Q99JF8
PR
Gene name |
Psip1 (Ledgf) |
Protein name |
PC4 and SFRS1-interacting protein |
Names |
Lens epithelium-derived growth factor, mLEDGF |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:101739 |
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 Q99JF8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q99JF8-F1 | Predicted | AlphaFoldDB |
24 variants for Q99JF8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388680053 | 38 | N>K | No | EVA | |
| rs3394327068 | 69 | G>V | No | EVA | |
| rs3388690702 | 103 | N>K | No | EVA | |
| rs3388692458 | 154 | E>V | No | EVA | |
| rs3388693711 | 161 | E>G | No | EVA | |
| rs28084954 | 162 | A>V | No | EVA | |
| rs3388696956 | 163 | G>V | No | EVA | |
| rs3388690031 | 175 | A>G | No | EVA | |
| rs3388693425 | 175 | A>P | No | EVA | |
| rs3388692817 | 249 | K>* | No | EVA | |
| rs3388672485 | 250 | K>R | No | EVA | |
| rs3388690072 | 253 | K>E | No | EVA | |
| rs3388696959 | 279 | D>G* | No | EVA | |
| rs3388693725 | 316 | Q>R | No | EVA | |
| rs3388691121 | 322 | T>N | No | EVA | |
| rs3388688583 | 372 | I>VSDG* | No | EVA | |
| rs3388680009 | 376 | D>G | No | EVA | |
| rs3388672471 | 390 | K>T | No | EVA | |
| rs3388688501 | 412 | E>D | No | EVA | |
| rs3388691065 | 472 | G>C | No | EVA | |
| rs213385959 | 473 | T>A | No | EVA | |
| rs3388672482 | 479 | G>E | No | EVA | |
| rs3388688164 | 514 | E>* | No | EVA | |
| rs3388693394 | 515 | R>S | No | EVA |
No associated diseases with Q99JF8
5 GO annotations of cellular component
| Name | Definition |
|---|---|
| euchromatin | A dispersed and relatively uncompacted form of chromatin that is in a transcription-competent conformation. |
| heterochromatin | A compact and highly condensed form of chromatin that is refractory to transcription. |
| nuclear periphery | The portion of the nuclear lumen proximal to the inner nuclear membrane. |
| nucleoplasm | That part of the nuclear content other than the chromosomes or the nucleolus. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| chromatin binding | Binding to chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase. |
| DNA-binding transcription factor binding | Binding to a DNA-binding transcription factor, a protein that interacts with a specific DNA sequence (sometimes referred to as a motif) within the regulatory region of a gene to modulate transcription. |
| double-stranded DNA binding | Binding to double-stranded DNA. |
| supercoiled DNA binding | Binding to supercoiled DNA. For example, during replication and transcription, template DNA is negatively supercoiled in the receding downstream DNA and positively supercoiled in the approaching downstream DNA. |
| transcription coactivator activity | A transcription coregulator activity that activates or increases the transcription of specific gene sets via binding to a DNA-bound DNA-binding transcription factor, either on its own or as part of a complex. Coactivators often act by altering chromatin structure and modifications. For example, one class of transcription coactivators modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators. A fourth class of coactivator activity is the bridging of a DNA-binding transcription factor to the general (basal) transcription machinery. The Mediator complex, which bridges sequence-specific DNA binding transcription factors and RNA polymerase, is also a transcription coactivator. |
| transcription coregulator activity | A transcription regulator activity that modulates the transcription of specific gene sets via binding to a DNA-bound DNA-binding transcription factor, either on its own or as part of a complex. Coregulators often act by altering chromatin structure and modifications. For example, one class of transcription coregulators modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| mRNA 5'-splice site recognition | Recognition of the intron 5'-splice site by components of the assembling spliceosome. |
| positive regulation of transcription by RNA polymerase II | Any process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter. |
| regulation of transcription by RNA polymerase II | Any process that modulates the frequency, rate or extent of transcription mediated by RNA polymerase II. |
| response to heat | 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 heat stimulus, a temperature stimulus above the optimal temperature for that organism. |
| response to oxidative stress | 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 oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. |
13 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9XSK7 | HDGF | Hepatoma-derived growth factor | Bos taurus (Bovine) | PR |
| Q8MJG1 | PSIP1 | PC4 and SFRS1-interacting protein | Bos taurus (Bovine) | PR |
| Q66T72 | PSIP1 | PC4 and SFRS1-interacting protein | Felis catus (Cat) (Felis silvestris catus) | PR |
| Q5XXA9 | PSIP1 | Lens epithelium-derived growth factor | Gallus gallus (Chicken) | PR |
| P51858 | HDGF | Hepatoma-derived growth factor | Homo sapiens (Human) | PR |
| Q7Z4V5 | HDGFL2 | Hepatoma-derived growth factor-related protein 2 | Homo sapiens (Human) | PR |
| Q9Y3E1 | HDGFL3 | Hepatoma-derived growth factor-related protein 3 | Homo sapiens (Human) | PR |
| O75475 | PSIP1 | PC4 and SFRS1-interacting protein | Homo sapiens (Human) | PR |
| P51859 | Hdgf | Hepatoma-derived growth factor | Mus musculus (Mouse) | PR |
| Q9JMG7 | Hdgfl3 | Hepatoma-derived growth factor-related protein 3 | Mus musculus (Mouse) | PR |
| Q8VHK7 | Hdgf | Hepatoma-derived growth factor | Rattus norvegicus (Rat) | PR |
| Q923W4 | Hdgfl3 | Hepatoma-derived growth factor-related protein 3 | Rattus norvegicus (Rat) | PR |
| Q812D1 | Psip1 | PC4 and SFRS1-interacting protein | Rattus norvegicus (Rat) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTRDFKPGDL | IFAKMKGYPH | WPARVDEVPD | GAVKPPTNKL | PIFFFGTHET | AFLGPKDIFP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| YSENKEKYGK | PNKRKGFNEG | LWEIDNNPKV | KFSSQQASTK | QSNASSDVEV | EEKETNVSKE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DTDQEEKASN | EDVTKAVDIT | TPKAARRGRK | RKAEKQVDTE | EAGMVTAATA | SNVKASPKRG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RPAATEVKIP | KPRGRPKVVK | QPCPSDGDMV | IDEDKSKKKG | PEEKQPKKQL | KKEEEGQKEE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EKPRKEPDKK | EGKKEVESKR | KNLAKPGVTS | TSDSEDEDDQ | EGEKKRKGGR | NFQAAHRRNM |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LKGQHEKEAG | DRKRKQEEQM | ETEQQNKDEG | KKPEVKKVEK | KRETSMDSRL | QRIHAEIKNS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LKIDNLDVNR | CIEALDELAS | LQVTMQQAQK | HTEMITTLKK | IRRFKVSQVI | MEKSTMLYNK |
| 430 | 440 | 450 | 460 | 470 | 480 |
| FKNMFLVGEG | DSVITQVLNK | SLAEQRQHEE | ANKTKDQGKK | GPNKKLEKEP | TGTKSLNGGS |
| 490 | 500 | 510 | 520 | ||
| DAQESNHPQH | NGDSNEDGKD | SREASSKTKP | PGEEREAEIS | LKESTLDN |