P06467
Gene name |
Hbz (Hba-x, Hbz1) |
Protein name |
Hemoglobin subunit zeta |
Names |
Alpha-like embryonic globin chain x, Hemoglobin zeta chain, Zeta-globin |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:15126 |
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 P06467
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P06467-F1 | Predicted | AlphaFoldDB |
12 variants for P06467
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389146750 | 16 | E>D | No | EVA | |
| rs13463378 | 27 | T>S | No | EVA | |
| rs252473648 | 28 | E>D | No | EVA | |
| rs3389159369 | 29 | T>I | No | EVA | |
| rs232347116 | 37 | Y>F | No | EVA | |
| rs3389148045 | 52 | G>E | No | EVA | |
| rs3389149458 | 52 | G>R | No | EVA | |
| rs3389120669 | 64 | M>L | No | EVA | |
| rs3389149776 | 74 | I>N | No | EVA | |
| rs3389145406 | 89 | A>G | No | EVA | |
| rs3389154592 | 105 | C>* | No | EVA | |
| rs3389149823 | 139 | E>K | No | EVA |
No associated diseases with P06467
1 regional properties for P06467
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Globin | 3 - 142 | IPR000971 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| haptoglobin-hemoglobin complex | A protein complex formed by the stable binding of a haptoglobin to hemoglobin. |
| hemoglobin complex | An iron-containing, oxygen carrying complex. In vertebrates it is made up of two pairs of associated globin polypeptide chains, each chain carrying a noncovalently bound heme prosthetic group. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| heme binding | Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring. |
| iron ion binding | Binding to an iron (Fe) ion. |
| organic acid binding | Binding to an organic acid, any acidic compound containing carbon in covalent linkage. |
| oxygen binding | Binding to oxygen (O2). |
| oxygen carrier activity | Binding to oxygen and delivering it to an acceptor molecule or a specific location. |
7 GO annotations of biological process
| Name | Definition |
|---|---|
| carbon dioxide transport | The directed movement of carbon dioxide (CO2) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
| cellular oxidant detoxification | Any process carried out at the cellular level that reduces or removes the toxicity superoxide radicals or hydrogen peroxide. |
| erythrocyte maturation | A developmental process, independent of morphogenetic (shape) change, that is required for an erythrocyte to attain its fully functional state. |
| hydrogen peroxide catabolic process | The chemical reactions and pathways resulting in the breakdown of hydrogen peroxide (H2O2). |
| negative regulation of transcription by RNA polymerase II | Any process that stops, prevents, or reduces the frequency, rate or extent of transcription mediated by RNA polymerase II. |
| oxygen transport | The directed movement of oxygen (O2) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
| positive regulation of cell death | Any process that increases the rate or frequency of cell death. Cell death is the specific activation or halting of processes within a cell so that its vital functions markedly cease, rather than simply deteriorating gradually over time, which culminates in cell death. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P02197 | MB | Myoglobin | Gallus gallus (Chicken) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSLMKNERAI | IMSMWEKMAA | QAEPIGTETL | ERLFCSYPQT | KTYFPHFDLH | HGSQQLRAHG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FKIMTAVGDA | VKSIDNLSSA | LTKLSELHAY | ILRVDPVNFK | LLSHCLLVTM | AARFPADFTP |
| 130 | 140 | ||||
| EVHEAWDKFM | SILSSILTEK | YR |