MAFK_HUMAN
ID MAFK_HUMAN Reviewed; 156 AA.
AC O60675; A4D214;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Transcription factor MafK;
DE AltName: Full=Erythroid transcription factor NF-E2 p18 subunit;
GN Name=MAFK;
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], FUNCTION IN TRANSCRIPTION, INTERACTION WITH
RP NFE2L1 AND NFE2L2, AND TISSUE SPECIFICITY.
RX PubMed=9150357; DOI=10.1038/sj.onc.1201024;
RA Toki T., Itoh J., Kitazawa J., Arai K., Hatakeyama K., Akasaka J.,
RA Igarashi K., Nomura N., Yokoyama M., Yamamoto M., Ito E.;
RT "Human small Maf proteins form heterodimers with CNC family transcription
RT factors and recognize the NF-E2 motif.";
RL Oncogene 14:1901-1910(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-130, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: Since they lack a putative transactivation domain, the small
CC Mafs behave as transcriptional repressors when they dimerize among
CC themselves (PubMed:9150357). 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:9150357,
CC PubMed:8932385). Small Maf proteins heterodimerize with Fos and may act
CC as competitive repressors of the NF-E2 transcription factor
CC (PubMed:9150357). {ECO:0000269|PubMed:8932385,
CC ECO:0000269|PubMed:9150357}.
CC -!- SUBUNIT: Homodimer or heterodimer. It can form high affinity
CC heterodimers with members of the CNC-bZIP family such as NFE2,
CC NFE2L1/NRF1, NFE2L2/NRF2 and NFE2L3/NRF3 (PubMed:9150357,
CC PubMed:8932385). {ECO:0000269|PubMed:8932385,
CC ECO:0000269|PubMed:9150357}.
CC -!- INTERACTION:
CC O60675; Q9BYV9: BACH2; NbExp=3; IntAct=EBI-2559512, EBI-1642333;
CC O60675; Q16236: NFE2L2; NbExp=6; IntAct=EBI-2559512, EBI-2007911;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the bZIP family. Maf subfamily. {ECO:0000305}.
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DR EMBL; AF059194; AAC14426.1; -; mRNA.
DR EMBL; AK092414; BAG52549.1; -; mRNA.
DR EMBL; AC093734; AAP21866.1; -; Genomic_DNA.
DR EMBL; CH236953; EAL23943.1; -; Genomic_DNA.
DR EMBL; CH471144; EAW87207.1; -; Genomic_DNA.
DR EMBL; BC148265; AAI48266.1; -; mRNA.
DR CCDS; CCDS5325.1; -.
DR RefSeq; NP_002351.1; NM_002360.3.
DR RefSeq; XP_005249908.2; XM_005249851.2.
DR RefSeq; XP_006715836.1; XM_006715773.2.
DR AlphaFoldDB; O60675; -.
DR SMR; O60675; -.
DR BioGRID; 113688; 30.
DR ComplexPortal; CPX-2482; bZIP transcription factor complex, BACH2-MAFK.
DR ComplexPortal; CPX-2493; bZIP transcription factor complex, BACH1-MAFK.
DR IntAct; O60675; 5.
DR STRING; 9606.ENSP00000344903; -.
DR ChEMBL; CHEMBL2346484; -.
DR GlyGen; O60675; 10 sites, 2 O-linked glycans (10 sites).
DR iPTMnet; O60675; -.
DR PhosphoSitePlus; O60675; -.
DR BioMuta; MAFK; -.
DR EPD; O60675; -.
DR jPOST; O60675; -.
DR MassIVE; O60675; -.
DR MaxQB; O60675; -.
DR PaxDb; O60675; -.
DR PeptideAtlas; O60675; -.
DR PRIDE; O60675; -.
DR ProteomicsDB; 49520; -.
DR Antibodypedia; 24241; 164 antibodies from 25 providers.
DR DNASU; 7975; -.
DR Ensembl; ENST00000343242.9; ENSP00000344903.4; ENSG00000198517.10.
DR Ensembl; ENST00000403150.5; ENSP00000386009.1; ENSG00000198517.10.
DR Ensembl; ENST00000406174.2; ENSP00000385437.2; ENSG00000198517.10.
DR GeneID; 7975; -.
DR KEGG; hsa:7975; -.
DR MANE-Select; ENST00000343242.9; ENSP00000344903.4; NM_002360.4; NP_002351.1.
DR UCSC; uc003skr.4; human.
DR CTD; 7975; -.
DR DisGeNET; 7975; -.
DR GeneCards; MAFK; -.
DR HGNC; HGNC:6782; MAFK.
DR HPA; ENSG00000198517; Low tissue specificity.
DR MIM; 600197; gene.
DR neXtProt; NX_O60675; -.
DR OpenTargets; ENSG00000198517; -.
DR PharmGKB; PA30540; -.
DR VEuPathDB; HostDB:ENSG00000198517; -.
DR eggNOG; KOG4196; Eukaryota.
DR GeneTree; ENSGT00940000160044; -.
DR HOGENOM; CLU_112948_0_0_1; -.
DR InParanoid; O60675; -.
DR OMA; LVHCCCF; -.
DR OrthoDB; 1395389at2759; -.
DR PhylomeDB; O60675; -.
DR TreeFam; TF325689; -.
DR PathwayCommons; O60675; -.
DR Reactome; R-HSA-9707587; Regulation of HMOX1 expression and activity.
DR Reactome; R-HSA-9707616; Heme signaling.
DR Reactome; R-HSA-9708530; Regulation of BACH1 activity.
DR Reactome; R-HSA-9759194; Nuclear events mediated by NFE2L2.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; O60675; -.
DR SIGNOR; O60675; -.
DR BioGRID-ORCS; 7975; 23 hits in 1099 CRISPR screens.
DR ChiTaRS; MAFK; human.
DR GeneWiki; MAFK; -.
DR GenomeRNAi; 7975; -.
DR Pharos; O60675; Tbio.
DR PRO; PR:O60675; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O60675; protein.
DR Bgee; ENSG00000198517; Expressed in apex of heart and 173 other tissues.
DR ExpressionAtlas; O60675; baseline and differential.
DR Genevisible; O60675; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA: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:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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_0000076503"
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:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT CROSSLNK 130
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ SEQUENCE 156 AA; 17523 MW; 39F98F8D550C168E CRC64;
MTTNPKPNKA LKVKKEAGEN APVLSDDELV SMSVRELNQH LRGLTKEEVT RLKQRRRTLK
NRGYAASCRI KRVTQKEELE RQRVELQQEV EKLARENSSM RLELDALRSK YEALQTFART
VARGPVAPSK VATTSVITIV KSTELSSTSV PFSAAS
