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Metal-response element-binding transcription factor 2 (Metal regulatory transcription factor 2) (Metal-response element DNA-binding protein M96) (Polycomb-like protein 2) (hPCl2)

 MTF2_HUMAN              Reviewed;         593 AA.
Q9Y483; A6NGQ9; A8K2Q3; B1AKT5; B1AKT6; Q96G26; Q9UES9; Q9UP40;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
28-MAR-2018, sequence version 3.
28-MAR-2018, entry version 145.
RecName: Full=Metal-response element-binding transcription factor 2;
AltName: Full=Metal regulatory transcription factor 2;
AltName: Full=Metal-response element DNA-binding protein M96;
AltName: Full=Polycomb-like protein 2;
Short=hPCl2;
Name=MTF2; Synonyms=PCL2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
Tao B., Wang J., Yuan J., Qiang B.;
"Isolation and cloning of a novel human M96 cDNA, spliced isoforms.";
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Holen T., Aasland R.;
"The polycomblike protein family.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Tongue;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Pre-B cell;
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24, 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).
[7]
H3K36ME3-BINDING.
PubMed=23142980; DOI=10.1038/nsmb.2435;
Musselman C.A., Avvakumov N., Watanabe R., Abraham C.G., Lalonde M.E.,
Hong Z., Allen C., Roy S., Nunez J.K., Nickoloff J., Kulesza C.A.,
Yasui A., Cote J., Kutateladze T.G.;
"Molecular basis for H3K36me3 recognition by the Tudor domain of
PHF1.";
Nat. Struct. Mol. Biol. 19:1266-1272(2012).
[8]
H3K36ME3-BINDING.
PubMed=23228662; DOI=10.1016/j.bbrc.2012.11.116;
Qin S., Guo Y., Xu C., Bian C., Fu M., Gong S., Min J.;
"Tudor domains of the PRC2 components PHF1 and PHF19 selectively bind
to histone H3K36me3.";
Biochem. Biophys. Res. Commun. 430:547-553(2013).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
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).
[10]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-360 AND LYS-522, 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: Polycomb group (PcG) that specifically binds histone H3
trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2
complex. Acts by binding to H3K36me3, a mark for transcriptional
activation, and recruiting the PRC2 complex, leading to enhance
PRC2 H3K27me3 methylation activity. Regulates the transcriptional
networks during embryonic stem cell self-renewal and
differentiation. Promotes recruitment of the PRC2 complex to the
inactive X chromosome in differentiating XX ES cells and PRC2
recruitment to target genes in undifferentiated ES cells. Required
to repress Hox genes by enhancing H3K27me3 methylation of the PRC2
complex. In some conditions may act as an inhibitor of PRC2
activity: able to activate the CDKN2A gene and promote cellular
senescence by suppressing the catalytic activity of the PRC2
complex locally. Binds to the metal-regulating-element (MRE) of
MT1A gene promoter (By similarity). {ECO:0000250}.
-!- SUBUNIT: Associated component of the PRC2 complex. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q9Y483-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y483-2; Sequence=VSP_004696;
Name=3;
IsoId=Q9Y483-3; Sequence=VSP_040329;
Name=4;
IsoId=Q9Y483-4; Sequence=VSP_053348;
Note=No experimental confirmation available.;
-!- DOMAIN: The Tudor domain recognizes and binds H3K36me3
(PubMed:23142980, PubMed:23228662). {ECO:0000269|PubMed:23142980,
ECO:0000269|PubMed:23228662}.
-!- SIMILARITY: Belongs to the Polycomblike family. {ECO:0000305}.
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EMBL; AF072814; AAC27618.1; -; mRNA.
EMBL; AF073293; AAC27080.1; -; mRNA.
EMBL; AJ010014; CAA08970.1; -; mRNA.
EMBL; AK290318; BAF83007.1; -; mRNA.
EMBL; AC093577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL117354; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; KF459519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC010013; AAH10013.1; -; mRNA.
CCDS; CCDS53340.1; -. [Q9Y483-4]
CCDS; CCDS53341.1; -. [Q9Y483-3]
RefSeq; NP_001157863.1; NM_001164391.1.
RefSeq; NP_001157865.1; NM_001164393.1.
RefSeq; NP_031384.1; NM_007358.3.
RefSeq; XP_011539318.1; XM_011541016.1.
RefSeq; XP_016856165.1; XM_017000676.1.
UniGene; Hs.31016; -.
PDB; 5XFR; X-ray; 2.25 A; A/B=43-358.
PDBsum; 5XFR; -.
ProteinModelPortal; Q9Y483; -.
SMR; Q9Y483; -.
BioGrid; 116499; 21.
IntAct; Q9Y483; 23.
MINT; Q9Y483; -.
STRING; 9606.ENSP00000359321; -.
iPTMnet; Q9Y483; -.
PhosphoSitePlus; Q9Y483; -.
BioMuta; MTF2; -.
DMDM; 317373393; -.
EPD; Q9Y483; -.
PaxDb; Q9Y483; -.
PeptideAtlas; Q9Y483; -.
PRIDE; Q9Y483; -.
Ensembl; ENST00000370298; ENSP00000359321; ENSG00000143033.
GeneID; 22823; -.
KEGG; hsa:22823; -.
UCSC; uc009wdj.4; human. [Q9Y483-1]
CTD; 22823; -.
EuPathDB; HostDB:ENSG00000143033.17; -.
GeneCards; MTF2; -.
HGNC; HGNC:29535; MTF2.
HPA; HPA069047; -.
HPA; HPA069066; -.
MIM; 609882; gene.
neXtProt; NX_Q9Y483; -.
OpenTargets; ENSG00000143033; -.
PharmGKB; PA128394586; -.
eggNOG; KOG4323; Eukaryota.
eggNOG; ENOG410XQ6E; LUCA.
GeneTree; ENSGT00390000009222; -.
HOGENOM; HOG000010307; -.
HOVERGEN; HBG004755; -.
InParanoid; Q9Y483; -.
KO; K11485; -.
OrthoDB; EOG091G01JL; -.
PhylomeDB; Q9Y483; -.
TreeFam; TF106420; -.
Reactome; R-HSA-212300; PRC2 methylates histones and DNA.
ChiTaRS; MTF2; human.
GenomeRNAi; 22823; -.
PRO; PR:Q9Y483; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000143033; -.
CleanEx; HS_MTF2; -.
ExpressionAtlas; Q9Y483; baseline and differential.
Genevisible; Q9Y483; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0035098; C:ESC/E(Z) complex; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0045814; P:negative regulation of gene expression, epigenetic; TAS:Reactome.
GO; GO:0061086; P:negative regulation of histone H3-K27 methylation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0061087; P:positive regulation of histone H3-K27 methylation; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0007379; P:segment specification; ISS:UniProtKB.
GO; GO:0048863; P:stem cell differentiation; ISS:UniProtKB.
GO; GO:0019827; P:stem cell population maintenance; ISS:UniProtKB.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR025894; Mtf2_C_dom.
InterPro; IPR002999; Tudor.
InterPro; IPR019786; Zinc_finger_PHD-type_CS.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF14061; Mtf2_C; 1.
Pfam; PF00628; PHD; 1.
SMART; SM00249; PHD; 2.
SMART; SM00333; TUDOR; 1.
SUPFAM; SSF57903; SSF57903; 2.
PROSITE; PS01359; ZF_PHD_1; 2.
PROSITE; PS50016; ZF_PHD_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromatin regulator;
Complete proteome; DNA-binding; Isopeptide bond; Metal-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 593 Metal-response element-binding
transcription factor 2.
/FTId=PRO_0000059317.
DOMAIN 44 101 Tudor.
ZN_FING 102 157 PHD-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 201 255 PHD-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
MOD_RES 24 24 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 452 452 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 360 360 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 522 522 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 331 Missing (in isoform 2).
{ECO:0000303|Ref.1}.
/FTId=VSP_004696.
VAR_SEQ 1 102 Missing (in isoform 3).
{ECO:0000303|Ref.1}.
/FTId=VSP_040329.
VAR_SEQ 331 387 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_053348.
VARIANT 140 140 S -> C (in dbSNP:rs2815427).
/FTId=VAR_054765.
STRAND 51 55 {ECO:0000244|PDB:5XFR}.
STRAND 61 70 {ECO:0000244|PDB:5XFR}.
TURN 71 74 {ECO:0000244|PDB:5XFR}.
STRAND 75 80 {ECO:0000244|PDB:5XFR}.
STRAND 85 89 {ECO:0000244|PDB:5XFR}.
HELIX 90 92 {ECO:0000244|PDB:5XFR}.
STRAND 93 95 {ECO:0000244|PDB:5XFR}.
TURN 106 108 {ECO:0000244|PDB:5XFR}.
STRAND 119 121 {ECO:0000244|PDB:5XFR}.
TURN 123 125 {ECO:0000244|PDB:5XFR}.
STRAND 128 130 {ECO:0000244|PDB:5XFR}.
TURN 131 133 {ECO:0000244|PDB:5XFR}.
STRAND 134 136 {ECO:0000244|PDB:5XFR}.
TURN 140 144 {ECO:0000244|PDB:5XFR}.
STRAND 145 147 {ECO:0000244|PDB:5XFR}.
HELIX 152 159 {ECO:0000244|PDB:5XFR}.
HELIX 170 178 {ECO:0000244|PDB:5XFR}.
HELIX 186 188 {ECO:0000244|PDB:5XFR}.
TURN 204 207 {ECO:0000244|PDB:5XFR}.
TURN 212 215 {ECO:0000244|PDB:5XFR}.
STRAND 216 219 {ECO:0000244|PDB:5XFR}.
TURN 220 222 {ECO:0000244|PDB:5XFR}.
STRAND 225 227 {ECO:0000244|PDB:5XFR}.
HELIX 228 230 {ECO:0000244|PDB:5XFR}.
STRAND 245 248 {ECO:0000244|PDB:5XFR}.
HELIX 250 253 {ECO:0000244|PDB:5XFR}.
STRAND 258 261 {ECO:0000244|PDB:5XFR}.
HELIX 266 281 {ECO:0000244|PDB:5XFR}.
TURN 288 291 {ECO:0000244|PDB:5XFR}.
HELIX 292 298 {ECO:0000244|PDB:5XFR}.
HELIX 300 303 {ECO:0000244|PDB:5XFR}.
HELIX 307 310 {ECO:0000244|PDB:5XFR}.
HELIX 313 326 {ECO:0000244|PDB:5XFR}.
TURN 328 330 {ECO:0000244|PDB:5XFR}.
STRAND 331 333 {ECO:0000244|PDB:5XFR}.
HELIX 334 337 {ECO:0000244|PDB:5XFR}.
STRAND 343 348 {ECO:0000244|PDB:5XFR}.
SEQUENCE 593 AA; 67090 MW; 4517B5DD61BB1AF4 CRC64;
MRDSTGAGNS LVHKRSPLRR NQKTPTSLTK LSLQDGHKAK KPACKFEEGQ DVLARWSDGL
FYLGTIKKIN ILKQSCFIIF EDSSKSWVLW KDIQTGATGS GEMVCTICQE EYSEAPNEMV
ICDKCGQGYH QLCHTPHIDS SVIDSDEKWL CRQCVFATTT KRGGALKKGP NAKALQVMKQ
TLPYSVADLE WDAGHKTNVQ QCYCYCGGPG DWYLKMLQCC KCKQWFHEAC VQCLQKPMLF
GDRFYTFICS VCSSGPEYLK RLPLQWVDIA HLCLYNLSVI HKKKYFDSEL ELMTYINENW
DRLHPGELAD TPKSERYEHV LEALNDYKTM FMSGKEIKKK KHLFGLRIRV PPVPPNVAFK
AEKEPEGTSH EFKIKGRKAS KPISDSREVS NGIEKKGKKK SVGRPPGPYT RKMIQKTAEP
LLDKESISEN PTLDLPCSIG RTEGTAHSSN TSDVDFTGAS SAKETTSSSI SRHYGLSDSR
KRTRTGRSWP AAIPHLRRRR GRLPRRALQT QNSEIVKDDE GKEDYQFDEL NTEILNNLAD
QELQLNHLKN SITSYFGAAG RIACGEKYRV LARRVTLDGK VQYLVEWEGA TAS


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18-785-210034 ATF4 (Ab-245) - Activating transcription factor 4; DNA-binding protein TAXREB67; Cyclic AMP response element-binding protein 2; CREB2 Polyclonal 0.05 mg


 

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