Q7ZWF4
Gene name |
rnf145 (zgc:56435) |
Protein name |
RING finger protein 145 |
Names |
|
Species |
Danio rerio (Zebrafish) (Brachydanio rerio) |
KEGG Pathway |
dre:327056 |
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 Q7ZWF4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q7ZWF4-F1 | Predicted | AlphaFoldDB |
No variants for Q7ZWF4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q7ZWF4 | |||||
No associated diseases with Q7ZWF4
No regional properties for Q7ZWF4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q7ZWF4 | |||
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| endomembrane system | A collection of membranous structures involved in transport within the cell. The main components of the endomembrane system are endoplasmic reticulum, Golgi bodies, vesicles, cell membrane and nuclear envelope. Members of the endomembrane system pass materials through each other or though the use of vesicles. |
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
| 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. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| ubiquitin protein ligase activity | Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond: an isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate or, in the linear extension of ubiquitin chains, a peptide bond the between the C-terminal glycine and N-terminal methionine of ubiquitin residues. |
| zinc ion binding | Binding to a zinc ion (Zn). |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| hemopoiesis | The process whose specific outcome is the progression of the myeloid and lymphoid derived organ/tissue systems of the blood and other parts of the body over time, from formation to the mature structure. The site of hemopoiesis is variable during development, but occurs primarily in bone marrow or kidney in many adult vertebrates. |
| myeloid cell development | The process whose specific outcome is the progression of a myeloid cell over time, from its formation to the mature structure. |
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 |
| A5WW08 | chfr | E3 ubiquitin-protein ligase CHFR | Danio rerio (Zebrafish) (Brachydanio rerio) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAMKARLESV | LNVGLRIPSI | MLLEVLYRWD | VSSFFQKIQR | SSLNNNPVFQ | YKYIALYLHY |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VGYILSLVLL | TLPRQHLVQL | YLYVLTALLL | FAGHQLSRDY | VRGELDSGYE | GPLYLEPLSM |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NRFTTALIGQ | VVVCTLCSCV | MQTRQIWLFS | AHLLPLVARL | CLVPLETIVF | INRFAMIFTG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LEVLYFIASN | LLVPYNLAKT | AYRELVQVVE | VYGLLALGMS | LWNQLVLPVL | FMCFWLVLFA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LQIYTYFSTR | DQPPSRERLL | FLFLTSIAEC | CSTPYSLLGL | VFTVSFVALG | VLTLCKFYLQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GYRAFMNDNA | MHRGMTEGIT | LLILAVQTGL | IELQVIHRAF | LLSIILFIVV | ASILQSMLEI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ADPIVLALGA | SRDKSLWKHF | RAVSLCLFLL | VFPAYMAYMI | CQFFRMDFWL | LIIISSSILT |
| 430 | 440 | 450 | 460 | 470 | 480 |
| SLQVLGTLLI | YVLFMVEEFR | KAPVENMDEV | IYYVNGTYRL | LEFLVAVCVV | AYGVSETLFG |
| 490 | 500 | 510 | 520 | 530 | 540 |
| EWTVMGSTII | LVHSYYNVWL | RAQLGWQSFL | LRRDAVHKIQ | SMPTASTLQL | QQHNDICSIC |
| 550 | 560 | 570 | 580 | 590 | 600 |
| FQDMKSAVIT | PCSHFFHAAC | LKKWLYVQET | CPLCHGQLKS | QLQPTSSPGT | PTQGTPAANQ |
| 610 | 620 | 630 | 640 | 650 | 660 |
| NPREVEQEQR | QPQVELNTEE | GIRAEEMKTS | AEQKLGMDLL | PGSLNTQPKE | CDLVAEGSAG |
| 670 | 680 | ||||
| TASNLKGDDY | YDDDDVSTSD | VNCAS |