MAF_HUMAN
ID MAF_HUMAN Reviewed; 373 AA.
AC O75444; Q66I47; Q9UP93;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Transcription factor Maf;
DE AltName: Full=Proto-oncogene c-Maf;
DE AltName: Full=V-maf musculoaponeurotic fibrosarcoma oncogene homolog;
GN Name=MAF;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND
RP ALTERNATIVE SPLICING.
RX PubMed=9616139;
RA Chesi M., Bergsagel P.L., Shonukan O.O., Martelli M.L., Brents L.A.,
RA Chen T., Schrock E., Ried T., Kuehl W.M.;
RT "Frequent dysregulation of the c-maf proto-oncogene at 16q23 by
RT translocation to an Ig locus in multiple myeloma.";
RL Blood 91:4457-4463(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
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, SUBUNIT, INDUCTION, AND DNA-BINDING.
RX PubMed=12149651; DOI=10.1038/sj.onc.1205642;
RA Dhakshinamoorthy S., Jaiswal A.K.;
RT "c-Maf negatively regulates ARE-mediated detoxifying enzyme genes
RT expression and anti-oxidant induction.";
RL Oncogene 21:5301-5312(2002).
RN [5]
RP FUNCTION.
RX PubMed=14998494; DOI=10.1016/s1535-6108(04)00019-4;
RA Hurt E.M., Wiestner A., Rosenwald A., Shaffer A.L., Campo E., Grogan T.,
RA Bergsagel P.L., Kuehl W.M., Staudt L.M.;
RT "Overexpression of c-maf is a frequent oncogenic event in multiple myeloma
RT that promotes proliferation and pathological interactions with bone marrow
RT stroma.";
RL Cancer Cell 5:191-199(2004).
RN [6]
RP FUNCTION.
RX PubMed=15007382; DOI=10.1038/sj.onc.1207474;
RA Watson J.E., Doggett N.A., Albertson D.G., Andaya A., Chinnaiyan A.,
RA van Dekken H., Ginzinger D., Haqq C., James K., Kamkar S., Kowbel D.,
RA Pinkel D., Schmitt L., Simko J.P., Volik S., Weinberg V.K., Paris P.L.,
RA Collins C.;
RT "Integration of high-resolution array comparative genomic hybridization
RT analysis of chromosome 16q with expression array data refines common
RT regions of loss at 16q23-qter and identifies underlying candidate tumor
RT suppressor genes in prostate cancer.";
RL Oncogene 23:3487-3494(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 UBIQUITINATION.
RX PubMed=17875808; DOI=10.1182/blood-2007-05-088666;
RA Mao X., Stewart A.K., Hurren R., Datti A., Zhu X., Zhu Y., Shi C., Lee K.,
RA Tiedemann R., Eberhard Y., Trudel S., Liang S., Corey S.J., Gillis L.C.,
RA Barber D.L., Wrana J.L., Ezzat S., Schimmer A.D.;
RT "A chemical biology screen identifies glucocorticoids that regulate c-maf
RT expression by increasing its proteasomal degradation through up-regulation
RT of ubiquitin.";
RL Blood 110:4047-4054(2007).
RN [9]
RP FUNCTION.
RX PubMed=16247450; DOI=10.1038/sj.onc.1209171;
RA Pouponnot C., Sii-Felice K., Hmitou I., Rocques N., Lecoin L.,
RA Druillennec S., Felder-Schmittbuhl M.-P., Eychene A.;
RT "Cell context reveals a dual role for Maf in oncogenesis.";
RL Oncogene 25:1299-1310(2006).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=17897790; DOI=10.1016/j.gene.2007.08.010;
RA Mahoney K.M., Petrovic N., Schacke W., Shapiro L.H.;
RT "CD13/APN transcription is regulated by the proto-oncogene c-Maf via an
RT atypical response element.";
RL Gene 403:178-187(2007).
RN [11]
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 [12]
RP INVOLVEMENT IN CTRCT21, AND VARIANT CTRCT21 LEU-303.
RX PubMed=24664492; DOI=10.1002/ajmg.a.36433;
RA Narumi Y., Nishina S., Tokimitsu M., Aoki Y., Kosaki R., Wakui K.,
RA Azuma N., Murata T., Takada F., Fukushima Y., Kosho T.;
RT "Identification of a novel missense mutation of MAF in a Japanese family
RT with congenital cataract by whole exome sequencing: a clinical report and
RT review of literature.";
RL Am. J. Med. Genet. A 164A:1272-1276(2014).
RN [13]
RP INVOLVEMENT IN AYGRP, AND VARIANTS AYGRP LEU-54; ALA-58; ILE-58; HIS-59;
RP LEU-59; ARG-62 AND ARG-69.
RX PubMed=25865493; DOI=10.1016/j.ajhg.2015.03.001;
RA Niceta M., Stellacci E., Gripp K.W., Zampino G., Kousi M., Anselmi M.,
RA Traversa A., Ciolfi A., Stabley D., Bruselles A., Caputo V., Cecchetti S.,
RA Prudente S., Fiorenza M.T., Boitani C., Philip N., Niyazov D., Leoni C.,
RA Nakane T., Keppler-Noreuil K., Braddock S.R., Gillessen-Kaesbach G.,
RA Palleschi A., Campeau P.M., Lee B.H., Pouponnot C., Stella L.,
RA Bocchinfuso G., Katsanis N., Sol-Church K., Tartaglia M.;
RT "Mutations impairing GSK3-mediated MAF phosphorylation cause cataract,
RT deafness, intellectual disability, seizures, and a Down syndrome-like
RT facies.";
RL Am. J. Hum. Genet. 96:816-825(2015).
RN [14]
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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-33, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-29; LYS-33 AND LYS-331,
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-379 (ISOFORM 1), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [17]
RP VARIANT CTRCT21 PRO-288.
RX PubMed=11772997; DOI=10.1093/hmg/11.1.33;
RA Jamieson R.V., Perveen R., Kerr B., Carette M., Yardley J., Heon E.,
RA Wirth M.G., van Heyningen V., Donnai D., Munier F., Black G.C.;
RT "Domain disruption and mutation of the bZIP transcription factor, MAF,
RT associated with cataract, ocular anterior segment dysgenesis and
RT coloboma.";
RL Hum. Mol. Genet. 11:33-42(2002).
RN [18]
RP VARIANT CTRCT21 ARG-297.
RX PubMed=16470690; DOI=10.1002/ajmg.a.31126;
RA Vanita V., Singh D., Robinson P.N., Sperling K., Singh J.R.;
RT "A novel mutation in the DNA-binding domain of MAF at 16q23.1 associated
RT with autosomal dominant 'cerulean cataract' in an Indian family.";
RL Am. J. Med. Genet. A 140:558-566(2006).
RN [19]
RP VARIANT CTRCT21 GLU-320.
RX PubMed=19182255; DOI=10.1167/iovs.08-3149;
RA Hansen L., Mikkelsen A., Nuernberg P., Nuernberg G., Anjum I., Eiberg H.,
RA Rosenberg T.;
RT "Comprehensive mutational screening in a cohort of Danish families with
RT hereditary congenital cataract.";
RL Invest. Ophthalmol. Vis. Sci. 50:3291-3303(2009).
RN [20]
RP VARIANT CTRCT21 GLY-317.
RX PubMed=29914532; DOI=10.1186/s13023-018-0828-0;
RA Li J., Leng Y., Han S., Yan L., Lu C., Luo Y., Zhang X., Cao L.;
RT "Clinical and genetic characteristics of Chinese patients with familial or
RT sporadic pediatric cataract.";
RL Orphanet J. Rare Dis. 13:94-94(2018).
CC -!- FUNCTION: Acts as a transcriptional activator or repressor. Involved in
CC embryonic lens fiber cell development. Recruits the transcriptional
CC coactivators CREBBP and/or EP300 to crystallin promoters leading to up-
CC regulation of crystallin gene during lens fiber cell differentiation.
CC Activates the expression of IL4 in T helper 2 (Th2) cells. Increases T-
CC cell susceptibility to apoptosis by interacting with MYB and decreasing
CC BCL2 expression. Together with PAX6, transactivates strongly the
CC glucagon gene promoter through the G1 element. Activates transcription
CC of the CD13 proximal promoter in endothelial cells. Represses
CC transcription of the CD13 promoter in early stages of myelopoiesis by
CC affecting the ETS1 and MYB cooperative interaction. Involved in the
CC initial chondrocyte terminal differentiation and the disappearance of
CC hypertrophic chondrocytes during endochondral bone development. Binds
CC to the sequence 5'-[GT]G[GC]N[GT]NCTCAGNN-3' in the L7 promoter. Binds
CC to the T-MARE (Maf response element) sites of lens-specific alpha- and
CC beta-crystallin gene promoters. Binds element G1 on the glucagon
CC promoter. Binds an AT-rich region adjacent to the TGC motif (atypical
CC Maf response element) in the CD13 proximal promoter in endothelial
CC cells (By similarity). When overexpressed, represses anti-oxidant
CC response element (ARE)-mediated transcription. Involved either as an
CC oncogene or as a tumor suppressor, depending on the cell context. Binds
CC to the ARE sites of detoxifying enzyme gene promoters. {ECO:0000250,
CC ECO:0000269|PubMed:12149651, ECO:0000269|PubMed:14998494,
CC ECO:0000269|PubMed:15007382, ECO:0000269|PubMed:16247450,
CC ECO:0000269|PubMed:19143053}.
CC -!- SUBUNIT: Homodimer or heterodimer with other bHLH-Zip transcription
CC factors. Binds DNA as a homodimer or as a heterodimer. Heterotetramer
CC of two MAF and two USF2. Interacts with PAX6; the interaction is
CC direct. Interacts with MYB; interaction takes place weakly in normal T-
CC cells and increases in T-cells following stimulation through the TCR
CC engagement. Interacts with MYB; the ternary complex formed with MYB and
CC the CD13 promoter is regulated in response to differentiating signals.
CC Interacts with USF2; the interaction inhibits its DNA-binding activity
CC on the L7 promoter. Interacts with CREBBP, EP300 and ETS1 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC O75444; P18848: ATF4; NbExp=3; IntAct=EBI-2805091, EBI-492498;
CC O75444; O14867: BACH1; NbExp=2; IntAct=EBI-2805091, EBI-1263541;
CC O75444; O75444: MAF; NbExp=2; IntAct=EBI-2805091, EBI-2805091;
CC O75444; Q9Y5Q3: MAFB; NbExp=4; IntAct=EBI-2805091, EBI-3649340;
CC O75444; P0C746: HBZ; Xeno; NbExp=2; IntAct=EBI-2805091, EBI-10890294;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2; Synonyms=Short;
CC IsoId=O75444-2; Sequence=Displayed;
CC Name=1; Synonyms=Long;
CC IsoId=O75444-1; Sequence=VSP_000583;
CC -!- TISSUE SPECIFICITY: Expressed in endothelial cells.
CC {ECO:0000269|PubMed:17897790}.
CC -!- INDUCTION: Up-regulated with tert-butyl hydroquinone (t-BHQ).
CC {ECO:0000269|PubMed:12149651}.
CC -!- PTM: Ubiquitinated, leading to its degradation by the proteasome.
CC Ubiquitination is triggered by glucocorticoids.
CC {ECO:0000269|PubMed:17875808}.
CC -!- PTM: Phosphorylated by GSK3 and MAPK13 on serine and threonine residues
CC (Probable). The phosphorylation status can serve to either stimulate or
CC inhibit transcription. {ECO:0000269|PubMed:15963504,
CC ECO:0000269|PubMed:18042454, ECO:0000305}.
CC -!- DISEASE: Note=A chromosomal aberration involving MAF is found in some
CC forms of multiple myeloma (MM). Translocation t(14;16)(q32.3;q23) with
CC an IgH locus.
CC -!- DISEASE: Cataract 21, multiple types (CTRCT21) [MIM:610202]: An
CC opacification of the crystalline lens of the eye that frequently
CC results in visual impairment or blindness. Opacities vary in
CC morphology, are often confined to a portion of the lens, and may be
CC static or progressive. In general, the more posteriorly located and
CC dense an opacity, the greater the impact on visual function. CTRCT21
CC includes cerulean and pulverulent cataracts. Cerulean cataracts are
CC characterized by peripheral bluish and white opacifications organized
CC in concentric layers with occasional central lesions arranged radially.
CC The opacities are observed in the superficial layers of the fetal
CC nucleus as well as the adult nucleus of the lens. Involvement is
CC usually bilateral. Visual acuity is only mildly reduced in childhood.
CC In adulthood, the opacifications may progress, making lens extraction
CC necessary. Histologically the lesions are described as fusiform
CC cavities between lens fibers which contain a deeply staining granular
CC material. Although the lesions may take on various colors, a dull blue
CC is the most common appearance and is responsible for the designation
CC cerulean cataract. Pulverulent cataracts are characterized by a dust-
CC like, 'pulverised' appearance of the opacities which can be found in
CC any part of the lens. In some cases cataract is associated with
CC microcornea without any other systemic anomaly or dysmorphism.
CC Microcornea is defined by a corneal diameter inferior to 10 mm in both
CC meridians in an otherwise normal eye. {ECO:0000269|PubMed:11772997,
CC ECO:0000269|PubMed:16470690, ECO:0000269|PubMed:19182255,
CC ECO:0000269|PubMed:24664492, ECO:0000269|PubMed:29914532}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Ayme-Gripp syndrome (AYGRP) [MIM:601088]: A multisystem
CC disorder characterized by congenital cataracts, sensorineural deafness,
CC intellectual disability, seizures, brachycephaly, distinctive flat
CC facial appearance, skeletal anomalies, mammary gland hypoplasia, and
CC reduced growth. {ECO:0000269|PubMed:25865493}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the bZIP family. Maf subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="https://atlasgeneticsoncology.org/gene/41234/maf-(v-maf-musculoaponeurotic-fibrosarcoma-oncogene-homolog-(avian))";
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; AF055376; AAC27037.1; -; mRNA.
DR EMBL; AF055377; AAC27038.1; -; mRNA.
DR EMBL; AF055378; AAC27039.1; -; Genomic_DNA.
DR EMBL; AC009159; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC081542; AAH81542.1; -; mRNA.
DR CCDS; CCDS10928.1; -. [O75444-1]
DR CCDS; CCDS42198.1; -. [O75444-2]
DR RefSeq; NP_001026974.1; NM_001031804.2. [O75444-2]
DR RefSeq; NP_005351.2; NM_005360.4. [O75444-1]
DR AlphaFoldDB; O75444; -.
DR SMR; O75444; -.
DR BioGRID; 110269; 57.
DR ComplexPortal; CPX-2483; bZIP transcription factor complex, BACH2-MAF.
DR ComplexPortal; CPX-2500; bZIP transcription factor complex, BACH1-MAF.
DR ComplexPortal; CPX-6566; bZIP transcription factor complex, ATF4-MAF.
DR ELM; O75444; -.
DR IntAct; O75444; 8.
DR STRING; 9606.ENSP00000327048; -.
DR iPTMnet; O75444; -.
DR PhosphoSitePlus; O75444; -.
DR BioMuta; MAF; -.
DR MassIVE; O75444; -.
DR PaxDb; O75444; -.
DR PeptideAtlas; O75444; -.
DR PRIDE; O75444; -.
DR Antibodypedia; 4143; 502 antibodies from 39 providers.
DR DNASU; 4094; -.
DR Ensembl; ENST00000326043.5; ENSP00000327048.4; ENSG00000178573.7. [O75444-1]
DR Ensembl; ENST00000393350.1; ENSP00000377019.1; ENSG00000178573.7. [O75444-2]
DR GeneID; 4094; -.
DR KEGG; hsa:4094; -.
DR MANE-Select; ENST00000326043.5; ENSP00000327048.4; NM_005360.5; NP_005351.2. [O75444-1]
DR UCSC; uc002ffm.4; human. [O75444-2]
DR CTD; 4094; -.
DR DisGeNET; 4094; -.
DR GeneCards; MAF; -.
DR GeneReviews; MAF; -.
DR HGNC; HGNC:6776; MAF.
DR HPA; ENSG00000178573; Low tissue specificity.
DR MalaCards; MAF; -.
DR MIM; 177075; gene.
DR MIM; 601088; phenotype.
DR MIM; 610202; phenotype.
DR neXtProt; NX_O75444; -.
DR NIAGADS; ENSG00000178573; -.
DR OpenTargets; ENSG00000178573; -.
DR Orphanet; 1272; Ayme-Gripp syndrome.
DR Orphanet; 1377; Cataract-microcornea syndrome.
DR Orphanet; 98989; Cerulean cataract.
DR Orphanet; 98984; Pulverulent cataract.
DR PharmGKB; PA30534; -.
DR VEuPathDB; HostDB:ENSG00000178573; -.
DR eggNOG; KOG4196; Eukaryota.
DR GeneTree; ENSGT00940000161531; -.
DR HOGENOM; CLU_063062_0_0_1; -.
DR InParanoid; O75444; -.
DR OMA; SMPGEEM; -.
DR OrthoDB; 1395389at2759; -.
DR PhylomeDB; O75444; -.
DR TreeFam; TF325689; -.
DR PathwayCommons; O75444; -.
DR Reactome; R-HSA-8940973; RUNX2 regulates osteoblast differentiation.
DR SignaLink; O75444; -.
DR SIGNOR; O75444; -.
DR BioGRID-ORCS; 4094; 21 hits in 1093 CRISPR screens.
DR ChiTaRS; MAF; human.
DR GeneWiki; MAF_(gene); -.
DR GenomeRNAi; 4094; -.
DR Pharos; O75444; Tbio.
DR PRO; PR:O75444; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; O75444; protein.
DR Bgee; ENSG00000178573; Expressed in jejunal mucosa and 205 other tissues.
DR ExpressionAtlas; O75444; baseline and differential.
DR Genevisible; O75444; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0048468; P:cell development; IEA:Ensembl.
DR GO; GO:0048839; P:inner ear development; IEA:Ensembl.
DR GO; GO:0140467; P:integrated stress response signaling; IC:ComplexPortal.
DR GO; GO:0070306; P:lens fiber cell differentiation; IBA:GO_Central.
DR GO; GO:0030219; P:megakaryocyte differentiation; IMP:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0032330; P:regulation of chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR004826; bZIP_Maf.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR028573; Maf/V-MAF.
DR InterPro; IPR013592; Maf_TF_N.
DR InterPro; IPR008917; TF_DNA-bd_sf.
DR InterPro; IPR024874; Transcription_factor_Maf_fam.
DR PANTHER; PTHR10129; PTHR10129; 1.
DR PANTHER; PTHR10129:SF9; PTHR10129:SF9; 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; Alternative splicing; Cataract; Chromosomal rearrangement;
KW Deafness; Disease variant; DNA-binding; Dwarfism; Intellectual disability;
KW Isopeptide bond; Nucleus; Proto-oncogene; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Tumor suppressor; Ubl conjugation.
FT CHAIN 1..373
FT /note="Transcription factor Maf"
FT /id="PRO_0000076491"
FT DOMAIN 288..351
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 57..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..373
FT /note="Represses ARE-mediated transcription"
FT REGION 175..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..313
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 316..337
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 354..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..193
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 29
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 33
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 331
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 373
FT /note="M -> ITEPTRKLEPSVGYATFWKPQHRVLTSVFTK (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:9616139"
FT /id="VSP_000583"
FT VARIANT 54
FT /note="S -> L (in AYGRP; dbSNP:rs727502766)"
FT /evidence="ECO:0000269|PubMed:25865493"
FT /id="VAR_073891"
FT VARIANT 58
FT /note="T -> A (in AYGRP; dbSNP:rs727502767)"
FT /evidence="ECO:0000269|PubMed:25865493"
FT /id="VAR_073892"
FT VARIANT 58
FT /note="T -> I (in AYGRP; dbSNP:rs727502769)"
FT /evidence="ECO:0000269|PubMed:25865493"
FT /id="VAR_073893"
FT VARIANT 59
FT /note="P -> H (in AYGRP; dbSNP:rs727502770)"
FT /evidence="ECO:0000269|PubMed:25865493"
FT /id="VAR_073894"
FT VARIANT 59
FT /note="P -> L (in AYGRP; dbSNP:rs727502770)"
FT /evidence="ECO:0000269|PubMed:25865493"
FT /id="VAR_073895"
FT VARIANT 62
FT /note="T -> R (in AYGRP; dbSNP:rs727502771)"
FT /evidence="ECO:0000269|PubMed:25865493"
FT /id="VAR_073896"
FT VARIANT 69
FT /note="P -> R (in AYGRP; dbSNP:rs727502768)"
FT /evidence="ECO:0000269|PubMed:25865493"
FT /id="VAR_073897"
FT VARIANT 288
FT /note="R -> P (in CTRCT21; dbSNP:rs121917735)"
FT /evidence="ECO:0000269|PubMed:11772997"
FT /id="VAR_029369"
FT VARIANT 297
FT /note="K -> R (in CTRCT21; dbSNP:rs121917736)"
FT /evidence="ECO:0000269|PubMed:16470690"
FT /id="VAR_029370"
FT VARIANT 303
FT /note="Q -> L (in CTRCT21)"
FT /evidence="ECO:0000269|PubMed:24664492"
FT /id="VAR_073898"
FT VARIANT 317
FT /note="E -> G (in CTRCT21; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:29914532"
FT /id="VAR_084822"
FT VARIANT 320
FT /note="K -> E (in CTRCT21; dbSNP:rs1435247084)"
FT /evidence="ECO:0000269|PubMed:19182255"
FT /id="VAR_084823"
FT CROSSLNK O75444-1:379
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ SEQUENCE 373 AA; 38492 MW; 566C2BC3E4A62762 CRC64;
MASELAMSNS DLPTSPLAME YVNDFDLMKF EVKKEPVETD RIISQCGRLI AGGSLSSTPM
STPCSSVPPS PSFSAPSPGS GSEQKAHLED YYWMTGYPQQ LNPEALGFSP EDAVEALISN
SHQLQGGFDG YARGAQQLAA AAGAGAGASL GGSGEEMGPA AAVVSAVIAA AAAQSGAGPH
YHHHHHHAAG HHHHPTAGAP GAAGSAAASA GGAGGAGGGG PASAGGGGGG GGGGGGGGAA
GAGGALHPHH AAGGLHFDDR FSDEQLVTMS VRELNRQLRG VSKEEVIRLK QKRRTLKNRG
YAQSCRFKRV QQRHVLESEK NQLLQQVDHL KQEISRLVRE RDAYKEKYEK LVSSGFRENG
SSSDNPSSPE FFM
