PRDM2_RAT
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 25-MAY-2022, entry version 144.
DE RecName: Full=PR domain zinc finger protein 2;
DE EC=2.1.1.355;
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 shares
RT an epitope with the adenovirus E1A protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:4467-4471(1995).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637; SER-776 AND SER-780, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent histone methyltransferase
CC that specifically methylates 'Lys-9' of histone H3. May function as a
CC DNA-binding transcription factor. Binds to the macrophage-specific TPA-
CC responsive element (MTE) of the HMOX1 (heme oxygenase 1) gene and may
CC act as a transcriptional activator of this gene (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)-
CC 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;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60276, Rhea:RHEA-COMP:15538, Rhea:RHEA-
CC COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.355;
CC -!- SUBUNIT: Binds to the retinoblastoma protein (RB). Interacts with GATA3
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; U17837; AAA74468.1; -; mRNA.
DR RefSeq; NP_001071116.1; NM_001077648.1.
DR AlphaFoldDB; Q63755; -.
DR SMR; Q63755; -.
DR DIP; DIP-473N; -.
DR STRING; 10116.ENSRNOP00000046011; -.
DR iPTMnet; Q63755; -.
DR PhosphoSitePlus; 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; KOG2461; Eukaryota.
DR InParanoid; Q63755; -.
DR PhylomeDB; Q63755; -.
DR PRO; PR:Q63755; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0008340; P:determination of adult lifespan; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0032355; P:response to estradiol; IDA:RGD.
DR CDD; cd19188; PR-SET_PRDM2; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR009170; PRDM2.
DR InterPro; IPR044414; PRDM2_PR-SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
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 SUPFAM; SSF57667; SSF57667; 3.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Isopeptide bond; Metal-binding; Methyltransferase;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1706
FT /note="PR domain zinc finger protein 2"
FT /id="PRO_0000047759"
FT DOMAIN 27..140
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 355..377
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 385..407
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 476..499
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1123..1145
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1151..1174
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1180..1203
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1321..1343
FT /note="C2H2-type 7; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1443..1465
FT /note="C2H2-type 8; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 154..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1218..1251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1466..1563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..179
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..293
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..506
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..868
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..908
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..957
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..986
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1015
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1035
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1075
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1510..1563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13029"
FT MOD_RES 637
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13029"
FT MOD_RES 776
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 780
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 791
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13029"
FT CROSSLNK 645
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13029"
FT CROSSLNK 684
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13029"
FT CROSSLNK 686
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13029"
FT CROSSLNK 769
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13029"
FT CROSSLNK 860
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13029"
FT CROSSLNK 870
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13029"
FT CROSSLNK 1136
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13029"
FT CROSSLNK 1140
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13029"
FT CROSSLNK 1269
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13029"
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
