6PGL_HUMAN - dbPTM
6PGL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID 6PGL_HUMAN
UniProt AC O95336
Protein Name 6-phosphogluconolactonase
Gene Name PGLS
Organism Homo sapiens (Human).
Sequence Length 258
Subcellular Localization Cytoplasm.
Protein Description Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate..
Protein Sequence MAAPAPGLISVFSSSQELGAALAQLVAQRAACCLAGARARFALGLSGGSLVSMLARELPAAVAPAGPASLARWTLGFCDERLVPFDHAESTYGLYRTHLLSRLPIPESQVITINPELPVEEAAEDYAKKLRQAFQGDSIPVFDLLILGVGPDGHTCSLFPDHPLLQEREKIVAPISDSPKPPPQRVTLTLPVLNAARTVIFVATGEGKAAVLKRILEDQEENPLPAALVQPHTGKLCWFLDEAAARLLTVPFEKHSTL
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
2Acetylation------MAAPAPGLI
------CCCCCCCCE		23.3525944712
10PhosphorylationAPAPGLISVFSSSQE
CCCCCCEEECCCCHH		23.3524043423
13PhosphorylationPGLISVFSSSQELGA
CCCEEECCCCHHHHH		27.2428348404
14PhosphorylationGLISVFSSSQELGAA
CCEEECCCCHHHHHH		25.2828348404
15PhosphorylationLISVFSSSQELGAAL
CEEECCCCHHHHHHH		26.8628464451
46PhosphorylationARFALGLSGGSLVSM
HHHHHCCCCHHHHHH		39.0330183078
49PhosphorylationALGLSGGSLVSMLAR
HHCCCCHHHHHHHHH		29.1722617229
52PhosphorylationLSGGSLVSMLARELP
CCCHHHHHHHHHHCC		17.2423403867
81MethylationTLGFCDERLVPFDHA
HHCCCCCCCCCCCCH		27.95115487241
91PhosphorylationPFDHAESTYGLYRTH
CCCCHHHHHHHHHHH		17.08-
92PhosphorylationFDHAESTYGLYRTHL
CCCHHHHHHHHHHHH		17.89-
128UbiquitinationEAAEDYAKKLRQAFQ
HHHHHHHHHHHHHHC		46.2221906983
176PhosphorylationEKIVAPISDSPKPPP
CEEEECCCCCCCCCC		30.8620068231
178PhosphorylationIVAPISDSPKPPPQR
EEECCCCCCCCCCCC		28.2125159151
180MalonylationAPISDSPKPPPQRVT
ECCCCCCCCCCCCEE		74.2826320211
180AcetylationAPISDSPKPPPQRVT
ECCCCCCCCCCCCEE		74.2819608861
187PhosphorylationKPPPQRVTLTLPVLN
CCCCCCEEEEHHHHC		19.0622210691
198PhosphorylationPVLNAARTVIFVATG
HHHCCCCEEEEEECC		17.1527251275
204PhosphorylationRTVIFVATGEGKAAV
CEEEEEECCCCHHHH		30.3921406692
233O-linked_GlycosylationAALVQPHTGKLCWFL
CHHHCCCCCCCCHHH		42.5723301498
235UbiquitinationLVQPHTGKLCWFLDE
HHCCCCCCCCHHHHH		41.44-
235AcetylationLVQPHTGKLCWFLDE
HHCCCCCCCCHHHHH		41.4426051181
237GlutathionylationQPHTGKLCWFLDEAA
CCCCCCCCHHHHHHH		2.4822555962
249PhosphorylationEAAARLLTVPFEKHS
HHHHHHHCCCCCCCC		30.6321406692
254AcetylationLLTVPFEKHSTL---
HHCCCCCCCCCC---		43.1425953088
2542-HydroxyisobutyrylationLLTVPFEKHSTL---
HHCCCCCCCCCC---		43.14-
254UbiquitinationLLTVPFEKHSTL---
HHCCCCCCCCCC---		43.14-
256PhosphorylationTVPFEKHSTL-----
CCCCCCCCCC-----		42.3323312004
257PhosphorylationVPFEKHSTL------
CCCCCCCCC------		35.8923312004
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 6PGL_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of 6PGL_HUMAN !!
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 6PGL_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZN363_HUMANRCHY1physical
25416956
KRA42_HUMANKRTAP4-2physical
25416956
K1C40_HUMANKRT40physical
25416956
KR109_HUMANKRTAP10-9physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
IMPA1_HUMANIMPA1physical
26344197
IMPA2_HUMANIMPA2physical
26344197
SSNA1_HUMANSSNA1physical
26344197
TALDO_HUMANTALDO1physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of 6PGL_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-180, AND MASS SPECTROMETRY.

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