P51534
Gene name |
SHE4 (YOR035C, OR26.26) |
Protein name |
SWI5-dependent HO expression protein 4 |
Names |
|
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YOR035C |
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
2 structures for P51534
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 3OPB | X-ray | 290 A | A/B | 1-789 | PDB |
| AF-P51534-F1 | Predicted | AlphaFoldDB |
13 variants for P51534
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s15-400021 | 28 | K>N | No | SGRP | |
| s15-400022 | 28 | K>T | No | SGRP | |
| s15-399994 | 37 | N>K | No | SGRP | |
| s15-399773 | 111 | S>F | No | SGRP | |
| s15-399654 | 151 | I>V | No | SGRP | |
| s15-399358 | 249 | K>N | No | SGRP | |
| s15-399212 | 298 | R>K | No | SGRP | |
| s15-399084 | 341 | R>G | No | SGRP | |
| s15-398939 | 389 | T>I | No | SGRP | |
| s15-398634 | 491 | V>I | No | SGRP | |
| s15-398436 | 557 | A>S | No | SGRP | |
| s15-398070 | 679 | V>I | No | SGRP | |
| s15-397763 | 781 | P>H | No | SGRP |
No associated diseases with P51534
1 regional properties for P51534
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | UNC-45/Cro1/She4, central domain | 174 - 316 | IPR024660 |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| Hsp90 protein binding | Binding to Hsp90 proteins, any of a group of heat shock proteins around 90kDa in size. |
| identical protein binding | Binding to an identical protein or proteins. |
| myosin binding | Binding to a myosin; myosins are any of a superfamily of molecular motor proteins that bind to actin and use the energy of ATP hydrolysis to generate force and movement along actin filaments. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| actin cytoskeleton organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins. |
| chaperone-mediated protein folding | The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone. |
| intracellular mRNA localization | Any process in which mRNA is transported to, or maintained in, a specific location within the cell. |
| mating type switching | The conversion of a single-cell organism from one mating type to another by the precise replacement of a DNA sequence at the expressed mating type locus with a copy of a sequence from a donor locus. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPLCEKGNDP | IDSSTIDSLC | AAFDKTLKST | PDVQKYNDAI | NTIFQLRQKS | ESGKMPADLT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NSEALKDRQK | IEEILTRSYQ | DHSESRVHLS | KLIQNDIPFA | LNLFEILSRS | SIHVFVGCFS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NKDATIALLN | ELQIRIHYGE | DTHVTYLLSI | ILQLLNKFKY | NFKEVRFLVK | ELILRISEDE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VKSMMLIIFA | ELQSSFQKDF | DKAVVDFMSS | LIVEAEIDVG | NDPLSIIVKT | LSELYPSLTT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LCSEIFLTKG | LSKLFKKRVF | EEQDLQFTKE | LLRLLSSACI | DETMRTYITE | NYLQLLERSL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| NVEDVQIYSA | LVLVKTWSFT | KLTCINLKQL | SEIFINAISR | RIMPKIENVN | ESAVKLEEVP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KVEMSVEALA | YLSLKASVKI | MIRSNESFTE | ILLTMIKSQK | MTHCLYGLLV | IMANLSTLPE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ESNGSSQSIN | DLKNYADLKG | PGADKVGAEK | ESKEDILLFN | EKYILRTELI | SFLKREMHNL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| SPNCKQQVVR | VIYNITRSKN | FIPQCISQGG | TTIILEYLAN | KQDIGEPIRI | LGCRALTRML |
| 550 | 560 | 570 | 580 | 590 | 600 |
| IFTNPGLIFK | KYSALNAIPF | LFELLPRSTP | VDDNPLHNDE | QIKLTDNYEA | LLALTNLASS |
| 610 | 620 | 630 | 640 | 650 | 660 |
| ETSDGEEVCK | HIVSTKVYWS | TIENLMLDEN | VPLQRSTLEL | ISNMMSHPLT | IAAKFFNLEN |
| 670 | 680 | 690 | 700 | 710 | 720 |
| PQSLRNFNIL | VKLLQLSDVE | SQRAVAAIFA | NIATTIPLIA | KELLTKKELI | ENAIQVFADQ |
| 730 | 740 | 750 | 760 | 770 | 780 |
| IDDIELRQRL | LMLFFGLFEV | IPDNGTNEVY | PLLQENQKLK | DALNMSLKRG | DSGPEFSAAI |
| PVILAKIKV |