Q6DFR2
Gene name |
cblb |
Protein name |
E3 ubiquitin-protein ligase CBL-B |
Names |
EC 2.3.2.27 , RING-type E3 ubiquitin transferase CBL-B , SH3-binding protein CBL-B , Signal transduction protein CBL-B |
Species |
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
KEGG Pathway |
xtr:448509 |
EC number |
2.3.2.-: Aminoacyltransferases |
Protein Class |
|

Descriptions
Autoinhibitory domains (AIDs)
Target domain |
50-354 (TKB domain) |
Relief mechanism |
PTM |
Assay |
|
Accessory elements
No accessory elements
References
- Kobashigawa Y et al. (2011) "Autoinhibition and phosphorylation-induced activation mechanisms of human cancer and autoimmune disease-related E3 protein Cbl-b", Proceedings of the National Academy of Sciences of the United States of America, 108, 20579-84
- Dou H et al. (2012) "Structural basis for autoinhibition and phosphorylation-dependent activation of c-Cbl", Nature structural & molecular biology, 19, 184-92
- Wybenga-Groot LE et al. (2021) "SLAP2 Adaptor Binding Disrupts c-CBL Autoinhibition to Activate Ubiquitin Ligase Function", Journal of molecular biology, 433, 166880
Autoinhibited structure

Activated structure

1 structures for Q6DFR2
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
AF-Q6DFR2-F1 | Predicted | AlphaFoldDB |
No variants for Q6DFR2
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
No variants for Q6DFR2 |
No associated diseases with Q6DFR2
8 regional properties for Q6DFR2
Type | Name | Position | InterPro Accession |
---|---|---|---|
domain | Zinc finger, RING-type | 384 - 423 | IPR001841 |
domain | Adaptor protein Cbl, N-terminal helical | 53 - 178 | IPR003153 |
domain | Adaptor protein Cbl, EF hand-like | 182 - 265 | IPR014741 |
domain | Adaptor protein Cbl, SH2-like domain | 259 - 353 | IPR014742 |
domain | Ubiquitin-associated domain | 927 - 970 | IPR015940 |
conserved_site | Zinc finger, RING-type, conserved site | 399 - 408 | IPR017907 |
domain | Zinc finger, C3HC4 RING-type | 384 - 422 | IPR018957 |
domain | Adaptor protein Cbl, PTB domain | 46 - 354 | IPR024159 |
Functions
Description | ||
---|---|---|
EC Number | 2.3.2.- | Aminoacyltransferases |
Subcellular Localization |
|
|
PANTHER Family | ||
PANTHER Subfamily | ||
PANTHER Protein Class | ||
PANTHER Pathway Category | No pathway information available |
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. |
membrane raft | Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions. |
plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
5 GO annotations of molecular function
Name | Definition |
---|---|
calcium ion binding | Binding to a calcium ion (Ca2+). |
phosphotyrosine residue binding | Binding to a phosphorylated tyrosine residue within a protein. |
receptor tyrosine kinase binding | Binding to a receptor that possesses protein tyrosine kinase activity. |
SH3 domain binding | Binding to a SH3 domain (Src homology 3) of a protein, small protein modules containing approximately 50 amino acid residues found in a great variety of intracellular or membrane-associated proteins. |
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 |
3 GO annotations of biological process
Name | Definition |
---|---|
cell surface receptor signaling pathway | The series of molecular signals initiated by activation of a receptor on the surface of a cell. The pathway begins with binding of an extracellular ligand to a cell surface receptor, or for receptors that signal in the absence of a ligand, by ligand-withdrawal or the activity of a constitutively active receptor. The pathway ends with regulation of a downstream cellular process, e.g. transcription. |
protein ubiquitination | The process in which one or more ubiquitin groups are added to a protein. |
regulation of platelet-derived growth factor receptor-alpha signaling pathway | Any process that modulates the frequency, rate or extent of platelet-derived growth factor receptor-alpha signaling pathway. |
10 | 20 | 30 | 40 | 50 | 60 |
MASSSSSSSS | TNSSAVTGRL | PGARSANPRK | ARILGLFDAI | QDAVGPPKQA | AADRRTVEKT |
70 | 80 | 90 | 100 | 110 | 120 |
WKLMDKVVRL | CQNPKLQLKN | SPPYILDILP | DTYQHLRLIL | SKYDDNQKLA | QLSENEYFKI |
130 | 140 | 150 | 160 | 170 | 180 |
YIDSLMKKSK | RAIRLFKEGK | ERMYEEQSQE | RRNLTKLSLI | FSHMLAEIKA | IFPSGQFQGD |
190 | 200 | 210 | 220 | 230 | 240 |
NFRITKADAA | EFWRKFFGER | TIVPWKIFRQ | CLHEVHQISS | GLEAMALKST | IDLTCNDYIS |
250 | 260 | 270 | 280 | 290 | 300 |
VFEFDIFTRL | FQPWTSILRN | WNFLAVTHPG | YMAFLTYDEV | KARLQKYSTK | PGSYIFRLSC |
310 | 320 | 330 | 340 | 350 | 360 |
TRLGQWAIGY | VTADGNILQT | IPHNKPLFQA | LIDGSREGFY | LYPDGRSYNP | DLTDLCEPTP |
370 | 380 | 390 | 400 | 410 | 420 |
HDHIKVTQEQ | YELYCEMGST | FQLCKICAEN | DKDVKIEPCG | HLMCTSCLTS | WQESDGQGCP |
430 | 440 | 450 | 460 | 470 | 480 |
FCRCEIKGTE | PIVVDPFDPR | DENRCCSFND | SLCTPMLDFD | DDDLREECLI | MNRLASLRKM |
490 | 500 | 510 | 520 | 530 | 540 |
NERQNSPVTS | PGSSPLSQRR | KTPPDPLQIP | HLNLPPVPPR | LDLIQKGLAR | SPCASPTGSP |
550 | 560 | 570 | 580 | 590 | 600 |
KSSPCMVRKQ | DKPLPAPPPP | LREPPPPPER | PPPIPPDSRT | CRHLHHTENV | PCRDQSTQHD |
610 | 620 | 630 | 640 | 650 | 660 |
AWCTRDISGA | SQPSICRVAH | DGSPKLGVPS | SSVLNGRHSR | MSTEAGFIRH | KHHKRRESPL |
670 | 680 | 690 | 700 | 710 | 720 |
ETIRVYNGLS | GNEEYDVPPR | LSPPPPPPTI | TIHPAIKCPL | LVNSVSDKVR | NSAEEDDSEY |
730 | 740 | 750 | 760 | 770 | 780 |
KIPSSHPVSS | RLPLHCHSIK | HFPRLCENGQ | CLSNGTHNGI | SEIKKLKQPD | QGDVIATSTV |
790 | 800 | 810 | 820 | 830 | 840 |
PVPLPSARTS | ARENHPHGSS | LTRTPSDYDL | LVPHPGEESF | DSSPPSQPPP | PPPARTCVPE |
850 | 860 | 870 | 880 | 890 | 900 |
HAMPTASGCR | PNSDVDLFLP | HSDPCPEAPL | PPARRGPGEA | KSNRLSQEYD | QLPSCPDCPQ |
910 | 920 | 930 | 940 | 950 | 960 |
APARPPKPVP | RRTAPEIHHR | RHYNCDSLAE | NVDAKIAKLM | GEGFPFEEVK | RALEIAQNNV |
970 | 980 | ||||
DVARSILREF | AFPPPVCPRL | HL |