MAFK_MOUSE
ID MAFK_MOUSE Reviewed; 156 AA.
AC Q61827; Q60600;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Transcription factor MafK;
DE AltName: Full=Erythroid transcription factor NF-E2 p18 subunit;
GN Name=Mafk; Synonyms=Nfe2u;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7706310; DOI=10.1074/jbc.270.13.7615;
RA Igarashi K., Itoh K., Motohashi H., Hayashi N., Matuzaki Y., Nakauchi H.,
RA Nishizawa M., Yamamoto M.;
RT "Activity and expression of murine small Maf family protein MafK.";
RL J. Biol. Chem. 270:7615-7624(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=DBA; TISSUE=Hematopoietic;
RX PubMed=8265578; DOI=10.1073/pnas.90.24.11488;
RA Andrews N.C., Kotkow K.J., Ney P.A., Erdjument-Bromage H., Tempst P.,
RA Orkin S.H.;
RT "The ubiquitous subunit of erythroid transcription factor NF-E2 is a small
RT basic-leucine zipper protein related to the v-maf oncogene.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:11488-11492(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND INTERACTION WITH NFE2L2.
RX PubMed=9240432; DOI=10.1006/bbrc.1997.6943;
RA Itoh K., Chiba T., Takahashi S., Ishii T., Igarashi K., Katoh Y., Oyake T.,
RA Hayashi N., Satoh K., Hatayama I., Yamamoto M., Nabeshima Y.;
RT "An Nrf2/small Maf heterodimer mediates the induction of phase II
RT detoxifying enzyme genes through antioxidant response elements.";
RL Biochem. Biophys. Res. Commun. 236:313-322(1997).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Since they lack a putative transactivation domain, the small
CC Mafs behave as transcriptional repressors when they dimerize among
CC themselves (By similarity). However, they act as transcriptional
CC activators by dimerizing with other (usually larger) basic-zipper
CC proteins, such as NFE2, NFE2L1/NRF1, NFE2L2/NRF2 and NFE2L3/NRF3, and
CC recruiting them to specific DNA-binding sites (PubMed:9240432). Small
CC Maf proteins heterodimerize with Fos and may act as competitive
CC repressors of the NF-E2 transcription factor (By similarity).
CC {ECO:0000250|UniProtKB:O60675, ECO:0000269|PubMed:9240432}.
CC -!- SUBUNIT: Homodimer or heterodimer (By similarity). It can form high
CC affinity heterodimers with members of the CNC-bZIP family such as NFE2,
CC NFE2L1/NRF1, NFE2L2/NRF2 and NFE2L3/NRF3 (PubMed:9240432).
CC {ECO:0000250|UniProtKB:O60675, ECO:0000269|PubMed:9240432}.
CC -!- INTERACTION:
CC Q61827; P97302: Bach1; NbExp=5; IntAct=EBI-15740843, EBI-2552417;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle and
CC placenta. Also expressed in erythroid cells.
CC -!- SIMILARITY: Belongs to the bZIP family. Maf subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D42124; BAA07704.1; -; mRNA.
DR EMBL; U01036; AAC52132.1; -; mRNA.
DR EMBL; BC014295; AAH14295.1; -; mRNA.
DR CCDS; CCDS19814.1; -.
DR PIR; A49391; A49391.
DR PIR; A56124; A56124.
DR RefSeq; NP_034887.1; NM_010757.2.
DR RefSeq; XP_006504716.1; XM_006504653.3.
DR AlphaFoldDB; Q61827; -.
DR SMR; Q61827; -.
DR BioGRID; 201284; 6.
DR DIP; DIP-46345N; -.
DR IntAct; Q61827; 3.
DR STRING; 10090.ENSMUSP00000018287; -.
DR iPTMnet; Q61827; -.
DR PhosphoSitePlus; Q61827; -.
DR EPD; Q61827; -.
DR MaxQB; Q61827; -.
DR PaxDb; Q61827; -.
DR PRIDE; Q61827; -.
DR ProteomicsDB; 252714; -.
DR Antibodypedia; 24241; 164 antibodies from 25 providers.
DR DNASU; 17135; -.
DR Ensembl; ENSMUST00000018287; ENSMUSP00000018287; ENSMUSG00000018143.
DR Ensembl; ENSMUST00000110836; ENSMUSP00000106460; ENSMUSG00000018143.
DR GeneID; 17135; -.
DR KEGG; mmu:17135; -.
DR UCSC; uc009ahd.1; mouse.
DR CTD; 7975; -.
DR MGI; MGI:99951; Mafk.
DR VEuPathDB; HostDB:ENSMUSG00000018143; -.
DR eggNOG; KOG4196; Eukaryota.
DR GeneTree; ENSGT00940000160044; -.
DR HOGENOM; CLU_112948_0_0_1; -.
DR InParanoid; Q61827; -.
DR OMA; KSANHNS; -.
DR OrthoDB; 1395389at2759; -.
DR PhylomeDB; Q61827; -.
DR TreeFam; TF325689; -.
DR Reactome; R-MMU-9707616; Heme signaling.
DR Reactome; R-MMU-9708530; Regulation of BACH1 activity.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 17135; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q61827; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q61827; protein.
DR Bgee; ENSMUSG00000018143; Expressed in granulocyte and 203 other tissues.
DR ExpressionAtlas; Q61827; baseline and differential.
DR Genevisible; Q61827; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0071535; F:RING-like zinc finger domain binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0007399; P:nervous system development; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR004826; bZIP_Maf.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR028574; MafK.
DR InterPro; IPR008917; TF_DNA-bd_sf.
DR InterPro; IPR024874; Transcription_factor_Maf_fam.
DR PANTHER; PTHR10129; PTHR10129; 1.
DR PANTHER; PTHR10129:SF26; PTHR10129:SF26; 1.
DR Pfam; PF03131; bZIP_Maf; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF47454; SSF47454; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..156
FT /note="Transcription factor MafK"
FT /id="PRO_0000076504"
FT DOMAIN 51..114
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 51..76
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 79..93
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 130
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60675"
FT CONFLICT 36..37
FT /note="EL -> DV (in Ref. 2; AAC52132)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 156 AA; 17537 MW; 39F98F8A257F46CB CRC64;
MTTNPKPNKA LKVKKEAGEN APVLSDDELV SMSVRELNQH LRGLTKEEVT RLKQRRRTLK
NRGYAASCRI KRVTQKEELE RQRVELQQEV EKLARENSSM RLELDALRSK YEALQTFART
VARGPVTPTK VATTSVITIV KSAELSSTSV PFSAAS
