EXG1_YEAST - dbPTM
EXG1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EXG1_YEAST
UniProt AC P23776
Protein Name Glucan 1,3-beta-glucosidase I/II
Gene Name EXG1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 448
Subcellular Localization Secreted, cell wall . Secreted .
Protein Description Glucanases possibly play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme hydrolyzes both 1,3-beta- and 1,6-beta-linkages and even has beta-glucosidase activity. It could also function biosynthetically as a transglycosylase..
Protein Sequence MLSLKTLLCTLLTVSSVLATPVPARDPSSIQFVHEENKKRYYDYDHGSLGEPIRGVNIGGWLLLEPYITPSLFEAFRTNDDNDEGIPVDEYHFCQYLGKDLAKSRLQSHWSTFYQEQDFANIASQGFNLVRIPIGYWAFQTLDDDPYVSGLQESYLDQAIGWARNNSLKVWVDLHGAAGSQNGFDNSGLRDSYKFLEDSNLAVTTNVLNYILKKYSAEEYLDTVIGIELINEPLGPVLDMDKMKNDYLAPAYEYLRNNIKSDQVIIIHDAFQPYNYWDDFMTENDGYWGVTIDHHHYQVFASDQLERSIDEHIKVACEWGTGVLNESHWTVCGEFAAALTDCTKWLNSVGFGARYDGSWVNGDQTSSYIGSCANNDDIAYWSDERKENTRRYVEAQLDAFEMRGGWIIWCYKTESSLEWDAQRLMFNGLFPQPLTDRKYPNQCGTISN
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
99UbiquitinationHFCQYLGKDLAKSRL
HHHHHHCHHHHHHHH		47.1517644757
99AcetylationHFCQYLGKDLAKSRL
HHHHHHCHHHHHHHH		47.1524489116
165N-linked_GlycosylationQAIGWARNNSLKVWV
HHHHHHHCCCCEEEE		34.3914730348
194UbiquitinationSGLRDSYKFLEDSNL
CCCCHHHHHHHCCCC		47.6417644757
213UbiquitinationNVLNYILKKYSAEEY
HHHHHHHHHCCHHHH		39.8617644757
214UbiquitinationVLNYILKKYSAEEYL
HHHHHHHHCCHHHHH		40.7817644757
325N-linked_GlycosylationEWGTGVLNESHWTVC
HCCCCCCCCCCCEEH		46.4414730348
344UbiquitinationAALTDCTKWLNSVGF
HHHHHHHHHHHHCCC		56.8917644757
438UbiquitinationPQPLTDRKYPNQCGT
CCCCCCCCCCCCCCC		68.8023749301
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 EXG1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EXG1_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 EXG1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RS8A_YEASTRPS8Agenetic
20093466
RS8B_YEASTRPS8Agenetic
20093466
CSG2_YEASTCSG2genetic
20093466
CCZ1_YEASTCCZ1genetic
20093466
SEC66_YEASTSEC66genetic
20093466
BEM1_YEASTBEM1genetic
20093466
CHK1_YEASTCHK1genetic
20093466
PER1_YEASTPER1genetic
20093466
MTU1_YEASTSLM3genetic
20093466
NHP10_YEASTNHP10genetic
20093466
PAA1_YEASTPAA1genetic
20093466
WDR59_YEASTMTC5genetic
20093466
ENT5_YEASTENT5genetic
20093466
MNN10_YEASTMNN10genetic
20093466
SSD1_YEASTSSD1genetic
20093466
EF2_YEASTEFT2genetic
20093466
EMI1_YEASTEMI1genetic
20093466
PT122_YEASTPET122genetic
20093466
IES1_YEASTIES1genetic
20093466
MTO1_YEASTMTO1genetic
20093466
YGY5_YEASTYGL235Wgenetic
20093466
VAM7_YEASTVAM7genetic
20093466
MED5_YEASTNUT1genetic
20093466
PALF_YEASTRIM8genetic
20093466
PACC_YEASTRIM101genetic
20093466
HAP4_YEASTHAP4genetic
20093466
IXR1_YEASTIXR1genetic
20093466
COX12_YEASTCOX12genetic
20093466
SIC1_YEASTSIC1genetic
20093466
CDC73_YEASTCDC73genetic
20093466
TSA1_YEASTTSA1genetic
20093466
MSS1_YEASTMSS1genetic
20093466
FUS2_YEASTFUS2genetic
20093466
ADE_YEASTAAH1genetic
20093466
ATP23_YEASTATP23genetic
20093466
MNE1_YEASTMNE1genetic
20093466
NCBP2_YEASTCBC2genetic
20093466
SYH1_YEASTSYH1genetic
20093466
MID2_YEASTMID2genetic
20526336
SWA2_YEASTSWA2genetic
20526336
ERG2_YEASTERG2genetic
21623372
CHK1_YEASTCHK1genetic
22282571
CHO2_YEASTCHO2genetic
27708008
EDE1_YEASTEDE1genetic
27708008
CSG2_YEASTCSG2genetic
27708008
SEC66_YEASTSEC66genetic
27708008
CHK1_YEASTCHK1genetic
27708008
RV161_YEASTRVS161genetic
27708008
RIM1_YEASTRIM1genetic
27708008
MTU1_YEASTSLM3genetic
27708008
BRE1_YEASTBRE1genetic
27708008
VPS41_YEASTVPS41genetic
27708008
WDR59_YEASTMTC5genetic
27708008
ENT5_YEASTENT5genetic
27708008
MNN10_YEASTMNN10genetic
27708008
PMP3_YEASTPMP3genetic
27708008
EF2_YEASTEFT2genetic
27708008
UBP3_YEASTUBP3genetic
27708008
PT122_YEASTPET122genetic
27708008
IES1_YEASTIES1genetic
27708008
HSP12_YEASTHSP12genetic
27708008
FAR7_YEASTFAR7genetic
27708008
UBP6_YEASTUBP6genetic
27708008
PALF_YEASTRIM8genetic
27708008
MRM2_YEASTMRM2genetic
27708008
MED5_YEASTNUT1genetic
27708008
HUR1_YEASTHUR1genetic
27708008
MTO1_YEASTMTO1genetic
27708008
SMI1_YEASTSMI1genetic
27708008
HSE1_YEASTHSE1genetic
27708008
SNF6_YEASTSNF6genetic
27708008
CYP7_YEASTCPR7genetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
ILM1_YEASTILM1genetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
IXR1_YEASTIXR1genetic
27708008
DOA1_YEASTDOA1genetic
27708008
COX12_YEASTCOX12genetic
27708008
SIC1_YEASTSIC1genetic
27708008
MSS1_YEASTMSS1genetic
27708008
RIM13_YEASTRIM13genetic
27708008
ATP23_YEASTATP23genetic
27708008
WHI2_YEASTWHI2genetic
27708008
MNE1_YEASTMNE1genetic
27708008
NCBP2_YEASTCBC2genetic
27708008
MSS18_YEASTMSS18genetic
27708008
VPS4_YEASTVPS4genetic
27708008
QCR2_YEASTQCR2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EXG1_YEAST

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"The ER protein folding sensor UDP-glucose glycoprotein-glucosyltransferase modifies substrates distant to local changes inglycoprotein conformation.";
Taylor S.C., Ferguson A.D., Bergeron J.J.M., Thomas D.Y.;
Nat. Struct. Mol. Biol. 11:128-134(2004).
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 41-448, AND GLYCOSYLATION ATASN-165 AND ASN-325.

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