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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
32 | Phosphorylation | MSPATTGTFLLTVYS CCCCCHHHHHHHHHH | 14.71 | 29759185 | |
36 | Phosphorylation | TTGTFLLTVYSIFSK CHHHHHHHHHHHHHH | 21.39 | - | |
38 | Phosphorylation | GTFLLTVYSIFSKVH HHHHHHHHHHHHHHC | 7.27 | - | |
39 | Phosphorylation | TFLLTVYSIFSKVHS HHHHHHHHHHHHHCC | 16.90 | - | |
42 | Phosphorylation | LTVYSIFSKVHSDRN HHHHHHHHHHCCCCC | 31.90 | 24719451 | |
46 | Phosphorylation | SIFSKVHSDRNVYPS HHHHHHCCCCCCCCC | 41.05 | - | |
200 | N-linked_Glycosylation | PERLNAINITSALDR HHHHCCCCCCHHHHC | 29.13 | 19159218 | |
249 | Phosphorylation | PQNQLRCSQEMEPVI HHHCCCCCCCCCCEE | 23.81 | - | |
257 | Phosphorylation | QEMEPVITCDKKFRT CCCCCEEECCHHHCE | 18.19 | - | |
278 | Ubiquitination | CKISLVDKTKQVSTY EEEEEECCCCCCCCH | 50.58 | - | |
280 | Ubiquitination | ISLVDKTKQVSTYQE EEEECCCCCCCCHHH | 55.21 | 21906983 | |
280 | Ubiquitination | ISLVDKTKQVSTYQE EEEECCCCCCCCHHH | 55.21 | 21906983 | |
283 | Phosphorylation | VDKTKQVSTYQEVIR ECCCCCCCCHHHHHC | 20.92 | 26657352 | |
284 | Phosphorylation | DKTKQVSTYQEVIRG CCCCCCCCHHHHHCC | 30.30 | 26657352 | |
285 | Phosphorylation | KTKQVSTYQEVIRGE CCCCCCCHHHHHCCC | 8.65 | 26657352 | |
302 | Ubiquitination | LPDGGEYKPPSDSLK CCCCCCCCCCCHHCC | 46.26 | 21906983 | |
302 | Ubiquitination | LPDGGEYKPPSDSLK CCCCCCCCCCCHHCC | 46.26 | 21906983 | |
337 | Phosphorylation | VLFLILAYIMCCRRE HHHHHHHHHHHHHHH | 5.92 | - | |
353 | Phosphorylation | VEKRNMQTPDIQLVH HHHCCCCCCCCCHHC | 16.50 | 25159151 | |
362 | Phosphorylation | DIQLVHHSAIQKSTK CCCHHCHHHHHHHHH | 16.52 | 28857561 | |
369 | Ubiquitination | SAIQKSTKELRDMSK HHHHHHHHHHHHHHH | 62.94 | - | |
406 | Phosphorylation | PPLHTDNYDSTNMPL CCCCCCCCCCCCCCC | 17.68 | - |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SGCE_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of SGCE_HUMAN !! |
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N-linked Glycosylation | |
Reference | PubMed |
"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. |