MTF1_HUMAN
ID MTF1_HUMAN Reviewed; 753 AA.
AC Q14872; B2RAK6; Q96CB1;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Metal regulatory transcription factor 1;
DE AltName: Full=MRE-binding transcription factor;
DE AltName: Full=Transcription factor MTF-1;
GN Name=MTF1;
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, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=8065932; DOI=10.1093/nar/22.15.3167;
RA Brugnera E., Georgiev O., Radtke F., Heuchel R., Baker E., Sutherland G.,
RA Schaffner W.;
RT "Cloning, chromosomal mapping and characterization of the human metal-
RT regulatory transcription factor MTF-1.";
RL Nucleic Acids Res. 22:3167-3173(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
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=Muscle;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
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).
CC -!- FUNCTION: Zinc-dependent transcriptional regulator of cellular adaption
CC to conditions of exposure to heavy metals (PubMed:8065932). Binds to
CC metal responsive elements (MRE) in promoters and activates the
CC transcription of metallothionein genes like metallothionein-2/MT2A
CC (PubMed:8065932). Also regulates the expression of metalloproteases in
CC response to intracellular zinc and functions as a catabolic regulator
CC of cartilages (By similarity). {ECO:0000250|UniProtKB:Q07243,
CC ECO:0000269|PubMed:8065932}.
CC -!- INTERACTION:
CC Q14872; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-747024, EBI-541426;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8065932}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q07243}. Note=Translocation to the nucleus is
CC induced by metals. {ECO:0000250|UniProtKB:Q07243}.
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DR EMBL; X78710; CAA55363.1; -; mRNA.
DR EMBL; AK314233; BAG36903.1; -; mRNA.
DR EMBL; AL929472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07312.1; -; Genomic_DNA.
DR EMBL; BC014454; AAH14454.1; -; mRNA.
DR CCDS; CCDS30676.1; -.
DR PIR; S48059; S48059.
DR RefSeq; NP_005946.2; NM_005955.2.
DR RefSeq; XP_011539793.1; XM_011541491.2.
DR AlphaFoldDB; Q14872; -.
DR SMR; Q14872; -.
DR BioGRID; 110620; 115.
DR IntAct; Q14872; 1.
DR STRING; 9606.ENSP00000362127; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB12965; Silver.
DR iPTMnet; Q14872; -.
DR PhosphoSitePlus; Q14872; -.
DR BioMuta; MTF1; -.
DR DMDM; 68052403; -.
DR EPD; Q14872; -.
DR jPOST; Q14872; -.
DR MassIVE; Q14872; -.
DR MaxQB; Q14872; -.
DR PaxDb; Q14872; -.
DR PeptideAtlas; Q14872; -.
DR PRIDE; Q14872; -.
DR ProteomicsDB; 60214; -.
DR Antibodypedia; 17617; 231 antibodies from 29 providers.
DR DNASU; 4520; -.
DR Ensembl; ENST00000373036.5; ENSP00000362127.3; ENSG00000188786.10.
DR GeneID; 4520; -.
DR KEGG; hsa:4520; -.
DR MANE-Select; ENST00000373036.5; ENSP00000362127.3; NM_005955.3; NP_005946.2.
DR UCSC; uc001cce.1; human.
DR CTD; 4520; -.
DR DisGeNET; 4520; -.
DR GeneCards; MTF1; -.
DR HGNC; HGNC:7428; MTF1.
DR HPA; ENSG00000188786; Tissue enhanced (bone).
DR MIM; 600172; gene.
DR neXtProt; NX_Q14872; -.
DR OpenTargets; ENSG00000188786; -.
DR PharmGKB; PA31235; -.
DR VEuPathDB; HostDB:ENSG00000188786; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157291; -.
DR HOGENOM; CLU_026685_0_0_1; -.
DR InParanoid; Q14872; -.
DR OMA; SMFQSPD; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q14872; -.
DR TreeFam; TF106493; -.
DR PathwayCommons; Q14872; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR Reactome; R-HSA-5660489; MTF1 activates gene expression.
DR SignaLink; Q14872; -.
DR SIGNOR; Q14872; -.
DR BioGRID-ORCS; 4520; 57 hits in 1105 CRISPR screens.
DR ChiTaRS; MTF1; human.
DR GeneWiki; MTF1; -.
DR GenomeRNAi; 4520; -.
DR Pharos; Q14872; Tbio.
DR PRO; PR:Q14872; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q14872; protein.
DR Bgee; ENSG00000188786; Expressed in secondary oocyte and 205 other tissues.
DR Genevisible; Q14872; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0035035; F:histone acetyltransferase binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:1990079; P:cartilage homeostasis; IEA:Ensembl.
DR GO; GO:0071294; P:cellular response to zinc ion; IEA:Ensembl.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0045944; P:positive 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 GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
DR GO; GO:0010038; P:response to metal ion; TAS:ProtInc.
DR GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:Ensembl.
DR InterPro; IPR029796; Metal_TF1.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR19818:SF131; PTHR19818:SF131; 1.
DR Pfam; PF00096; zf-C2H2; 6.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q07243"
FT CHAIN 2..753
FT /note="Metal regulatory transcription factor 1"
FT /id="PRO_0000047220"
FT ZN_FING 140..164
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 170..194
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 200..224
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 229..253
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 259..283
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 289..313
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 308..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 133..138
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 395..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..450
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..668
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:Q07243"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07243"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CONFLICT 185
FT /note="Y -> H (in Ref. 1; CAA55363)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 753 AA; 80957 MW; CC96518824170E98 CRC64;
MGEHSPDNNI IYFEAEEDEL TPDDKMLRFV DKNGLVPSSS GTVYDRTTVL IEQDPGTLED
EDDDGQCGEH LPFLVGGEEG FHLIDHEAMS QGYVQHIISP DQIHLTINPG STPMPRNIEG
ATLTLQSECP ETKRKEVKRY QCTFEGCPRT YSTAGNLRTH QKTHRGEYTF VCNQEGCGKA
FLTSYSLRIH VRVHTKEKPF ECDVQGCEKA FNTLYRLKAH QRLHTGKTFN CESEGCSKYF
TTLSDLRKHI RTHTGEKPFR CDHDGCGKAF AASHHLKTHV RTHTGERPFF CPSNGCEKTF
STQYSLKSHM KGHDNKGHSY NALPQHNGSE DTNHSLCLSD LSLLSTDSEL RENSSTTQGQ
DLSTISPAII FESMFQNSDD TAIQEDPQQT ASLTESFNGD AESVSDVPPS TGNSASLSLP
LVLQPGLSEP PQPLLPASAP SAPPPAPSLG PGSQQAAFGN PPALLQPPEV PVPHSTQFAA
NHQEFLPHPQ APQPIVPGLS VVAGASASAA AVASAVAAPA PPQSTTEPLP AMVQTLPLGA
NSVLTNNPTI TITPTPNTAI LQSSLVMGEQ NLQWILNGAT SSPQNQEQIQ QASKVEKVFF
TTAVPVASSP GSSVQQIGLS VPVIIIKQEE ACQCQCACRD SAKERASSRR KGCSSPPPPE
PSPQAPDGPS LQLPAQTFSS APVPGSSSST LPSSCEQSRQ AETPSDPQTE TLSAMDVSEF
LSLQSLDTPS NLIPIEALLQ GEEEMGLTSS FSK
