SBE2_YEAST - dbPTM
SBE2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SBE2_YEAST
UniProt AC P42223
Protein Name Protein SBE2
Gene Name SBE2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 864
Subcellular Localization Golgi apparatus .
Protein Description With SBE22, is involved in cell wall integrity and polarity processes like bud growth, through the transport of CHS3 and UTR2 to sites of growth..
Protein Sequence MTARRLINIVPNTSKLDPLKEEDSTHLKQNQPKKFSTKELMLSEYTERKSCSLPLSKSRSGSSASSSTTGSNGKNIGTRRPSSNLDFNFASQDVVKNVLGNNNPHVPTAKCIRPISDDSIGTSSTEIFSSSHSNTTSDSLCTSDISSEEGEIANSKMEDNCFFKSMREADHRSNITPLKKSRPGSILQKTRTASSADKTICSMSTITTCIPSRQNSVSTPKLSRTVGLPGSSNTTNSIAASQTSFISENDSPLKHHCMSTATIQEPKLMPITKTPYVHSNSTSVILPYKTTQLTPSQRYRLRKEQNDQSLRKAIKMKEKFYEDQDVNLELQEGDVDGSLIWNIPMASLSTSSFLTLSKFNRKEMSLDSARGDEEILIQENNCEGKQHSSSALCVDKTFHQVHSTRKHTSNSSNTLKESCLDYKELPPTCIPGISPVSDSQYIQDTMKNLSQIYLHSSEKISKSILSGRSRSVQSLPLEFKEASSQGMEDLMLVSEDKLKAVSHFRPSWLPPKDFKERKLQDKQIYKNIDLASMEELQKNKERDEKAKKNEQNKVKFQHLLDRGITRNSSLSELKKIIWETPLISKVRLQIYSQLLQSDNCLITKCFIESFEEVMQLLNKMDFPKDKEFEIRQLIEHDVQEKVFYKNGTDKQVVSDLMLLLQLKSISQQGLVTGDEMLFYHFLTDQSFGTLKETWEMVNLIQMTCFSEICKEKYDSRILNPRGIVAHLLRKDEFKNEFNGGCLNSNTWWNILQRMDHKLFMWVMDVIIVHNGQNFANYPVKMEIFKDKVWEYYRSKKVIVNYKILVSLTVNVLLNYHFGYDNLKHLSDLDDKHFCIPLYTEDSIEEENLNNIFTKWWLHYYRKLR
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
2Phosphorylation------MTARRLINI
------CCHHHHHCC		28.9530377154
13PhosphorylationLINIVPNTSKLDPLK
HHCCCCCCCCCCCCC		22.5930377154
50PhosphorylationSEYTERKSCSLPLSK
HHHHCCCCCCCCCCC		18.3728889911
58PhosphorylationCSLPLSKSRSGSSAS
CCCCCCCCCCCCCCC		28.4423749301
71PhosphorylationASSSTTGSNGKNIGT
CCCCCCCCCCCCCCC		40.0723749301
78PhosphorylationSNGKNIGTRRPSSNL
CCCCCCCCCCCCCCC		21.5119823750
82PhosphorylationNIGTRRPSSNLDFNF
CCCCCCCCCCCCCCC		30.0122369663
83PhosphorylationIGTRRPSSNLDFNFA
CCCCCCCCCCCCCCC		44.0622369663
91PhosphorylationNLDFNFASQDVVKNV
CCCCCCCCHHHHHHH		23.8319823750
96UbiquitinationFASQDVVKNVLGNNN
CCCHHHHHHHHCCCC		40.9817644757
110UbiquitinationNPHVPTAKCIRPISD
CCCCCCCCEECCCCC		32.4517644757
176PhosphorylationADHRSNITPLKKSRP
HHHHCCCCCCCCCCC		27.1523749301
181PhosphorylationNITPLKKSRPGSILQ
CCCCCCCCCCCCHHH		41.9619684113
185PhosphorylationLKKSRPGSILQKTRT
CCCCCCCCHHHHCCC		23.8619684113
192PhosphorylationSILQKTRTASSADKT
CHHHHCCCCCCCCCE		35.8023749301
212PhosphorylationTITTCIPSRQNSVST
CEEECCCCCCCCCCC		26.9621440633
216PhosphorylationCIPSRQNSVSTPKLS
CCCCCCCCCCCCCCC		14.7621440633
218PhosphorylationPSRQNSVSTPKLSRT
CCCCCCCCCCCCCCC		38.5223749301
219PhosphorylationSRQNSVSTPKLSRTV
CCCCCCCCCCCCCCC		23.4528889911
234PhosphorylationGLPGSSNTTNSIAAS
CCCCCCCCCCCCHHC		29.3327017623
235PhosphorylationLPGSSNTTNSIAASQ
CCCCCCCCCCCHHCC		31.0827017623
237PhosphorylationGSSNTTNSIAASQTS
CCCCCCCCCHHCCCC		16.1227017623
241PhosphorylationTTNSIAASQTSFISE
CCCCCHHCCCCEECC		25.6021551504
244PhosphorylationSIAASQTSFISENDS
CCHHCCCCEECCCCC		16.9721551504
247PhosphorylationASQTSFISENDSPLK
HCCCCEECCCCCCCC		28.4720377248
251PhosphorylationSFISENDSPLKHHCM
CEECCCCCCCCCCCC		43.6520377248
259PhosphorylationPLKHHCMSTATIQEP
CCCCCCCCCCEECCC		21.9321440633
273UbiquitinationPKLMPITKTPYVHSN
CCCCCCCCCCEECCC		48.5017644757
274PhosphorylationKLMPITKTPYVHSNS
CCCCCCCCCEECCCC		15.9424961812
276PhosphorylationMPITKTPYVHSNSTS
CCCCCCCEECCCCCE		18.9421440633
279PhosphorylationTKTPYVHSNSTSVIL
CCCCEECCCCCEEEE		23.5621440633
281PhosphorylationTPYVHSNSTSVILPY
CCEECCCCCEEEECC		25.6919684113
282PhosphorylationPYVHSNSTSVILPYK
CEECCCCCEEEECCC		31.1219684113
283PhosphorylationYVHSNSTSVILPYKT
EECCCCCEEEECCCC		13.6421440633
289UbiquitinationTSVILPYKTTQLTPS
CEEEECCCCCCCCHH		43.0617644757
290PhosphorylationSVILPYKTTQLTPSQ
EEEECCCCCCCCHHH		17.5821551504
388PhosphorylationNCEGKQHSSSALCVD
CCCCCCCCCCEEEEC		24.4022369663
389PhosphorylationCEGKQHSSSALCVDK
CCCCCCCCCEEEECC		19.9422369663
390PhosphorylationEGKQHSSSALCVDKT
CCCCCCCCEEEECCC		28.4222369663
408PhosphorylationVHSTRKHTSNSSNTL
HHHCCCCCCCCCCCH		32.4128889911
411PhosphorylationTRKHTSNSSNTLKES
CCCCCCCCCCCHHHH		25.4021440633
412PhosphorylationRKHTSNSSNTLKESC
CCCCCCCCCCHHHHH		37.7828889911
414PhosphorylationHTSNSSNTLKESCLD
CCCCCCCCHHHHHCC		40.9521440633
447UbiquitinationQYIQDTMKNLSQIYL
HHHHHHHHHHHHHHH		57.7517644757
450PhosphorylationQDTMKNLSQIYLHSS
HHHHHHHHHHHHCCC		24.7522369663
453PhosphorylationMKNLSQIYLHSSEKI
HHHHHHHHHCCCHHH		7.2522369663
456PhosphorylationLSQIYLHSSEKISKS
HHHHHHCCCHHHHHH		37.2824961812
457PhosphorylationSQIYLHSSEKISKSI
HHHHHCCCHHHHHHH		31.9621440633
459UbiquitinationIYLHSSEKISKSILS
HHHCCCHHHHHHHHC		54.9817644757
461PhosphorylationLHSSEKISKSILSGR
HCCCHHHHHHHHCCC		31.2724961812
463PhosphorylationSSEKISKSILSGRSR
CCHHHHHHHHCCCCC		23.2119823750
466PhosphorylationKISKSILSGRSRSVQ
HHHHHHHCCCCCCCC		30.4121440633
469PhosphorylationKSILSGRSRSVQSLP
HHHHCCCCCCCCCCC		32.2222369663
471PhosphorylationILSGRSRSVQSLPLE
HHCCCCCCCCCCCEE		26.2522369663
474PhosphorylationGRSRSVQSLPLEFKE
CCCCCCCCCCEEHHH		29.7822369663
532PhosphorylationYKNIDLASMEELQKN
HHHCCHHHHHHHHHH		33.7422369663
571PhosphorylationITRNSSLSELKKIIW
CCCCCCHHHHHHHHH		42.7127017623
609PhosphorylationITKCFIESFEEVMQL
EEHHHHHHHHHHHHH		32.8928889911
713PhosphorylationSEICKEKYDSRILNP
HHHHHHHHHCCCCCH		21.9028889911
715PhosphorylationICKEKYDSRILNPRG
HHHHHHHCCCCCHHH		20.3828889911
730UbiquitinationIVAHLLRKDEFKNEF
HHHHHHCCHHHCCCC		62.6717644757
734UbiquitinationLLRKDEFKNEFNGGC
HHCCHHHCCCCCCCC		54.2217644757
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 SBE2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SBE2_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 SBE2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SBE22_YEASTSBE22genetic
10679005
CHS5_YEASTCHS5genetic
10679005
BCK1_YEASTBCK1genetic
10679005
CDC24_YEASTCDC24genetic
10679005
CDC12_YEASTCDC12genetic
10679005
SMI1_YEASTSMI1genetic
23891562
SBE22_YEASTSBE22genetic
23891562
NAB3_YEASTNAB3genetic
27708008
KPC1_YEASTPKC1genetic
27708008
MCM7_YEASTMCM7genetic
27708008
MOB2_YEASTMOB2genetic
27708008
ACT_YEASTACT1genetic
27708008
SMD1_YEASTSMD1genetic
27708008
EI2BG_YEASTGCD1genetic
27708008
PEX22_YEASTPEX22genetic
27708008
PP2C1_YEASTPTC1genetic
27708008
MTU1_YEASTSLM3genetic
27708008
BRE1_YEASTBRE1genetic
27708008
RAD4_YEASTRAD4genetic
27708008
SMI1_YEASTSMI1genetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
MSC1_YEASTMSC1genetic
27708008
SCS7_YEASTSCS7genetic
27708008
PUB1_YEASTPUB1genetic
27708008
INO4_YEASTINO4genetic
27708008
KES1_YEASTKES1genetic
27708008
AIM44_YEASTAIM44genetic
27708008
THI21_YEASTTHI21genetic
27708008
MED1_YEASTMED1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SBE2_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-450; SER-471; SER-474AND SER-532, AND MASS SPECTROMETRY.
"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-471, AND MASSSPECTROMETRY.

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