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Database: UniProt
Entry: A6QPM3
LinkDB: A6QPM3
Original site: A6QPM3 
ID   PRDM6_BOVIN             Reviewed;         590 AA.
AC   A6QPM3;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   13-FEB-2019, entry version 83.
DE   RecName: Full=Putative histone-lysine N-methyltransferase PRDM6;
DE            EC=2.1.1.43;
DE   AltName: Full=PR domain zinc finger protein 6;
DE   AltName: Full=PR domain-containing protein 6;
GN   Name=PRDM6;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal spinal cord;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Putative histone methyltransferase that acts as a
CC       transcriptional repressor of smooth muscle gene expression.
CC       Promotes the transition from differentiated to proliferative
CC       smooth muscle by suppressing differentiation and maintaining the
CC       proliferative potential of vascular smooth muscle cells. Also
CC       plays a role in endothelial cells by inhibiting endothelial cell
CC       proliferation, survival and differentiation. It is unclear whether
CC       it has histone methyltransferase activity in vivo. According to
CC       some authors, it does not act as a histone methyltransferase by
CC       itself and represses transcription by recruiting EHMT2/G9a.
CC       According to others, it possesses histone methyltransferase
CC       activity when associated with other proteins and specifically
CC       methylates 'Lys-20' of histone H4 in vitro. 'Lys-20' methylation
CC       represents a specific tag for epigenetic transcriptional
CC       repression. {ECO:0000250|UniProtKB:Q3UZD5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC   -!- SUBUNIT: Interacts with HDAC1, HDAC2, HDAC3, CBX1 and EP300.
CC       {ECO:0000250|UniProtKB:Q3UZD5}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3UZD5}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
DR   EMBL; BC149387; AAI49388.1; -; mRNA.
DR   RefSeq; NP_001096725.1; NM_001103255.2.
DR   UniGene; Bt.36375; -.
DR   ProteinModelPortal; A6QPM3; -.
DR   SMR; A6QPM3; -.
DR   STRING; 9913.ENSBTAP00000027421; -.
DR   PaxDb; A6QPM3; -.
DR   Ensembl; ENSBTAT00000027421; ENSBTAP00000027421; ENSBTAG00000020578.
DR   GeneID; 519857; -.
DR   KEGG; bta:519857; -.
DR   CTD; 93166; -.
DR   VGNC; VGNC:33298; PRDM6.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; KOG2461; Eukaryota.
DR   eggNOG; ENOG410XRVC; LUCA.
DR   GeneTree; ENSGT00940000155852; -.
DR   HOGENOM; HOG000090218; -.
DR   HOVERGEN; HBG108289; -.
DR   InParanoid; A6QPM3; -.
DR   KO; K20795; -.
DR   OMA; PPEIPEW; -.
DR   OrthoDB; 1318335at2759; -.
DR   TreeFam; TF106403; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000020578; Expressed in 6 organ(s), highest expression level in lung.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:0022008; P:neurogenesis; IBA:GO_Central.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF00096; zf-C2H2; 3.
DR   SMART; SM00317; SET; 1.
DR   SMART; SM00355; ZnF_C2H2; 4.
DR   SUPFAM; SSF57667; SSF57667; 2.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; Complete proteome; Metal-binding;
KW   Methyltransferase; Nucleus; Reference proteome; Repeat; Repressor;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN         1    590       Putative histone-lysine N-
FT                                methyltransferase PRDM6.
FT                                /FTId=PRO_0000363958.
FT   DOMAIN      241    360       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING     468    490       C2H2-type 1; degenerate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     496    518       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     524    546       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     552    574       C2H2-type 4; degenerate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   COMPBIAS     30     33       Poly-Gly.
FT   COMPBIAS     43     70       Pro-rich.
FT   COMPBIAS     94    106       Poly-Ala.
FT   COMPBIAS    223    227       Poly-Ala.
SQ   SEQUENCE   590 AA;  63989 MW;  B7D55FF617059231 CRC64;
     MLKPGDPGGS AFLKVDPAYL QHWQQLFPHG GGGPLKGGGA AGPLGAPQPL QPPPPPERAE
     PQPDSLRPRP ASLSSASSTP ASSSTSASSA SSCAAAAAAA AAAALAGLSA LPVAQLPVFA
     PLATVAAEPL PPKDLCLGAT SGPGPSKCGG SGGDGRGVPR FRCSAEELDY YLYGQQRMEI
     IPLNQHTSDP NNRCDMCADN RNGECPMHGP LHSLRRLVGT SSAAAAAPPP ELPEWLRDLP
     REVCLCTSTV PGLAYGICAA QRIQQGTWIG PFQGVLLPPE KVQAGAVRNT QHLWEIYDQD
     GTLQHFIDGG EPSKSSWMRY IRCARHCGEQ NLTVVQYRSN IFYRACIDIP RGTELLVWYN
     DSYTSFFGIP LQCIAQDENL NVPSTVMEAM CRQDALQPFN KSSKLSQAPQ QRSVVFPQTP
     CGRNFSLLDK SGPLESGFNQ ISVKNQRVLA SPTSTSQLHS EFSDWHLWKC GQCFKTFTQR
     ILLQMHVCTQ NPDRPYQCGH CSQSFSQPSE LRNHVVTHSS DRPFKCGYCG RAFAGATTLN
     NHIRTHTGEK PFKCERCERS FTQATQLSRH QRMPNECKPI TESPESIEVD
//
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