Q924Z5
Gene name |
Tram2 |
Protein name |
Translocating chain-associated membrane protein 2 |
Names |
|
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:170829 |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q924Z5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q924Z5-F1 | Predicted | AlphaFoldDB |
26 variants for Q924Z5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388459091 | 42 | T>I | No | EVA | |
| rs3388460166 | 59 | P>S | No | EVA | |
| rs3389711843 | 65 | T>S | No | EVA | |
| rs3388459238 | 68 | Y>F | No | EVA | |
| rs3388459192 | 95 | Y>N | No | EVA | |
| rs3389688220 | 101 | S>* | No | EVA | |
| rs3389688220 | 101 | S>L | No | EVA | |
| rs3389649974 | 104 | L>H | No | EVA | |
| rs3388459872 | 130 | W>L | No | EVA | |
| rs3388460173 | 132 | F>I | No | EVA | |
| rs36818066 | 136 | V>I | No | EVA | |
| rs3388461301 | 140 | Y>F | No | EVA | |
| rs3388460040 | 194 | Y>* | No | EVA | |
| rs3388460187 | 206 | Y>H | No | EVA | |
| rs3389711811 | 228 | F>L | No | EVA | |
| rs3389722244 | 228 | F>Y | No | EVA | |
| rs3388459049 | 233 | L>F | No | EVA | |
| rs3388459009 | 245 | F>Y | No | EVA | |
| rs3413018967 | 278 | V>L | No | EVA | |
| rs3388459806 | 290 | P>T | No | EVA | |
| rs864262112 | 291 | C>S | No | EVA | |
| rs3388460124 | 326 | S>N | No | EVA | |
| rs260142904 | 329 | R>H | No | EVA | |
| rs236000505 | 334 | V>A | No | EVA | |
| rs220774931 | 337 | P>L | No | EVA | |
| rs3388459335 | 349 | H>Q | No | EVA |
No associated diseases with Q924Z5
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| integral component of endoplasmic reticulum membrane | The component of the endoplasmic reticulum membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
No GO annotations of molecular function
| Name | Definition |
|---|---|
| No GO annotations for molecular function |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| collagen biosynthetic process | The chemical reactions and pathways resulting in the formation of collagen, any of a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals. Collagen is highly enriched in glycine (some regions are 33% glycine) and proline, occurring predominantly as 3-hydroxyproline (about 20%). |
| protein insertion into ER membrane | The process that results in incorporation of a protein into an endoplasmic reticulum (ER) membrane. It depends on specific topogenic sequences of amino acids that ensure that a protein acquires the proper orientation during its insertion into the ER membrane. |
| SRP-dependent cotranslational protein targeting to membrane, translocation | The process during cotranslational membrane targeting wherein proteins move across a membrane. SRP and its receptor initiate the transfer of the nascent chain across the endoplasmic reticulum (ER) membrane; they then dissociate from the chain, which is transferred to a set of transmembrane proteins, collectively called the translocon. Once the nascent chain translocon complex is assembled, the elongating chain passes directly from the large ribosomal subunit into the centers of the translocon, a protein-lined channel within the membrane. The growing chain is never exposed to the cytosol and does not fold until it reaches the ER lumen. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q15035 | TRAM2 | Translocating chain-associated membrane protein 2 | Homo sapiens (Human) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAFRRRTKSY | PLFSQEFIIH | NHADIGFCLV | LCVLIGLMFE | VTAKTAFLFI | LPQYNISVPT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ADSETVHYHY | GPKDLVTILF | YVVITIIFHA | VVQEYILDKI | SKRLHLSKVK | HSKFNESGQL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LVFHLSAVAW | CFYVIVTEGY | LTNPRSLWED | YPHVYLSFQV | KFFYLGQLAY | WLHSLPELYF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QKVRKEEVPR | QLQYICLYLL | HITGAYLLNL | SRLGLILLLL | QYSTEALFHM | ARLFHFADEN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NERLFNAWAA | VFGVTRLFIL | TLAVLTIGFG | LARVENQVFD | PEKGNFNTLP | CRLGMLLLVC |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VAQAWLMWRF | IHSQLRHWRE | YWKEQSAKRR | VSAVPRPPAK | LLKREPGYHE | NGVVKAENGT |
| SSRTKKLKSP |