SAG1_YEAST - dbPTM
SAG1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SAG1_YEAST
UniProt AC P20840
Protein Name Alpha-agglutinin
Gene Name SAG1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 650
Subcellular Localization Secreted, cell wall. Membrane
Lipid-anchor, GPI-anchor. Covalently-linked GPI-modified cell wall protein (GPI-CWP).
Protein Description Cell surface glycoprotein promoting cell-cell contact to facilitate mating. Saccharomyces cerevisiae A and alpha cells express the complementary cell surface glycoproteins A-agglutinin and alpha-, respectively, which interact with one another to promote cellular aggregation during mating..
Protein Sequence MFTFLKIILWLFSLALASAININDITFSNLEITPLTANKQPDQGWTATFDFSIADASSIREGDEFTLSMPHVYRIKLLNSSQTATISLADGTEAFKCYVSQQAAYLYENTTFTCTAQNDLSSYNTIDGSITFSLNFSDGGSSYEYELENAKFFKSGPMLVKLGNQMSDVVNFDPAAFTENVFHSGRSTGYGSFESYHLGMYCPNGYFLGGTEKIDYDSSNNNVDLDCSSVQVYSSNDFNDWWFPQSYNDTNADVTCFGSNLWITLDEKLYDGEMLWVNALQSLPANVNTIDHALEFQYTCLDTIANTTYATQFSTTREFIVYQGRNLGTASAKSSFISTTTTDLTSINTSAYSTGSISTVETGNRTTSEVISHVVTTSTKLSPTATTSLTIAQTSIYSTDSNITVGTDIHTTSEVISDVETISRETASTVVAAPTSTTGWTGAMNTYISQFTSSSFATINSTPIISSSAVFETSDASIVNVHTENITNTAAVPSEEPTFVNATRNSLNSFCSSKQPSSPSSYTSSPLVSSLSVSKTLLSTSFTPSVPTSNTYIKTKNTGYFEHTALTTSSVGLNSFSETAVSSQGTKIDTFLVSSLIAYPSSASGSQLSGIQQNFTSTSLMISTYEGKASIFFSAELGSIIFLLLSYLLF
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
79N-linked_GlycosylationVYRIKLLNSSQTATI
EEEEEECCCCCEEEE		50.48-
109N-linked_GlycosylationQAAYLYENTTFTCTA
CCEEEEECCEEEEEE		30.75-
135N-linked_GlycosylationGSITFSLNFSDGGSS
CEEEEEEECCCCCCC		32.93-
248N-linked_GlycosylationWWFPQSYNDTNADVT
CCCCCCCCCCCCCEE		55.687592821
282O-linked_GlycosylationLWVNALQSLPANVNT
EEHHHHHHCCCCCCC		36.857592821
289O-linked_GlycosylationSLPANVNTIDHALEF
HCCCCCCCHHHHHHH		24.417592821
299O-linked_GlycosylationHALEFQYTCLDTIAN
HHHHHHHHHHHHHCC		8.877592821
303O-linked_GlycosylationFQYTCLDTIANTTYA
HHHHHHHHHCCCCCE		14.727592821
306N-linked_GlycosylationTCLDTIANTTYATQF
HHHHHHCCCCCEEEC		29.157592821
307O-linked_GlycosylationCLDTIANTTYATQFS
HHHHHCCCCCEEECE		16.507592821
308O-linked_GlycosylationLDTIANTTYATQFST
HHHHCCCCCEEECEE		15.807592821
311O-linked_GlycosylationIANTTYATQFSTTRE
HCCCCCEEECEECCE		21.527592821
314O-linked_GlycosylationTTYATQFSTTREFIV
CCCEEECEECCEEEE		21.037592821
315O-linked_GlycosylationTYATQFSTTREFIVY
CCEEECEECCEEEEE		31.037592821
316O-linked_GlycosylationYATQFSTTREFIVYQ
CEEECEECCEEEEEC		27.317592821
329O-linked_GlycosylationYQGRNLGTASAKSSF
ECCCCCCCCCCCCCC		22.177592821
331O-linked_GlycosylationGRNLGTASAKSSFIS
CCCCCCCCCCCCCEE		35.757592821
334O-linked_GlycosylationLGTASAKSSFISTTT
CCCCCCCCCCEEEEC		30.147592821
335O-linked_GlycosylationGTASAKSSFISTTTT
CCCCCCCCCEEEECC		26.377592821
338O-linked_GlycosylationSAKSSFISTTTTDLT
CCCCCCEEEECCCCC		20.077592821
339O-linked_GlycosylationAKSSFISTTTTDLTS
CCCCCEEEECCCCCC		24.287592821
340O-linked_GlycosylationKSSFISTTTTDLTSI
CCCCEEEECCCCCCC		22.407592821
341O-linked_GlycosylationSSFISTTTTDLTSIN
CCCEEEECCCCCCCC		20.577592821
342O-linked_GlycosylationSFISTTTTDLTSINT
CCEEEECCCCCCCCC		27.247592821
345O-linked_GlycosylationSTTTTDLTSINTSAY
EEECCCCCCCCCCCC		30.307592821
346O-linked_GlycosylationTTTTDLTSINTSAYS
EECCCCCCCCCCCCC		22.577592821
349O-linked_GlycosylationTDLTSINTSAYSTGS
CCCCCCCCCCCCCCC		17.057592821
350O-linked_GlycosylationDLTSINTSAYSTGSI
CCCCCCCCCCCCCCC		22.267592821
364N-linked_GlycosylationISTVETGNRTTSEVI
CEEEECCCCCHHHHH		45.61-
402N-linked_GlycosylationSIYSTDSNITVGTDI
EEEECCCCEEECCCE		36.44-
485N-linked_GlycosylationIVNVHTENITNTAAV
EEEEEECCCCCCCCC		47.76-
501N-linked_GlycosylationSEEPTFVNATRNSLN
CCCCCCCCCCHHHHH		31.25-
560PhosphorylationIKTKNTGYFEHTALT
EEECCCCCEEEEEEE		12.0727017623
568PhosphorylationFEHTALTTSSVGLNS
EEEEEEEECCCCCCC		21.6127017623
579PhosphorylationGLNSFSETAVSSQGT
CCCCCCCCCCCCCCC		31.0327017623
614N-linked_GlycosylationQLSGIQQNFTSTSLM
CCCCCCCCCCCCEEE		26.28-
627GPI-anchorLMISTYEGKASIFFS
EEEEEECCCEEEEEE		22.03-
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 SAG1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SAG1_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 SAG1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MNN10_YEASTMNN10genetic
27708008
KPC1_YEASTPKC1genetic
27708008
EXO84_YEASTEXO84genetic
27708008
PRS4_YEASTRPT2genetic
27708008
ARP2_YEASTARP2genetic
27708008
GLE1_YEASTGLE1genetic
27708008
CDC13_YEASTCDC13genetic
27708008
PCF11_YEASTPCF11genetic
27708008
TFB1_YEASTTFB1genetic
27708008
TBP_YEASTSPT15genetic
27708008
ACT_YEASTACT1genetic
27708008
CDC14_YEASTCDC14genetic
27708008
PRS8_YEASTRPT6genetic
27708008
RPN1_YEASTRPN1genetic
27708008
MET30_YEASTMET30genetic
27708008
SWD2_YEASTSWD2genetic
27708008
CDC3_YEASTCDC3genetic
27708008
CDC91_YEASTGAB1genetic
27708008
TIM23_YEASTTIM23genetic
27708008
SMP3_YEASTSMP3genetic
27708008
HRR25_YEASTHRR25genetic
27708008
PSB5_YEASTPRE2genetic
27708008
SNF5_YEASTSNF5genetic
27708008
THRC_YEASTTHR4genetic
27708008
HXKB_YEASTHXK2genetic
27708008
DLT1_YEASTDLT1genetic
27708008
FSH3_YEASTFSH3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SAG1_YEAST

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Structure of Saccharomyces cerevisiae alpha-agglutinin. Evidence fora yeast cell wall protein with multiple immunoglobulin-like domainswith atypical disulfides.";
Chen M.-H., Shen Z.-M., Bobin S., Kahn P.C., Lipke P.N.;
J. Biol. Chem. 270:26168-26177(1995).
Cited for: PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-248; SER-282; THR-289;THR-299; THR-303; ASN-306; THR-307; THR-308; THR-311; SER-314;THR-315; THR-316; THR-329; SER-331; SER-334; SER-335; SER-338;THR-339; THR-340; THR-341; THR-342; THR-345; SER-346; THR-349 ANDSER-350, ABSENCE OF GLYCOSYLATION AT ASN-348, AND DISULFIDE BONDS.
O-linked Glycosylation
ReferencePubMed
"Structure of Saccharomyces cerevisiae alpha-agglutinin. Evidence fora yeast cell wall protein with multiple immunoglobulin-like domainswith atypical disulfides.";
Chen M.-H., Shen Z.-M., Bobin S., Kahn P.C., Lipke P.N.;
J. Biol. Chem. 270:26168-26177(1995).
Cited for: PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-248; SER-282; THR-289;THR-299; THR-303; ASN-306; THR-307; THR-308; THR-311; SER-314;THR-315; THR-316; THR-329; SER-331; SER-334; SER-335; SER-338;THR-339; THR-340; THR-341; THR-342; THR-345; SER-346; THR-349 ANDSER-350, ABSENCE OF GLYCOSYLATION AT ASN-348, AND DISULFIDE BONDS.

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