Q9JLV2
Gene name |
Trpc4ap |
Protein name |
Short transient receptor potential channel 4-associated protein |
Names |
Trp4-associated protein, Trpc4-associated protein, Protein TAP1, Rabex-5/Rin2-interacting protein, TNF-receptor ubiquitous scaffolding/signaling protein, Protein TRUSS |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:56407 |
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 Q9JLV2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9JLV2-F1 | Predicted | AlphaFoldDB |
30 variants for Q9JLV2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388601179 | 58 | T>VSDG* | No | EVA | |
| rs3388601660 | 60 | T>I | No | EVA | |
| rs3388605229 | 98 | L>H | No | EVA | |
| rs3388605316 | 162 | M>L | No | EVA | |
| rs3388606594 | 170 | L>M | No | EVA | |
| rs3388605563 | 216 | G>VSDG* | No | EVA | |
| rs3388607468 | 218 | K>E | No | EVA | |
| rs3388596970 | 253 | I>F | No | EVA | |
| rs3388596980 | 276 | S>N | No | EVA | |
| rs3388601652 | 310 | S>* | No | EVA | |
| rs250781560 | 347 | E>D | No | EVA | |
| rs3388601152 | 421 | N>D | No | EVA | |
| rs13466894 | 421 | N>K | No | EVA | |
| rs3388601150 | 448 | C>Y | No | EVA | |
| rs3388601625 | 455 | K>R | No | EVA | |
| rs3392498661 | 459 | L>V | No | EVA | |
| rs3388601144 | 481 | L>P | No | EVA | |
| rs3388601165 | 560 | L>P | No | EVA | |
| rs3388605599 | 591 | K>R | No | EVA | |
| rs3388602956 | 601 | N>S | No | EVA | |
| rs3388598651 | 632 | T>I | No | EVA | |
| rs3388595553 | 636 | D>Y | No | EVA | |
| rs3388603025 | 652 | E>D | No | EVA | |
| rs3388605518 | 662 | V>M | No | EVA | |
| rs3388605552 | 674 | N>K | No | EVA | |
| rs3388605603 | 674 | N>Y | No | EVA | |
| rs3388605724 | 681 | L>Q | No | EVA | |
| rs3388607458 | 720 | K>N | No | EVA | |
| rs3388605299 | 726 | L>F | No | EVA | |
| rs3388601119 | 788 | M>K | No | EVA |
No associated diseases with Q9JLV2
No regional properties for Q9JLV2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q9JLV2 | |||
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| Cul4-RING E3 ubiquitin ligase complex | A ubiquitin ligase complex in which a cullin from the Cul4 family and a RING domain protein form the catalytic core; substrate specificity is conferred by an adaptor protein. |
| Cul4A-RING E3 ubiquitin ligase complex | A ubiquitin ligase complex in which a cullin from the Cul4A subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by an adaptor protein. |
| perinuclear region of cytoplasm | Cytoplasm situated near, or occurring around, the nucleus. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| phosphatase binding | Binding to a phosphatase. |
| ubiquitin ligase-substrate adaptor activity | The binding activity of a molecule that brings together a ubiquitin ligase and its substrate. Usually mediated by F-box BTB/POZ domain proteins. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| hair follicle maturation | A developmental process, independent of morphogenetic (shape) change, that is required for a hair follicle to attain its fully functional state. |
| protein ubiquitination | The process in which one or more ubiquitin groups are added to a protein. |
| ubiquitin-dependent protein catabolic process | The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein. |
| ubiquitin-dependent protein catabolic process via the C-end degron rule pathway | The chemical reactions and pathways resulting in the breakdown of a protein or peptide covalently tagged with ubiquitin, via the DesCEND (destruction via C-end degron) pathway. In the DesCEND pathway, C-terminal residues (C-end degrons) in substrates are recognized by Cul2-RING and Cul4-RING E3 ligases, whereupon the substrates are linked to ubiquitin and then delivered to the proteasome for degradation. C-end degrons can be present in full-length proteins, truncated proteins or proteolytically cleaved forms. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAAAPAAAGA | GASRGRRLAA | TAAAWGGWGG | RPRPGNILLQ | LRQGQLTGRG | LVRAVQFTET |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FLTERDKLSK | WSGIPQLLLK | LYATSHLHSD | FVECQSILKE | ISPLLSMEAM | AFVTEDRKFT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QEATYPNTYI | FDLFGGVDLL | VEILMRPTIS | IRGQKLKISD | EMSKDCLSIL | YNTCVCTEGV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TKRLAEKNDF | VIFLFTLMTS | KKTFLQTATL | IEDILGVKKE | MIRLDEVPNL | SSLVSNFDQQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QLANFCRILA | VTISEMDTGN | DDKHTLLAKN | AQQKKSLSLG | PSAAEINQAA | LLSIPGFVER |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LCKLATRKVS | ESTGTASFLQ | ELEEWYTWLD | NALVLDALMR | VANEESEHNQ | APTVFPSLGT |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SEEGGLPHTS | ARAQLPQSMK | IMHEIMYKLE | VLYVLCVLLM | GRQRNQVHRM | IAEFKLIPGL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| NNLFDKLIWR | KHSASALVLH | GHNQNCDCSP | DITLKIQFLR | LLQSFSDHHE | NKYLLLNNQE |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LNELSAISLK | ANIPEVEAVL | NTDRSLVCDG | KRGLLTRLLQ | VMKKEPAESS | FRFWQARAVE |
| 550 | 560 | 570 | 580 | 590 | 600 |
| SFLRGTTSYA | DQMFLLKRGL | LEHILYCIVD | SECKSRDVLQ | SYFDLLGELM | KFNVDAFKRF |
| 610 | 620 | 630 | 640 | 650 | 660 |
| NKYINTDAKF | QVFLKQINSS | LVDSNMLVRC | VTLSLDRFEN | QVDMKVAEVL | SECRLLAYIS |
| 670 | 680 | 690 | 700 | 710 | 720 |
| QVPTQMSFLF | RLINIIHVQT | LTQENVSCLN | TSLVILMLAR | RKERLPLYLR | LLQRMEHSKK |
| 730 | 740 | 750 | 760 | 770 | 780 |
| YPGFLLNNFH | NLLRFWQQHY | LHKDKDSTCL | ENSSCISFSY | WKETVSILLN | PDRQSPSALV |
| 790 | |||||
| SYIEEPYMDI | DRDFTEE |