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Transcription factor MafK (Erythroid transcription factor NF-E2 p18 subunit)

 MAFK_HUMAN              Reviewed;         156 AA.
O60675; A4D214;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
12-SEP-2018, entry version 153.
RecName: Full=Transcription factor MafK;
AltName: Full=Erythroid transcription factor NF-E2 p18 subunit;
Name=MAFK;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN TRANSCRIPTION, INTERACTION
WITH NFE2L1 AND NFE2L2, AND TISSUE SPECIFICITY.
PubMed=9150357; DOI=10.1038/sj.onc.1201024;
Toki T., Itoh J., Kitazawa J., Arai K., Hatakeyama K., Akasaka J.,
Igarashi K., Nomura N., Yokoyama M., Yamamoto M., Ito E.;
"Human small Maf proteins form heterodimers with CNC family
transcription factors and recognize the NF-E2 motif.";
Oncogene 14:1901-1910(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION, DNA-BINDING, AND INTERACTION WITH NFE2L1.
PubMed=8932385;
Johnsen O., Skammelsrud N., Luna L., Nishizawa M., Prydz H.,
Kolstoe A.B.;
"Small Maf proteins interact with the human transcription factor
TCF11/Nrf1/LCR-F1.";
Nucleic Acids Res. 24:4289-4297(1996).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-130, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Since they lack a putative transactivation domain, the
small Mafs behave as transcriptional repressors when they dimerize
among themselves (PubMed:9150357). However, they seem to serve as
transcriptional activators by dimerizing with other (usually
larger) basic-zipper proteins, such as NFE2, NFE2L1/NRF1,
NFE2L2/NRF2 and NFE2L3/NRF3, and recruiting them to specific DNA-
binding sites (PubMed:9150357, PubMed:8932385). Small Maf proteins
heterodimerize with Fos and may act as competitive repressors of
the NF-E2 transcription factor (PubMed:9150357).
{ECO:0000269|PubMed:8932385, ECO:0000269|PubMed:9150357}.
-!- SUBUNIT: Homodimer or heterodimer. It can form high affinity
heterodimers with members of the CNC-bZIP family such as NFE2,
NFE2L1/NRF1, NFE2L2/NRF2 and NFE2L3/NRF3 (PubMed:9150357,
PubMed:8932385). {ECO:0000269|PubMed:8932385,
ECO:0000269|PubMed:9150357}.
-!- INTERACTION:
Q16236:NFE2L2; NbExp=3; IntAct=EBI-2559512, EBI-2007911;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- SIMILARITY: Belongs to the bZIP family. Maf subfamily.
{ECO:0000305}.
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EMBL; AF059194; AAC14426.1; -; mRNA.
EMBL; AK092414; BAG52549.1; -; mRNA.
EMBL; AC093734; AAP21866.1; -; Genomic_DNA.
EMBL; CH236953; EAL23943.1; -; Genomic_DNA.
EMBL; CH471144; EAW87207.1; -; Genomic_DNA.
EMBL; BC148265; AAI48266.1; -; mRNA.
CCDS; CCDS5325.1; -.
RefSeq; NP_002351.1; NM_002360.3.
RefSeq; XP_005249908.2; XM_005249851.2.
RefSeq; XP_006715836.1; XM_006715773.2.
UniGene; Hs.520612; -.
ProteinModelPortal; O60675; -.
SMR; O60675; -.
BioGrid; 113688; 18.
IntAct; O60675; 4.
STRING; 9606.ENSP00000344903; -.
ChEMBL; CHEMBL2346484; -.
iPTMnet; O60675; -.
PhosphoSitePlus; O60675; -.
BioMuta; MAFK; -.
EPD; O60675; -.
MaxQB; O60675; -.
PaxDb; O60675; -.
PeptideAtlas; O60675; -.
PRIDE; O60675; -.
ProteomicsDB; 49520; -.
DNASU; 7975; -.
Ensembl; ENST00000343242; ENSP00000344903; ENSG00000198517.
Ensembl; ENST00000403150; ENSP00000386009; ENSG00000198517.
Ensembl; ENST00000406174; ENSP00000385437; ENSG00000198517.
GeneID; 7975; -.
KEGG; hsa:7975; -.
UCSC; uc003skr.4; human.
CTD; 7975; -.
DisGeNET; 7975; -.
EuPathDB; HostDB:ENSG00000198517.9; -.
GeneCards; MAFK; -.
HGNC; HGNC:6782; MAFK.
HPA; CAB026820; -.
HPA; HPA060841; -.
MIM; 600197; gene.
neXtProt; NX_O60675; -.
OpenTargets; ENSG00000198517; -.
PharmGKB; PA30540; -.
eggNOG; ENOG410ISHX; Eukaryota.
eggNOG; ENOG4111MYK; LUCA.
GeneTree; ENSGT00550000074549; -.
HOVERGEN; HBG001725; -.
InParanoid; O60675; -.
KO; K09037; -.
OMA; LQCFART; -.
OrthoDB; EOG091G0H46; -.
PhylomeDB; O60675; -.
TreeFam; TF325689; -.
Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
SIGNOR; O60675; -.
ChiTaRS; MAFK; human.
GeneWiki; MAFK; -.
GenomeRNAi; 7975; -.
PRO; PR:O60675; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000198517; Expressed in 198 organ(s), highest expression level in vagina.
CleanEx; HS_MAFK; -.
ExpressionAtlas; O60675; baseline and differential.
Genevisible; O60675; HS.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:ProtInc.
GO; GO:0071535; F:RING-like zinc finger domain binding; IEA:Ensembl.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0001221; F:transcription cofactor binding; IEA:Ensembl.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific DNA binding; IC:NTNU_SB.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
GO; GO:0007399; P:nervous system development; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR004827; bZIP.
InterPro; IPR004826; bZIP_Maf.
InterPro; IPR028574; MafK.
InterPro; IPR008917; TF_DNA-bd_sf.
InterPro; IPR024874; Transciption_factor_Maf_fam.
PANTHER; PTHR10129; PTHR10129; 1.
PANTHER; PTHR10129:SF26; PTHR10129:SF26; 1.
Pfam; PF03131; bZIP_Maf; 1.
SMART; SM00338; BRLZ; 1.
SUPFAM; SSF47454; SSF47454; 1.
PROSITE; PS50217; BZIP; 1.
1: Evidence at protein level;
Complete proteome; DNA-binding; Isopeptide bond; Nucleus;
Phosphoprotein; Reference proteome; Repressor; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 156 Transcription factor MafK.
/FTId=PRO_0000076503.
DOMAIN 51 114 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 51 76 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 79 93 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
MOD_RES 25 25 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
CROSSLNK 130 130 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
SEQUENCE 156 AA; 17523 MW; 39F98F8D550C168E CRC64;
MTTNPKPNKA LKVKKEAGEN APVLSDDELV SMSVRELNQH LRGLTKEEVT RLKQRRRTLK
NRGYAASCRI KRVTQKEELE RQRVELQQEV EKLARENSSM RLELDALRSK YEALQTFART
VARGPVAPSK VATTSVITIV KSTELSSTSV PFSAAS


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