNKMKTFKPHQLQTFKVGNLFRNSVEFTEYNKLLNEKILCLSKLSTMNKINLIKFLSLNNGIDPEPKFEEIKDILYEFTYHSISPCEKIKALLKLHEIMTYSQEMSNDDYLSLLIYYIITIVPRDIFLNAEFIRLFRYKKKLVETESFALTNLEAALVFVEGLTKNDFSNELQDKLTVNESKILENSISSRVSLPSKTAIMHKNNGNNGSNLGDIVTPTIQRPDVTRSNSYDGFRTVFDSSLKNIIGKIRSYTPPHPNNTSNNNLHSSNNLNIPRSSSQLSMELSNRDTTEMSRDGSRSTSSSSRSSASLEHGNREFTGDLTVTASINGADKKEFQKSWKKYKGYKFEDLTICELRDLFEIYQKMMQ
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
7Phosphorylation-MARQLFTPPITNPR
-CCCCCCCCCCCCCC		36.4327214570
48PhosphorylationDQNDNERSSCDGDEN
CCCCCCCCCCCCCCC		29.1928889911
49PhosphorylationQNDNERSSCDGDENS
CCCCCCCCCCCCCCC		23.5828889911
56PhosphorylationSCDGDENSTTGERLE
CCCCCCCCCHHHHHH		25.8729136822
57PhosphorylationCDGDENSTTGERLEN
CCCCCCCCHHHHHHC		50.8623749301
58PhosphorylationDGDENSTTGERLENN
CCCCCCCHHHHHHCC		36.5519779198
67PhosphorylationERLENNKSPILTKQE
HHHHCCCCCCCCHHH		21.2122369663
71PhosphorylationNNKSPILTKQEIDEA
CCCCCCCCHHHHHHH		31.2522369663
81PhosphorylationEIDEALNTVTNLPPE
HHHHHHHHHHCCCHH		29.5619779198
157PhosphorylationSFLAAKETLSSGLSG
HHHHHHHHHHCCCCC		31.1021126336
159PhosphorylationLAAKETLSSGLSGIF
HHHHHHHHCCCCCHH		29.7623607784
160PhosphorylationAAKETLSSGLSGIFG
HHHHHHHCCCCCHHC		47.0323607784
163PhosphorylationETLSSGLSGIFGRSR
HHHHCCCCCHHCCCC		33.1122369663
169PhosphorylationLSGIFGRSRSSSGNS
CCCHHCCCCCCCCCC		36.5721440633
171PhosphorylationGIFGRSRSSSGNSLM
CHHCCCCCCCCCCCC		30.0629136822
172PhosphorylationIFGRSRSSSGNSLMR
HHCCCCCCCCCCCCC		40.9528889911
173PhosphorylationFGRSRSSSGNSLMRP
HCCCCCCCCCCCCCC		43.1529136822
176PhosphorylationSRSSSGNSLMRPRRS
CCCCCCCCCCCCCCC		27.3729136822
183PhosphorylationSLMRPRRSSSLFSNE
CCCCCCCCCCCCCCC		26.0923607784
184PhosphorylationLMRPRRSSSLFSNES
CCCCCCCCCCCCCCC		29.2817330950
185PhosphorylationMRPRRSSSLFSNESI
CCCCCCCCCCCCCCC		34.3817330950
188PhosphorylationRRSSSLFSNESISNS
CCCCCCCCCCCCCCC		45.0123607784
191PhosphorylationSSLFSNESISNSTNA
CCCCCCCCCCCCCCC		35.2519779198
193PhosphorylationLFSNESISNSTNATQ
CCCCCCCCCCCCCHH		33.7223607784
195PhosphorylationSNESISNSTNATQML
CCCCCCCCCCCHHCC		19.0923607784
196PhosphorylationNESISNSTNATQMLS
CCCCCCCCCCHHCCC		32.8723607784
199PhosphorylationISNSTNATQMLSPEE
CCCCCCCHHCCCHHH		19.3127738172
241PhosphorylationKKILIVGTSVSSPNK
CCEEEEECCCCCCCC		18.3022890988
242PhosphorylationKILIVGTSVSSPNKM
CEEEEECCCCCCCCC		17.6722890988
244PhosphorylationLIVGTSVSSPNKMKT
EEEECCCCCCCCCCC		39.5822890988
245PhosphorylationIVGTSVSSPNKMKTF
EEECCCCCCCCCCCC		30.2725521595
427UbiquitinationKLTVNESKILENSIS
CCCCCHHHHHHCHHH		45.1723749301
435PhosphorylationILENSISSRVSLPSK
HHHCHHHCCCCCCCC		34.7227214570
462PhosphorylationSNLGDIVTPTIQRPD
CCCCCCCCCCCCCCC		18.3023749301
473PhosphorylationQRPDVTRSNSYDGFR
CCCCCCCCCCCCCHH		22.2922890988
475PhosphorylationPDVTRSNSYDGFRTV
CCCCCCCCCCCHHHH		26.3322369663
476PhosphorylationDVTRSNSYDGFRTVF
CCCCCCCCCCHHHHC		25.0822890988
481PhosphorylationNSYDGFRTVFDSSLK
CCCCCHHHHCCHHHH		24.2221551504
486PhosphorylationFRTVFDSSLKNIIGK
HHHHCCHHHHHHHHH		45.2521551504
496PhosphorylationNIIGKIRSYTPPHPN
HHHHHHHHCCCCCCC		36.5129136822
497PhosphorylationIIGKIRSYTPPHPNN
HHHHHHHCCCCCCCC		17.2629136822
498PhosphorylationIGKIRSYTPPHPNNT
HHHHHHCCCCCCCCC		31.4329136822
505PhosphorylationTPPHPNNTSNNNLHS
CCCCCCCCCCCCCCC		39.2019779198
506PhosphorylationPPHPNNTSNNNLHSS
CCCCCCCCCCCCCCC		39.4219779198
512PhosphorylationTSNNNLHSSNNLNIP
CCCCCCCCCCCCCCC		37.6223749301
521PhosphorylationNNLNIPRSSSQLSME
CCCCCCCCHHHHHHH		29.0522369663
522PhosphorylationNLNIPRSSSQLSMEL
CCCCCCCHHHHHHHH		24.3122369663
523PhosphorylationLNIPRSSSQLSMELS
CCCCCCHHHHHHHHH		36.0722369663
526PhosphorylationPRSSSQLSMELSNRD
CCCHHHHHHHHHCCC		11.5422369663
530PhosphorylationSQLSMELSNRDTTEM
HHHHHHHHCCCCCCC		19.2622369663
534PhosphorylationMELSNRDTTEMSRDG
HHHHCCCCCCCCCCC		22.7822369663
535PhosphorylationELSNRDTTEMSRDGS
HHHCCCCCCCCCCCC		33.7022369663
538PhosphorylationNRDTTEMSRDGSRST
CCCCCCCCCCCCCCC		22.4622369663
542PhosphorylationTEMSRDGSRSTSSSS
CCCCCCCCCCCCCCC		27.6128889911
544PhosphorylationMSRDGSRSTSSSSRS
CCCCCCCCCCCCCCC		34.0528889911
546PhosphorylationRDGSRSTSSSSRSSA
CCCCCCCCCCCCCCC		29.4828889911
552PhosphorylationTSSSSRSSASLEHGN
CCCCCCCCCCCCCCC		22.2928889911
554PhosphorylationSSSRSSASLEHGNRE
CCCCCCCCCCCCCEE		35.9228889911
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 MUK1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MUK1_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 MUK1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PANB_YEASTECM31physical
11283351
CDD_YEASTCDD1physical
11283351
ISN1_YEASTISN1physical
11283351
HPA2_YEASTHPA2physical
11283351
MUK1_YEASTMUK1physical
18719252
NNRD_YEASTYKL151Cphysical
18719252
PNC1_YEASTPNC1physical
18719252
UBA4_YEASTUBA4physical
18719252
CATA_YEASTCTA1physical
18719252
SFH1_YEASTSFH1physical
18719252
PHS_YEASTYHL018Wphysical
18719252
YJV8_YEASTYJL218Wphysical
18719252
PRA1_YEASTYIP3physical
18719252
SEC18_YEASTSEC18physical
18719252
ARP1_YEASTARP1physical
18719252
CACP_YEASTCAT2physical
18719252
DIG1_YEASTDIG1physical
18719252
THDH_YEASTILV1physical
18719252
URE2_YEASTURE2physical
18719252
AAD16_YEASTYPL088Wphysical
18719252
RNQ1_YEASTRNQ1physical
18719252
SNO1_YEASTSNO1physical
18719252
DHYS_YEASTDYS1physical
18719252
CDD_YEASTCDD1physical
18719252
HPA2_YEASTHPA2physical
18719252
AMPD_YEASTAMD1physical
18719252
SNZ3_YEASTSNZ3physical
18719252
ENO2_YEASTENO2physical
22940862
VPS9_YEASTVPS9genetic
23612966
YPT7_YEASTYPT7physical
23612966
VPS21_YEASTVPS21physical
23612966
MON1_YEASTMON1physical
23612966
YIP1_YEASTYIP1physical
23612966
YPT6_YEASTYPT6physical
23612966
ADY3_YEASTADY3physical
23612966
BZZ1_YEASTBZZ1physical
23612966
EXO84_YEASTEXO84physical
23612966
EI2BB_YEASTGCD7physical
23612966
VPS9_YEASTVPS9genetic
25673804
PRP6_YEASTPRP6genetic
27708008
RRP1_YEASTRRP1genetic
27708008
CDC1_YEASTCDC1genetic
27708008
TCPA_YEASTTCP1genetic
27708008
TFC6_YEASTTFC6genetic
27708008
RMRP_YEASTSNM1genetic
27708008
GNA1_YEASTGNA1genetic
27708008
FDFT_YEASTERG9genetic
27708008
KTHY_YEASTCDC8genetic
27708008
UTP13_YEASTUTP13genetic
27708008
TAD3_YEASTTAD3genetic
27708008
NBP1_YEASTNBP1genetic
27708008
PROF_YEASTPFY1genetic
27708008
RPB2_YEASTRPB2genetic
27708008
DIB1_YEASTDIB1genetic
27708008
BUR1_YEASTSGV1genetic
27708008
VPS5_YEASTVPS5physical
25609093
VPS17_YEASTVPS17physical
25609093
PEP8_YEASTPEP8physical
25609093
VPS29_YEASTVPS29physical
25609093
VPS35_YEASTVPS35physical
25609093
VPS9_YEASTVPS9genetic
25609093
U5071_YEASTYML003Wgenetic
25609093
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MUK1_YEAST

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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-67; SER-163; SER-184;SER-185; SER-244; SER-245; SER-475; SER-522 AND SER-523, AND MASSSPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184 AND SER-185, ANDMASS SPECTROMETRY.
"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-185, AND MASSSPECTROMETRY.

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