UniProt ID | MAFB_MOUSE | |
---|---|---|
UniProt AC | P54841 | |
Protein Name | Transcription factor MafB | |
Gene Name | Mafb | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 323 | |
Subcellular Localization | Nucleus . | |
Protein Description | Acts as a transcriptional activator or repressor. Plays a pivotal role in regulating lineage-specific hematopoiesis by repressing ETS1-mediated transcription of erythroid-specific genes in myeloid cells. Required for monocytic, macrophage, osteoclast, podocyte and islet beta cell differentiation. Involved in renal tubule survival and F4/80 maturation. Activates the insulin and glucagon promoters. Together with PAX6, transactivates weakly the glucagon gene promoter through the G1 element. SUMO modification controls its transcriptional activity and ability to specify macrophage fate. Binds element G1 on the glucagon promoter. Involved either as an oncogene or as a tumor suppressor, depending on the cell context.. | |
Protein Sequence | MAAELSMGQELPTSPLAMEYVNDFDLLKFDVKKEPLGRAERPGRPCTRLQPAGSVSSTPLSTPCSSVPSSPSFSPTEPKTHLEDLYWMASNYQQMNPEALNLTPEDAVEALIGSHPVPQPLQSFDGFRSAHHHHHHHHPHPHHGYPGAGVTHDDLGQHAHPHHHHHHQASPPPSSAASPAQQLPTSHPGPGPHATAAATAAGGNGSVEDRFSDDQLVSMSVRELNRHLRGFTKDEVIRLKQKRRTLKNRGYAQSCRYKRVQQKHHLENEKTQLIQQVEQLKQEVSRLARERDAYKVKCEKLANSGFREAGSTSDSPSSPEFFL | |
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 |
---|---|---|---|---|---|
13 | Phosphorylation | SMGQELPTSPLAMEY CCCCCCCCCCCHHHH | 56.45 | 24719451 | |
14 | Phosphorylation | MGQELPTSPLAMEYV CCCCCCCCCCHHHHC | 18.90 | 26824392 | |
32 | Sumoylation | DLLKFDVKKEPLGRA HCEECCCCCCCCCCC | 53.95 | - | |
32 | Sumoylation | DLLKFDVKKEPLGRA HCEECCCCCCCCCCC | 53.95 | 17548468 | |
58 | Phosphorylation | PAGSVSSTPLSTPCS CCCCCCCCCCCCCCC | 22.27 | 23984901 | |
61 | Phosphorylation | SVSSTPLSTPCSSVP CCCCCCCCCCCCCCC | 31.35 | 20208071 | |
62 | Phosphorylation | VSSTPLSTPCSSVPS CCCCCCCCCCCCCCC | 35.68 | 19932079 | |
65 | Phosphorylation | TPLSTPCSSVPSSPS CCCCCCCCCCCCCCC | 35.26 | 20208071 | |
66 | Phosphorylation | PLSTPCSSVPSSPSF CCCCCCCCCCCCCCC | 44.77 | 20208071 | |
69 | Phosphorylation | TPCSSVPSSPSFSPT CCCCCCCCCCCCCCC | 53.37 | 20208071 | |
70 | Phosphorylation | PCSSVPSSPSFSPTE CCCCCCCCCCCCCCC | 20.63 | 20208071 | |
72 | Phosphorylation | SSVPSSPSFSPTEPK CCCCCCCCCCCCCCC | 40.06 | 20208071 | |
74 | Phosphorylation | VPSSPSFSPTEPKTH CCCCCCCCCCCCCCH | 34.94 | 20208071 | |
76 | Phosphorylation | SSPSFSPTEPKTHLE CCCCCCCCCCCCHHH | 64.82 | 20208071 | |
103 | Phosphorylation | NPEALNLTPEDAVEA CHHHHCCCHHHHHHH | 24.45 | 20208071 | |
114 | Phosphorylation | AVEALIGSHPVPQPL HHHHHHCCCCCCCCC | 20.02 | 20208071 | |
123 | Phosphorylation | PVPQPLQSFDGFRSA CCCCCCCCCCCCCCC | 32.75 | 20208071 | |
151 | Phosphorylation | GYPGAGVTHDDLGQH CCCCCCCCCCCCCCC | 20.76 | 20208071 | |
170 | Phosphorylation | HHHHHQASPPPSSAA CCCCCCCCCCCCCCC | 31.22 | 20208071 | |
174 | Phosphorylation | HQASPPPSSAASPAQ CCCCCCCCCCCCHHH | 38.08 | 20208071 | |
178 | Phosphorylation | PPPSSAASPAQQLPT CCCCCCCCHHHHCCC | 22.08 | 20208071 | |
206 | Phosphorylation | TAAGGNGSVEDRFSD HHCCCCCCHHHCCCH | 26.74 | 20208071 | |
212 | Phosphorylation | GSVEDRFSDDQLVSM CCHHHCCCHHHHHHH | 40.97 | 20208071 | |
218 | Phosphorylation | FSDDQLVSMSVRELN CCHHHHHHHHHHHHH | 17.58 | 22817900 | |
220 | Phosphorylation | DDQLVSMSVRELNRH HHHHHHHHHHHHHHH | 15.54 | 22817900 | |
297 | Sumoylation | ERDAYKVKCEKLANS HHHHHHHHHHHHHHC | 32.31 | - | |
297 | Sumoylation | ERDAYKVKCEKLANS HHHHHHHHHHHHHHC | 32.31 | 17548468 | |
304 | Phosphorylation | KCEKLANSGFREAGS HHHHHHHCCCCCCCC | 33.43 | 20208071 | |
311 | Phosphorylation | SGFREAGSTSDSPSS CCCCCCCCCCCCCCC | 31.61 | 20208071 | |
312 | Phosphorylation | GFREAGSTSDSPSSP CCCCCCCCCCCCCCC | 35.32 | 20208071 | |
313 | Phosphorylation | FREAGSTSDSPSSPE CCCCCCCCCCCCCCC | 37.48 | 20208071 | |
315 | Phosphorylation | EAGSTSDSPSSPEFF CCCCCCCCCCCCCCC | 26.84 | 20208071 | |
317 | Phosphorylation | GSTSDSPSSPEFFL- CCCCCCCCCCCCCC- | 63.58 | 20208071 | |
318 | Phosphorylation | STSDSPSSPEFFL-- CCCCCCCCCCCCC-- | 31.65 | 20208071 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
62 | T | Phosphorylation | Kinase | MAPK8 | P45983 | GPS |
* 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 MAFB_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
TAF5_MOUSE | Taf5 | physical | 20211142 | |
JUN_MOUSE | Jun | physical | 12798298 | |
SUMO1_HUMAN | SUMO1 | physical | 17548468 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Sumoylation | |
Reference | PubMed |
"SUMO modification regulates MafB-driven macrophage differentiation byenabling Myb-dependent transcriptional repression."; Tillmanns S., Otto C., Jaffray E., Du Roure C., Bakri Y., Vanhille L.,Sarrazin S., Hay R.T., Sieweke M.H.; Mol. Cell. Biol. 27:5554-5564(2007). Cited for: FUNCTION, SUMOYLATION AT LYS-32 AND LYS-297, AND MUTAGENESIS OF LYS-32AND LYS-297. |