ID   A2A7B5_MOUSE            Unreviewed;      1709 AA.
AC   A2A7B5;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 133.
DE   SubName: Full=PR domain containing 2, with ZNF domain {ECO:0000313|Ensembl:ENSMUSP00000101404.2};
GN   Name=Prdm2 {ECO:0000313|Ensembl:ENSMUSP00000101404.2,
GN   ECO:0000313|MGI:MGI:107628};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000101404.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0007829|PubMed:17242355}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMUSP00000101404.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000101404.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [4] {ECO:0000313|Ensembl:ENSMUSP00000101404.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000101404.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; NP_001074824.3; NM_001081355.3.
DR   RefSeq; XP_017175407.1; XM_017319918.1.
DR   AlphaFoldDB; A2A7B5; -.
DR   SMR; A2A7B5; -.
DR   STRING; 10090.ENSMUSP00000101404; -.
DR   iPTMnet; A2A7B5; -.
DR   PhosphoSitePlus; A2A7B5; -.
DR   jPOST; A2A7B5; -.
DR   MaxQB; A2A7B5; -.
DR   PaxDb; 10090-ENSMUSP00000101404; -.
DR   PeptideAtlas; A2A7B5; -.
DR   ProteomicsDB; 371305; -.
DR   Antibodypedia; 1774; 288 antibodies from 25 providers.
DR   Ensembl; ENSMUST00000105778.8; ENSMUSP00000101404.2; ENSMUSG00000057637.14.
DR   GeneID; 110593; -.
DR   KEGG; mmu:110593; -.
DR   UCSC; uc012doh.1; mouse.
DR   AGR; MGI:107628; -.
DR   CTD; 7799; -.
DR   MGI; MGI:107628; Prdm2.
DR   VEuPathDB; HostDB:ENSMUSG00000057637; -.
DR   eggNOG; KOG2461; Eukaryota.
DR   GeneTree; ENSGT00940000159410; -.
DR   HOGENOM; CLU_002916_1_0_1; -.
DR   InParanoid; A2A7B5; -.
DR   OMA; MASRCPS; -.
DR   OrthoDB; 5399106at2759; -.
DR   PhylomeDB; A2A7B5; -.
DR   TreeFam; TF332173; -.
DR   BioGRID-ORCS; 110593; 3 hits in 83 CRISPR screens.
DR   ChiTaRS; Prdm2; mouse.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; A2A7B5; Protein.
DR   Bgee; ENSMUSG00000057637; Expressed in interventricular septum and 99 other cell types or tissues.
DR   ExpressionAtlas; A2A7B5; baseline and differential.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
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:MGI.
DR   GO; GO:0042054; F:histone methyltransferase activity; IEA:InterPro.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0008340; P:determination of adult lifespan; IMP:MGI.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0032355; P:response to estradiol; ISO:MGI.
DR   CDD; cd19188; PR-SET_PRDM2; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 3.
DR   Gene3D; 2.170.270.10; SET domain; 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   PANTHER; PTHR16515; PR DOMAIN ZINC FINGER PROTEIN; 1.
DR   PANTHER; PTHR16515:SF37; PR DOMAIN ZINC FINGER PROTEIN 2; 1.
DR   Pfam; PF21549; PRDM2_PR; 1.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   Pfam; PF13912; zf-C2H2_6; 2.
DR   PIRSF; PIRSF002395; RIZ_SET; 1.
DR   SMART; SM00317; SET; 1.
DR   SMART; SM00355; ZnF_C2H2; 8.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
DR   Genevisible; A2A7B5; MM.
PE   1: Evidence at protein level;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Proteomics identification {ECO:0007829|EPD:A2A7B5,
KW   ECO:0007829|MaxQB:A2A7B5};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT   DOMAIN          27..140
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          356..378
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          386..408
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          477..500
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          1126..1153
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          1154..1177
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          1183..1209
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          1446..1473
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          154..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          399..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          493..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          615..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          726..795
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          853..877
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          890..1116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1221..1255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1469..1607
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..176
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        263..294
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..321
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        493..507
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        615..634
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        726..746
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        853..869
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        890..909
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        916..930
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        943..958
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        959..996
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        997..1016
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1017..1036
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1039..1086
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1235..1255
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1487..1502
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1529..1570
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1587..1607
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        646
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002395-1"
FT   CROSSLNK        770
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002395-1"
SQ   SEQUENCE   1709 AA;  187203 MW;  F719B0D1A70DE1B2 CRC64;
     MHQNTESVAV TETLAEVPEH VLRGLPEEVR LLPSAVDKTR IGVWATKPIL KGKKFGPFVG
     DKKKRSQVRN NVYMWEVYYP NLGWMCIDAT DPEKGNWLRY VNWACSGEEQ NLFPLEINRA
     IYYKTLKPIA PGEELLVWYN GEDNPEIAAA IEEERASARS KRSSPKSRRG KKKSQENKNK
     GVRTQAAARK ASELDSTSAN MRGSAEGPKE EDERPLASAP EQPALLPEVV SQDAVPQVAI
     PLPACESQPG ADGKQEVTDC EVNNMKEEEE EEEEELEEEE EEEELGEDGE EEADMPNESS
     VKEPEIRCEE KPEDLLEEPR SVPTETSEGS PGATPPPHAP RAREEANGEG LETFMFPCQH
     CERKFATKQG LERHMHIHIS TINHAFKCKY CGKPFGTQIN RRRHERRHET GLKRRPSMAL
     QSSEDPDDGK GENVTSKDES SPPQLGQDCL ILNSEKTSQE ILNSSFVEEN GEVKELHPCK
     YCKKVFGTHT NMRRHQRRVH ERHLIPKGVR RKGGLLEEPQ PPAEQAPPSQ NVYVPSTEPE
     EDGDADDVYI MDISSNISEN LNYYIDGKIQ TNNSTSDCDV IEMESNSAHL YGIDCLLTPV
     TVEITQNIKS TQGSVTDDLL KESPSSTNCE SKKRRTASPP VLPKIKAETD SDSTAPSCSL
     SLPLSISTTE VVSFHKEKGV YLSSKLKQLL QTQDKLTPPA GISTAEIPKL GPVCVSAPAS
     MLAVTSSRFK RRTSSPPSSP QHSPALRDFG KQSDGKAAWT DTALTSKKPK LESRSDSPAW
     SLSGRDERET GSPPCFDEYK ISKEWAASST FSSVCNQQPL DLSSGVKQKS EGTGKTPVPW
     ESVLDLSVHK KPCDSEGKEF KENHLAQPAA KKKKPTTCML QKVLLNEYNG VSLPTESTPE
     ATRSPSPCKS PDTQPDPELA TDSSCSAPTA ESPPEVVGPS SPPLQAASLS SGQLPPLLIP
     TEPSSPPPCP PVLTVATPPP PLLPTVPLPN PSCDASPQQC PSPFSNATAQ SPLPILSPTV
     SPSPSPIPPV EPLMSAASPG PPTLSSSSSS SSSSSFSSSS CSSSSPSPPP LSAVSSVVSS
     GDNLEASLPA ITLKQEESES EGLKRKEEAP AAGGQSAVQE TFSRNFVCNV CASPFLSIKD
     LTKHLSVHAE EWPFKCEFCV QLFKGKTDLS EHRFLLHGVG NIFVCSVCKK EFAFLCNLQQ
     HQRDLHPDEL CTHHEFESGT LRPQNFTDPS KAHVEHMPSL PEEPAEASRE EELNDSSEEL
     YTTIKIMASG IKTKEPDVRL GLNQHYPSFK PPPFQYHHRN PMGIGVTATN FTTHNIPQTF
     TTAIRCTKCG KSVDNMPELH KHILACASAS DKKRYTPKKN PVPLRQTVQP KNGVLVLDNS
     GKNAFRRMGQ PKRLSFNVEL SKMSPNKLKL NALKKKNQLV QKAILQKNRS AKQKADLRDT
     SEASSHICPY CDREFTYIGS LNKHAAFSCP KKPLSPSKRK VSHSSKKGGH TSSASSDRNS
     SSNPRRRTAD TEIKMQSMQA PLGKTRARST GPAQASLPSS SFRSRQNVKF AASVKSKKAS
     SSSLRNSSPV RMAKITHVEG KKSKAVAKSH STQLSSKASR SLHVKVQKSK AVLQSKTALA
     SKKRTDRFIV KSRERSGGPI TRSLQLAAAA DLSESRREDS SARHELKDLS YSLRLASRCA
     SSTAPYITRQ CRKVKAAAAT QFQGPFFKE
//