Q80TI0
Gene name |
Gramd1b (Kiaa1201) |
Protein name |
Protein Aster-B |
Names |
GRAM domain-containing protein 1B |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:235283 |
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 Q80TI0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q80TI0-F1 | Predicted | AlphaFoldDB |
No variants for Q80TI0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q80TI0 | |||||
No associated diseases with Q80TI0
Functions
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| endoplasmic reticulum-plasma membrane contact site | A contact site between the endoplasmic reticulum membrane and the plasma membrane, structured by bridging complexes. |
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| cholesterol binding | Binding to cholesterol (cholest-5-en-3-beta-ol); the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones. |
| cholesterol transfer activity | Removes cholesterol from a membrane or a monolayer lipid particle, transports it through the aqueous phase while protected in a hydrophobic pocket, and brings it to an acceptor membrane or lipid particle. |
| phosphatidic acid binding | Binding to phosphatidic acid, any of a class of glycerol phosphate in which both the remaining hydroxyl groups of the glycerol moiety are esterified with fatty acids. |
| phosphatidylserine binding | Binding to phosphatidylserine, a class of glycophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of L-serine. |
| sterol binding | Binding to a sterol, a steroid containing a hydroxy group in the 3 position, closely related to cholestan-3-ol. |
| sterol transfer activity | Removes a sterol from a membrane or a monolayer lipid particle, transports it through the aqueous phase while protected in a hydrophobic pocket, and brings it to an acceptor membrane or lipid particle. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular response to cholesterol | 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 cholesterol stimulus. |
| cholesterol homeostasis | Any process involved in the maintenance of an internal steady state of cholesterol within an organism or cell. |
| intracellular sterol transport | The directed movement of sterols within cells. |
5 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q8IYS0 | GRAMD1C | Protein Aster-C | Homo sapiens (Human) | PR |
| Q96CP6 | GRAMD1A | Protein Aster-A | Homo sapiens (Human) | PR |
| Q3KR37 | GRAMD1B | Protein Aster-B | Homo sapiens (Human) | PR |
| Q9ZVT9 | At1g03370 | C2 and GRAM domain-containing protein At1g03370 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q9FGS8 | At5g50170 | C2 and GRAM domain-containing protein At5g50170 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKGFKLSCTA | SNSNRSTPAC | SPILRKRSRS | PTPQNQDGDT | MVEKGSDHSS | DKSPSTPEQG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VQRSCSSQSG | RSGGKNSKKS | QSWYNVLSPT | YKQRNEDFRK | LFKQLPDTER | LIVDYSCALQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RDILLQGRLY | LSENWICFYS | NIFRWETLLT | VRLKDICSMT | KEKTARLIPN | AIQVCTDSEK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| HFFTSFGARD | RTYMMMFRLW | QNALLEKPLC | PKELWHFVHQ | CYGNELGLTS | DDEDYVPPDD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DFNTMGYCEE | IPIEENEVND | SSSKSSIETK | PDASPQLPKK | SITNSTLTST | GSSEAPVSFD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GLPLEEEVME | GDGSLEKELA | IDNIIGEKIE | IMAPVTSPSL | DFNDNEDIPT | ELSDSSDTHD |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EGEVQAFYED | LSGRQYVNEV | FNFSVDKLYD | LLFTNSPFLR | DFMEQRRFSD | IIFHPWKKEE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| NGNQSRVILY | TITLTNPLAP | KTATVRETQT | MYKASQESEC | YVIDAEVLTH | DVPYHDYFYT |
| 490 | 500 | 510 | 520 | 530 | 540 |
| INRYTLTRVA | RNKSRLRVST | ELRYRKQPWG | FVKTFIEKNF | WSGLEDYFRH | LETELTKTES |
| 550 | 560 | 570 | 580 | 590 | 600 |
| TYLAEIHRQS | PKEKASKSSA | VRRRKRPHAH | LRVPHLEEVM | SPVTTPTDED | VGHRIKHVAG |
| 610 | 620 | 630 | 640 | 650 | 660 |
| STQTRHIPED | TPDGFHLQSV | SKLLLVISCV | ICFSLVLLVV | LNMMLFYKLW | MLEYTTQTLT |
| 670 | 680 | 690 | 700 | 710 | 720 |
| AWQGLRLQER | LPQSQTEWAQ | LLESQQKYHD | TELQKWREII | KSSVLLLDQM | KDSLINLQNG |
| 730 | |||||
| IRSRDYTAES | DEKRNRYH |