Q9Z1F9
Gene name |
Uba2 (Sae2, Uble1b) |
Protein name |
SUMO-activating enzyme subunit 2 |
Names |
Anthracycline-associated resistance ARX, Ubiquitin-like 1-activating enzyme E1B, Ubiquitin-like modifier-activating enzyme 2 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:50995 |
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 Q9Z1F9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9Z1F9-F1 | Predicted | AlphaFoldDB |
20 variants for Q9Z1F9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388903733 | 65 | K>R | No | EVA | |
| rs3397814172 | 67 | H>Q | No | EVA | |
| rs3388891426 | 113 | M>I | No | EVA | |
| rs3388897289 | 119 | R>I | No | EVA | |
| rs3388873235 | 141 | T>S | No | EVA | |
| rs3388903048 | 158 | C>Y | No | EVA | |
| rs3388873290 | 174 | T>M | No | EVA | |
| rs3388903738 | 197 | F>* | No | EVA | |
| rs3388888043 | 214 | E>* | No | EVA | |
| rs223332811 | 220 | T>A | No | EVA | |
| rs3388901337 | 220 | T>K | No | EVA | |
| rs3397911847 | 257 | K>* | No | EVA | |
| rs3388873247 | 259 | F>L | No | EVA | |
| rs3388897749 | 264 | R>I | No | EVA | |
| rs3388900407 | 370 | S>C | No | EVA | |
| rs3388859933 | 448 | V>M | No | EVA | |
| rs3388904651 | 480 | I>F | No | EVA | |
| rs3388893257 | 516 | Q>R | No | EVA | |
| rs3388897711 | 519 | D>V | No | EVA | |
| rs3388903763 | 563 | S>C | No | EVA |
No associated diseases with Q9Z1F9
5 regional properties for Q9Z1F9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | THIF-type NAD/FAD binding fold | 9 - 440 | IPR000594 |
| conserved_site | Ubiquitin-activating enzyme E1, conserved site | 402 - 410 | IPR018074 |
| domain | Ubiquitin/SUMO-activating enzyme ubiquitin-like domain | 450 - 535 | IPR028077 |
| domain | SUMO-activating enzyme subunit 2, C-terminal domain | 547 - 628 | IPR032426 |
| active_site | Ubiquitin-activating enzyme E1, Cys active site | 171 - 179 | IPR033127 |
Functions
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| nucleoplasm | That part of the nuclear content other than the chromosomes or the nucleolus. |
| SUMO activating enzyme complex | A conserved heterodimeric complex with SUMO activating enzyme activity. |
8 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
| protein heterodimerization activity | Binding to a nonidentical protein to form a heterodimer. |
| small protein activating enzyme binding | Binding to a small protein activating enzyme, such as ubiquitin-activating enzyme. |
| SUMO activating enzyme activity | Catalysis of the activation of the proteolytically processed small ubiquitin-related modifier SUMO, through the formation of an ATP-dependent high-energy thiolester bond. |
| SUMO binding | Binding to the small ubiquitin-like protein SUMO. |
| transferase activity | Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2. |
| ubiquitin-like protein conjugating enzyme binding | Binding to a ubiquitin-like protein conjugating enzyme such as ubiquitin conjugating enzyme. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| positive regulation of protein sumoylation | Any process that activates or increases the frequency, rate or extent of the addition of SUMO groups to a protein. |
| protein modification by small protein conjugation | A protein modification process in which one or more groups of a small protein, such as ubiquitin or a ubiquitin-like protein, are covalently attached to a target protein. |
| protein sumoylation | The process in which a SUMO protein (small ubiquitin-related modifier) is conjugated to a target protein via an isopeptide bond between the carboxy-terminus of SUMO with an epsilon-amino group of a lysine residue of the target protein. |
6 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9UBT2 | UBA2 | SUMO-activating enzyme subunit 2 | Homo sapiens (Human) | PR |
| Q02053 | Uba1 | Ubiquitin-like modifier-activating enzyme 1 | Mus musculus (Mouse) | PR |
| Q8VE47 | Uba5 | Ubiquitin-like modifier-activating enzyme 5 | Mus musculus (Mouse) | PR |
| P31254 | Uba1y | Ubiquitin-like modifier-activating enzyme 1 Y | Mus musculus (Mouse) | PR |
| Q8C878 | Uba3 | NEDD8-activating enzyme E1 catalytic subunit | Mus musculus (Mouse) | PR |
| Q7SXG4 | uba2 | SUMO-activating enzyme subunit 2 | Danio rerio (Zebrafish) (Brachydanio rerio) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MALSRGLPRE | LAEAVSGGRV | LVVGAGGIGC | ELLKNLVLTG | FSHIDLIDLD | TIDVSNLNRQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FLFQKKHVGR | SKAQVAKESV | LQFHPQANIE | AHHDSIMNPD | YNVEFFRQFI | LVMNALDNRA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ARNHVNRMCL | AADVPLIESG | TAGYLGQVTT | IKKGVTECYE | CHPKPTQRTF | PGCTIRNTPS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EPIHCIVWAK | YLFNQLFGEE | DADQEVSPDR | ADPEAAWEPT | EAEARARASN | EDGDIKRIST |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KEWAKSTGYD | PVKLFTKLFK | DDIRYLLTMD | KLWRKRKPPV | PLDWAEVQSQ | GEANADQQNE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PQLGLKDQQV | LDVKSYASLF | SKSIETLRVH | LAEKGDGAEL | IWDKDDPPAM | DFVTSAANLR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| MHIFSMNMKS | RFDIKSMAGN | IIPAIATTNA | VIAGLIVLEG | LKILSGKIDQ | CRTIFLNKQP |
| 430 | 440 | 450 | 460 | 470 | 480 |
| NPRKKLLVPC | ALDPPNTNCY | VCASKPEVTV | RLNVHKVTVL | TLQDKIVKEK | FAMVAPDVQI |
| 490 | 500 | 510 | 520 | 530 | 540 |
| EDGKGTILIS | SEEGETEANN | PKKLSDFGIR | NGSRLQADDF | LQDYTLLINI | LHSEDLGKDV |
| 550 | 560 | 570 | 580 | 590 | 600 |
| EFEVVGDSPE | KVGPKQAEDA | AKSIANGSDD | GAQPSTSTAQ | EQDDVLIVDS | DEEGPSNSTD |
| 610 | 620 | 630 | |||
| CSGDDKARKR | KLEENEAAST | KKCRLEQMED | PDDVIALD |