Q9JKR6
PR
Gene name |
Hyou1 (Grp170) |
Protein name |
Hypoxia up-regulated protein 1 |
Names |
GRP-170, 140 kDa Ca(2+)-binding protein, CBP-140 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:12282 |
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 Q9JKR6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9JKR6-F1 | Predicted | AlphaFoldDB |
39 variants for Q9JKR6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389027410 | 35 | V>L | No | EVA | |
| rs3389019138 | 37 | S>Y | No | EVA | |
| rs3389041987 | 103 | L>I | No | EVA | |
| rs3389040547 | 139 | S>N | No | EVA | |
| rs3389046236 | 141 | Q>* | No | EVA | |
| rs3389042886 | 141 | Q>L | No | EVA | |
| rs223841154 | 143 | Q>L | No | EVA | |
| rs3389036525 | 190 | Q>H | No | EVA | |
| rs254161713 | 209 | T>I | No | EVA | |
| rs3389040544 | 230 | F>S | No | EVA | |
| rs3389014397 | 262 | R>L | No | EVA | |
| rs3389037031 | 332 | G>D | No | EVA | |
| rs217295649 | 360 | P>S | No | EVA | |
| rs3389033969 | 398 | K>N | No | EVA | |
| rs3389040524 | 400 | V>M | No | EVA | |
| rs3389007252 | 445 | I>V | No | EVA | |
| rs3389033488 | 491 | F>Y | No | EVA | |
| rs3389042904 | 533 | D>H | No | EVA | |
| rs6393860 | 659 | D>H | No | EVA | |
| rs3389042903 | 680 | A>P | No | EVA | |
| rs3399535344 | 682 | E>K | No | EVA | |
| rs3389034060 | 686 | K>R | No | EVA | |
| rs51288525 | 687 | P>L | No | EVA | |
| rs3412655831 | 691 | R>Q | No | EVA | |
| rs3389019216 | 695 | M>L | No | EVA | |
| rs29687128 | 710 | D>N | No | EVA | |
| rs3389027440 | 728 | L>M | No | EVA | |
| rs3389040341 | 741 | N>K | No | EVA | |
| rs3389040335 | 770 | E>V | No | EVA | |
| rs3400078228 | 793 | M>I* | No | EVA | |
| rs3389014423 | 812 | V>A | No | EVA | |
| rs3389045212 | 815 | R>C | No | EVA | |
| rs3388988736 | 886 | L>V | No | EVA | |
| rs253968760 | 951 | A>G | No | EVA | |
| rs3389046235 | 962 | T>I | No | EVA | |
| rs3389046235 | 962 | T>S | No | EVA | |
| rs3388988704 | 969 | S>W | No | EVA | |
| rs3389019153 | 979 | A>T | No | EVA | |
| rs247366935 | 987 | S>T | No | EVA |
No associated diseases with Q9JKR6
2 regional properties for Q9JKR6
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Heat shock protein 70, conserved site | 230 - 243 | IPR018181-1 |
| conserved_site | Heat shock protein 70, conserved site | 380 - 394 | IPR018181-2 |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum chaperone complex | A protein complex that is located in the endoplasmic reticulum and is composed of chaperone proteins, including BiP, GRP94; CaBP1, protein disulfide isomerase (PDI), ERdj3, cyclophilin B, ERp72, GRP170, UDP-glucosyltransferase, and SDF2-L1. |
| endoplasmic reticulum lumen | The volume enclosed by the membranes of the endoplasmic reticulum. |
| extracellular region | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. |
| smooth endoplasmic reticulum | The smooth endoplasmic reticulum (smooth ER or SER) has no ribosomes attached to it. The smooth ER is the recipient of the proteins synthesized in the rough ER. Those proteins to be exported are passed to the Golgi complex, the resident proteins are returned to the rough ER and the lysosomal proteins after phosphorylation of their mannose residues are passed to the lysosomes. Glycosylation of the glycoproteins also continues. The smooth ER is the site of synthesis of lipids, including the phospholipids. The membranes of the smooth ER also contain enzymes that catalyze a series of reactions to detoxify both lipid-soluble drugs and harmful products of metabolism. Large quantities of certain compounds such as phenobarbital cause an increase in the amount of the smooth ER. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP-dependent protein folding chaperone | Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis. |
8 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular response to hypoxia | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level. |
| endoplasmic reticulum to Golgi vesicle-mediated transport | The directed movement of substances from the endoplasmic reticulum (ER) to the Golgi, mediated by COP II vesicles. Small COP II coated vesicles form from the ER and then fuse directly with the cis-Golgi. Larger structures are transported along microtubules to the cis-Golgi. |
| negative regulation of apoptotic process | Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process. |
| negative regulation of endoplasmic reticulum stress-induced neuron intrinsic apoptotic signaling pathway | Any process that stops, prevents or reduces the frequency, rate or extent of an endoplasmic reticulum stress-induced neuron intrinsic apoptotic signaling pathway. |
| negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway | Any process that stops, prevents or reduces the frequency, rate or extent of hypoxia-induced intrinsic apoptotic signaling pathway. |
| response to endoplasmic reticulum stress | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen. |
| response to hypoxia | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level. |
| response to ischemia | Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a inadequate blood supply. |
3 homologous proteins in AiPD
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAATVRRQRP | RRLLCWALVA | VLLADLLALS | DTLAVMSVDL | GSESMKVAIV | KPGVPMEIVL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NKESRRKTPV | TVTLKENERF | LGDSAAGMAI | KNPKATLRYF | QHLLGKQADN | PHVALYRSRF |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PEHELIVDPQ | RQTVRFQISP | QLQFSPEEVL | GMVLNYSRSL | AEDFAEQPIK | DAVITVPAFF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NQAERRAVLQ | AARMAGLKVL | QLINDNTATA | LSYGVFRRKD | INSTAQNVMF | YDMGSGSTVC |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TIVTYQTVKT | KEAGMQPQLQ | IRGVGFDRTL | GGLEMELRLR | EHLAKLFNEQ | RKGQKAKDVR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ENPRAMAKLL | REANRLKTVL | SANADHMAQI | EGLMDDVDFK | AKVTRVEFEE | LCADLFDRVP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GPVQQALQSA | EMSLDQIEQV | ILVGGATRVP | KVQEVLLKAV | GKEELGKNIN | ADEAAAMGAV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| YQAAALSKAF | KVKPFVVRDA | VIYPILVEFT | REVEEEPGLR | SLKHNKRVLF | SRMGPYPQRK |
| 490 | 500 | 510 | 520 | 530 | 540 |
| VITFNRYSHD | FNFHINYGDL | GFLGPEDLRV | FGSQNLTTVK | LKGVGESFKK | YPDYESKGIK |
| 550 | 560 | 570 | 580 | 590 | 600 |
| AHFNLDESGV | LSLDRVESVF | ETLVEDSPEE | ESTLTKLGNT | ISSLFGGGTS | SDAKENGTDA |
| 610 | 620 | 630 | 640 | 650 | 660 |
| VQEEEESPAE | GSKDEPAEQG | ELKEEAEPPA | EETSQPPPSE | PKGDAAREGE | KPDEKESGDK |
| 670 | 680 | 690 | 700 | 710 | 720 |
| PEAQKPNEKG | QAGPEGAAPA | PEEDKKPKPA | RKQKMVEEIG | VELAVLDLPD | LPEDELARSV |
| 730 | 740 | 750 | 760 | 770 | 780 |
| QKLEELTLRD | LEKQEREKAA | NSLEAFIFET | QDKLYQPEYQ | EVSTEEQREE | ISGKLSATST |
| 790 | 800 | 810 | 820 | 830 | 840 |
| WLEDEGFGAT | TVMLKDKLAE | LRKLCQGLFF | RVEERRKWPE | RLSALDNLLN | HSSIFLKGAR |
| 850 | 860 | 870 | 880 | 890 | 900 |
| LIPEMDQVFT | EVEMTTLEKV | INDTWAWKNA | TLAEQAKLPA | TEKPVLLSKD | IEAKMMALDR |
| 910 | 920 | 930 | 940 | 950 | 960 |
| EVQYLLNKAK | FTKPRPRPKD | KNGTRAEPPL | NASAGDQEEK | VIPPAGQTEE | AKPILEPDKE |
| 970 | 980 | 990 | |||
| ETGTEPADSE | PLELGGPGAG | PEQEEQSAGQ | KRPSKNDEL |