KRE6_YEAST - dbPTM
KRE6_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KRE6_YEAST
UniProt AC P32486
Protein Name Beta-glucan synthesis-associated protein KRE6
Gene Name KRE6
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 720
Subcellular Localization Golgi apparatus membrane
Single-pass type II membrane protein .
Protein Description Involved in the synthesis of (1->6)- and (1->3)-beta-D-glucan polymers of the yeast cell wall in vivo. It is required for full activity of beta-glucan synthase in vitro. May be involved in the maturation and transport of cell wall proteins (CWP) to the cell wall. May act as a transglucosidase and contribute to the construction of a protein-bound glucan-structure that acts as an acceptor site for the addition of (1->6)-beta-D-glucan at the cell surface..
Protein Sequence MPLRNLTETHNFSSTNLDTDGTGDDHDGAPLSSSPSFGQQNDNSTNDNAGLTNPFMGSDEESNARDGESLSSSVHYQPQGSDSSLLHDNSRLDLSQNKGVSDYKGYYSRNNSRAVSTANDNSFLQPPHRAIASSPSLNSNLSKNDILSPPEFDRYPLVGSRVTSMTQLNHHGRSPTSSPGNESSASFSSNPFLGEQDFSPFGGYPASSFPLMIDEKEEDDYLHNPDPEEEARLDRRRFIDDFKYMDKRSASGLAGVLLLFLAAIFIFIVLPALTFTGAIDHESNTEEVTYLTQYQYPQLSAIRTSLVDPDTPDTAKTREAMDGSKWELVFSDEFNAEGRTFYDGDDPYWTAPDVHYDATKDLEWYSPDASTTVNGTLQLRMDAFKNHGLYYRSGMLQSWNKVCFTQGALEISANLPNYGRVSGLWPGLWTMGNLGRPGYLASTQGVWPYSYESCDAGITPNQSSPDGISYLPGQKLSICTCDGEDHPNQGVGRGAPEIDVLEGETDTKIGVGIASQSLQIAPFDIWYMPDYDFIEVYNFTTTTMNTYAGGPFQQAVSAVSTLNVTWYEFGEYGGYFQKYAIEYLNDDDNGYIRWFVGDTPTYTIHAKALHPDGNIGWRRISKEPMSIILNLGISNNWAYIDWQYIFFPVVMSIDYVRIYQPSNAISVTCDPSDYPTYDYIQSHLNAFQNANLTTWEDAGYTFPKNILTGKCTSSKFKLSS
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
69PhosphorylationSNARDGESLSSSVHY
CCCCCCCCCCCCEEC		38.8023749301
71PhosphorylationARDGESLSSSVHYQP
CCCCCCCCCCEECCC		29.8219795423
72PhosphorylationRDGESLSSSVHYQPQ
CCCCCCCCCEECCCC		41.4919795423
73PhosphorylationDGESLSSSVHYQPQG
CCCCCCCCEECCCCC		14.9919795423
76PhosphorylationSLSSSVHYQPQGSDS
CCCCCEECCCCCCCC		21.5219795423
81PhosphorylationVHYQPQGSDSSLLHD
EECCCCCCCCCCCCC		29.1323749301
83PhosphorylationYQPQGSDSSLLHDNS
CCCCCCCCCCCCCCC		25.2823749301
84PhosphorylationQPQGSDSSLLHDNSR
CCCCCCCCCCCCCCC		39.6823749301
90PhosphorylationSSLLHDNSRLDLSQN
CCCCCCCCCEECCCC		40.0323749301
95PhosphorylationDNSRLDLSQNKGVSD
CCCCEECCCCCCCCC		31.2323749301
98UbiquitinationRLDLSQNKGVSDYKG
CEECCCCCCCCCHHH		53.7223749301
98SuccinylationRLDLSQNKGVSDYKG
CEECCCCCCCCCHHH		53.7223954790
104UbiquitinationNKGVSDYKGYYSRNN
CCCCCCHHHEECCCC		45.4823749301
104AcetylationNKGVSDYKGYYSRNN
CCCCCCHHHEECCCC		45.4824489116
104SuccinylationNKGVSDYKGYYSRNN
CCCCCCHHHEECCCC		45.4823954790
106PhosphorylationGVSDYKGYYSRNNSR
CCCCHHHEECCCCCC		8.3020377248
107PhosphorylationVSDYKGYYSRNNSRA
CCCHHHEECCCCCCC		15.1521440633
108PhosphorylationSDYKGYYSRNNSRAV
CCHHHEECCCCCCCC		21.7620377248
112PhosphorylationGYYSRNNSRAVSTAN
HEECCCCCCCCCCCC		25.7622369663
116PhosphorylationRNNSRAVSTANDNSF
CCCCCCCCCCCCCCC		22.3322369663
117PhosphorylationNNSRAVSTANDNSFL
CCCCCCCCCCCCCCC		23.9222369663
122PhosphorylationVSTANDNSFLQPPHR
CCCCCCCCCCCCCCH		30.1422369663
133PhosphorylationPPHRAIASSPSLNSN
CCCHHHCCCCCCCCC		36.3522369663
134PhosphorylationPHRAIASSPSLNSNL
CCHHHCCCCCCCCCC		14.9722369663
136PhosphorylationRAIASSPSLNSNLSK
HHHCCCCCCCCCCCC		41.9722369663
139PhosphorylationASSPSLNSNLSKNDI
CCCCCCCCCCCCCCC		44.4322369663
142PhosphorylationPSLNSNLSKNDILSP
CCCCCCCCCCCCCCC		33.3922369663
143UbiquitinationSLNSNLSKNDILSPP
CCCCCCCCCCCCCCC		62.9017644757
148PhosphorylationLSKNDILSPPEFDRY
CCCCCCCCCCCCCCC		38.4522369663
155PhosphorylationSPPEFDRYPLVGSRV
CCCCCCCCCCCCCCC		11.6322369663
160PhosphorylationDRYPLVGSRVTSMTQ
CCCCCCCCCCCCCCC		18.9922369663
163PhosphorylationPLVGSRVTSMTQLNH
CCCCCCCCCCCCCCC		16.2122369663
164PhosphorylationLVGSRVTSMTQLNHH
CCCCCCCCCCCCCCC		19.5822369663
166PhosphorylationGSRVTSMTQLNHHGR
CCCCCCCCCCCCCCC		29.6728132839
243AcetylationRRFIDDFKYMDKRSA
HHHHHHHHHCCHHCH		46.8124489116
243UbiquitinationRRFIDDFKYMDKRSA
HHHHHHHHHCCHHCH		46.8124961812
316UbiquitinationPDTPDTAKTREAMDG
CCCCCCHHHHHHHCC		50.6523749301
374N-linked_GlycosylationPDASTTVNGTLQLRM
CCCCCEECCEEEEEH		35.32-
385AcetylationQLRMDAFKNHGLYYR
EEEHHHHHHCCCCHH		50.1624489116
461N-linked_GlycosylationCDAGITPNQSSPDGI
CCCCCCCCCCCCCCC		45.79-
508UbiquitinationLEGETDTKIGVGIAS
EECCCCCCEECCHHH		40.0317644757
538N-linked_GlycosylationYDFIEVYNFTTTTMN
CCEEEEEEEEECCCC		32.72-
563N-linked_GlycosylationVSAVSTLNVTWYEFG
HHHHHEEEEEEEECH		29.30-
578UbiquitinationEYGGYFQKYAIEYLN
HHCCHHHEEEEEECC		27.1017644757
607UbiquitinationPTYTIHAKALHPDGN
CCEEEEEEEECCCCC		37.0017644757
607AcetylationPTYTIHAKALHPDGN
CCEEEEEEEECCCCC		37.0024489116
691N-linked_GlycosylationLNAFQNANLTTWEDA
HHHHHHCCCCCHHHC		45.53-
710AcetylationPKNILTGKCTSSKFK
CCCCCCCCCCCCCCC		29.1624489116
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 KRE6_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KRE6_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 KRE6_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CST26_YEASTCST26genetic
14764870
YD206_YEASTYDL206Wgenetic
14764870
RGP1_YEASTRGP1genetic
14764870
RTN1_YEASTRTN1genetic
14764870
GNTK_YEASTYDR248Cgenetic
14764870
GGA1_YEASTGGA1genetic
14764870
EF2_YEASTEFT2genetic
14764870
FRDS_YEASTFRD1genetic
14764870
YGI1_YEASTYGL081Wgenetic
14764870
RL1A_YEASTRPL1Bgenetic
14764870
RL1B_YEASTRPL1Bgenetic
14764870
DSD1_YEASTDSD1genetic
14764870
CLG1_YEASTCLG1genetic
14764870
RTF1_YEASTRTF1genetic
14764870
SWI3_YEASTSWI3genetic
14764870
POM34_YEASTPOM34genetic
14764870
PUS5_YEASTPUS5genetic
14764870
VAN1_YEASTVAN1genetic
14764870
PRM3_YEASTPRM3genetic
14764870
LAS17_YEASTLAS17physical
12237851
SLA1_YEASTSLA1physical
12237851
SKN1_YEASTSKN1genetic
8321211
SKN1_YEASTSKN1genetic
7929594
SED1_YEASTSED1genetic
15093776
TRS65_YEASTTRS65genetic
8321211
KEG1_YEASTKEG1physical
17893149
MID2_YEASTMID2genetic
10348843
PEX22_YEASTPEX22genetic
14764870
RPOM_YEASTRPO41genetic
14764870
EMP24_YEASTEMP24genetic
14764870
VMA21_YEASTVMA21genetic
14764870
RL34B_YEASTRPL34Bgenetic
14764870
VPS24_YEASTVPS24genetic
14764870
OAC1_YEASTOAC1genetic
14764870
FPS1_YEASTFPS1genetic
14764870
ACE2_YEASTACE2genetic
14764870
VAM10_YEASTVAM10genetic
14764870
DIA2_YEASTDIA2genetic
14764870
KEG1_YEASTKEG1physical
22447934
SKN1_YEASTSKN1genetic
22447934
EF2_YEASTEFT2physical
22940862
HSP72_YEASTSSA2physical
22940862
HSP71_YEASTSSA1physical
22940862
SSB1_YEASTSSB1physical
22940862
HSC82_YEASTHSC82physical
22940862
KPYK1_YEASTCDC19physical
22940862
G3P3_YEASTTDH3physical
22940862
SPT16_YEASTSPT16physical
22940862
HSP60_YEASTHSP60physical
22940862
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KRE6_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-116; SER-133; SER-134;SER-136; SER-139; SER-160 AND SER-164, AND MASS SPECTROMETRY.
"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-116, 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-134, AND MASSSPECTROMETRY.

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