PRD11_MOUSE
ID PRD11_MOUSE Reviewed; 565 AA.
AC A2AGX3; A2AGX2; A2AGX4;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=PR domain-containing protein 11;
DE EC=2.1.1.-;
GN Name=Prdm11;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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 [3]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=25499759; DOI=10.1182/blood-2014-03-560805;
RA Fog C.K., Asmar F., Come C., Jensen K.T., Johansen J.V., Kheir T.B.,
RA Jacobsen L., Friis C., Louw A., Rosgaard L., Obro N.F., Marquart H.V.,
RA Anthonsen K., Braat A.K., van Lohuizen M., Ralfkiaer E., Gronbaek K.,
RA Lund A.H.;
RT "Loss of PRDM11 promotes MYC-driven lymphomagenesis.";
RL Blood 125:1272-1281(2015).
CC -!- FUNCTION: May be involved in transcription regulation.
CC {ECO:0000250|UniProtKB:Q9NQV5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NQV5}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9NQV5}.
CC -!- TISSUE SPECIFICITY: Widely expressed, with the highest levels in
CC spleen, lung, mesenteric lymph node and kidney. Among splenocytes,
CC predominantly expressed by B-cells (at protein level).
CC {ECO:0000269|PubMed:25499759}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are born in expected Mendelian ratios
CC and exhibit no apparent phenotype. Mutant embryonic fibroblasts show an
CC increased oncogenic transformation capacity.
CC {ECO:0000269|PubMed:25499759}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM14370.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM14372.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL713913; CAM14370.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL713913; CAM14371.1; -; Genomic_DNA.
DR EMBL; AL713913; CAM14372.1; ALT_SEQ; Genomic_DNA.
DR CCDS; CCDS50647.1; -.
DR RefSeq; NP_001171007.1; NM_001177536.1.
DR AlphaFoldDB; A2AGX3; -.
DR SMR; A2AGX3; -.
DR BioGRID; 786018; 1.
DR STRING; 10090.ENSMUSP00000106905; -.
DR iPTMnet; A2AGX3; -.
DR PhosphoSitePlus; A2AGX3; -.
DR EPD; A2AGX3; -.
DR MaxQB; A2AGX3; -.
DR PaxDb; A2AGX3; -.
DR PRIDE; A2AGX3; -.
DR ProteomicsDB; 289837; -.
DR Antibodypedia; 26153; 147 antibodies from 26 providers.
DR Ensembl; ENSMUST00000111274; ENSMUSP00000106905; ENSMUSG00000075028.
DR Ensembl; ENSMUST00000178666; ENSMUSP00000136795; ENSMUSG00000075028.
DR GeneID; 100042784; -.
DR KEGG; mmu:100042784; -.
DR UCSC; uc012bzp.1; mouse.
DR CTD; 56981; -.
DR MGI; MGI:2685553; Prdm11.
DR VEuPathDB; HostDB:ENSMUSG00000075028; -.
DR eggNOG; KOG2461; Eukaryota.
DR GeneTree; ENSGT00940000159837; -.
DR HOGENOM; CLU_593911_0_0_1; -.
DR InParanoid; A2AGX3; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; A2AGX3; -.
DR TreeFam; TF316279; -.
DR BioGRID-ORCS; 100042784; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Prdm11; mouse.
DR PRO; PR:A2AGX3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2AGX3; protein.
DR Bgee; ENSMUSG00000075028; Expressed in aortic valve and 114 other tissues.
DR ExpressionAtlas; A2AGX3; baseline and differential.
DR Genevisible; A2AGX3; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:2000271; P:positive regulation of fibroblast apoptotic process; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0043408; P:regulation of MAPK cascade; ISS:UniProtKB.
DR CDD; cd19195; PR-SET_PRDM11; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR044405; PRDM11_PR/SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR Pfam; PF00856; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Isopeptide bond; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation.
FT CHAIN 1..565
FT /note="PR domain-containing protein 11"
FT /id="PRO_0000416113"
FT DOMAIN 115..226
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 371..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 54
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV5"
FT CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV5"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV5"
FT CROSSLNK 166
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV5"
FT CROSSLNK 180
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV5"
SQ SEQUENCE 565 AA; 63383 MW; 20FB804E1834B418 CRC64;
MTENMKECLA HTKAAVGDMV TVVKTEVCSP LRDQEYGQPC SRRLEPSSME VEPKKLKGKR
DLIVTKSFQQ VDFWFCESCQ EYFVDECPNH GPPVFVSDTP VPVGIPDRAA LTIPQGMEVV
KDAGGESDVR CINEVIPKGH IFGPYEGQIS TQDKSAGFFS WLIVDKNNRY KSIDGSDETK
ANWMRYVVIS REEREQNLLA FQHSERIYFR ACRDIRPGER LRVWYSEDYM KRLHSMSQET
IHRNLARGEK RLQREKAEQA LENPEDLRGP TQFPVLKQGR SPYKRSFDEG DIHPQAKKKK
IDLIFKDVLE ASLESGNVEA RQLALSTSLV IRKVPKYQDD DYGRAALTQG ICRTPGEGDW
KVPQRVAKEL GPLEDEEEEP TSFKADSPAE ASLASDPHEL PTTSFCPNCI RLKKKVRELQ
AELDMLKSGK LPEPSLLPPQ VLELPEFSDP AGKFLRMRLL LKGRVCSATR AHCVEGGPER
SALSQPPARR PEECNSAEAA PSWGGSPVPQ VTEAGWLEDR GREGIACANL YILLVNKICP
ICRRAVCCVL DLVFSLGGGA HCCLP
