| UniProt ID | S61A1_MOUSE | |
|---|---|---|
| UniProt AC | P61620 | |
| Protein Name | Protein transport protein Sec61 subunit alpha isoform 1 | |
| Gene Name | Sec61a1 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 476 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . Localizes exclusively in granular structures in the endoplasmic reticulum (ER). |
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| Protein Description | Plays a crucial role in the insertion of secretory and membrane polypeptides into the ER. Required for assembly of membrane and secretory proteins. Tightly associated with membrane-bound ribosomes, either directly or through adapter proteins (By similarity). Plays a role in the pronephric kidney tubule development. [PubMed: 27392076] | |
| Protein Sequence | MAIKFLEVIKPFCVILPEIQKPERKIQFKEKVLWTAITLFIFLVCCQIPLFGIMSSDSADPFYWMRVILASNRGTLMELGISPIVTSGLIMQLLAGAKIIEVGDTPKDRALFNGAQKLFGMIITIGQSIVYVMTGMYGDPSEMGAGICLLITIQLFVAGLIVLLLDELLQKGYGLGSGISLFIATNICETIVWKAFSPTTVNTGRGMEFEGAIIALFHLLATRTDKVRALREAFYRQNLPNLMNLIATIFVFAVVIYFQGFRVDLPIKSARYRGQYNTYPIKLFYTSNIPIILQSALVSNLYVISQMLSARFSGNLLVSLLGTWSDTSSGGPARAYPVGGLCYYLSPPESFGSVLEDPVHAVVYIVFMLGSCAFFSKTWIEVSGSSAKDVAKQLKEQQMVMRGHRETSMVHELNRYIPTAAAFGGLCIGALSVLADFLGAIGSGTGILLAVTIIYQYFEIFVKEQSEVGSMGALLF | |
| 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 |
|---|---|---|---|---|---|
| 10 | Acetylation | IKFLEVIKPFCVILP HHHHHHHHHHEEECC | 36.90 | 22826441 | |
| 13 | S-nitrosocysteine | LEVIKPFCVILPEIQ HHHHHHHEEECCCCC | 2.23 | - | |
| 13 | S-palmitoylation | LEVIKPFCVILPEIQ HHHHHHHEEECCCCC | 2.23 | 28526873 | |
| 13 | S-nitrosylation | LEVIKPFCVILPEIQ HHHHHHHEEECCCCC | 2.23 | 22178444 | |
| 13 | Glutathionylation | LEVIKPFCVILPEIQ HHHHHHHEEECCCCC | 2.23 | 24333276 | |
| 107 | Acetylation | IEVGDTPKDRALFNG EEECCCHHHHHHHCH | 63.04 | 23954790 | |
| 107 | Succinylation | IEVGDTPKDRALFNG EEECCCHHHHHHHCH | 63.04 | 23954790 | |
| 107 | Malonylation | IEVGDTPKDRALFNG EEECCCHHHHHHHCH | 63.04 | 26320211 | |
| 287 | Phosphorylation | PIKLFYTSNIPIILQ CEEEEEECCCCHHHH | 22.76 | - | |
| 295 | Phosphorylation | NIPIILQSALVSNLY CCCHHHHHHHHHHHH | 21.81 | - | |
| 392 | Ubiquitination | SSAKDVAKQLKEQQM CCHHHHHHHHHHHHH | 56.88 | 22790023 | |
| 392 | Acetylation | SSAKDVAKQLKEQQM CCHHHHHHHHHHHHH | 56.88 | 2393157 | |
| 395 | Malonylation | KDVAKQLKEQQMVMR HHHHHHHHHHHHHHH | 51.49 | 26320211 | |
| 395 | Ubiquitination | KDVAKQLKEQQMVMR HHHHHHHHHHHHHHH | 51.49 | 27667366 | |
| 407 | Phosphorylation | VMRGHRETSMVHELN HHHCCHHHHHHHHHH | 23.29 | 28833060 | |
| 408 | Phosphorylation | MRGHRETSMVHELNR HHCCHHHHHHHHHHH | 17.66 | 26824392 | |
| 466 | Phosphorylation | EIFVKEQSEVGSMGA HHHCHHHCCCCCCCH | 35.03 | 28066266 | |
| 470 | Phosphorylation | KEQSEVGSMGALLF- HHHCCCCCCCHHCC- | 21.15 | 28066266 |
| 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 S61A1_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of S61A1_MOUSE !! | ||||||
* 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 S61A1_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| HYOU1_MOUSE | Hyou1 | physical | 24218449 | |
| CHIP_MOUSE | Stub1 | physical | 24218449 | |
| TERA_MOUSE | Vcp | physical | 24218449 | |
| PSN1_MOUSE | Psen1 | physical | 20541250 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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