MAFF_HUMAN
ID MAFF_HUMAN Reviewed; 164 AA.
AC Q9ULX9; B4DV49; Q9Y525;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Transcription factor MafF;
DE AltName: Full=U-Maf;
DE AltName: Full=V-maf musculoaponeurotic fibrosarcoma oncogene homolog F;
GN Name=MAFF;
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] (ISOFORM 1), AND FUNCTION.
RC TISSUE=Term myometrium;
RX PubMed=10527846; DOI=10.1006/bbrc.1999.1487;
RA Kimura T., Ivell R., Rust W., Mizumoto Y., Ogita K., Kusui C.,
RA Matsumura Y., Azuma C., Murata Y.;
RT "Molecular cloning of a human MafF homologue, which specifically binds to
RT the oxytocin receptor gene in term myometrium.";
RL Biochem. Biophys. Res. Commun. 264:86-92(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta, and Small intestine;
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=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta, and Skin;
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 [5]
RP FUNCTION, DNA-BINDING, AND INTERACTION WITH NFE2L1.
RX PubMed=8932385; DOI=10.1093/nar/24.21.4289;
RA Johnsen O., Skammelsrud N., Luna L., Nishizawa M., Prydz H., Kolstoe A.B.;
RT "Small Maf proteins interact with the human transcription factor
RT TCF11/Nrf1/LCR-F1.";
RL Nucleic Acids Res. 24:4289-4297(1996).
RN [6]
RP INDUCTION.
RX PubMed=11772409; DOI=10.1042/0264-6021:3610371;
RA Moran J.A., Dahl E.L., Mulcahy R.T.;
RT "Differential induction of mafF, mafG and mafK expression by electrophile-
RT response-element activators.";
RL Biochem. J. 361:371-377(2002).
RN [7]
RP FUNCTION, AND INTERACTION WITH MIP.
RX PubMed=16549056; DOI=10.1016/j.abb.2006.02.011;
RA Ye X., Li Y., Huang Q., Yu Y., Yuan H., Wang P., Wan D., Gu J., Huo K.,
RA Li Y.-Y., Lu H.;
RT "The novel human gene MIP functions as a co-activator of hMafF.";
RL Arch. Biochem. Biophys. 449:87-93(2006).
CC -!- FUNCTION: Since they lack a putative transactivation domain, the small
CC Mafs behave as transcriptional repressors when they dimerize among
CC themselves (PubMed:8932385). However, they seem to serve as
CC transcriptional activators by dimerizing with other (usually larger)
CC basic-zipper proteins, such as NFE2L1/NRF1, and recruiting them to
CC specific DNA-binding sites. Interacts with the upstream promoter region
CC of the oxytocin receptor gene (PubMed:8932385, PubMed:16549056). May be
CC a transcriptional enhancer in the up-regulation of the oxytocin
CC receptor gene at parturition (PubMed:10527846).
CC {ECO:0000269|PubMed:10527846, ECO:0000269|PubMed:16549056,
CC ECO:0000269|PubMed:8932385}.
CC -!- SUBUNIT: Monomer and homo- or heterodimer. Interacts with MIP
CC (PubMed:16549056). Forms high affinity heterodimers with members of the
CC CNC-bZIP family such as NFE2L1/NRF1 (PubMed:8932385).
CC {ECO:0000269|PubMed:16549056, ECO:0000269|PubMed:8932385}.
CC -!- INTERACTION:
CC Q9ULX9; P18847: ATF3; NbExp=2; IntAct=EBI-721128, EBI-712767;
CC Q9ULX9; O14867: BACH1; NbExp=4; IntAct=EBI-721128, EBI-1263541;
CC Q9ULX9; Q9BYV9: BACH2; NbExp=3; IntAct=EBI-721128, EBI-1642333;
CC Q9ULX9; Q8N1L9: BATF2; NbExp=2; IntAct=EBI-721128, EBI-742695;
CC Q9ULX9; Q9NR55: BATF3; NbExp=2; IntAct=EBI-721128, EBI-10312707;
CC Q9ULX9; O15525: MAFG; NbExp=2; IntAct=EBI-721128, EBI-713514;
CC Q9ULX9; Q14494: NFE2L1; NbExp=2; IntAct=EBI-721128, EBI-2804436;
CC Q9ULX9; Q16236: NFE2L2; NbExp=3; IntAct=EBI-721128, EBI-2007911;
CC Q9ULX9; Q9Y4A8: NFE2L3; NbExp=3; IntAct=EBI-721128, EBI-10890629;
CC Q9ULX9; Q16649: NFIL3; NbExp=2; IntAct=EBI-721128, EBI-3951858;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ULX9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ULX9-2; Sequence=VSP_043029;
CC -!- TISSUE SPECIFICITY: Expressed in the term myometrium and kidney.
CC -!- INDUCTION: By oxidative stress. {ECO:0000269|PubMed:11772409}.
CC -!- SIMILARITY: Belongs to the bZIP family. Maf subfamily. {ECO:0000305}.
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DR EMBL; AB025247; BAA86871.1; -; mRNA.
DR EMBL; AJ010857; CAB52435.1; -; mRNA.
DR EMBL; AK002001; BAA92029.1; -; mRNA.
DR EMBL; AK300932; BAG62561.1; -; mRNA.
DR EMBL; AL021977; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015037; AAH15037.1; -; mRNA.
DR EMBL; BC067751; AAH67751.1; -; mRNA.
DR CCDS; CCDS13968.1; -. [Q9ULX9-1]
DR CCDS; CCDS54528.1; -. [Q9ULX9-2]
DR PIR; JC7112; JC7112.
DR RefSeq; NP_001155044.1; NM_001161572.1. [Q9ULX9-1]
DR RefSeq; NP_001155045.1; NM_001161573.1. [Q9ULX9-1]
DR RefSeq; NP_001155046.1; NM_001161574.1. [Q9ULX9-2]
DR RefSeq; NP_036455.1; NM_012323.3. [Q9ULX9-1]
DR AlphaFoldDB; Q9ULX9; -.
DR SMR; Q9ULX9; -.
DR BioGRID; 117264; 43.
DR ComplexPortal; CPX-2484; bZIP transcription factor complex, BACH2-MAFF.
DR ComplexPortal; CPX-6480; bZIP transcription factor complex, ATF3-MAFF.
DR ComplexPortal; CPX-7085; bZIP transcription factor complex, BATF2-MAFF.
DR ComplexPortal; CPX-7103; bZIP transcription factor complex, BATF3-MAFF.
DR ComplexPortal; CPX-7165; bZIP transcription factor complex, BACH1-MAFF.
DR IntAct; Q9ULX9; 30.
DR MINT; Q9ULX9; -.
DR STRING; 9606.ENSP00000345393; -.
DR iPTMnet; Q9ULX9; -.
DR PhosphoSitePlus; Q9ULX9; -.
DR BioMuta; MAFF; -.
DR DMDM; 21542145; -.
DR EPD; Q9ULX9; -.
DR jPOST; Q9ULX9; -.
DR MassIVE; Q9ULX9; -.
DR MaxQB; Q9ULX9; -.
DR PaxDb; Q9ULX9; -.
DR PeptideAtlas; Q9ULX9; -.
DR PRIDE; Q9ULX9; -.
DR ProteomicsDB; 85150; -. [Q9ULX9-1]
DR ProteomicsDB; 85151; -. [Q9ULX9-2]
DR Antibodypedia; 12337; 161 antibodies from 30 providers.
DR DNASU; 23764; -.
DR Ensembl; ENST00000338483.7; ENSP00000345393.2; ENSG00000185022.12. [Q9ULX9-1]
DR Ensembl; ENST00000407965.1; ENSP00000384094.1; ENSG00000185022.12. [Q9ULX9-1]
DR Ensembl; ENST00000426621.6; ENSP00000388882.2; ENSG00000185022.12. [Q9ULX9-1]
DR Ensembl; ENST00000538320.5; ENSP00000442060.1; ENSG00000185022.12. [Q9ULX9-1]
DR Ensembl; ENST00000538999.1; ENSP00000441482.1; ENSG00000185022.12. [Q9ULX9-2]
DR GeneID; 23764; -.
DR KEGG; hsa:23764; -.
DR MANE-Select; ENST00000338483.7; ENSP00000345393.2; NM_012323.4; NP_036455.1.
DR UCSC; uc003avc.4; human. [Q9ULX9-1]
DR CTD; 23764; -.
DR DisGeNET; 23764; -.
DR GeneCards; MAFF; -.
DR HGNC; HGNC:6780; MAFF.
DR HPA; ENSG00000185022; Low tissue specificity.
DR MIM; 604877; gene.
DR neXtProt; NX_Q9ULX9; -.
DR OpenTargets; ENSG00000185022; -.
DR PharmGKB; PA30538; -.
DR VEuPathDB; HostDB:ENSG00000185022; -.
DR eggNOG; KOG4196; Eukaryota.
DR GeneTree; ENSGT00940000161112; -.
DR HOGENOM; CLU_112948_0_1_1; -.
DR InParanoid; Q9ULX9; -.
DR OMA; MGENTPH; -.
DR OrthoDB; 1395389at2759; -.
DR PhylomeDB; Q9ULX9; -.
DR TreeFam; TF325689; -.
DR PathwayCommons; Q9ULX9; -.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; Q9ULX9; -.
DR SIGNOR; Q9ULX9; -.
DR BioGRID-ORCS; 23764; 28 hits in 1091 CRISPR screens.
DR ChiTaRS; MAFF; human.
DR GeneWiki; MAFF_(gene); -.
DR GenomeRNAi; 23764; -.
DR Pharos; Q9ULX9; Tbio.
DR PRO; PR:Q9ULX9; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9ULX9; protein.
DR Bgee; ENSG00000185022; Expressed in amniotic fluid and 201 other tissues.
DR ExpressionAtlas; Q9ULX9; baseline and differential.
DR Genevisible; Q9ULX9; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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; IDA:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
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:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0007567; P:parturition; TAS:ProtInc.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045604; P:regulation of epidermal cell differentiation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR004826; bZIP_Maf.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR033531; MafF.
DR InterPro; IPR008917; TF_DNA-bd_sf.
DR InterPro; IPR024874; Transcription_factor_Maf_fam.
DR PANTHER; PTHR10129; PTHR10129; 1.
DR PANTHER; PTHR10129:SF25; PTHR10129:SF25; 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 Alternative splicing; DNA-binding; Nucleus; Reference proteome; Repressor;
KW Stress response; Transcription; Transcription regulation.
FT CHAIN 1..164
FT /note="Transcription factor MafF"
FT /id="PRO_0000076497"
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 REGION 141..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..29
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043029"
FT CONFLICT 116
FT /note="G -> A (in Ref. 2; BAA86871)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 164 AA; 17760 MW; FC34D9FF317E5EE1 CRC64;
MSVDPLSSKA LKIKRELSEN TPHLSDEALM GLSVRELNRH LRGLSAEEVT RLKQRRRTLK
NRGYAASCRV KRVCQKEELQ KQKSELEREV DKLARENAAM RLELDALRGK CEALQGFARS
VAAARGPATL VAPASVITIV KSTPGSGSGP AHGPDPAHGP ASCS
