| UniProt ID | SIL1_HUMAN | |
|---|---|---|
| UniProt AC | Q9H173 | |
| Protein Name | Nucleotide exchange factor SIL1 | |
| Gene Name | SIL1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 461 | |
| Subcellular Localization | Endoplasmic reticulum lumen . | |
| Protein Description | Required for protein translocation and folding in the endoplasmic reticulum (ER). Functions as a nucleotide exchange factor for the ER lumenal chaperone HSPA5.. | |
| Protein Sequence | MAPQSLPSSRMAPLGMLLGLLMAACFTFCLSHQNLKEFALTNPEKSSTKETERKETKAEEELDAEVLEVFHPTHEWQALQPGQAVPAGSHVRLNLQTGEREAKLQYEDKFRNNLKGKRLDINTNTYTSQDLKSALAKFKEGAEMESSKEDKARQAEVKRLFRPIEELKKDFDELNVVIETDMQIMVRLINKFNSSSSSLEEKIAALFDLEYYVHQMDNAQDLLSFGGLQVVINGLNSTEPLVKEYAAFVLGAAFSSNPKVQVEAIEGGALQKLLVILATEQPLTAKKKVLFALCSLLRHFPYAQRQFLKLGGLQVLRTLVQEKGTEVLAVRVVTLLYDLVTEKMFAEEEAELTQEMSPEKLQQYRQVHLLPGLWEQGWCEITAHLLALPEHDAREKVLQTLGVLLTTCRDRYRQDPQLGRTLASLQAEYQVLASLELQDGEDEGYFQELLGSVNSLLKELR | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 5 | Phosphorylation | ---MAPQSLPSSRMA ---CCCCCCCCCCHH | 40.98 | 29255136 | |
| 8 | Phosphorylation | MAPQSLPSSRMAPLG CCCCCCCCCCHHHHH | 35.55 | 29255136 | |
| 8 | O-linked_Glycosylation | MAPQSLPSSRMAPLG CCCCCCCCCCHHHHH | 35.55 | 23301498 | |
| 9 | Phosphorylation | APQSLPSSRMAPLGM CCCCCCCCCHHHHHH | 24.92 | 29255136 | |
| 41 | O-linked_Glycosylation | NLKEFALTNPEKSST CHHHHHHHCCCCCCC | 45.35 | 55828421 | |
| 45 | Ubiquitination | FALTNPEKSSTKETE HHHHCCCCCCCHHHH | 51.46 | - | |
| 46 | O-linked_Glycosylation | ALTNPEKSSTKETER HHHCCCCCCCHHHHH | 41.39 | 55828427 | |
| 47 | O-linked_Glycosylation | LTNPEKSSTKETERK HHCCCCCCCHHHHHH | 55.34 | 55828433 | |
| 48 | O-linked_Glycosylation | TNPEKSSTKETERKE HCCCCCCCHHHHHHH | 39.74 | 55828437 | |
| 49 | Ubiquitination | NPEKSSTKETERKET CCCCCCCHHHHHHHH | 65.67 | - | |
| 54 | Acetylation | STKETERKETKAEEE CCHHHHHHHHHHHHH | 64.60 | 11412715 | |
| 73 | O-linked_Glycosylation | VLEVFHPTHEWQALQ HHHHHCCCCCCCCCC | 24.69 | OGP | |
| 97 | O-linked_Glycosylation | HVRLNLQTGEREAKL EEEEECCCCCCCHHH | 44.14 | 55828761 | |
| 106 | Phosphorylation | EREAKLQYEDKFRNN CCCHHHHHHHHHHHH | 36.21 | - | |
| 109 | Methylation | AKLQYEDKFRNNLKG HHHHHHHHHHHHCCC | 33.99 | 23644510 | |
| 109 | Ubiquitination | AKLQYEDKFRNNLKG HHHHHHHHHHHHCCC | 33.99 | - | |
| 123 | O-linked_Glycosylation | GKRLDINTNTYTSQD CCEEECCCCCCCHHH | 29.31 | OGP | |
| 123 | Phosphorylation | GKRLDINTNTYTSQD CCEEECCCCCCCHHH | 29.31 | 20873877 | |
| 125 | Phosphorylation | RLDINTNTYTSQDLK EEECCCCCCCHHHHH | 26.58 | 20873877 | |
| 126 | Phosphorylation | LDINTNTYTSQDLKS EECCCCCCCHHHHHH | 13.38 | 20873877 | |
| 127 | O-linked_Glycosylation | DINTNTYTSQDLKSA ECCCCCCCHHHHHHH | 20.20 | 55825063 | |
| 127 | Phosphorylation | DINTNTYTSQDLKSA ECCCCCCCHHHHHHH | 20.20 | 20873877 | |
| 128 | O-linked_Glycosylation | INTNTYTSQDLKSAL CCCCCCCHHHHHHHH | 15.98 | 55825069 | |
| 128 | Phosphorylation | INTNTYTSQDLKSAL CCCCCCCHHHHHHHH | 15.98 | 20873877 | |
| 132 | Ubiquitination | TYTSQDLKSALAKFK CCCHHHHHHHHHHHH | 41.81 | - | |
| 146 | Phosphorylation | KEGAEMESSKEDKAR HHHCCCCCCHHHHHH | 45.45 | 29255136 | |
| 147 | Phosphorylation | EGAEMESSKEDKARQ HHCCCCCCHHHHHHH | 27.10 | 26657352 | |
| 193 | N-linked_Glycosylation | VRLINKFNSSSSSLE HHHHHHCCCCCCCHH | 42.46 | 19159218 | |
| 236 | N-linked_Glycosylation | QVVINGLNSTEPLVK EEEECCCCCCCHHHH | 48.56 | UniProtKB CARBOHYD | |
| 286 | 2-Hydroxyisobutyrylation | TEQPLTAKKKVLFAL CCCCCCHHHHHHHHH | 48.14 | - | |
| 309 | Ubiquitination | YAQRQFLKLGGLQVL HHHHHHHHHCCHHHH | 46.50 | 21890473 | |
| 323 | Ubiquitination | LRTLVQEKGTEVLAV HHHHHHHCCCHHHHH | 54.78 | 21890473 | |
| 396 | Ubiquitination | PEHDAREKVLQTLGV CCCHHHHHHHHHHHH | 42.57 | - | |
| 400 | Phosphorylation | AREKVLQTLGVLLTT HHHHHHHHHHHHHHH | 22.71 | 20068231 | |
| 406 | Phosphorylation | QTLGVLLTTCRDRYR HHHHHHHHHHHHHHH | 21.49 | 20068231 | |
| 407 | Phosphorylation | TLGVLLTTCRDRYRQ HHHHHHHHHHHHHHH | 12.91 | 20068231 | |
| 455 | Phosphorylation | ELLGSVNSLLKELR- HHHHHHHHHHHHHC- | 32.68 | 24719451 |
| 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 SIL1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SIL1_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 SIL1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| GRP78_HUMAN | HSPA5 | physical | 25877869 | |
| POC1A_HUMAN | POC1A | physical | 28514442 | |
| POC1B_HUMAN | POC1B | physical | 28514442 | |
| EDRF1_HUMAN | EDRF1 | physical | 28514442 | |
| CNTP1_HUMAN | CNTNAP1 | physical | 28514442 | |
| ERGI2_HUMAN | ERGIC2 | physical | 28514442 | |
| GRP78_HUMAN | HSPA5 | physical | 28514442 | |
| PON2_HUMAN | PON2 | physical | 28514442 | |
| UBR1_HUMAN | UBR1 | physical | 28514442 | |
| UBR2_HUMAN | UBR2 | physical | 28514442 | |
| COEA1_HUMAN | COL14A1 | physical | 28514442 | |
| OMA1_HUMAN | OMA1 | physical | 28514442 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 248800 | Marinesco-Sjoegren syndrome (MSS) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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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-193, AND MASSSPECTROMETRY. | |