Q9VXH9
Gene name |
SWIP |
Protein name |
WASH complex subunit 4 |
Names |
Strumpellin and WASH-interacting protein homolog, WASH complex subunit SWIP homolog |
Species |
Drosophila melanogaster (Fruit fly) |
KEGG Pathway |
dme:Dmel_CG13957 |
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 Q9VXH9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9VXH9-F1 | Predicted | AlphaFoldDB |
No variants for Q9VXH9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9VXH9 | |||||
No associated diseases with Q9VXH9
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| early endosome | A membrane-bounded organelle that receives incoming material from primary endocytic vesicles that have been generated by clathrin-dependent and clathrin-independent endocytosis; vesicles fuse with the early endosome to deliver cargo for sorting into recycling or degradation pathways. |
| endosome | A vacuole to which materials ingested by endocytosis are delivered. |
| nucleoplasm | That part of the nuclear content other than the chromosomes or the nucleolus. |
| WASH complex | A protein complex that localizes at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization. In human, the WASH complex is composed of F-actin-capping protein subunits alpha and beta, WASH1, FAM21, KIAA1033, KIAA0196 and CCDC53. |
No GO annotations of molecular function
| Name | Definition |
|---|---|
| No GO annotations for molecular function |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| endosomal transport | The directed movement of substances mediated by an endosome, a membrane-bounded organelle that carries materials enclosed in the lumen or located in the endosomal membrane. |
| endosome organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of endosomes. |
| nuclear envelope budding | The process by which large macromolecular complexes are budded through the inner nuclear membrane, into the perinuclear space, thus acquiring a membrane envelope. The enveloped particle fuses with the outer nuclear membrane and is released into the cytoplasm. |
| positive regulation of cell adhesion | Any process that activates or increases the frequency, rate or extent of cell adhesion. |
| protein transport | The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MFAEDILRDY | GSFISEHDGK | LKLLRDKVPN | RDVSESAQCV | YMSPVVEVNF | MGNDSMAPDR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SFEESELVAN | KPLTTLANLC | NQCRNLSRKA | KRFQLAFLFS | DFRLDDTLPP | HTHTSEGSAG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LEGSLVRMSS | SMDFFCQVYF | LLNRMIVILQ | NLWRQIAASV | SVPMDINEVH | IFAVFDAMSE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LLEHIVVFNE | LANQSKISTM | WALYKKWLMN | LSNSQSANLE | LNGLSTSLMD | IENLITKDFF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RILLDNLMEL | KKQFGLNSVS | PITQHSNAYI | RRQLLDVDAN | PSNELKNYED | PKHIIRLTTF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VVVVHELGIQ | MEGKLVKNVI | DLVARHKQVP | LNRSVFWSPS | GFLSLHAKTL | MKSSARSQDG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| QGPKVHSTVL | EKFRLSDQRT | CRQLGVQLSL | WSIQMQRVFD | VGVFGHLKTF | LQLILNGHSY |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ADQVNLLAVA | LINRHVALMT | PMTRNDWIVV | SRLLQYLKVI | QKTFESNQIN | FVRFISSLIQ |
| 490 | 500 | 510 | 520 | 530 | 540 |
| WQKQKVIHLL | HTTKKKIVVL | KLLQRKINFL | ATIKLAEKSI | MGFPSKQRLT | FVNLALGEFL |
| 550 | 560 | 570 | 580 | 590 | 600 |
| DNRLLPADNQ | KLIKSILHRV | NSISDIMRNI | GGQLNTSESS | SLVYNHWFLD | TSVLKEYTEL |
| 610 | 620 | 630 | 640 | 650 | 660 |
| QRNPYSLQNL | VSVSHHLDKI | MAMFRGSRCP | KQSANDLIIE | FLSNHLEFFL | RVEALSHLFQ |
| 670 | 680 | 690 | 700 | 710 | 720 |
| SQDQPFQQSA | LDYRLCINAV | AVENDGDYNI | IKDHLENYFT | ATFYNLTTIA | PHDWKSYEKM |
| 730 | 740 | 750 | 760 | 770 | 780 |
| RHLANKVLQL | QPIDDHLPNQ | IIDQGIDVLQ | IMRNIHTFAS | SYAYNMNLQV | FVETNSRSKH |
| 790 | 800 | 810 | 820 | 830 | 840 |
| LDIIGTRHVA | NSVQTHGTGI | INTTVNFIYQ | FLRQKFYTFS | TFLHDEQIKS | RLLKELRFHT |
| 850 | 860 | 870 | 880 | 890 | 900 |
| EHKHSKSYQS | YPYERADSFL | KKIRRLGCSS | NGETYMDLFR | KVITQVGNAV | GYVRLLQAGS |
| 910 | 920 | 930 | 940 | 950 | 960 |
| KNANFRNRSY | KTRFDSNFSC | GGSKVHEATE | GSIREYEKSL | GHMKECYSDS | TNYFKLLLQG |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| FQPFLCNPHN | HHLRTFYLIT | PALIMNYIDY | RVKQKLKIYK | KDQTKISLFE | DGFAIGLVYI |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| LNMLNQQTEF | HELGWSQTIT | QHLNAERSKV | RDILAGQQRT | APEQLDEKLH | QTVAITERHV |
| 1090 | 1100 | ||||
| NAYEHEYNLL | YATLSSSEIF | FQ |