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Protein

Metal regulatory transcription factor 1

Gene

MTF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Activates the metallothionein I promoter. Binds to the metal responsive element (MRE).1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri140 – 16425C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri170 – 19425C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri200 – 22425C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri229 – 25325C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri259 – 28325C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri289 – 31325C2H2-type 6PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • core promoter binding Source: UniProtKB
  • DNA binding Source: ProtInc
  • metal ion binding Source: UniProtKB-KW
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
  • RNA polymerase II core promoter sequence-specific DNA binding Source: Ensembl
  • sequence-specific DNA binding transcription factor activity Source: ProtInc
  • transcription coactivator activity Source: ProtInc

GO - Biological processi

  • positive regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
  • regulation of transcription from RNA polymerase II promoter Source: ProtInc
  • response to cadmium ion Source: Ensembl
  • response to metal ion Source: ProtInc
  • response to oxidative stress Source: Ensembl
  • transition metal ion homeostasis Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_116145. PPARA activates gene expression.
REACT_147904. Activation of gene expression by SREBF (SREBP).

Names & Taxonomyi

Protein namesi
Recommended name:
Metal regulatory transcription factor 1
Alternative name(s):
MRE-binding transcription factor
Transcription factor MTF-1
Gene namesi
Name:MTF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:7428. MTF1.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: HPA
  • nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31235.

Polymorphism and mutation databases

BioMutaiMTF1.
DMDMi68052403.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 753752Metal regulatory transcription factor 1PRO_0000047220Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglycineBy similarity
Modified residuei5 – 51PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ14872.
PaxDbiQ14872.
PRIDEiQ14872.

PTM databases

PhosphoSiteiQ14872.

Expressioni

Gene expression databases

BgeeiQ14872.
CleanExiHS_MTF1.
GenevisibleiQ14872. HS.

Organism-specific databases

HPAiHPA028604.
HPA028689.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
AP1M1Q9BXS53EBI-747024,EBI-541426

Protein-protein interaction databases

BioGridi110620. 3 interactions.
IntActiQ14872. 1 interaction.
MINTiMINT-1456332.
STRINGi9606.ENSP00000362127.

Structurei

3D structure databases

ProteinModelPortaliQ14872.
SMRiQ14872. Positions 138-316.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi133 – 1386Nuclear localization signalSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi420 – 49778Pro-richAdd
BLAST

Sequence similaritiesi

Contains 6 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri140 – 16425C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri170 – 19425C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri200 – 22425C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri229 – 25325C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri259 – 28325C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri289 – 31325C2H2-type 6PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5048.
GeneTreeiENSGT00760000118771.
HOGENOMiHOG000059609.
HOVERGENiHBG006412.
InParanoidiQ14872.
OMAiEDTNHSL.
OrthoDBiEOG76T9QH.
PhylomeDBiQ14872.
TreeFamiTF106493.

Family and domain databases

Gene3Di3.30.160.60. 6 hits.
InterProiIPR029796. Metal_TF1.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PANTHERiPTHR11389:SF347. PTHR11389:SF347. 1 hit.
PfamiPF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 6 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 6 hits.
PS50157. ZINC_FINGER_C2H2_2. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q14872-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGEHSPDNNI IYFEAEEDEL TPDDKMLRFV DKNGLVPSSS GTVYDRTTVL
60 70 80 90 100
IEQDPGTLED EDDDGQCGEH LPFLVGGEEG FHLIDHEAMS QGYVQHIISP
110 120 130 140 150
DQIHLTINPG STPMPRNIEG ATLTLQSECP ETKRKEVKRY QCTFEGCPRT
160 170 180 190 200
YSTAGNLRTH QKTHRGEYTF VCNQEGCGKA FLTSYSLRIH VRVHTKEKPF
210 220 230 240 250
ECDVQGCEKA FNTLYRLKAH QRLHTGKTFN CESEGCSKYF TTLSDLRKHI
260 270 280 290 300
RTHTGEKPFR CDHDGCGKAF AASHHLKTHV RTHTGERPFF CPSNGCEKTF
310 320 330 340 350
STQYSLKSHM KGHDNKGHSY NALPQHNGSE DTNHSLCLSD LSLLSTDSEL
360 370 380 390 400
RENSSTTQGQ DLSTISPAII FESMFQNSDD TAIQEDPQQT ASLTESFNGD
410 420 430 440 450
AESVSDVPPS TGNSASLSLP LVLQPGLSEP PQPLLPASAP SAPPPAPSLG
460 470 480 490 500
PGSQQAAFGN PPALLQPPEV PVPHSTQFAA NHQEFLPHPQ APQPIVPGLS
510 520 530 540 550
VVAGASASAA AVASAVAAPA PPQSTTEPLP AMVQTLPLGA NSVLTNNPTI
560 570 580 590 600
TITPTPNTAI LQSSLVMGEQ NLQWILNGAT SSPQNQEQIQ QASKVEKVFF
610 620 630 640 650
TTAVPVASSP GSSVQQIGLS VPVIIIKQEE ACQCQCACRD SAKERASSRR
660 670 680 690 700
KGCSSPPPPE PSPQAPDGPS LQLPAQTFSS APVPGSSSST LPSSCEQSRQ
710 720 730 740 750
AETPSDPQTE TLSAMDVSEF LSLQSLDTPS NLIPIEALLQ GEEEMGLTSS

FSK
Length:753
Mass (Da):80,957
Last modified:June 21, 2005 - v2
Checksum:iCC96518824170E98
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti185 – 1851Y → H in CAA55363 (PubMed:8065932).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78710 mRNA. Translation: CAA55363.1.
AK314233 mRNA. Translation: BAG36903.1.
AL929472 Genomic DNA. Translation: CAH70087.1.
CH471059 Genomic DNA. Translation: EAX07312.1.
BC014454 mRNA. Translation: AAH14454.1.
CCDSiCCDS30676.1.
PIRiS48059.
RefSeqiNP_005946.2. NM_005955.2.
UniGeneiHs.471991.

Genome annotation databases

EnsembliENST00000373036; ENSP00000362127; ENSG00000188786.
GeneIDi4520.
KEGGihsa:4520.
UCSCiuc001cce.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78710 mRNA. Translation: CAA55363.1.
AK314233 mRNA. Translation: BAG36903.1.
AL929472 Genomic DNA. Translation: CAH70087.1.
CH471059 Genomic DNA. Translation: EAX07312.1.
BC014454 mRNA. Translation: AAH14454.1.
CCDSiCCDS30676.1.
PIRiS48059.
RefSeqiNP_005946.2. NM_005955.2.
UniGeneiHs.471991.

3D structure databases

ProteinModelPortaliQ14872.
SMRiQ14872. Positions 138-316.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110620. 3 interactions.
IntActiQ14872. 1 interaction.
MINTiMINT-1456332.
STRINGi9606.ENSP00000362127.

PTM databases

PhosphoSiteiQ14872.

Polymorphism and mutation databases

BioMutaiMTF1.
DMDMi68052403.

Proteomic databases

MaxQBiQ14872.
PaxDbiQ14872.
PRIDEiQ14872.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373036; ENSP00000362127; ENSG00000188786.
GeneIDi4520.
KEGGihsa:4520.
UCSCiuc001cce.1. human.

Organism-specific databases

CTDi4520.
GeneCardsiGC01M038275.
HGNCiHGNC:7428. MTF1.
HPAiHPA028604.
HPA028689.
MIMi600172. gene.
neXtProtiNX_Q14872.
PharmGKBiPA31235.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5048.
GeneTreeiENSGT00760000118771.
HOGENOMiHOG000059609.
HOVERGENiHBG006412.
InParanoidiQ14872.
OMAiEDTNHSL.
OrthoDBiEOG76T9QH.
PhylomeDBiQ14872.
TreeFamiTF106493.

Enzyme and pathway databases

ReactomeiREACT_116145. PPARA activates gene expression.
REACT_147904. Activation of gene expression by SREBF (SREBP).

Miscellaneous databases

ChiTaRSiMTF1. human.
GeneWikiiMTF1.
GenomeRNAii4520.
NextBioi17448.
PROiQ14872.
SOURCEiSearch...

Gene expression databases

BgeeiQ14872.
CleanExiHS_MTF1.
GenevisibleiQ14872. HS.

Family and domain databases

Gene3Di3.30.160.60. 6 hits.
InterProiIPR029796. Metal_TF1.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PANTHERiPTHR11389:SF347. PTHR11389:SF347. 1 hit.
PfamiPF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 6 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 6 hits.
PS50157. ZINC_FINGER_C2H2_2. 6 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, chromosomal mapping and characterization of the human metal-regulatory transcription factor MTF-1."
    Brugnera E., Georgiev O., Radtke F., Heuchel R., Baker E., Sutherland G., Schaffner W.
    Nucleic Acids Res. 22:3167-3173(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Tissue: Liver.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Muscle.

Entry informationi

Entry nameiMTF1_HUMAN
AccessioniPrimary (citable) accession number: Q14872
Secondary accession number(s): B2RAK6, Q96CB1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: June 21, 2005
Last modified: June 24, 2015
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.