SKN1_YEAST - dbPTM
SKN1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SKN1_YEAST
UniProt AC P33336
Protein Name Beta-glucan synthesis-associated protein SKN1
Gene Name SKN1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 771
Subcellular Localization Membrane
Single-pass type II membrane protein.
Protein Description Required for synthesis of the major beta-glucans of the yeast cell wall..
Protein Sequence MSVRNLTNNRHSNSENSVSGSENSFYSSNEQSRQSSSLEPADGQNVRVSGNPFLGSEEFDEDYNSPSGDDERRGANEYSSSSSINYNNDPNSDTSLLANEKNSPERNGQRMSDYKGYYAKTNLTSANNLNNHNNNNYKNIISSSNDNSFASHLQPPDRNLPSHPSSNNMSSFSNNSLIKSPPPFDRYPLVGTRHISAAQSQSQNLINEKKRANMTGSSSSAHDSSLSSTNLYMGEQDFSPFGGYPASFFPLTLDEKEDDDYIHNPNVEEEAKLDRRRFVDDFKHMDRRSFLGLLGILFLFMAGIFIFIVLPAITFSGVVYHHEHVHAANSAGSSSSNTTSKSLTEYQYPQLAAIRTTLVDPDTPDSAKTRVAKDGSKWQLVFSDEFNAEGRTFYDGDDQFWTAPDIHYDATKDLEWYSPDAVTTTNGTLTLRMDAFRNHDLYYRSGMVQSWNKLCFTEGALEVSANLPNYGRVTGLWPGMWTMGNLGRPGYLASTQGVWPYSYEACDAGITPNQSSPDGISYLPGQKLSVCTCDNEDHPNQGVGRGAPEIDILEGEADTILGVGVASQSLQIAPFDIWYMPDYDFIEVYNFTTTTMNTYAGGPFQQAVSAISTLNVTWYEFGEEAGYFQKYAIEYLNDDDNGYIRWFVGENPTFTLYATSLHPSGNIDWRRISKEPMSAILNLGISNNWAYIDWQYIFFPVTMSIDYVRLYQPKGSTSITCDPEDYPTYDYIQSHLNAYYNANLTDWEQAGYTFPKNILTGGCSSSKFSLS
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
24PhosphorylationSVSGSENSFYSSNEQ
CCCCCCCCCCCCCHH		22.8523749301
35PhosphorylationSNEQSRQSSSLEPAD
CCHHHCCCCCCCCCC		22.3028889911
37PhosphorylationEQSRQSSSLEPADGQ
HHHCCCCCCCCCCCC		41.8328889911
49PhosphorylationDGQNVRVSGNPFLGS
CCCCEEECCCCCCCC		23.4522369663
56PhosphorylationSGNPFLGSEEFDEDY
CCCCCCCCCCCCCCC		35.7822369663
63PhosphorylationSEEFDEDYNSPSGDD
CCCCCCCCCCCCCCC		18.5822369663
65PhosphorylationEFDEDYNSPSGDDER
CCCCCCCCCCCCCCC		17.7622369663
67PhosphorylationDEDYNSPSGDDERRG
CCCCCCCCCCCCCCC		55.4622369663
80PhosphorylationRGANEYSSSSSINYN
CCCCCCCCCCCCCCC		33.0819779198
86PhosphorylationSSSSSINYNNDPNSD
CCCCCCCCCCCCCCC		17.4219779198
92PhosphorylationNYNNDPNSDTSLLAN
CCCCCCCCCCHHHHC		47.88-
94PhosphorylationNNDPNSDTSLLANEK
CCCCCCCCHHHHCCC		22.5419779198
103PhosphorylationLLANEKNSPERNGQR
HHHCCCCCCCCCCCC		38.9220377248
112PhosphorylationERNGQRMSDYKGYYA
CCCCCCHHHHCCEEE		39.7223749301
115UbiquitinationGQRMSDYKGYYAKTN
CCCHHHHCCEEECCC		45.4823749301
120UbiquitinationDYKGYYAKTNLTSAN
HHCCEEECCCCCCCC		23.0923749301
121PhosphorylationYKGYYAKTNLTSANN
HCCEEECCCCCCCCC		27.5622369663
124PhosphorylationYYAKTNLTSANNLNN
EEECCCCCCCCCCCC		28.0622369663
125PhosphorylationYAKTNLTSANNLNNH
EECCCCCCCCCCCCC		31.9722369663
142PhosphorylationNNYKNIISSSNDNSF
CCHHHEECCCCCCCH		24.7429688323
143PhosphorylationNYKNIISSSNDNSFA
CHHHEECCCCCCCHH		23.8129688323
144PhosphorylationYKNIISSSNDNSFAS
HHHEECCCCCCCHHH		41.2223749301
148PhosphorylationISSSNDNSFASHLQP
ECCCCCCCHHHHCCC		25.6723749301
151PhosphorylationSNDNSFASHLQPPDR
CCCCCHHHHCCCCCC		23.7929688323
162PhosphorylationPPDRNLPSHPSSNNM
CCCCCCCCCCCCCCC		51.72-
165PhosphorylationRNLPSHPSSNNMSSF
CCCCCCCCCCCCCCC		40.0323749301
166PhosphorylationNLPSHPSSNNMSSFS
CCCCCCCCCCCCCCC		36.3523749301
170PhosphorylationHPSSNNMSSFSNNSL
CCCCCCCCCCCCCCC		30.2923749301
173PhosphorylationSNNMSSFSNNSLIKS
CCCCCCCCCCCCCCC		36.7323749301
176PhosphorylationMSSFSNNSLIKSPPP
CCCCCCCCCCCCCCC		35.4023749301
192PhosphorylationDRYPLVGTRHISAAQ
CCCCCCCHHHHHHHH		16.1724961812
196PhosphorylationLVGTRHISAAQSQSQ
CCCHHHHHHHHHHHH		16.0722369663
200PhosphorylationRHISAAQSQSQNLIN
HHHHHHHHHHHHHHC		27.3722369663
202PhosphorylationISAAQSQSQNLINEK
HHHHHHHHHHHHCHH		26.7022369663
209UbiquitinationSQNLINEKKRANMTG
HHHHHCHHHHHCCCC		42.9723749301
210UbiquitinationQNLINEKKRANMTGS
HHHHCHHHHHCCCCC		51.0317644757
337N-linked_GlycosylationSAGSSSSNTTSKSLT
CCCCCCCCCCCCCCC		49.69-
341UbiquitinationSSSNTTSKSLTEYQY
CCCCCCCCCCCCCCC		47.6017644757
368UbiquitinationPDTPDSAKTRVAKDG
CCCCCCHHCEECCCC		40.5923749301
426N-linked_GlycosylationPDAVTTTNGTLTLRM
CCCEEECCCEEEEEE		39.08-
442PhosphorylationAFRNHDLYYRSGMVQ
HHCCCCCCHHCCCCC		11.6828889911
450PhosphorylationYRSGMVQSWNKLCFT
HHCCCCCHHHHCEEC		22.6228889911
513N-linked_GlycosylationCDAGITPNQSSPDGI
CCCCCCCCCCCCCCC		45.79-
590N-linked_GlycosylationYDFIEVYNFTTTTMN
CCEEEEEEEEECCCC		32.72-
615N-linked_GlycosylationVSAISTLNVTWYEFG
HHHHHHCEEEEEECC		29.30-
630UbiquitinationEEAGYFQKYAIEYLN
HHCCCEEEEEEEECC		27.1017644757
743N-linked_GlycosylationLNAYYNANLTDWEQA
HHHHHCCCCCCHHHC		39.57-
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 SKN1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SKN1_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 SKN1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RRN10_YEASTRRN10genetic
14764870
PEX5_YEASTPEX5genetic
14764870
UBCX_YEASTPEX4genetic
14764870
PSA3_YEASTPRE9genetic
14764870
IF2M_YEASTIFM1genetic
14764870
KRE6_YEASTKRE6genetic
8321211
KRE6_YEASTKRE6genetic
12185837
LST4_YEASTLST4genetic
14764870
COQ3_YEASTCOQ3genetic
21623372
LCB5_YEASTLCB5genetic
21623372
CY1_YEASTCYT1genetic
21623372
QCR2_YEASTQCR2genetic
21623372
PDX3_YEASTPDX3genetic
21623372
COQ7_YEASTCAT5genetic
21623372
ADK_YEASTADO1genetic
21623372
KEG1_YEASTKEG1physical
22447934
PIL1_YEASTPIL1physical
22940862
HSP71_YEASTSSA1physical
22940862
YBP1_YEASTYBP1genetic
27708008
BCS1_YEASTBCS1genetic
27708008
ODPA_YEASTPDA1genetic
27708008
UBA4_YEASTUBA4genetic
27708008
SDS3_YEASTSDS3genetic
27708008
RL16A_YEASTRPL16Agenetic
27708008
SNX4_YEASTSNX4genetic
27708008
RNP1_YEASTRNP1genetic
27708008
CSF1_YEASTCSF1genetic
27708008
EIF3J_YEASTHCR1genetic
27708008
HMX1_YEASTHMX1genetic
27708008
NKP2_YEASTNKP2genetic
27708008
MAC1_YEASTMAC1genetic
27708008
PKR1_YEASTPKR1genetic
27708008
INP2_YEASTINP2genetic
27708008
AEP2_YEASTAEP2genetic
27708008
EOS1_YEASTEOS1genetic
27708008
YNO0_YEASTYNL140Cgenetic
27708008
HAP5_YEASTHAP5genetic
27708008
MSS18_YEASTMSS18genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SKN1_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-176, 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-67, AND MASSSPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103, AND MASSSPECTROMETRY.

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