PST1_YEAST - dbPTM
PST1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PST1_YEAST
UniProt AC Q12355
Protein Name Cell wall mannoprotein PST1
Gene Name PST1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 444
Subcellular Localization Cell membrane
Lipid-anchor, GPI-anchor. Secreted, cell wall. Identified as GPI-anchored plasma membrane protein (GPI-PMP) as well as non-covalently-linked, soluble protein of the cell wall. Secreted by regenerating protoplasts. In budded cells, conc
Protein Description Has a partially redundant function to ECM33 in cell wall integrity. May be involved in a repair mechanism activated in response to cell wall damage..
Protein Sequence MQLHSLIASTALLITSALAATSSSSSIPSSCTISSHATATAQSDLDKYSRCDTLVGNLTIGGGLKTGALANVKEINGSLTIFNATNLTSFAADSLESITDSLNLQSLTILTSASFGSLQSVDSIKLITLPAISSFTSNIKSANNIYISDTSLQSVDGFSALKKVNVFNVNNNKKLTSIKSPVETVSDSLQFSFNGNQTKITFDDLVWANNISLTDVHSVSFANLQKINSSLGFINNSISSLNFTKLNTIGQTFSIVSNDYLKNLSFSNLSTIGGALVVANNTGLQKIGGLDNLTTIGGTLEVVGNFTSLNLDSLKSVKGGADVESKSSNFSCNALKALQKKGGIKGESFVCKNGASSTSVKLSSTSKSQSSQTTAKVSKSSSKAEEKKFTSGDIKAAASASSVSSSGASSSSSKSSKGNAAIMAPIGQTTPLVGLLTAIIMSIM
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
57N-linked_GlycosylationRCDTLVGNLTIGGGL
CCCEEEECEEECCCC		26.91-
76N-linked_GlycosylationLANVKEINGSLTIFN
CCCCEEECCEEEEEE		34.78-
83N-linked_GlycosylationNGSLTIFNATNLTSF
CCEEEEEECCCCCHH		41.84-
86N-linked_GlycosylationLTIFNATNLTSFAAD
EEEEECCCCCHHHHH		38.62-
133PhosphorylationLITLPAISSFTSNIK
EEEHHHHHHHCCCCC		22.8524909858
134PhosphorylationITLPAISSFTSNIKS
EEHHHHHHHCCCCCC		26.8224909858
136PhosphorylationLPAISSFTSNIKSAN
HHHHHHHCCCCCCCC		23.8624909858
137PhosphorylationPAISSFTSNIKSANN
HHHHHHCCCCCCCCC		34.2524909858
196N-linked_GlycosylationLQFSFNGNQTKITFD
EEEEECCCCCEEECC		47.67-
210N-linked_GlycosylationDDLVWANNISLTDVH
CCEEEECCCCCCCCE		19.9217024473
228N-linked_GlycosylationFANLQKINSSLGFIN
HHHHHHHHHHHCCCC		32.3617024473
235N-linked_GlycosylationNSSLGFINNSISSLN
HHHHCCCCCCHHHCC		33.6617024473
242N-linked_GlycosylationNNSISSLNFTKLNTI
CCCHHHCCCEECCCC		44.4817024473
263N-linked_GlycosylationVSNDYLKNLSFSNLS
ECCHHHHCCCCCCCC		38.02-
268N-linked_GlycosylationLKNLSFSNLSTIGGA
HHCCCCCCCCCCCCE		35.68-
280N-linked_GlycosylationGGALVVANNTGLQKI
CCEEEEECCCCCCEE		34.68-
292N-linked_GlycosylationQKIGGLDNLTTIGGT
CEECCCCCCEEECCE		44.31-
305N-linked_GlycosylationGTLEVVGNFTSLNLD
CEEEEECCCEECCHH		25.97-
327PhosphorylationGADVESKSSNFSCNA
CCCCCCCCCCCCHHH		39.5327017623
328PhosphorylationADVESKSSNFSCNAL
CCCCCCCCCCCHHHH		45.7027017623
329N-linked_GlycosylationDVESKSSNFSCNALK
CCCCCCCCCCHHHHH		39.6817024473
331PhosphorylationESKSSNFSCNALKAL
CCCCCCCCHHHHHHH		15.6527017623
359PhosphorylationKNGASSTSVKLSSTS
CCCCCCCEEEEECCC		21.1428889911
363PhosphorylationSSTSVKLSSTSKSQS
CCCEEEEECCCCCCC		26.3328889911
364PhosphorylationSTSVKLSSTSKSQSS
CCEEEEECCCCCCCC		47.3228889911
365PhosphorylationTSVKLSSTSKSQSSQ
CEEEEECCCCCCCCC		36.4828889911
366PhosphorylationSVKLSSTSKSQSSQT
EEEEECCCCCCCCCE		32.0528889911
368PhosphorylationKLSSTSKSQSSQTTA
EEECCCCCCCCCEEE		34.7528889911
371PhosphorylationSTSKSQSSQTTAKVS
CCCCCCCCCEEEEEC		24.7428889911
373PhosphorylationSKSQSSQTTAKVSKS
CCCCCCCEEEEECCC		30.5728889911
374PhosphorylationKSQSSQTTAKVSKSS
CCCCCCEEEEECCCC		19.4928889911
390PhosphorylationKAEEKKFTSGDIKAA
HHHHCCCCCHHHHHH		40.4519823750
391PhosphorylationAEEKKFTSGDIKAAA
HHHCCCCCHHHHHHH		37.2919823750
399PhosphorylationGDIKAAASASSVSSS
HHHHHHHHCCCCCCC		24.7728889911
401PhosphorylationIKAAASASSVSSSGA
HHHHHHCCCCCCCCC		28.8628889911
402PhosphorylationKAAASASSVSSSGAS
HHHHHCCCCCCCCCC		26.2428889911
404PhosphorylationAASASSVSSSGASSS
HHHCCCCCCCCCCCC		22.2728889911
419GPI-anchorSSKSSKGNAAIMAPI
CCCCCCCCEEEECCC		29.90-
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 PST1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PST1_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 PST1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSP71_YEASTSSA1physical
22940862
SSB1_YEASTSSB1physical
22940862
HSP72_YEASTSSA2physical
22940862
BPH1_YEASTBPH1genetic
23891562
ICS2_YEASTICS2genetic
27708008
PMS1_YEASTPMS1genetic
27708008
DGK1_YEASTDGK1genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
COG3_YEASTCOG3genetic
27708008
NUP57_YEASTNUP57genetic
27708008
ORC4_YEASTORC4genetic
27708008
SCO2_YEASTSCO2genetic
27708008
IML3_YEASTIML3genetic
27708008
YPQ3_YEASTRTC2genetic
27708008
ODPB_YEASTPDB1genetic
27708008
PEX19_YEASTPEX19genetic
27708008
AAD4_YEASTAAD4genetic
27708008
SPR6_YEASTSPR6genetic
27708008
ACOX_YEASTPOX1genetic
27708008
YG1X_YEASTYGR050Cgenetic
27708008
UBCX_YEASTPEX4genetic
27708008
TIM13_YEASTTIM13genetic
27708008
TNA1_YEASTTNA1genetic
27708008
OPI1_YEASTOPI1genetic
27708008
ATP10_YEASTATP10genetic
27708008
RCM1_YEASTRCM1genetic
27708008
YORA4_YEASTYOR114Wgenetic
27708008
RAX1_YEASTRAX1genetic
27708008
UME1_YEASTUME1genetic
27708008
THI6_YEASTTHI6genetic
27708008
UBA3_YEASTUBA3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PST1_YEAST

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Reducing haziness in white wine by overexpression of Saccharomycescerevisiae genes YOL155c and YDR055w.";
Brown S.L., Stockdale V.J., Pettolino F., Pocock K.F.,de Barros Lopes M., Williams P.J., Bacic A., Fincher G.B., Hoej P.B.,Waters E.J.;
Appl. Microbiol. Biotechnol. 73:1363-1376(2007).
Cited for: PROTEIN SEQUENCE OF 48-52; 65-71; 126-146; 164-173; 180-185; 201-225;227-260 AND 327-334, GLYCOSYLATION AT ASN-210; ASN-228; ASN-235;ASN-242 AND ASN-329, FUNCTION, AND BIOTECHNOLOGY.

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