SBE22_YEAST - dbPTM
SBE22_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SBE22_YEAST
UniProt AC P38814
Protein Name Protein SBE22
Gene Name SBE22
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 852
Subcellular Localization Cytoplasm . Golgi apparatus.
Protein Description With SBE2, 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 MTSIQERGTSAHLHSLKEGEASDRSSEMLPKQRSIIGSHVQRPPSQTTLGRSRAGSNTMNKVSGLDIARRPSENLLSNMNCSDNGNGGNMLNSFVNSALPPPKVNPAQTRRERPASNSSIGTKTTEVFSSTSASSSLGDTSDEGEGSDADKSKINTFPSILMEKATQGRGADGNGMRSASNNTIVEATTDGSKMALQKSMSFDDTAAEKTMNKSRHSYQEQFSSKKSQSSLLNSKQRSRAKSQTCSSTGYNNSSILKTFGISSKISNSSDRIEASSLEFNVPSQKPLNCKPLTPSQKYRLRKEQSEMNLRNTIKRKEKFYDSQEQILELQEGDVDDSLIWNVPMASLSTNSFLASAKPDDMNNLAGKNDLSEYTGGLVNDNSEISYTKQNHRYSNISFASTTSNASLLDFNEMPTSPIPGLNKVTDFQFIQDTTKSLASVYLHSSNRLSRSKLSERTKSSDFLPIELKEAQNQGMEDLILVSENKLDVVSHSRPSWLPPKDRQEKKLHERQINKSMSVASLDQLGKNKDREEKLIRDETNRQKYVLLLDRDITRNSSLQSLSKMVWDTPFSDETRSTIYSEILQSKTRFITKNYIQPFHELQELLTKMGDFPKNKEIEISQLIETSLRRKVSGLHDICPDLMLLLKIKSISSQGIVTGDELLFHHFLVSESFQNLGLNEIWNIVNLVQMTCFNDLCKEKFDAKVLERKGVVAGYLSQNEEFKDEFNTECINSTTWWNILERIDHKLFMWIMDIIVVNNSQSYKNSPINEDEFVNKDWEYYRSKKVVINYKILISFALNVLLNYHFGFTDLRSLCNVNDQRFCIPVFINDEFVDADTVNAVFIKKWAHYYKKF
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------MTSIQERGT
------CCCHHHCCC		34.2424961812
3Phosphorylation-----MTSIQERGTS
-----CCCHHHCCCH		22.4524961812
9PhosphorylationTSIQERGTSAHLHSL
CCHHHCCCHHHHHHC		29.0324961812
10PhosphorylationSIQERGTSAHLHSLK
CHHHCCCHHHHHHCC		19.2624961812
25PhosphorylationEGEASDRSSEMLPKQ
CCCCCCCCCCCCHHH		35.3228889911
26PhosphorylationGEASDRSSEMLPKQR
CCCCCCCCCCCHHHH		28.1121551504
34PhosphorylationEMLPKQRSIIGSHVQ
CCCHHHHHCCCHHCC		18.9619823750
38PhosphorylationKQRSIIGSHVQRPPS
HHHHCCCHHCCCCCC		15.2919823750
45PhosphorylationSHVQRPPSQTTLGRS
HHCCCCCCCCCCCCC		42.7319823750
47PhosphorylationVQRPPSQTTLGRSRA
CCCCCCCCCCCCCCC		28.4619823750
48PhosphorylationQRPPSQTTLGRSRAG
CCCCCCCCCCCCCCC		21.4119823750
52PhosphorylationSQTTLGRSRAGSNTM
CCCCCCCCCCCCCCH		25.3719823750
56PhosphorylationLGRSRAGSNTMNKVS
CCCCCCCCCCHHHCC		28.3019823750
58PhosphorylationRSRAGSNTMNKVSGL
CCCCCCCCHHHCCCC		24.6621440633
63PhosphorylationSNTMNKVSGLDIARR
CCCHHHCCCCCCCCC		34.9421440633
72PhosphorylationLDIARRPSENLLSNM
CCCCCCCCCCCHHCC		36.9920377248
93PhosphorylationNGGNMLNSFVNSALP
CCHHHHHHHHHHCCC		26.9827017623
116PhosphorylationTRRERPASNSSIGTK
CCCCCCCCCCCCCCC		39.6721440633
118PhosphorylationRERPASNSSIGTKTT
CCCCCCCCCCCCCCC		22.3421440633
119PhosphorylationERPASNSSIGTKTTE
CCCCCCCCCCCCCCE		29.3221440633
122PhosphorylationASNSSIGTKTTEVFS
CCCCCCCCCCCEEEE		24.4521551504
131PhosphorylationTTEVFSSTSASSSLG
CCEEEECCCCCCCCC		27.4121551504
132PhosphorylationTEVFSSTSASSSLGD
CEEEECCCCCCCCCC		28.2721551504
140PhosphorylationASSSLGDTSDEGEGS
CCCCCCCCCCCCCCC		35.9619779198
141PhosphorylationSSSLGDTSDEGEGSD
CCCCCCCCCCCCCCC		38.1028889911
147PhosphorylationTSDEGEGSDADKSKI
CCCCCCCCCCCHHHH		25.8921551504
166PhosphorylationSILMEKATQGRGADG
HHHHHHHHCCCCCCC		42.5019823750
178PhosphorylationADGNGMRSASNNTIV
CCCCCCCCCCCCEEE		27.4422890988
180PhosphorylationGNGMRSASNNTIVEA
CCCCCCCCCCEEEEE		31.6822890988
183PhosphorylationMRSASNNTIVEATTD
CCCCCCCEEEEEECC		30.5622890988
188PhosphorylationNNTIVEATTDGSKMA
CCEEEEEECCHHHHH		16.3519823750
189PhosphorylationNTIVEATTDGSKMAL
CEEEEEECCHHHHHH		45.4719823750
192PhosphorylationVEATTDGSKMALQKS
EEEECCHHHHHHHHH		23.2819823750
199PhosphorylationSKMALQKSMSFDDTA
HHHHHHHHCCCCHHH		13.4922369663
201PhosphorylationMALQKSMSFDDTAAE
HHHHHHCCCCHHHHH		32.3922369663
205PhosphorylationKSMSFDDTAAEKTMN
HHCCCCHHHHHHHHH		29.6119823750
214PhosphorylationAEKTMNKSRHSYQEQ
HHHHHHHHHHCHHHH		30.1621551504
217PhosphorylationTMNKSRHSYQEQFSS
HHHHHHHCHHHHHCC		27.6621440633
218PhosphorylationMNKSRHSYQEQFSSK
HHHHHHCHHHHHCCH		15.2219823750
223PhosphorylationHSYQEQFSSKKSQSS
HCHHHHHCCHHHHHH		40.7319823750
224PhosphorylationSYQEQFSSKKSQSSL
CHHHHHCCHHHHHHH		45.4519823750
227PhosphorylationEQFSSKKSQSSLLNS
HHHCCHHHHHHHHCH		38.7422369663
229PhosphorylationFSSKKSQSSLLNSKQ
HCCHHHHHHHHCHHH		30.0022369663
230PhosphorylationSSKKSQSSLLNSKQR
CCHHHHHHHHCHHHH		29.2822369663
242PhosphorylationKQRSRAKSQTCSSTG
HHHHHHHHHCCCCCC		29.7224930733
244PhosphorylationRSRAKSQTCSSTGYN
HHHHHHHCCCCCCCC		22.8028889911
246PhosphorylationRAKSQTCSSTGYNNS
HHHHHCCCCCCCCCH		34.0321440633
247PhosphorylationAKSQTCSSTGYNNSS
HHHHCCCCCCCCCHH		28.1819779198
266PhosphorylationFGISSKISNSSDRIE
HCCCCCCCCCCCCEE		34.1021440633
269PhosphorylationSSKISNSSDRIEASS
CCCCCCCCCCEEEEE		34.8521551504
275PhosphorylationSSDRIEASSLEFNVP
CCCCEEEEEEEECCC		23.7523607784
276PhosphorylationSDRIEASSLEFNVPS
CCCEEEEEEEECCCC		38.6819779198
283PhosphorylationSLEFNVPSQKPLNCK
EEEECCCCCCCCCCC		46.7023607784
293PhosphorylationPLNCKPLTPSQKYRL
CCCCCCCCHHHHHHH		29.4423607784
295PhosphorylationNCKPLTPSQKYRLRK
CCCCCCHHHHHHHHH		33.7923607784
298PhosphorylationPLTPSQKYRLRKEQS
CCCHHHHHHHHHHHH		13.7724961812
305PhosphorylationYRLRKEQSEMNLRNT
HHHHHHHHHHHHHHH		39.6521440633
312PhosphorylationSEMNLRNTIKRKEKF
HHHHHHHHHHHHHHH		22.8019823750
382PhosphorylationGGLVNDNSEISYTKQ
CCCCCCCCCEEEECC		38.8921551504
385PhosphorylationVNDNSEISYTKQNHR
CCCCCCEEEECCCCC		23.7728889911
387PhosphorylationDNSEISYTKQNHRYS
CCCCEEEECCCCCCC		21.2624961812
436PhosphorylationFIQDTTKSLASVYLH
HHHHHCHHHHHHHHH		27.3719823750
439PhosphorylationDTTKSLASVYLHSSN
HHCHHHHHHHHHHCC		19.3119823750
441PhosphorylationTKSLASVYLHSSNRL
CHHHHHHHHHHCCCC		9.0121440633
444PhosphorylationLASVYLHSSNRLSRS
HHHHHHHHCCCCCHH		27.0619823750
445PhosphorylationASVYLHSSNRLSRSK
HHHHHHHCCCCCHHH		18.4119823750
449PhosphorylationLHSSNRLSRSKLSER
HHHCCCCCHHHHCHH		31.1317287358
451PhosphorylationSSNRLSRSKLSERTK
HCCCCCHHHHCHHHC		34.2719823750
457PhosphorylationRSKLSERTKSSDFLP
HHHHCHHHCCCCCCC		31.0922369663
459PhosphorylationKLSERTKSSDFLPIE
HHCHHHCCCCCCCCC		34.2322369663
460PhosphorylationLSERTKSSDFLPIEL
HCHHHCCCCCCCCCH		33.6622369663
515PhosphorylationHERQINKSMSVASLD
HHHHHHHHHCHHHHH		16.2922890988
517PhosphorylationRQINKSMSVASLDQL
HHHHHHHCHHHHHHH		22.9422369663
520PhosphorylationNKSMSVASLDQLGKN
HHHHCHHHHHHHCCC		30.2622369663
556PhosphorylationDRDITRNSSLQSLSK
CCCCCCCHHHHHHHH		29.1826447709
557PhosphorylationRDITRNSSLQSLSKM
CCCCCCHHHHHHHHH		33.7023749301
560PhosphorylationTRNSSLQSLSKMVWD
CCCHHHHHHHHHHHC		39.6526447709
562PhosphorylationNSSLQSLSKMVWDTP
CHHHHHHHHHHHCCC		24.7726447709
613UbiquitinationTKMGDFPKNKEIEIS
HHCCCCCCCCCCCHH		79.3117644757
615UbiquitinationMGDFPKNKEIEISQL
CCCCCCCCCCCHHHH		67.2217644757
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 SBE22_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SBE22_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 SBE22_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YAJ9_YEASTYAR029Wgenetic
20093466
SWI5_YEASTSWI5genetic
20093466
ASPG1_YEASTASP1genetic
20093466
YOR1_YEASTYOR1genetic
20093466
GPDM_YEASTGUT2genetic
20093466
PLMT_YEASTOPI3genetic
20093466
DCOR_YEASTSPE1genetic
20093466
RHO2_YEASTRHO2genetic
20093466
YVC1_YEASTYVC1genetic
20093466
KIN4_YEASTKIN4genetic
20093466
AIM44_YEASTAIM44genetic
20093466
ZRG17_YEASTZRG17physical
16093310
YAJ9_YEASTYAR029Wgenetic
27708008
SWI5_YEASTSWI5genetic
27708008
SAC3_YEASTSAC3genetic
27708008
ASPG1_YEASTASP1genetic
27708008
BUB1_YEASTBUB1genetic
27708008
YOR1_YEASTYOR1genetic
27708008
VPS53_YEASTVPS53genetic
27708008
DCOR_YEASTSPE1genetic
27708008
HMX1_YEASTHMX1genetic
27708008
PHO80_YEASTPHO80genetic
27708008
YVC1_YEASTYVC1genetic
27708008
AIM44_YEASTAIM44genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SBE22_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-72; SER-201; SER-459;SER-517 AND SER-520, 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-459, 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-449, 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-459, AND MASSSPECTROMETRY.
"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-459, AND MASSSPECTROMETRY.

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