UniProt ID | I2BP1_MOUSE | |
---|---|---|
UniProt AC | Q8R3Y8 | |
Protein Name | Interferon regulatory factor 2-binding protein 1 | |
Gene Name | Irf2bp1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 584 | |
Subcellular Localization | Nucleus . | |
Protein Description | Acts as a transcriptional corepressor in a IRF2-dependent manner; this repression is not mediated by histone deacetylase activities. May act as an E3 ligase towards JDP2, enhancing its polyubiquitination. Represses ATF2-dependent transcriptional activation.. | |
Protein Sequence | MASVQASRRQWCYLCDLPKMPWAMVWDFSEAVCRGCVNFEGADRIELLIDAARQLKRSHVLPEGRSPGPPALKHPTSKDLASTGSQGSQLPPPQAQAQPSGTGGSVSGPDRYDRATSSSRLALPSPALEYTLGSRLANGLGREEAVAEGARRALLGSIPSLMPPGLLAAAVSGLGGRALTLAPGLSPARPLFGSDFEKEKQQRNADCLAELNEAMRGRAEEWHGRPKAVREQLLALSACAPFNVRFKKDHGLVGRVFAFDATARPPGYEFELKLFTEYPCGSGNVYAGVLAVARQMFHDALREPGKALASSGFKYLEYERRHGSGEWRQLGELLTDGVRSFREPAPAEALPQQYPEPAPAALCGPPPRAPSRNLAPTPRRRKASPEPEGETAGKMTTEEQQQRHWVAPGGPYSSETPGVPSPIAALKNVAEALGHSPKDPGGGGGSVRAGGASPAASSTTQPPAQHRLVARNGEAEVSPTAGAEAVSGGGSGTGATPGAPLCCTLCRERLEDTHFVQCPSVPGHKFCFPCSREFIKAQGPAGEVYCPSGDKCPLVGSSVPWAFMQGEIATILAGDIKVKKERDP | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
66 | Phosphorylation | HVLPEGRSPGPPALK CCCCCCCCCCCCCCC | 45.10 | 25521595 | |
125 | Phosphorylation | SSRLALPSPALEYTL CCCCCCCCHHHHHHH | 24.53 | 26239621 | |
130 | Phosphorylation | LPSPALEYTLGSRLA CCCHHHHHHHHHHHH | 14.23 | 28066266 | |
177 | Methylation | AVSGLGGRALTLAPG HHHCCCCCHHHCCCC | 25.32 | - | |
180 | Phosphorylation | GLGGRALTLAPGLSP CCCCCHHHCCCCCCC | 21.64 | 27600695 | |
186 | Phosphorylation | LTLAPGLSPARPLFG HHCCCCCCCCCCCCC | 23.56 | 26824392 | |
194 | Phosphorylation | PARPLFGSDFEKEKQ CCCCCCCCHHHHHHH | 31.62 | 27717184 | |
314 | Ubiquitination | ALASSGFKYLEYERR HHHHCCCCEEEEEHH | 53.07 | 22790023 | |
354 | Phosphorylation | AEALPQQYPEPAPAA HHHCCCCCCCCCCHH | 12.33 | 24759943 | |
371 | Phosphorylation | GPPPRAPSRNLAPTP CCCCCCCCCCCCCCC | 32.58 | 24453211 | |
377 | Phosphorylation | PSRNLAPTPRRRKAS CCCCCCCCCCCCCCC | 24.66 | 24453211 | |
384 | Phosphorylation | TPRRRKASPEPEGET CCCCCCCCCCCCCCC | 32.60 | 27087446 | |
391 | Phosphorylation | SPEPEGETAGKMTTE CCCCCCCCCCCCCHH | 52.12 | 28833060 | |
413 | Phosphorylation | VAPGGPYSSETPGVP CCCCCCCCCCCCCCC | 25.49 | 29472430 | |
414 | Phosphorylation | APGGPYSSETPGVPS CCCCCCCCCCCCCCC | 39.38 | 29472430 | |
416 | Phosphorylation | GGPYSSETPGVPSPI CCCCCCCCCCCCCHH | 27.56 | 29514104 | |
421 | Phosphorylation | SETPGVPSPIAALKN CCCCCCCCHHHHHHH | 26.91 | 25521595 | |
436 | Phosphorylation | VAEALGHSPKDPGGG HHHHHCCCCCCCCCC | 31.67 | 27087446 | |
446 | Phosphorylation | DPGGGGGSVRAGGAS CCCCCCCCCCCCCCC | 16.23 | 25619855 | |
453 | Phosphorylation | SVRAGGASPAASSTT CCCCCCCCCCCCCCC | 20.53 | 27087446 | |
457 | Phosphorylation | GGASPAASSTTQPPA CCCCCCCCCCCCCCH | 30.26 | 23984901 | |
458 | Phosphorylation | GASPAASSTTQPPAQ CCCCCCCCCCCCCHH | 30.65 | 25619855 | |
459 | Phosphorylation | ASPAASSTTQPPAQH CCCCCCCCCCCCHHH | 27.27 | 25619855 | |
460 | Phosphorylation | SPAASSTTQPPAQHR CCCCCCCCCCCHHHC | 40.81 | 25619855 | |
478 | Phosphorylation | RNGEAEVSPTAGAEA ECCEEEECCCCCCCC | 14.19 | 24453211 | |
480 | Phosphorylation | GEAEVSPTAGAEAVS CEEEECCCCCCCCCC | 30.16 | 21183079 | |
487 | Phosphorylation | TAGAEAVSGGGSGTG CCCCCCCCCCCCCCC | 38.48 | 23984901 | |
491 | Phosphorylation | EAVSGGGSGTGATPG CCCCCCCCCCCCCCC | 36.13 | 23984901 | |
493 | Phosphorylation | VSGGGSGTGATPGAP CCCCCCCCCCCCCCC | 25.91 | 23984901 | |
496 | Phosphorylation | GGSGTGATPGAPLCC CCCCCCCCCCCCCEE | 24.49 | 23984901 | |
504 | Phosphorylation | PGAPLCCTLCRERLE CCCCCEEHHHHHHHC | 28.09 | 25777480 | |
548 | Phosphorylation | AGEVYCPSGDKCPLV CCEEECCCCCCCCCC | 56.94 | 29899451 |
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 I2BP1_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of I2BP1_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 I2BP1_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of I2BP1_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453, AND MASSSPECTROMETRY. | |
"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-384; SER-436 ANDSER-453, AND MASS SPECTROMETRY. |