UniProt ID | MAFK_HUMAN | |
---|---|---|
UniProt AC | O60675 | |
Protein Name | Transcription factor MafK | |
Gene Name | MAFK | |
Organism | Homo sapiens (Human). | |
Sequence Length | 156 | |
Subcellular Localization | Nucleus. | |
Protein Description | Since they lack a putative transactivation domain, the small Mafs behave as transcriptional repressors when they dimerize among themselves. [PubMed: 9150357 However, they seem to serve as transcriptional activators by dimerizing with other (usually larger) basic-zipper proteins, such as NFE2, NFE2L1/NRF1, NFE2L2/NRF2 and NFE2L3/NRF3, and recruiting them to specific DNA-binding sites] | |
Protein Sequence | MTTNPKPNKALKVKKEAGENAPVLSDDELVSMSVRELNQHLRGLTKEEVTRLKQRRRTLKNRGYAASCRIKRVTQKEELERQRVELQQEVEKLARENSSMRLELDALRSKYEALQTFARTVARGPVAPSKVATTSVITIVKSTELSSTSVPFSAAS | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MTTNPKPNK ------CCCCCCCCC | 34.97 | 26699800 | |
3 | Phosphorylation | -----MTTNPKPNKA -----CCCCCCCCCC | 48.50 | 26699800 | |
9 | Ubiquitination | TTNPKPNKALKVKKE CCCCCCCCCCCCCCC | 64.72 | - | |
25 | Phosphorylation | GENAPVLSDDELVSM CCCCCCCCHHHHHHH | 43.16 | 29255136 | |
31 | Phosphorylation | LSDDELVSMSVRELN CCHHHHHHHHHHHHH | 20.26 | 29255136 | |
33 | Phosphorylation | DDELVSMSVRELNQH HHHHHHHHHHHHHHH | 15.54 | 29396449 | |
46 | Sumoylation | QHLRGLTKEEVTRLK HHHCCCCHHHHHHHH | 57.85 | - | |
46 | Ubiquitination | QHLRGLTKEEVTRLK HHHCCCCHHHHHHHH | 57.85 | - | |
46 | Sumoylation | QHLRGLTKEEVTRLK HHHCCCCHHHHHHHH | 57.85 | - | |
71 | Acetylation | YAASCRIKRVTQKEE HHHHHHEEECCCHHH | 22.82 | 20167786 | |
74 | Phosphorylation | SCRIKRVTQKEELER HHHEEECCCHHHHHH | 37.65 | - | |
76 | Ubiquitination | RIKRVTQKEELERQR HEEECCCHHHHHHHH | 43.73 | - | |
76 | Sumoylation | RIKRVTQKEELERQR HEEECCCHHHHHHHH | 43.73 | - | |
76 | Sumoylation | RIKRVTQKEELERQR HEEECCCHHHHHHHH | 43.73 | - | |
92 | Ubiquitination | ELQQEVEKLARENSS HHHHHHHHHHHHCCC | 53.26 | - | |
98 | Phosphorylation | EKLARENSSMRLELD HHHHHHCCCHHHHHH | 22.28 | 28555341 | |
99 | Phosphorylation | KLARENSSMRLELDA HHHHHCCCHHHHHHH | 21.36 | 25954137 | |
109 | Phosphorylation | LELDALRSKYEALQT HHHHHHHHHHHHHHH | 40.20 | 25954137 | |
110 | Ubiquitination | ELDALRSKYEALQTF HHHHHHHHHHHHHHH | 40.45 | 21890473 | |
110 | Ubiquitination | ELDALRSKYEALQTF HHHHHHHHHHHHHHH | 40.45 | 21890473 | |
110 | Sumoylation | ELDALRSKYEALQTF HHHHHHHHHHHHHHH | 40.45 | - | |
110 | Sumoylation | ELDALRSKYEALQTF HHHHHHHHHHHHHHH | 40.45 | - | |
111 | Phosphorylation | LDALRSKYEALQTFA HHHHHHHHHHHHHHH | 14.00 | - | |
120 | O-linked_Glycosylation | ALQTFARTVARGPVA HHHHHHHHHHCCCCC | 18.32 | 20068230 | |
130 | Sumoylation | RGPVAPSKVATTSVI CCCCCCCCCEECEEE | 34.53 | 28112733 | |
130 | Ubiquitination | RGPVAPSKVATTSVI CCCCCCCCCEECEEE | 34.53 | - | |
133 | Phosphorylation | VAPSKVATTSVITIV CCCCCCEECEEEEEE | 23.69 | - | |
133 | O-linked_Glycosylation | VAPSKVATTSVITIV CCCCCCEECEEEEEE | 23.69 | 20068230 | |
134 | Phosphorylation | APSKVATTSVITIVK CCCCCEECEEEEEEE | 15.97 | 20068230 | |
134 | O-linked_Glycosylation | APSKVATTSVITIVK CCCCCEECEEEEEEE | 15.97 | 20068230 | |
134 | O-linked_Glycosylation | APSKVATTSVITIVK CCCCCEECEEEEEEE | 15.97 | 30059200 | |
135 | O-linked_Glycosylation | PSKVATTSVITIVKS CCCCEECEEEEEEEC | 13.73 | 20068230 | |
138 | O-linked_Glycosylation | VATTSVITIVKSTEL CEECEEEEEEECCCC | 19.98 | 20068230 | |
142 | O-linked_Glycosylation | SVITIVKSTELSSTS EEEEEEECCCCCCCC | 19.07 | 20068230 | |
146 | O-linked_Glycosylation | IVKSTELSSTSVPFS EEECCCCCCCCCCCC | 25.90 | 20068230 | |
147 | O-linked_Glycosylation | VKSTELSSTSVPFSA EECCCCCCCCCCCCC | 37.01 | 20068230 | |
153 | O-linked_Glycosylation | SSTSVPFSAAS---- CCCCCCCCCCC---- | 19.49 | 30059200 | |
153 | O-linked_Glycosylation | SSTSVPFSAAS---- CCCCCCCCCCC---- | 19.49 | 20068230 | |
156 | O-linked_Glycosylation | SVPFSAAS------- CCCCCCCC------- | 40.23 | 20068230 |
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 MAFK_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MAFK_HUMAN !! |
* 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 MAFK_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
NF2L2_HUMAN | NFE2L2 | physical | 10747902 | |
KAT6A_HUMAN | KAT6A | physical | 17083329 | |
BACH1_HUMAN | BACH1 | physical | 19011633 | |
HDAC1_HUMAN | HDAC1 | physical | 18241676 | |
HDAC2_HUMAN | HDAC2 | physical | 18241676 | |
HDAC3_HUMAN | HDAC3 | physical | 18241676 | |
TF65_HUMAN | RELA | physical | 18241676 | |
NF2L2_HUMAN | NFE2L2 | physical | 21988832 | |
NF2L2_HUMAN | NFE2L2 | physical | 23737527 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASSSPECTROMETRY. | |
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASSSPECTROMETRY. | |
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASSSPECTROMETRY. |