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 | ||
|
* 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. |