UniProt ID | ARI3A_MOUSE | |
---|---|---|
UniProt AC | Q62431 | |
Protein Name | AT-rich interactive domain-containing protein 3A | |
Gene Name | Arid3a | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 601 | |
Subcellular Localization | Nucleus. Cytoplasm. Shuttles between nucleus and cytoplasm. | |
Protein Description | Transcription factor involved in B-cell differentiation. Binds a VH promoter proximal site necessary for induced mu-heavy-chain transcription. Binds the minor groove of a restricted ATC sequence that is sufficient for nuclear matrix association. This sequence motif is present in matrix-associating regions (MARS) proximal to the promoter and flanking E mu. Activates E mu-driven transcription by binding these sites. May be involved in the control of cell cycle progression by the RB1/E2F1 pathway.. | |
Protein Sequence | MKLQAVMETLIQRQQRARQELEARQAPPPPPPEPTGVRARTTMTDEDREPENARMHRTQMAALAAMRAAAAGLGHPSSPGGSEDGPPISGDEDTAREGTLSSPALHGSVLEGAGHAEGDRHLMDVGSDDDDTKSKWEEQELEELGEEEEEEEEEDDFEEEEEEEEGLGPPESASLGTAGLFTRKAPPAQAFRGDGGPRMLSGPERLGPGPAHPSHMASQMPPPDHGDWTFEEQFKQLYELDADPKRKEFLDDLFSFMQKRGTPVNRIPIMAKQVLDLFMLYVLVTEKGGLVEVINKKLWREITKGLNLPTSITSAAFTLRTQYMKYLYPYECERRGLSSPNELQAAIDSNRREGRRQSFGGSLFAYSPSGAHSMLPSPKLPVTPLGLAASTNGSSITPAPKIKKEEDSAIPITVPGRLPVSLAGHPVVAAQAAAVQAAAAQAAVAAQAAALEQLREKLESTEPPEKKMALVADEQQRLMQRAVQQSFLAMTAQLPMNIRINSQASESRQDSAVSLTSANGSNSISMSVEMNGIVYTGVLFAQPPPPTAPSAPGKGGVSSIGTNTTTGSRTGASGSTVSGGQVGLPGVSTPTMSSTSNNSLP | |
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 |
---|---|---|---|---|---|
41 | Phosphorylation | PTGVRARTTMTDEDR CCCCCCCCCCCCCCC | 21.67 | 24759943 | |
42 | Phosphorylation | TGVRARTTMTDEDRE CCCCCCCCCCCCCCC | 16.72 | 24759943 | |
44 | Phosphorylation | VRARTTMTDEDREPE CCCCCCCCCCCCCHH | 33.86 | 24759943 | |
77 | Phosphorylation | AAGLGHPSSPGGSED HHCCCCCCCCCCCCC | 43.41 | 22942356 | |
78 | Phosphorylation | AGLGHPSSPGGSEDG HCCCCCCCCCCCCCC | 31.83 | 22942356 | |
82 | Phosphorylation | HPSSPGGSEDGPPIS CCCCCCCCCCCCCCC | 38.13 | 22942356 | |
89 | Phosphorylation | SEDGPPISGDEDTAR CCCCCCCCCCCCCCC | 46.06 | 21082442 | |
94 | Phosphorylation | PISGDEDTAREGTLS CCCCCCCCCCCCCCC | 26.10 | 25619855 | |
99 | Phosphorylation | EDTAREGTLSSPALH CCCCCCCCCCCHHHC | 20.79 | 25159016 | |
101 | Phosphorylation | TAREGTLSSPALHGS CCCCCCCCCHHHCCH | 33.83 | 28507225 | |
102 | Phosphorylation | AREGTLSSPALHGSV CCCCCCCCHHHCCHH | 19.80 | 24704852 | |
108 | Phosphorylation | SSPALHGSVLEGAGH CCHHHCCHHHCCCCC | 16.87 | 28066266 | |
127 | Phosphorylation | RHLMDVGSDDDDTKS CCEECCCCCCCCHHH | 37.40 | 27742792 | |
132 | Phosphorylation | VGSDDDDTKSKWEEQ CCCCCCCHHHHHHHH | 44.18 | 25619855 | |
134 | Phosphorylation | SDDDDTKSKWEEQEL CCCCCHHHHHHHHHH | 45.13 | 25367039 | |
338 | Phosphorylation | ECERRGLSSPNELQA HHHHCCCCCHHHHHH | 46.72 | 24719451 | |
339 | Phosphorylation | CERRGLSSPNELQAA HHHCCCCCHHHHHHH | 36.47 | 26745281 | |
358 | Phosphorylation | RREGRRQSFGGSLFA CCCCCCCCCCCCEEE | 24.85 | 25266776 | |
362 | Phosphorylation | RRQSFGGSLFAYSPS CCCCCCCCEEEECCC | 22.24 | 26745281 | |
366 | Phosphorylation | FGGSLFAYSPSGAHS CCCCEEEECCCCCCC | 17.49 | 30635358 | |
367 | Phosphorylation | GGSLFAYSPSGAHSM CCCEEEECCCCCCCC | 14.79 | 19060867 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of ARI3A_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ARI3A_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 ARI3A_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, 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-127, AND MASSSPECTROMETRY. |