CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023809
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Metal-response element-binding transcription factor 2 
Protein Synonyms/Alias
 Metal regulatory transcription factor 2; Metal-response element DNA-binding protein M96; Polycomb-like protein 2; hPCl2 
Gene Name
 MTF2 
Gene Synonyms/Alias
 PCL2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
161CVFATTTKRGGALKKubiquitination[1]
313GELADTPKSERYEHVubiquitination[1, 2]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983
Functional Description
 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). 
Sequence Annotation
 DOMAIN 44 101 Tudor.
 ZN_FING 102 157 PHD-type 1.
 ZN_FING 201 255 PHD-type 2.
 MOD_RES 24 24 Phosphothreonine.  
Keyword
 Alternative splicing; Chromatin regulator; Complete proteome; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 593 AA 
Protein Sequence
MRDSTGAGNS LVHKRSPLRR NQKTPTSLTK LSLQDGHKAK KPACKFEEGQ DVLARWSDGL 60
FYLGTIKKIN ILKQSCFIIF EDSSKSWVLW KDIQTGATGS GEMVCTICQE EYSEAPNEMV 120
ICDKCGQGYH QLCHTPHIDC SVIDSDEKWL CRQCVFATTT KRGGALKKGP NAKALQVMKQ 180
TLPYSVADLE WDAGHKTNVQ QCYCYCGGPG DWYLKMLQCC KCKQWFHEAC VQCLQKPMLF 240
GDRFYTFICS VCSSGPEYLK RLPLQWVDIA HLCLYNLSVI HKKKYFDSEL ELMTYINENW 300
DRLHPGELAD TPKSERYEHV LEALNDYKTM FMSGKEIKKK KHLFGLRIRV PPVPPNVAFK 360
AEKEPEGTSH EFKIKGRKAS KPISDSREVS NGIEKKGKKK SVGRPPGPYT RKMIQKTAEP 420
LLDKESISEN PTLDLPCSIG RTEGTAHSSN TSDVDFTGAS SAKETTSSSI SRHYGLSDSR 480
KRTRTGRSWP AAIPHLRRRR GRLPRRALQT QNSEIVKDDE GKEDYQFDEL NTEILNNLAD 540
QELQLNHLKN SITSYFGAAG RIACGEKYRV LARRVTLDGK VQYLVEWEGA TAS 593 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0035064; F:methylated histone residue binding; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
 GO:0061086; P:negative regulation of histone H3-K27 methylation; ISS:UniProtKB.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
 GO:0061087; P:positive regulation of histone H3-K27 methylation; ISS:UniProtKB.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
 GO:0007379; P:segment specification; ISS:UniProtKB.
 GO:0019827; P:stem cell maintenance; ISS:UniProtKB. 
Interpro
 IPR025894; Mtf2_C_dom.
 IPR002999; Tudor.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF14061; Mtf2_C
 PF00628; PHD 
SMART
 SM00249; PHD
 SM00333; TUDOR 
PROSITE
 PS50304; TUDOR
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS