MAFB_HUMAN
ID MAFB_HUMAN Reviewed; 323 AA.
AC Q9Y5Q3; B3KNE1; Q9H1F1;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Transcription factor MafB;
DE Short=Maf-B;
DE AltName: Full=V-maf musculoaponeurotic fibrosarcoma oncogene homolog B;
GN Name=MAFB; Synonyms=KRML;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Bone marrow;
RX PubMed=10444328; DOI=10.1006/geno.1999.5884;
RA Wang P.W., Eisenbart J.D., Cordes S.P., Barsh G.S., Stoffel M.,
RA Le Beau M.M.;
RT "Human KRML (MAFB): cDNA cloning, genomic structure, and evaluation as a
RT candidate tumor suppressor gene in myeloid leukemias.";
RL Genomics 59:275-281(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [6]
RP INTERACTION WITH LRP1.
RX PubMed=15135046; DOI=10.1016/j.febslet.2004.03.069;
RA Petersen H.H., Hilpert J., Jacobsen C., Lauwers A., Roebroek A.J.M.,
RA Willnow T.E.;
RT "Low-density lipoprotein receptor-related protein interacts with MafB, a
RT regulator of hindbrain development.";
RL FEBS Lett. 565:23-27(2004).
RN [7]
RP PHOSPHORYLATION.
RX PubMed=15963504; DOI=10.1016/j.febslet.2005.04.086;
RA Sii-Felice K., Pouponnot C., Gillet S., Lecoin L., Girault J.-A.,
RA Eychene A., Felder-Schmittbuhl M.-P.;
RT "MafA transcription factor is phosphorylated by p38 MAP kinase.";
RL FEBS Lett. 579:3547-3554(2005).
RN [8]
RP PHOSPHORYLATION.
RX PubMed=18042454; DOI=10.1016/j.molcel.2007.11.009;
RA Rocques N., Abou Zeid N., Sii-Felice K., Lecoin L.,
RA Felder-Schmittbuhl M.-P., Eychene A., Pouponnot C.;
RT "GSK-3-mediated phosphorylation enhances Maf-transforming activity.";
RL Mol. Cell 28:584-597(2007).
RN [9]
RP REVIEW, AND FUNCTION.
RX PubMed=19143053; DOI=10.1038/nrc2460;
RA Eychene A., Rocques N., Pouponnot C.;
RT "A new MAFia in cancer.";
RL Nat. Rev. Cancer 8:683-693(2008).
RN [10]
RP INVOLVEMENT IN MCTO, AND VARIANTS MCTO LEU-54; LEU-59; PRO-62; ARG-63;
RP CYS-66; LEU-69; ALA-70; LEU-70; SER-71 AND LEU-71.
RX PubMed=22387013; DOI=10.1016/j.ajhg.2012.01.003;
RA Zankl A., Duncan E.L., Leo P.J., Clark G.R., Glazov E.A., Addor M.C.,
RA Herlin T., Kim C.A., Leheup B.P., McGill J., McTaggart S., Mittas S.,
RA Mitchell A.L., Mortier G.R., Robertson S.P., Schroeder M., Terhal P.,
RA Brown M.A.;
RT "Multicentric carpotarsal osteolysis is caused by mutations clustering in
RT the amino-terminal transcriptional activation domain of MAFB.";
RL Am. J. Hum. Genet. 90:494-501(2012).
RN [11]
RP INVOLVEMENT IN DURS3, AND FUNCTION.
RX PubMed=27181683; DOI=10.1016/j.ajhg.2016.03.023;
RA Park J.G., Tischfield M.A., Nugent A.A., Cheng L., Di Gioia S.A.,
RA Chan W.M., Maconachie G., Bosley T.M., Summers C.G., Hunter D.G.,
RA Robson C.D., Gottlob I., Engle E.C.;
RT "Loss of MAFB function in humans and mice causes Duane syndrome, aberrant
RT extraocular muscle innervation, and inner-ear defects.";
RL Am. J. Hum. Genet. 98:1220-1227(2016).
CC -!- FUNCTION: Acts as a transcriptional activator or repressor
CC (PubMed:27181683). Plays a pivotal role in regulating lineage-specific
CC hematopoiesis by repressing ETS1-mediated transcription of erythroid-
CC specific genes in myeloid cells. Required for monocytic, macrophage,
CC osteoclast, podocyte and islet beta cell differentiation. Involved in
CC renal tubule survival and F4/80 maturation. Activates the insulin and
CC glucagon promoters. Together with PAX6, transactivates weakly the
CC glucagon gene promoter through the G1 element. SUMO modification
CC controls its transcriptional activity and ability to specify macrophage
CC fate. Binds element G1 on the glucagon promoter (By similarity).
CC Involved either as an oncogene or as a tumor suppressor, depending on
CC the cell context. Required for the transcriptional activation of HOXB3
CC in the rhombomere r5 in the hindbrain (By similarity).
CC {ECO:0000250|UniProtKB:P54841, ECO:0000269|PubMed:19143053,
CC ECO:0000269|PubMed:27181683}.
CC -!- SUBUNIT: Homodimer or heterodimer with other bHLH-Zip transcription
CC factors. Binds DNA as a homodimer or a heterodimer. Forms homodimers
CC and heterodimers with FOS, FOSB and FOSL2, but not with JUN proteins
CC (JUN, JUNB and JUND). Interacts with PAX6; the interaction is direct.
CC Interacts with ETS1 and LRP1 (By similarity). Interacts with the
CC intracellular cytoplasmic domain of LRP1 (LRPICD); the interaction
CC results in a moderate reduction of MAFB transcriptional potential.
CC {ECO:0000250, ECO:0000269|PubMed:15135046}.
CC -!- INTERACTION:
CC Q9Y5Q3; O14867: BACH1; NbExp=3; IntAct=EBI-3649340, EBI-1263541;
CC Q9Y5Q3; P01100: FOS; NbExp=2; IntAct=EBI-3649340, EBI-852851;
CC Q9Y5Q3; Q14653: IRF3; NbExp=4; IntAct=EBI-3649340, EBI-2650369;
CC Q9Y5Q3; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-3649340, EBI-10172511;
CC Q9Y5Q3; O75444: MAF; NbExp=4; IntAct=EBI-3649340, EBI-2805091;
CC Q9Y5Q3; Q9Y5Q3: MAFB; NbExp=3; IntAct=EBI-3649340, EBI-3649340;
CC Q9Y5Q3; P0C746: HBZ; Xeno; NbExp=3; IntAct=EBI-3649340, EBI-10890294;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10444328}.
CC -!- DOMAIN: The leucine-zipper domain is involved in the interaction with
CC LRPICD.
CC -!- PTM: Phosphorylated by GSK3 and MAPK13 on serine and threonine
CC residues. {ECO:0000305|PubMed:15963504, ECO:0000305|PubMed:18042454}.
CC -!- PTM: Sumoylated. Sumoylation on Lys-32 and Lys-297 stimulates its
CC transcriptional repression activity and promotes macrophage
CC differentiation from myeloid progenitors (By similarity).
CC {ECO:0000250}.
CC -!- DISEASE: Multicentric carpotarsal osteolysis syndrome (MCTO)
CC [MIM:166300]: A rare skeletal disorder, usually presenting in early
CC childhood with a clinical picture mimicking juvenile rheumatoid
CC arthritis. Progressive destruction of the carpal and tarsal bone
CC usually occurs and other bones may also be involved. Chronic renal
CC failure is a frequent component of the syndrome. Intellectual
CC disability and minor facial anomalies have been noted in some patients.
CC {ECO:0000269|PubMed:22387013}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Duane retraction syndrome 3 with or without deafness (DURS3)
CC [MIM:617041]: A form of Duane retraction syndrome, a congenital eye
CC movement disorder characterized by a failure of cranial nerve VI (the
CC abducens nerve) to develop normally, resulting in restriction or
CC absence of abduction, adduction or both, narrowing of the palpebral
CC fissure, and retraction of the globe on attempted adduction.
CC Undiagnosed in children, it can lead to amblyopia, a permanent
CC uncorrectable loss of vision. Some DURS3 patients manifest
CC sensorineural hearing loss. {ECO:0000269|PubMed:27181683}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the bZIP family. Maf subfamily. {ECO:0000305}.
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DR EMBL; AF134157; AAD30106.1; -; mRNA.
DR EMBL; AK027324; BAG51303.1; -; mRNA.
DR EMBL; AL035665; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW76000.1; -; Genomic_DNA.
DR EMBL; BC028098; AAH28098.1; -; mRNA.
DR EMBL; BC036689; AAH36689.1; -; mRNA.
DR CCDS; CCDS13311.1; -.
DR RefSeq; NP_005452.2; NM_005461.4.
DR AlphaFoldDB; Q9Y5Q3; -.
DR SMR; Q9Y5Q3; -.
DR BioGRID; 115261; 271.
DR ComplexPortal; CPX-2479; bZIP transcription factor complex, BACH2-MAFB.
DR ComplexPortal; CPX-2497; bZIP transcription factor complex, BACH1-MAFB.
DR ComplexPortal; CPX-6567; bZIP transcription factor complex, ATF4-MAFB.
DR ELM; Q9Y5Q3; -.
DR IntAct; Q9Y5Q3; 19.
DR MINT; Q9Y5Q3; -.
DR STRING; 9606.ENSP00000362410; -.
DR iPTMnet; Q9Y5Q3; -.
DR PhosphoSitePlus; Q9Y5Q3; -.
DR BioMuta; MAFB; -.
DR DMDM; 21759268; -.
DR EPD; Q9Y5Q3; -.
DR MassIVE; Q9Y5Q3; -.
DR PaxDb; Q9Y5Q3; -.
DR PeptideAtlas; Q9Y5Q3; -.
DR PRIDE; Q9Y5Q3; -.
DR ProteomicsDB; 86471; -.
DR Antibodypedia; 956; 311 antibodies from 33 providers.
DR DNASU; 9935; -.
DR Ensembl; ENST00000373313.3; ENSP00000362410.2; ENSG00000204103.4.
DR GeneID; 9935; -.
DR KEGG; hsa:9935; -.
DR MANE-Select; ENST00000373313.3; ENSP00000362410.2; NM_005461.5; NP_005452.2.
DR UCSC; uc002xji.4; human.
DR CTD; 9935; -.
DR DisGeNET; 9935; -.
DR GeneCards; MAFB; -.
DR GeneReviews; MAFB; -.
DR HGNC; HGNC:6408; MAFB.
DR HPA; ENSG00000204103; Tissue enhanced (parathyroid).
DR MalaCards; MAFB; -.
DR MIM; 166300; phenotype.
DR MIM; 608968; gene.
DR MIM; 617041; phenotype.
DR neXtProt; NX_Q9Y5Q3; -.
DR OpenTargets; ENSG00000204103; -.
DR Orphanet; 233; Duane retraction syndrome.
DR Orphanet; 529574; Duane retraction syndrome with congenital deafness.
DR Orphanet; 2774; Multicentric carpo-tarsal osteolysis with or without nephropathy.
DR PharmGKB; PA30535; -.
DR VEuPathDB; HostDB:ENSG00000204103; -.
DR eggNOG; KOG4196; Eukaryota.
DR GeneTree; ENSGT00940000160486; -.
DR HOGENOM; CLU_063062_0_0_1; -.
DR InParanoid; Q9Y5Q3; -.
DR OMA; ESHQPLH; -.
DR OrthoDB; 1395389at2759; -.
DR PhylomeDB; Q9Y5Q3; -.
DR TreeFam; TF325689; -.
DR PathwayCommons; Q9Y5Q3; -.
DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
DR SignaLink; Q9Y5Q3; -.
DR SIGNOR; Q9Y5Q3; -.
DR BioGRID-ORCS; 9935; 17 hits in 1098 CRISPR screens.
DR ChiTaRS; MAFB; human.
DR GeneWiki; MAFB_(gene); -.
DR GenomeRNAi; 9935; -.
DR Pharos; Q9Y5Q3; Tbio.
DR PRO; PR:Q9Y5Q3; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9Y5Q3; protein.
DR Bgee; ENSG00000204103; Expressed in renal glomerulus and 197 other tissues.
DR Genevisible; Q9Y5Q3; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
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; ISS:UniProtKB.
DR GO; GO:0021599; P:abducens nerve formation; ISS:UniProtKB.
DR GO; GO:0035284; P:brain segmentation; IEA:Ensembl.
DR GO; GO:1903575; P:cornified envelope assembly; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
DR GO; GO:0140467; P:integrated stress response signaling; IC:ComplexPortal.
DR GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl.
DR GO; GO:0045647; P:negative regulation of erythrocyte differentiation; IDA:UniProtKB.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0016485; P:protein processing; IEA:Ensembl.
DR GO; GO:0045637; P:regulation of myeloid cell differentiation; IBA:GO_Central.
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; IMP:UniProtKB.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IEA:Ensembl.
DR GO; GO:0021571; P:rhombomere 5 development; IEA:Ensembl.
DR GO; GO:0021572; P:rhombomere 6 development; IEA:Ensembl.
DR GO; GO:0007379; P:segment specification; IEA:Ensembl.
DR GO; GO:0007423; P:sensory organ development; TAS:ProtInc.
DR GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
DR GO; GO:0048538; P:thymus development; IEA:Ensembl.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR004826; bZIP_Maf.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR013592; Maf_TF_N.
DR InterPro; IPR028571; MafB.
DR InterPro; IPR008917; TF_DNA-bd_sf.
DR InterPro; IPR024874; Transcription_factor_Maf_fam.
DR PANTHER; PTHR10129; PTHR10129; 1.
DR PANTHER; PTHR10129:SF10; PTHR10129:SF10; 1.
DR Pfam; PF03131; bZIP_Maf; 1.
DR Pfam; PF08383; Maf_N; 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 Activator; Disease variant; DNA-binding; Isopeptide bond; Nucleus;
KW Proto-oncogene; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Tumor suppressor; Ubl conjugation.
FT CHAIN 1..323
FT /note="Transcription factor MafB"
FT /id="PRO_0000076494"
FT DOMAIN 238..301
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 34..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..263
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 266..287
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 50..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..143
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 32
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT VARIANT 54
FT /note="S -> L (in MCTO; dbSNP:rs730880014)"
FT /evidence="ECO:0000269|PubMed:22387013"
FT /id="VAR_067979"
FT VARIANT 59
FT /note="P -> L (in MCTO)"
FT /evidence="ECO:0000269|PubMed:22387013"
FT /id="VAR_067980"
FT VARIANT 62
FT /note="T -> P (in MCTO; dbSNP:rs387907004)"
FT /evidence="ECO:0000269|PubMed:22387013"
FT /id="VAR_067981"
FT VARIANT 63
FT /note="P -> R (in MCTO)"
FT /evidence="ECO:0000269|PubMed:22387013"
FT /id="VAR_067982"
FT VARIANT 66
FT /note="S -> C (in MCTO)"
FT /evidence="ECO:0000269|PubMed:22387013"
FT /id="VAR_067983"
FT VARIANT 69
FT /note="S -> L (in MCTO; dbSNP:rs1555826433)"
FT /evidence="ECO:0000269|PubMed:22387013"
FT /id="VAR_067984"
FT VARIANT 70
FT /note="S -> A (in MCTO; dbSNP:rs387907005)"
FT /evidence="ECO:0000269|PubMed:22387013"
FT /id="VAR_067985"
FT VARIANT 70
FT /note="S -> L (in MCTO; dbSNP:rs387907006)"
FT /evidence="ECO:0000269|PubMed:22387013"
FT /id="VAR_067986"
FT VARIANT 71
FT /note="P -> L (in MCTO; dbSNP:rs387907008)"
FT /evidence="ECO:0000269|PubMed:22387013"
FT /id="VAR_067987"
FT VARIANT 71
FT /note="P -> S (in MCTO; dbSNP:rs387907007)"
FT /evidence="ECO:0000269|PubMed:22387013"
FT /id="VAR_067988"
FT CONFLICT 52
FT /note="A -> V (in Ref. 1; AAD30106)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="Q -> H (in Ref. 1; AAD30106)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 323 AA; 35792 MW; A0F3C09F8936CB16 CRC64;
MAAELSMGPE LPTSPLAMEY VNDFDLLKFD VKKEPLGRAE RPGRPCTRLQ PAGSVSSTPL
STPCSSVPSS PSFSPTEQKT HLEDLYWMAS NYQQMNPEAL NLTPEDAVEA LIGSHPVPQP
LQSFDSFRGA HHHHHHHHPH PHHAYPGAGV AHDELGPHAH PHHHHHHQAS PPPSSAASPA
QQLPTSHPGP GPHATASATA AGGNGSVEDR FSDDQLVSMS VRELNRHLRG FTKDEVIRLK
QKRRTLKNRG YAQSCRYKRV QQKHHLENEK TQLIQQVEQL KQEVSRLARE RDAYKVKCEK
LANSGFREAG STSDSPSSPE FFL
