| UniProt ID | HDGR3_MOUSE | |
|---|---|---|
| UniProt AC | Q9JMG7 | |
| Protein Name | Hepatoma-derived growth factor-related protein 3 | |
| Gene Name | Hdgfl3 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 202 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | Enhances DNA synthesis and may play a role in cell proliferation.. | |
| Protein Sequence | MARPRPREYKAGDLVFAKMKGYPHWPARIDELPEGAVKPPANKYPIFFFGTHETAFLGPKDLFPYKEYKDKFGKSNKRKGFNEGLWEIENNPGVKFTGYQTIQQQSSSETEGEGGNTADASSEEEGDRVEDGKGKRKNEKGGSKRKKSYTSKKSSKQSRKSPGDEDDKDCKEEENKSSSEGGDAGNDTRNTTADLQKAGEGT | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 10 | Ubiquitination | RPRPREYKAGDLVFA CCCCCCCCCCCEEEE | 40.93 | 22790023 | |
| 10 (in isoform 2) | Ubiquitination | - | 40.93 | 22790023 | |
| 66 | Ubiquitination | PKDLFPYKEYKDKFG HHHCCCHHHHHHHHC | 55.60 | 22790023 | |
| 66 (in isoform 2) | Ubiquitination | - | 55.60 | 22790023 | |
| 97 | Phosphorylation | NNPGVKFTGYQTIQQ CCCCCCEEEEEEEEC | 29.30 | 25293948 | |
| 99 | Phosphorylation | PGVKFTGYQTIQQQS CCCCEEEEEEEECCC | 10.22 | 24925903 | |
| 101 | Phosphorylation | VKFTGYQTIQQQSSS CCEEEEEEEECCCCC | 16.57 | 25293948 | |
| 106 | Phosphorylation | YQTIQQQSSSETEGE EEEEECCCCCCCCCC | 31.34 | 24925903 | |
| 107 | Phosphorylation | QTIQQQSSSETEGEG EEEECCCCCCCCCCC | 28.05 | 24925903 | |
| 108 | Phosphorylation | TIQQQSSSETEGEGG EEECCCCCCCCCCCC | 54.51 | 24925903 | |
| 110 | Phosphorylation | QQQSSSETEGEGGNT ECCCCCCCCCCCCCC | 51.76 | 24925903 | |
| 117 | Phosphorylation | TEGEGGNTADASSEE CCCCCCCCCCCCCHH | 29.23 | 24925903 | |
| 121 | Phosphorylation | GGNTADASSEEEGDR CCCCCCCCCHHCCCC | 38.54 | 24925903 | |
| 122 | Phosphorylation | GNTADASSEEEGDRV CCCCCCCCHHCCCCC | 51.23 | 24925903 | |
| 158 | Phosphorylation | SKKSSKQSRKSPGDE CCCCCCCCCCCCCCC | 45.47 | 23684622 | |
| 161 | Phosphorylation | SSKQSRKSPGDEDDK CCCCCCCCCCCCCCH | 32.76 | 27087446 | |
| 176 | Ubiquitination | DCKEEENKSSSEGGD HHHHHHHHCCCCCCC | 55.80 | 27667366 | |
| 177 | Phosphorylation | CKEEENKSSSEGGDA HHHHHHHCCCCCCCC | 51.16 | 25521595 | |
| 178 | Phosphorylation | KEEENKSSSEGGDAG HHHHHHCCCCCCCCC | 33.74 | 22324799 | |
| 179 | Phosphorylation | EEENKSSSEGGDAGN HHHHHCCCCCCCCCC | 47.56 | 25521595 | |
| 188 | Phosphorylation | GGDAGNDTRNTTADL CCCCCCCCCCCHHHH | 29.80 | 29899451 | |
| 191 | Phosphorylation | AGNDTRNTTADLQKA CCCCCCCCHHHHHHH | 21.77 | 22324799 | |
| 192 | Phosphorylation | GNDTRNTTADLQKAG CCCCCCCHHHHHHHC | 23.02 | 22324799 | |
| 197 | Ubiquitination | NTTADLQKAGEGT-- CCHHHHHHHCCCC-- | 66.70 | - |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of HDGR3_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HDGR3_MOUSE !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of HDGR3_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of HDGR3_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-178 ANDSER-179, AND MASS SPECTROMETRY. | |