SGCE_HUMAN - dbPTM
SGCE_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SGCE_HUMAN
UniProt AC O43556
Protein Name Epsilon-sarcoglycan
Gene Name SGCE
Organism Homo sapiens (Human).
Sequence Length 437
Subcellular Localization Cell membrane, sarcolemma
Single-pass membrane protein. Cytoplasm, cytoskeleton. Cell projection, dendrite. Golgi apparatus.
Protein Description Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix..
Protein Sequence MQLPRWWELGDPCAWTGQGRGTRRMSPATTGTFLLTVYSIFSKVHSDRNVYPSAGVLFVHVLEREYFKGEFPPYPKPGEISNDPITFNTNLMGYPDRPGWLRYIQRTPYSDGVLYGSPTAENVGKPTIIEITAYNRRTFETARHNLIINIMSAEDFPLPYQAEFFIKNMNVEEMLASEVLGDFLGAVKNVWQPERLNAINITSALDRGGRVPLPINDLKEGVYVMVGADVPFSSCLREVENPQNQLRCSQEMEPVITCDKKFRTQFYIDWCKISLVDKTKQVSTYQEVIRGEGILPDGGEYKPPSDSLKSRDYYTDFLITLAVPSAVALVLFLILAYIMCCRREGVEKRNMQTPDIQLVHHSAIQKSTKELRDMSKNREIAWPLSTLPVFHPVTGEIIPPLHTDNYDSTNMPLMQTQQNLPHQTQIPQQQTTGKWYP
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
32PhosphorylationMSPATTGTFLLTVYS
CCCCCHHHHHHHHHH
14.7129759185
36PhosphorylationTTGTFLLTVYSIFSK
CHHHHHHHHHHHHHH
21.39-
38PhosphorylationGTFLLTVYSIFSKVH
HHHHHHHHHHHHHHC
7.27-
39PhosphorylationTFLLTVYSIFSKVHS
HHHHHHHHHHHHHCC
16.90-
42PhosphorylationLTVYSIFSKVHSDRN
HHHHHHHHHHCCCCC
31.9024719451
46PhosphorylationSIFSKVHSDRNVYPS
HHHHHHCCCCCCCCC
41.05-
200N-linked_GlycosylationPERLNAINITSALDR
HHHHCCCCCCHHHHC
29.1319159218
249PhosphorylationPQNQLRCSQEMEPVI
HHHCCCCCCCCCCEE
23.81-
257PhosphorylationQEMEPVITCDKKFRT
CCCCCEEECCHHHCE
18.19-
278UbiquitinationCKISLVDKTKQVSTY
EEEEEECCCCCCCCH
50.58-
280UbiquitinationISLVDKTKQVSTYQE
EEEECCCCCCCCHHH
55.2121906983
280UbiquitinationISLVDKTKQVSTYQE
EEEECCCCCCCCHHH
55.2121906983
283PhosphorylationVDKTKQVSTYQEVIR
ECCCCCCCCHHHHHC
20.9226657352
284PhosphorylationDKTKQVSTYQEVIRG
CCCCCCCCHHHHHCC
30.3026657352
285PhosphorylationKTKQVSTYQEVIRGE
CCCCCCCHHHHHCCC
8.6526657352
302UbiquitinationLPDGGEYKPPSDSLK
CCCCCCCCCCCHHCC
46.2621906983
302UbiquitinationLPDGGEYKPPSDSLK
CCCCCCCCCCCHHCC
46.2621906983
337PhosphorylationVLFLILAYIMCCRRE
HHHHHHHHHHHHHHH
5.92-
353PhosphorylationVEKRNMQTPDIQLVH
HHHCCCCCCCCCHHC
16.5025159151
362PhosphorylationDIQLVHHSAIQKSTK
CCCHHCHHHHHHHHH
16.5228857561
369UbiquitinationSAIQKSTKELRDMSK
HHHHHHHHHHHHHHH
62.94-
406PhosphorylationPPLHTDNYDSTNMPL
CCCCCCCCCCCCCCC
17.68-

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 SGCE_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SGCE_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 SGCE_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SGCE_HUMAN !!

Drug and Disease Associations
Kegg Disease
H00831 Primary dystonia
OMIM Disease
159900Dystonia 11 (DYT11)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SGCE_HUMAN

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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-200, AND MASSSPECTROMETRY.

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