GLGB_YEAST - dbPTM
GLGB_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLGB_YEAST
UniProt AC P32775
Protein Name 1,4-alpha-glucan-branching enzyme
Gene Name GLC3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 704
Subcellular Localization
Protein Description
Protein Sequence MYNIPDNVKGAVEFDPWLKPFADVLSERRYLADKWLYDITHATPDGSYQSLSKFARDSYKSYGLHANPETKEITYKEWAPNAERAFLVGDFNNWDTTSHELKNKDEFGNFTITLHPLPNGDFAIPHDSKIKVMFILPDGSKIFRLPAWITRATQPSKETSKQFGPAYEGRFWNPENPYKFVHPRPKFSESVDSLRIYEAHVGISSPEPKITTYKEFTEKVLPRIKYLGYDAIQLMAIMEHAYYASFGYQVTNFFAASSRFGTPEELKELIDTAHSMGILVLLDVVHSHASKNVEDGLNMFDGSDHQYFHSISSGRGEHPLWDSRLFNYGKFEVQRFLLANLAFYVDVYQFDGFRFDGVTSMLYVHHGVGAGGSFSGDYNEYLSRDRSFVDHEALAYLMLANDLVHEMLPNLAVTVAEDVSGYPTLCLPRSIGGTGFDYRLAMALPDMWIKLIKEKKDDEWEMGSIVYTLTNRRYGEKVVAYCESHDQALVGDKTLAFWLMDAAMYTDMTVLKEPSIVIDRGIALHKMIRLITHSLGGEAYLNFEGNEFGHPEWLDFPNVNNGDSYKYARRQFNLADDPLLRYQNLNEFDRSMQLCEKRHKWLNTKQAYVSLKHEGDKMIVFERNNLLFIFNFHPTNSYSDYRVGVEKAGTYHIVLNSDRAEFGGHNRINESSEFFTTDLEWNNRKNFLQVYIPSRVALVLALKE
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
62PhosphorylationARDSYKSYGLHANPE
HHHHHHHCCCCCCCC		21.3927017623
70PhosphorylationGLHANPETKEITYKE
CCCCCCCCCCCCHHH		34.9227017623
179AcetylationWNPENPYKFVHPRPK
CCCCCCCCCCCCCCC		42.0124489116
186AcetylationKFVHPRPKFSESVDS
CCCCCCCCCCCCCCC		63.9024489116
188PhosphorylationVHPRPKFSESVDSLR
CCCCCCCCCCCCCEE		34.7828889911
190PhosphorylationPRPKFSESVDSLRIY
CCCCCCCCCCCEEEE		29.9922369663
193PhosphorylationKFSESVDSLRIYEAH
CCCCCCCCEEEEEEE		19.8622369663
204PhosphorylationYEAHVGISSPEPKIT
EEEECCCCCCCCCCC		33.6322369663
205PhosphorylationEAHVGISSPEPKITT
EEECCCCCCCCCCCC		31.2122369663
330AcetylationSRLFNYGKFEVQRFL
CCCCCCCHHHHHHHH		28.1724489116
359PhosphorylationGFRFDGVTSMLYVHH
CEEEECCEEEEEEEC		17.5919779198
360PhosphorylationFRFDGVTSMLYVHHG
EEEECCEEEEEEECC		12.3719779198
363PhosphorylationDGVTSMLYVHHGVGA
ECCEEEEEEECCCCC		6.7919779198
375PhosphorylationVGAGGSFSGDYNEYL
CCCCCCCCCCHHHHH		32.2419779198
378PhosphorylationGGSFSGDYNEYLSRD
CCCCCCCHHHHHCCC		17.2619779198
381PhosphorylationFSGDYNEYLSRDRSF
CCCCHHHHHCCCCCC		13.3119779198
383PhosphorylationGDYNEYLSRDRSFVD
CCHHHHHCCCCCCCC		31.1019779198
430PhosphorylationPTLCLPRSIGGTGFD
CEEECCCCCCCCCHH		24.5228889911
467PhosphorylationWEMGSIVYTLTNRRY
CCCCEEEEEHHCCCC		8.3830377154
468PhosphorylationEMGSIVYTLTNRRYG
CCCEEEEEHHCCCCC		19.0630377154
470PhosphorylationGSIVYTLTNRRYGEK
CEEEEEHHCCCCCCE		20.9127017623
474PhosphorylationYTLTNRRYGEKVVAY
EEHHCCCCCCEEEEE		26.8027017623
597UbiquitinationRSMQLCEKRHKWLNT
HHHHHHHHHHHHCCC		59.8223749301
605UbiquitinationRHKWLNTKQAYVSLK
HHHHCCCCCEEEEEE		31.6823749301
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 GLGB_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GLGB_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 GLGB_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TPS1_YEASTTPS1genetic
20093466
EMC4_YEASTEMC4genetic
20093466
ASK10_YEASTASK10genetic
20093466
COX12_YEASTCOX12genetic
20093466
TPS1_YEASTTPS1genetic
20427572
BPH1_YEASTBPH1genetic
23891562
ASK10_YEASTASK10genetic
27708008
TPS1_YEASTTPS1genetic
27708008
DAL81_YEASTDAL81genetic
27708008
CBT1_YEASTCBT1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GLGB_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-190, AND MASSSPECTROMETRY.

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