PRDM1_HUMAN
ID PRDM1_HUMAN Reviewed; 825 AA.
AC O75626; B2REA6; E1P5E0; Q86WM7;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=PR domain zinc finger protein 1;
DE EC=2.1.1.-;
DE AltName: Full=BLIMP-1;
DE AltName: Full=Beta-interferon gene positive regulatory domain I-binding factor;
DE AltName: Full=PR domain-containing protein 1;
DE AltName: Full=Positive regulatory domain I-binding factor 1;
DE Short=PRDI-BF1;
DE Short=PRDI-binding factor 1;
GN Name=PRDM1; Synonyms=BLIMP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION.
RX PubMed=1851123; DOI=10.1101/gad.5.5.868;
RA Keller A.D., Maniatis T.;
RT "Identification and characterization of a novel repressor of beta-
RT interferon gene expression.";
RL Genes Dev. 5:868-879(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), AND FUNCTION.
RX PubMed=12626569; DOI=10.4049/jimmunol.170.6.3125;
RA Gyory I., Fejer G., Ghosh N., Seto E., Wright K.L.;
RT "Identification of a functionally impaired positive regulatory domain I
RT binding factor 1 transcription repressor in myeloma cell lines.";
RL J. Immunol. 170:3125-3133(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=21421998; DOI=10.1093/hmg/ddr114;
RA Julaton V.T., Reijo Pera R.A.;
RT "NANOS3 function in human germ cell development.";
RL Hum. Mol. Genet. 20:2238-2250(2011).
RN [7]
RP SUMOYLATION AT LYS-816.
RX PubMed=22555612; DOI=10.1038/embor.2012.60;
RA Ying H.Y., Su S.T., Hsu P.H., Chang C.C., Lin I.Y., Tseng Y.H., Tsai M.D.,
RA Shih H.M., Lin K.I.;
RT "SUMOylation of Blimp-1 is critical for plasma cell differentiation.";
RL EMBO Rep. 13:631-637(2012).
RN [8]
RP INTERACTION WITH FBXO10 AND FBXO11, AND UBIQUITINATION.
RX PubMed=24613396; DOI=10.1016/j.devcel.2014.01.028;
RA Horn M., Geisen C., Cermak L., Becker B., Nakamura S., Klein C., Pagano M.,
RA Antebi A.;
RT "DRE-1/FBXO11-dependent degradation of BLMP-1/BLIMP-1 governs C. elegans
RT developmental timing and maturation.";
RL Dev. Cell 28:697-710(2014).
RN [9]
RP INTERACTION WITH FBXO11.
RX PubMed=24968003; DOI=10.1371/journal.pgen.1004428;
RA Huang T.F., Cho C.Y., Cheng Y.T., Huang J.W., Wu Y.Z., Yeh A.Y.,
RA Nishiwaki K., Chang S.C., Wu Y.C.;
RT "BLMP-1/Blimp-1 regulates the spatiotemporal cell migration pattern in C.
RT elegans.";
RL PLoS Genet. 10:E1004428-E1004428(2014).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-816, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [11]
RP INTERACTION WITH LDB1; SMARCD3 AND SMARCC1.
RX PubMed=32417234; DOI=10.1016/j.bbagrm.2020.194577;
RA Fong H.T., Hagen T., Inoue T.;
RT "LDB1 and the SWI/SNF complex participate in both transcriptional
RT activation and repression by Caenorhabditis elegans BLIMP1/PRDM1.";
RL Biochim. Biophys. Acta 1863:194577-194577(2020).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 38-223.
RG Structural genomics consortium (SGC);
RT "The crystal structure of methyltransferase domain of human PR domain-
RT containing protein 1.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [13]
RP VARIANTS ARG-84 AND ARG-107, CHARACTERIZATION OF VARIANTS ARG-84 AND
RP ARG-107, INVOLVEMENT IN ABC-DLBCL, MUTAGENESIS OF PRO-84 AND ILE-107,
RP UBIQUITINATION, SUMOYLATION, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP CBX4; PIAS1; PIAS2; PIAS3; PIAS4; PML AND RNF4.
RX PubMed=28842558; DOI=10.1038/s41467-017-00476-w;
RA Wang W.F., Yan L., Liu Z., Liu L.X., Lin J., Liu Z.Y., Chen X.P., Zhang W.,
RA Xu Z.Z., Shi T., Li J.M., Zhao Y.L., Meng G., Xia Y., Li J.Y., Zhu J.;
RT "HSP70-Hrd1 axis precludes the oncorepressor potential of N-terminal
RT misfolded Blimp-1s in lymphoma cells.";
RL Nat. Commun. 8:363-363(2017).
CC -!- FUNCTION: Transcription factor that mediates a transcriptional program
CC in various innate and adaptive immune tissue-resident lymphocyte T cell
CC types such as tissue-resident memory T (Trm), natural killer (trNK) and
CC natural killer T (NKT) cells and negatively regulates gene expression
CC of proteins that promote the egress of tissue-resident T-cell
CC populations from non-lymphoid organs. Plays a role in the development,
CC retention and long-term establishment of adaptive and innate tissue-
CC resident lymphocyte T cell types in non-lymphoid organs, such as the
CC skin and gut, but also in other nonbarrier tissues like liver and
CC kidney, and therefore may provide immediate immunological protection
CC against reactivating infections or viral reinfection (By similarity).
CC Binds specifically to the PRDI element in the promoter of the beta-
CC interferon gene (PubMed:1851123). Drives the maturation of B-
CC lymphocytes into Ig secreting cells (PubMed:12626569). Associates with
CC the transcriptional repressor ZNF683 to chromatin at gene promoter
CC regions (By similarity). {ECO:0000250|UniProtKB:Q60636,
CC ECO:0000269|PubMed:12626569, ECO:0000269|PubMed:1851123}.
CC -!- SUBUNIT: Interacts with PRMT5 (By similarity). Interacts with FBXO10
CC (PubMed:24613396). Interacts with FBXO11 (PubMed:24613396,
CC PubMed:24968003). Interacts with multiple nuclear sumoylation E3
CC ligases, including CBX4, PIAS1, PIAS2, PIAS3, PIAS4, PML and RNF4, but
CC not RANBP2 (PubMed:28842558). Interacts with LDB1, SMARCD3 and SMARCC1
CC (PubMed:32417234). {ECO:0000250|UniProtKB:Q60636,
CC ECO:0000269|PubMed:24613396, ECO:0000269|PubMed:24968003,
CC ECO:0000269|PubMed:28842558, ECO:0000269|PubMed:32417234}.
CC -!- INTERACTION:
CC O75626; O75925: PIAS1; NbExp=2; IntAct=EBI-948789, EBI-629434;
CC O75626-2; P63165: SUMO1; NbExp=2; IntAct=EBI-7839538, EBI-80140;
CC O75626-3; P01023: A2M; NbExp=3; IntAct=EBI-25829882, EBI-640741;
CC O75626-3; P50570-2: DNM2; NbExp=3; IntAct=EBI-25829882, EBI-10968534;
CC O75626-3; O14656-2: TOR1A; NbExp=3; IntAct=EBI-25829882, EBI-25847109;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28842558}. Cytoplasm
CC {ECO:0000269|PubMed:21421998}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O75626-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75626-2; Sequence=VSP_039188;
CC Name=3;
CC IsoId=O75626-3; Sequence=VSP_043646, VSP_043647;
CC -!- PTM: Sumoylation at Lys-816 by PIAS1 augments transcriptional repressor
CC activity, and is critical for plasma cell differentiation
CC (PubMed:22555612). Can be sumoylated with SUMO1 and SUMO2 by PML.
CC Degradation of the wild-type protein mostly depends upon sumoylation,
CC rather than ubiquitination (PubMed:28842558). Desumoylated by SENP1 and
CC SENP6 (PubMed:28842558). {ECO:0000269|PubMed:22555612,
CC ECO:0000269|PubMed:28842558}.
CC -!- PTM: Ubiquitinated by the SCF(FBXO11) complex, leading to its
CC degradation by the proteasome. {ECO:0000269|PubMed:24613396}.
CC -!- DISEASE: Note=In certain aggressive cases of activated B cell-like
CC diffuse large B-cell lymphoma (ABC-DLBCL), PRDM1 protein instability
CC has been observed. This instability, which impairs B-cell
CC differentiation, is caused by N-terminal misfolding mutations,
CC including those occurring at positions Pro-84 and Ile-107, and results
CC in PRDM1 protein sequestration in the cytoplasm, followed by
CC proteasomal degradation via a heat shock protein 70 HSPA1A-SYNV1/HRD1
CC pathway. These N-terminal mutations do not affect PRDM1 transcription
CC regulation activity. HSPA1A inhibition restores PRDM1 nuclear
CC localization and transcriptional activity in lymphoma cell lines and
CC suppresses tumor growth in xenografts, more efficiently than proteasome
CC inhibition. {ECO:0000269|PubMed:28842558}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO45623.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PRDM1ID41831ch6q21.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF084199; AAC33300.1; -; mRNA.
DR EMBL; AY198414; AAO45623.1; ALT_INIT; mRNA.
DR EMBL; AY198415; AAO45624.1; -; mRNA.
DR EMBL; AL358952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL022067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48419.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48421.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48422.1; -; Genomic_DNA.
DR EMBL; BC103832; AAI03833.1; -; mRNA.
DR EMBL; BC103833; AAI03834.1; -; mRNA.
DR EMBL; BC103834; AAI03835.1; -; mRNA.
DR CCDS; CCDS34505.1; -. [O75626-3]
DR CCDS; CCDS5054.2; -. [O75626-1]
DR PIR; A39564; A39564.
DR RefSeq; NP_001189.2; NM_001198.3. [O75626-1]
DR RefSeq; NP_878911.1; NM_182907.2. [O75626-3]
DR RefSeq; XP_011534365.1; XM_011536063.2. [O75626-2]
DR RefSeq; XP_016866676.1; XM_017011187.1. [O75626-2]
DR PDB; 3DAL; X-ray; 1.65 A; A/B=38-223.
DR PDBsum; 3DAL; -.
DR AlphaFoldDB; O75626; -.
DR SMR; O75626; -.
DR BioGRID; 107108; 78.
DR IntAct; O75626; 60.
DR MINT; O75626; -.
DR STRING; 9606.ENSP00000358092; -.
DR iPTMnet; O75626; -.
DR PhosphoSitePlus; O75626; -.
DR BioMuta; PRDM1; -.
DR EPD; O75626; -.
DR jPOST; O75626; -.
DR MassIVE; O75626; -.
DR MaxQB; O75626; -.
DR PaxDb; O75626; -.
DR PeptideAtlas; O75626; -.
DR PRIDE; O75626; -.
DR ProteomicsDB; 50124; -. [O75626-1]
DR ProteomicsDB; 50125; -. [O75626-2]
DR ProteomicsDB; 50126; -. [O75626-3]
DR Antibodypedia; 19038; 697 antibodies from 39 providers.
DR DNASU; 639; -.
DR Ensembl; ENST00000369089.3; ENSP00000358085.3; ENSG00000057657.17. [O75626-3]
DR Ensembl; ENST00000369091.6; ENSP00000358087.2; ENSG00000057657.17. [O75626-2]
DR Ensembl; ENST00000369096.9; ENSP00000358092.4; ENSG00000057657.17. [O75626-1]
DR Ensembl; ENST00000651185.1; ENSP00000498716.1; ENSG00000057657.17. [O75626-2]
DR Ensembl; ENST00000652320.1; ENSP00000498580.1; ENSG00000057657.17. [O75626-2]
DR GeneID; 639; -.
DR KEGG; hsa:639; -.
DR MANE-Select; ENST00000369096.9; ENSP00000358092.4; NM_001198.4; NP_001189.2.
DR UCSC; uc003prd.3; human. [O75626-1]
DR CTD; 639; -.
DR DisGeNET; 639; -.
DR GeneCards; PRDM1; -.
DR HGNC; HGNC:9346; PRDM1.
DR HPA; ENSG00000057657; Tissue enhanced (esophagus).
DR MIM; 603423; gene.
DR neXtProt; NX_O75626; -.
DR OpenTargets; ENSG00000057657; -.
DR PharmGKB; PA33707; -.
DR VEuPathDB; HostDB:ENSG00000057657; -.
DR eggNOG; KOG2461; Eukaryota.
DR GeneTree; ENSGT00940000154798; -.
DR HOGENOM; CLU_007033_2_1_1; -.
DR InParanoid; O75626; -.
DR OMA; CQNGMNV; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; O75626; -.
DR TreeFam; TF316545; -.
DR PathwayCommons; O75626; -.
DR Reactome; R-HSA-6804754; Regulation of TP53 Expression.
DR Reactome; R-HSA-9701898; STAT3 nuclear events downstream of ALK signaling.
DR SignaLink; O75626; -.
DR SIGNOR; O75626; -.
DR BioGRID-ORCS; 639; 24 hits in 1102 CRISPR screens.
DR ChiTaRS; PRDM1; human.
DR EvolutionaryTrace; O75626; -.
DR GeneWiki; PRDM1; -.
DR GenomeRNAi; 639; -.
DR Pharos; O75626; Tbio.
DR PRO; PR:O75626; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O75626; protein.
DR Bgee; ENSG00000057657; Expressed in lower esophagus mucosa and 143 other tissues.
DR ExpressionAtlas; O75626; baseline and differential.
DR Genevisible; O75626; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0042826; F:histone deacetylase binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0035904; P:aorta development; IEA:Ensembl.
DR GO; GO:0048844; P:artery morphogenesis; IEA:Ensembl.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl.
DR GO; GO:0042462; P:eye photoreceptor cell development; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0007281; P:germ cell development; IEA:Ensembl.
DR GO; GO:0003170; P:heart valve development; IEA:Ensembl.
DR GO; GO:0034969; P:histone arginine methylation; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0060576; P:intestinal epithelial cell development; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0001893; P:maternal placenta development; IEA:Ensembl.
DR GO; GO:0001763; P:morphogenesis of a branching structure; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0033082; P:regulation of extrathymic T cell differentiation; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0032823; P:regulation of natural killer cell differentiation; ISS:UniProtKB.
DR GO; GO:0051136; P:regulation of NK T cell differentiation; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009314; P:response to radiation; IEA:Ensembl.
DR GO; GO:1990654; P:sebum secreting cell proliferation; IEA:Ensembl.
DR GO; GO:0060707; P:trophoblast giant cell differentiation; IEA:Ensembl.
DR GO; GO:0003281; P:ventricular septum development; IEA:Ensembl.
DR CDD; cd19187; PR-SET_PRDM1; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR016608; PRDM1.
DR InterPro; IPR044413; PRDM1_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; PIRSF013212; PRDM1; 1.
DR SMART; SM00317; SET; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 3.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Cytoplasm;
KW DNA-binding; Immunity; Innate immunity; Isopeptide bond; Metal-binding;
KW Methyltransferase; Nucleus; Reference proteome; Repeat; Repressor;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..825
FT /note="PR domain zinc finger protein 1"
FT /id="PRO_0000047757"
FT DOMAIN 84..201
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 575..597
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 603..625
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 631..653
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 659..681
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 324..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..574
FT /note="Interaction with PIAS1"
FT COMPBIAS 325..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 816
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000269|PubMed:22555612"
FT CROSSLNK 816
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..36
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1851123"
FT /id="VSP_039188"
FT VAR_SEQ 1..3
FT /note="MLD -> MEK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12626569,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_043646"
FT VAR_SEQ 4..137
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12626569,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_043647"
FT VARIANT 74
FT /note="G -> S (in dbSNP:rs2185379)"
FT /id="VAR_019983"
FT VARIANT 84
FT /note="P -> R (found in an activated B cell-like diffuse
FT large B-cell lymphoma (ABC-DLBCL) cell line; protein
FT instability caused by increased susceptibility to
FT proteasomal degradation)"
FT /evidence="ECO:0000269|PubMed:28842558"
FT /id="VAR_083591"
FT VARIANT 107
FT /note="I -> R (found in an activated B cell-like diffuse
FT large B-cell lymphoma (ABC-DLBCL) cell line; protein
FT instability caused by increased susceptibility to
FT proteasomal degradation)"
FT /evidence="ECO:0000269|PubMed:28842558"
FT /id="VAR_083592"
FT VARIANT 203
FT /note="D -> E (in dbSNP:rs811925)"
FT /id="VAR_024221"
FT MUTAGEN 84
FT /note="P->G,K: Protein instability caused by increased
FT susceptibility to proteasomal degradation."
FT /evidence="ECO:0000269|PubMed:28842558"
FT MUTAGEN 107
FT /note="I->G,K: Protein instability caused by increased
FT susceptibility to proteasomal degradation."
FT /evidence="ECO:0000269|PubMed:28842558"
FT HELIX 51..57
FT /evidence="ECO:0007829|PDB:3DAL"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:3DAL"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:3DAL"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:3DAL"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:3DAL"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:3DAL"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:3DAL"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:3DAL"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:3DAL"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:3DAL"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:3DAL"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:3DAL"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:3DAL"
FT STRAND 181..188
FT /evidence="ECO:0007829|PDB:3DAL"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:3DAL"
FT HELIX 202..207
FT /evidence="ECO:0007829|PDB:3DAL"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:3DAL"
SQ SEQUENCE 825 AA; 91771 MW; 07B389BACCD6172F CRC64;
MLDICLEKRV GTTLAAPKCN SSTVRFQGLA EGTKGTMKMD MEDADMTLWT EAEFEEKCTY
IVNDHPWDSG ADGGTSVQAE ASLPRNLLFK YATNSEEVIG VMSKEYIPKG TRFGPLIGEI
YTNDTVPKNA NRKYFWRIYS RGELHHFIDG FNEEKSNWMR YVNPAHSPRE QNLAACQNGM
NIYFYTIKPI PANQELLVWY CRDFAERLHY PYPGELTMMN LTQTQSSLKQ PSTEKNELCP
KNVPKREYSV KEILKLDSNP SKGKDLYRSN ISPLTSEKDL DDFRRRGSPE MPFYPRVVYP
IRAPLPEDFL KASLAYGIER PTYITRSPIP SSTTPSPSAR SSPDQSLKSS SPHSSPGNTV
SPVGPGSQEH RDSYAYLNAS YGTEGLGSYP GYAPLPHLPP AFIPSYNAHY PKFLLPPYGM
NCNGLSAVSS MNGINNFGLF PRLCPVYSNL LGGGSLPHPM LNPTSLPSSL PSDGARRLLQ
PEHPREVLVP APHSAFSFTG AAASMKDKAC SPTSGSPTAG TAATAEHVVQ PKATSAAMAA
PSSDEAMNLI KNKRNMTGYK TLPYPLKKQN GKIKYECNVC AKTFGQLSNL KVHLRVHSGE
RPFKCQTCNK GFTQLAHLQK HYLVHTGEKP HECQVCHKRF SSTSNLKTHL RLHSGEKPYQ
CKVCPAKFTQ FVHLKLHKRL HTRERPHKCS QCHKNYIHLC SLKVHLKGNC AAAPAPGLPL
EDLTRINEEI EKFDISDNAD RLEDVEDDIS VISVVEKEIL AVVRKEKEET GLKVSLQRNM
GNGLLSSGCS LYESSDLPLM KLPPSNPLPL VPVKVKQETV EPMDP
