Q5R5P0
Gene name |
WASHC5 |
Protein name |
WASH complex subunit 5 |
Names |
WASH complex subunit strumpellin |
Species |
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
KEGG Pathway |
pon:100173723 |
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 Q5R5P0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5R5P0-F1 | Predicted | AlphaFoldDB |
No variants for Q5R5P0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5R5P0 | |||||
No associated diseases with Q5R5P0
No regional properties for Q5R5P0
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q5R5P0 | |||
Functions
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| 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. |
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
| 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 |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| 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 |
| MLDFLAENNL | CGQAILRIVS | CGNAIIAELL | RLSEFIPAVF | RLKDRADQQK | YGDIIFDFSY |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FKGPELWESK | LDAKPELQDL | DEEFRENNIE | IVTRFYLAFQ | SVHKYIVDLN | RYLDDLNEGV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| YIQQTLETVL | LNEDGKQLLC | EALYLYGVML | LVIDQKIEGE | VRERMLVSYY | RYSAARSSAD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SNMDDICKLL | RSTGYSSQPG | ARRPPNYPES | YFQRVPINES | FISMVIGRLR | SDDIYNQVSA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| YPLPEHRSTA | LANQAAMLYV | ILYFEPSILH | THQAKMREIV | DKYFPDNWVI | SIYMGITVNL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VDAWEPYKAA | KTALNNTLDL | SNVREQASRY | ATVSERVHAQ | VQQFLKEGYL | REEMVLDNIP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KLLNCLRDCN | VAIRWLMLHT | ADSACDPNNK | RLRQIKDQIL | TDSRYNPRIL | FQLLLDTAQF |
| 430 | 440 | 450 | 460 | 470 | 480 |
| EFILKEMFKQ | MLSEKQTKWE | HYKKEGSERM | TELADVFSGV | KPLTRVEKNE | NLQAWFREIS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| KQILSLNYDD | STAAGRKTVQ | LIQALEEVQE | FHQLESNLQV | CQFLADTRKF | LHQMIRTINI |
| 550 | 560 | 570 | 580 | 590 | 600 |
| KEEVLITMQI | VGDLSFAWQL | IDSFTSIMQE | SIRVNPSMVT | KLRATFLKLA | SALDLPLLRI |
| 610 | 620 | 630 | 640 | 650 | 660 |
| NQANSPDLLS | VSQYYSGELV | SYVRKVLQII | PESMFTSLLK | IIKLQTHDII | EVPTRLDKDK |
| 670 | 680 | 690 | 700 | 710 | 720 |
| LRDYAQLGPR | YEVAKLTHAI | SIFTEGILMM | KTTLVGIIKV | DPKQLLEDGI | RKELVKRVAF |
| 730 | 740 | 750 | 760 | 770 | 780 |
| ALHRGLIFNP | RAKPSELMPK | LKELGATMDG | FHRSFEYIQD | YVNIYGLKIW | QEEVSRIINY |
| 790 | 800 | 810 | 820 | 830 | 840 |
| NVEQECNNFL | RTKIQDWQSM | YQSTHIPIPK | FTPVDESVTF | IGRLCREILR | ITDPKMTCHI |
| 850 | 860 | 870 | 880 | 890 | 900 |
| DQLNTWYDMK | THQEVTSSRL | FSEIQTTLGT | FGLNGLDRLL | CFMIVKELQN | FLSMFQKIIL |
| 910 | 920 | 930 | 940 | 950 | 960 |
| RDRTVQDTLK | TLMNAVSPLK | SIVANSNKIY | FSAIAKTQKI | WTAYLEAIMK | VGQMQILRQQ |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| IANELNYSCR | FDSKHLAAAL | ENLNKALLAD | IEAHYQDPSL | PYPKEDNTLL | YEITAYLEAA |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| GIHNPLNKIY | ITTKRLPYFP | IVNFLFLIAQ | LPKLQYNKNL | GMVCRKPTDP | VDWPPLVLGL |
| 1090 | 1100 | 1110 | 1120 | 1130 | 1140 |
| LTLLKQFHSR | YTEQFLALIG | QFICSTVEQC | TSQKIPEIPA | DVVGALLFLE | DYARYTKLPR |
| 1150 | |||||
| RVAEAHVPNF | IFDEFRTVL |