A5WW08
Gene name |
chfr (si:dkey-69h6.7) |
Protein name |
E3 ubiquitin-protein ligase CHFR |
Names |
Checkpoint with forkhead and RING finger domains protein, RING-type E3 ubiquitin transferase CHFR |
Species |
Danio rerio (Zebrafish) (Brachydanio rerio) |
KEGG Pathway |
dre:564271 |
EC number |
2.3.2.27: Aminoacyltransferases |
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 A5WW08
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A5WW08-F1 | Predicted | AlphaFoldDB |
No variants for A5WW08
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A5WW08 | |||||
No associated diseases with A5WW08
5 regional properties for A5WW08
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Forkhead-associated (FHA) domain | 30 - 98 | IPR000253 |
| domain | Zinc finger, RING-type | 277 - 316 | IPR001841 |
| conserved_site | Zinc finger, RING-type, conserved site | 293 - 302 | IPR017907 |
| domain | Aprataxin and PNK-like factor, PBZ domain | 605 - 628 | IPR019406 |
| domain | E3 ubiquitin-protein ligase CHFR, cysteine rich domain with multizinc binding | 441 - 593 | IPR040909 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.3.2.27 | Aminoacyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
| PML body | A class of nuclear body; they react against SP100 auto-antibodies (PML, promyelocytic leukemia); cells typically contain 10-30 PML bodies per nucleus; alterations in the localization of PML bodies occurs after viral infection. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| metal ion binding | Binding to a metal ion. |
| nucleotide binding | Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose. |
| ubiquitin-protein transferase activity | Catalysis of the transfer of ubiquitin from one protein to another via the reaction X-Ub + Y --> Y-Ub + X, where both X-Ub and Y-Ub are covalent linkages. |
6 GO annotations of biological process
| Name | Definition |
|---|---|
| cell division | The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells. |
| mitotic G2/M transition checkpoint | A cell cycle checkpoint that detects and negatively regulates progression from G2 to M phase as part of a mitotic cell cycle. |
| modification-dependent protein catabolic process | The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent modification of the target protein. |
| protein polyubiquitination | Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain. |
| protein ubiquitination | The process in which one or more ubiquitin groups are added to a protein. |
| ubiquitin-dependent protein catabolic process | The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein. |
8 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9UKV5 | AMFR | E3 ubiquitin-protein ligase AMFR | Homo sapiens (Human) | PR |
| Q8WU17 | RNF139 | E3 ubiquitin-protein ligase RNF139 | Homo sapiens (Human) | PR |
| Q5M7Z0 | RNFT1 | E3 ubiquitin-protein ligase RNFT1 | Homo sapiens (Human) | PR |
| Q9DCN7 | Rnft1 | E3 ubiquitin-protein ligase RNFT1 | Mus musculus (Mouse) | PR |
| Q7TMV1 | Rnf139 | E3 ubiquitin-protein ligase RNF139 | Mus musculus (Mouse) | PR |
| Q9R049 | Amfr | E3 ubiquitin-protein ligase AMFR | Mus musculus (Mouse) | PR |
| P90859 | F26E4.3 | E3 ubiquitin-protein ligase hrd-like protein 1 | Caenorhabditis elegans | PR |
| Q7ZWF4 | rnf145 | RING finger protein 145 | Danio rerio (Zebrafish) (Brachydanio rerio) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTNQDSDQAW | GKLVKVDASP | GSEIVLINSE | CTVGRKKDCD | LSFPANKLVS | GNHCKITHDQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NSGKVWLEDM | STNGTVINMS | KVVKKQTHLL | QNGDVIYFVY | RKNEPEQNIA | YVYQSITPQE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SASHDVEDAG | REEDSDLTET | ESEPAPVEPV | IVKPLPQSGH | EDPQPSTSSS | SLHFYNMPLS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TCSDVSARKN | PVSSSAVCKG | DSTSSGSPAQ | TRLKWTCWTD | GEPEEEMQRK | RRKTDRDDPG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FGSAHSDASA | DIPLRGASGK | EKTEGATTDK | MEESLTCIIC | QDLLYDCISV | QPCMHTFCAA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| CYSGWMERSS | FCPTCRCPVE | RIRKNHILNN | LVEAYLLQHP | EKCRTEDDLR | SMDARNKITQ |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DMLQPKVERS | FSDEEASSDY | LFELSDNDSD | ISDMSQPYMM | CRQCPGYRKE | LSSALWICES |
| 430 | 440 | 450 | 460 | 470 | 480 |
| AQSESLAKTA | GDGPSTSSDS | TTAAPQEFRC | PPQASHLICT | CCLQPMPDRR | FEHLPPQVSP |
| 490 | 500 | 510 | 520 | 530 | 540 |
| QHCLVCQKPF | CHVYWGCPRI | GCHGCLARFS | ELNLNDKCLD | GVFNGNQYES | EVLQNYLSCR |
| 550 | 560 | 570 | 580 | 590 | 600 |
| GMSWRHLLQD | SLQALQQGLY | HLSDYRITAN | SFLCYCCGLR | TFRELAYKYR | ERIPPSELPD |
| 610 | 620 | 630 | |||
| AVTNRPNCYW | GRNCRTQVKA | HHALKFNHIC | EQTRFKN |