GLCE_HUMAN - dbPTM
GLCE_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLCE_HUMAN
UniProt AC O94923
Protein Name D-glucuronyl C5-epimerase
Gene Name GLCE
Organism Homo sapiens (Human).
Sequence Length 617
Subcellular Localization Golgi apparatus membrane
Single-pass type II membrane protein.
Protein Description Converts D-glucuronic acid residues adjacent to N-sulfate sugar residues to L-iduronic acid residues, both in maturing heparan sulfate (HS) and heparin chains. This is important for further modifications that determine the specificity of interactions between these glycosaminoglycans and proteins..
Protein Sequence MRCLAARVNYKTLIIICALFTLVTVLLWNKCSSDKAIQFPRRSSSGFRVDGFEKRAAASESNNYMNHVAKQQSEEAFPQEQQKAPPVVGGFNSNVGSKVLGLKYEEIDCLINDEHTIKGRREGNEVFLPFTWVEKYFDVYGKVVQYDGYDRFEFSHSYSKVYAQRAPYHPDGVFMSFEGYNVEVRDRVKCISGVEGVPLSTQWGPQGYFYPIQIAQYGLSHYSKNLTEKPPHIEVYETAEDRDKNKPNDWTVPKGCFMANVADKSRFTNVKQFIAPETSEGVSLQLGNTKDFIISFDLKFLTNGSVSVVLETTEKNQLFTIHYVSNAQLIAFKERDIYYGIGPRTSWSTVTRDLVTDLRKGVGLSNTKAVKPTKIMPKKVVRLIAKGKGFLDNITISTTAHMAAFFAASDWLVRNQDEKGGWPIMVTRKLGEGFKSLEPGWYSAMAQGQAISTLVRAYLLTKDHIFLNSALRATAPYKFLSEQHGVKAVFMNKHDWYEEYPTTPSSFVLNGFMYSLIGLYDLKETAGEKLGKEARSLYERGMESLKAMLPLYDTGSGTIYDLRHFMLGIAPNLARWDYHTTHINQLQLLSTIDESPVFKEFVKRWKSYLKGSRAKHN
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
43PhosphorylationAIQFPRRSSSGFRVD
CCCCCCCCCCCCCCC		30.0923882029
44PhosphorylationIQFPRRSSSGFRVDG
CCCCCCCCCCCCCCC		32.4427174698
44O-linked_GlycosylationIQFPRRSSSGFRVDG
CCCCCCCCCCCCCCC		32.4455827439
45O-linked_GlycosylationQFPRRSSSGFRVDGF
CCCCCCCCCCCCCCH		43.10OGP
45PhosphorylationQFPRRSSSGFRVDGF
CCCCCCCCCCCCCCH		43.1027174698
54AcetylationFRVDGFEKRAAASES
CCCCCHHHHHHHHHC		45.1130588931
59O-linked_GlycosylationFEKRAAASESNNYMN
HHHHHHHHHCCHHHH		36.5155825171
61O-linked_GlycosylationKRAAASESNNYMNHV
HHHHHHHCCHHHHHH		28.07OGP
73PhosphorylationNHVAKQQSEEAFPQE
HHHHHHHHHHHCCHH		34.6029255136
98UbiquitinationFNSNVGSKVLGLKYE
CCCCCCHHCCCCEEE		35.2321890473
103UbiquitinationGSKVLGLKYEEIDCL
CHHCCCCEEEEEEEE		49.1422817900
104UbiquitinationSKVLGLKYEEIDCLI
HHCCCCEEEEEEEEE		24.6821890473
109UbiquitinationLKYEEIDCLINDEHT
CEEEEEEEEECCCCC		5.1622817900
118UbiquitinationINDEHTIKGRREGNE
ECCCCCCCCCCCCCE		47.7429967540
140PhosphorylationVEKYFDVYGKVVQYD
HHHHHCEECEEEEEC		17.0521253578
225N-linked_GlycosylationGLSHYSKNLTEKPPH
HHHHCCCCCCCCCCC		46.3719159218
302PhosphorylationSFDLKFLTNGSVSVV
EEEEEECCCCCEEEE		40.4426074081
303N-linked_GlycosylationFDLKFLTNGSVSVVL
EEEEECCCCCEEEEE		42.7830872481
305PhosphorylationLKFLTNGSVSVVLET
EEECCCCCEEEEEEE		17.1826074081
307PhosphorylationFLTNGSVSVVLETTE
ECCCCCEEEEEEECC		14.2726074081
371AcetylationLSNTKAVKPTKIMPK
CCCCCCCCCCCCCCH		52.4019817253
393N-linked_GlycosylationKGKGFLDNITISTTA
CCCCCHHCEEEECHH		35.1430872481
409PhosphorylationMAAFFAASDWLVRNQ
HHHHHHHHHHHHHCC		26.3722210691
436PhosphorylationKLGEGFKSLEPGWYS
ECCCCCCCCCCCHHH		35.3923663014
442PhosphorylationKSLEPGWYSAMAQGQ
CCCCCCHHHHHHHHH		7.7723663014
443PhosphorylationSLEPGWYSAMAQGQA
CCCCCHHHHHHHHHH		12.6923663014
458PhosphorylationISTLVRAYLLTKDHI
HHHHHHHHHHCCCHH		7.5318491316
536PhosphorylationKLGKEARSLYERGME
HHHHHHHHHHHHHHH		42.2128796482
538PhosphorylationGKEARSLYERGMESL
HHHHHHHHHHHHHHH		12.5828796482
544PhosphorylationLYERGMESLKAMLPL
HHHHHHHHHHHHHCE		26.6928796482
552PhosphorylationLKAMLPLYDTGSGTI
HHHHHCEEECCCCEE		14.9825072903
554PhosphorylationAMLPLYDTGSGTIYD
HHHCEEECCCCEEEE		21.4925072903
556PhosphorylationLPLYDTGSGTIYDLR
HCEEECCCCEEEEHH		34.5525072903
558PhosphorylationLYDTGSGTIYDLRHF
EEECCCCEEEEHHHH		20.3325072903
560PhosphorylationDTGSGTIYDLRHFML
ECCCCEEEEHHHHHH		14.5722817900
612PhosphorylationWKSYLKGSRAKHN--
HHHHHHCCCCCCC--		27.7223186163
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 GLCE_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GLCE_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 GLCE_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of GLCE_HUMAN !!
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 GLCE_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-225, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-560, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory