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Database: UniProt
Entry: Q63755
LinkDB: Q63755
Original site: Q63755 
ID   PRDM2_RAT               Reviewed;        1706 AA.
AC   Q63755;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   01-OCT-2014, entry version 107.
DE   RecName: Full=PR domain zinc finger protein 2;
DE            EC=2.1.1.43;
DE   AltName: Full=PR domain-containing protein 2;
DE   AltName: Full=Retinoblastoma protein-interacting zinc finger protein;
DE   AltName: Full=Zinc finger protein RIZ;
GN   Name=Prdm2; Synonyms=Riz;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RX   PubMed=7538672; DOI=10.1073/pnas.92.10.4467;
RA   Buyse I.M., Shao G., Huang S.;
RT   "The retinoblastoma protein binds to RIZ, a zinc-finger protein that
RT   shares an epitope with the adenovirus E1A protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:4467-4471(1995).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent histone
CC       methyltransferase that specifically methylates 'Lys-9' of histone
CC       H3. May function as a DNA-binding transcription factor. Binds to
CC       the macrophage-specific TPA-responsive element (MTE) of the HMOX1
CC       (heme oxygenase 1) gene and may act as a transcriptional activator
CC       of this gene (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC   -!- SUBUNIT: Binds to the retinoblastoma protein (RB). Interacts with
CC       GATA3 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
CC   -!- SIMILARITY: Contains 8 C2H2-type zinc fingers.
CC       {ECO:0000255|PROSITE-ProRule:PRU00042}.
CC   -!- SIMILARITY: Contains 1 SET domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
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DR   EMBL; U17837; AAA74468.1; -; mRNA.
DR   RefSeq; NP_001071116.1; NM_001077648.1.
DR   UniGene; Rn.202632; -.
DR   ProteinModelPortal; Q63755; -.
DR   SMR; Q63755; 1-160.
DR   DIP; DIP-473N; -.
DR   STRING; 10116.ENSRNOP00000046011; -.
DR   PhosphoSite; Q63755; -.
DR   PaxDb; Q63755; -.
DR   PRIDE; Q63755; -.
DR   GeneID; 313678; -.
DR   KEGG; rno:313678; -.
DR   UCSC; RGD:1594531; rat.
DR   CTD; 7799; -.
DR   RGD; 1594531; Prdm2.
DR   eggNOG; NOG258873; -.
DR   HOGENOM; HOG000231078; -.
DR   HOVERGEN; HBG053671; -.
DR   InParanoid; Q63755; -.
DR   KO; K11432; -.
DR   PhylomeDB; Q63755; -.
DR   NextBio; 666643; -.
DR   PRO; PR:Q63755; -.
DR   Genevestigator; Q63755; -.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0005515; F:protein binding; IPI:RGD.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0032355; P:response to estradiol; IDA:RGD.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.160.60; -; 1.
DR   InterPro; IPR009170; RIZ_retinblastoma-bd_prot.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   PIRSF; PIRSF002395; RIZ_SET; 1.
DR   SMART; SM00317; SET; 1.
DR   SMART; SM00355; ZnF_C2H2; 8.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE   2: Evidence at transcript level;
KW   Activator; Complete proteome; DNA-binding; Metal-binding;
KW   Methyltransferase; Nucleus; Reference proteome; Repeat;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN         1   1706       PR domain zinc finger protein 2.
FT                                /FTId=PRO_0000047759.
FT   DOMAIN       27    140       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING     355    377       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     385    407       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     476    499       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING    1123   1145       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING    1151   1174       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING    1180   1203       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING    1321   1343       C2H2-type 7; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING    1443   1465       C2H2-type 8; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   COMPBIAS    246    327       Glu-rich.
FT   COMPBIAS    893   1067       Pro-rich.
FT   COMPBIAS   1472   1565       Ser-rich.
SQ   SEQUENCE   1706 AA;  187555 MW;  55EA419491D2D68C CRC64;
     MHQNTESVAA TETLAEVPEH VLRGLPEEVR LFPSAVDKTR IGVWATKPIL KGKKFGPFVG
     DKKKRSQVRN NVYMWEVYYP NLGWMCIDAT DPEKGNWLRY VNWACSGEEQ NLFPLEINRA
     IYYKTLKPIA PGEELLVWYN GEDNPEIAAA IEEERASARS KRSSPKSRRG KKKSHENKNK
     GIRTHPTQLK ASELDSTFAN MRGSAEGPKE EDERPLASAP EQPAPLPEVG NQDAVPQVAI
     PLPACEPQPE VDGKQEVTDC EVNDVEEEEL EEEEELEEEE EEELGEDGVE EADMPNESSA
     KEPEIRCEEK PEDLLEEPQS MSNEAREDSP DVTPPPHTPR AREEANGDVL ETFMFPCQHC
     ERKFATKQGL ERHMHIHIST INHAFKCKYC GKRFGTQINR RRHERRHETG LKRRPSMTLQ
     SSEDPDDGKG ENVTSKDESS PPQLGQDCLI LNSEKTSQEV LNSSFVEENG EVKELHPCKY
     CKKVFGTHTN MRRHQRRVHE RHLIPKGVRR KGGLLEEPQP PAEQAPPSQN VYVPSTEPEE
     EGETDDVYIM DISSNISENL NYYIDGKIQT NSSTSNCDVI EMESNSAHLY GIDCLLTPVT
     VEITQNIKST QVSVTDDLLK DSPSSTNCES KKRRTASPPV LPKIKTETES DSTAPSCSLS
     LPLSISTAEV VSFHKEKGVY LSSKLKQLLQ TQDKLTLPAG FSAAEIPKLG PVCASAPASM
     LPVTSSRFKR RTSSPPSSPQ HSPALRDFGK PNDGKAAWTD TVLTSKKPKL ESRSDSPAWS
     LSGRDERETG SPPCFDEYKI SKEWAASSTF SSVCNQQPLD LSSGVKQKSE GTGKTPVPWE
     SVLDLSVHKK PCDSEGKEFK ENHLAQPAAK KKKPTTCMLQ KVLLNEYNGV SLPTETTPEV
     TRSPSPCKSP DTQPDPELGP DSSCSVPTAE SPPEVVGPSS PPLQTASLSS GQLPPLLTPT
     EPSSPPPCPP VLTVATPPPP LLPTVPLSHP SSDASPQQCP SPFSNTTAQS PLPILSPTVS
     PSPSPIPPVE PLMSAASPGP PTLSSSSSSS SSFPSSSCSS TSPSPPPLSA VSSVVSSGDN
     LEASLPAVTF KQEESESEGL KPKEEAPPAG GQSVVQETFS KNFICNVCES PFLSIKDLTK
     HLSVHAEEWP FKCEFCVQLF KVKTDLSEHR FLLHGVGNIF VCSVCKKEFA FLCNLQQHQR
     DLHPDEVCTH HEFESGTLRP QNFTDPSKAN VEHMPSLPEE PLETSREEEL NDSSEELYTT
     IKIMASGIKT KDPDVRLGLN QHYPSFKPPP FQYHHRNPMG IGVTATNFTT HNIPQTFTTA
     IRCTKCGKGV DNMPELHKHI LACASASDKK RYTPKKNPVP LKQTVQPKNG VVVLDNSGKN
     AFRRMGQPKR LSFNVELGKM SPNKLKLSAL KKKNQLVQKA ILQKNRAAKQ KADLRDTSEA
     SSHICPYCDR EFTYIGSLNK HAAFSCPKKP LSPSKRKVSH SSKKGGHASS SSSDRNSSCH
     PRRRTADTEI KMQSTQAPLG KTRARSTGPA QASLPSSSFR SRQNVKFAAS VKSKKASSSS
     LRNSSPIRMA KITHVEGKKP KAVAKSHSAQ LSSKSSRGLH VRVQKSKAVI QSKTALASKR
     RTDRFIVKSR ERSGGPITRS LQLAAAADLS ESRREDSSAR HELKDFSYSL RLASRCGSST
     ASYITRQCRK VKAAAATPFQ GPFLKE
//
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