SPI1_MOUSE
ID SPI1_MOUSE Reviewed; 272 AA.
AC P17433; Q99L57;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Transcription factor PU.1;
DE AltName: Full=31 kDa-transforming protein;
DE AltName: Full=SFFV proviral integration 1 protein;
GN Name=Spi1; Synonyms=Sfpi-1, Sfpi1;
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 [MRNA], AND INVOLVEMENT IN ERYTHROLEUKEMIA.
RC STRAIN=ICFW;
RX PubMed=2594367;
RA Moreau-Gachelin F., Ray D., Mattei M.-G., Tambourin P., Tavitian A.;
RT "The putative oncogene Spi-1: murine chromosomal localization and
RT transcriptional activation in murine acute erythroleukemias.";
RL Oncogene 4:1449-1456(1989).
RN [2]
RP ERRATUM OF PUBMED:2594367, AND SEQUENCE REVISION.
RA Moreau-Gachelin F., Ray D., Mattei M.-G., Tambourin P., Tavitian A.;
RL Oncogene 5:941-941(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2180582; DOI=10.1016/0092-8674(90)90219-5;
RA Klemsz M.J., McKercher S.R., Celada A., van Beveren C., Maki R.A.;
RT "The macrophage and B cell-specific transcription factor PU.1 is related to
RT the ets oncogene.";
RL Cell 61:113-124(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1985210; DOI=10.1128/jvi.65.1.464-467.1991;
RA Paul R., Schuetze S., Kozak S.L., Kozak C.A., Kabat D.;
RT "The Sfpi-1 proviral integration site of Friend erythroleukemia encodes the
RT ets-related transcription factor Pu.1.";
RL J. Virol. 65:464-467(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 INTERACTION WITH CEBPD.
RX PubMed=7594592;
RA Nagulapalli S., Pongubala J.M., Atchison M.L.;
RT "Multiple proteins physically interact with PU.1. Transcriptional synergy
RT with NF-IL6 beta (C/EBP delta, CRP3).";
RL J. Immunol. 155:4330-4338(1995).
RN [7]
RP RNA-BINDING, FUNCTION, AND INTERACTION WITH NONO.
RX PubMed=8626664; DOI=10.1074/jbc.271.19.11177;
RA Hallier M., Tavitian A., Moreau-Gachelin F.;
RT "The transcription factor Spi-1/PU.1 binds RNA and interferes with the RNA-
RT binding protein p54nrb.";
RL J. Biol. Chem. 271:11177-11181(1996).
RN [8]
RP INTERACTION WITH GFI1.
RX PubMed=17197705; DOI=10.1074/jbc.m607613200;
RA Dahl R., Iyer S.R., Owens K.S., Cuylear D.D., Simon M.C.;
RT "The transcriptional repressor GFI-1 antagonizes PU.1 activity through
RT protein-protein interaction.";
RL J. Biol. Chem. 282:6473-6483(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 171-259.
RX PubMed=8602247; DOI=10.1038/380456a0;
RA Kodandapani R., Pio F., Ni C.-Z., Piccialli G., Klemsz M., McKercher S.,
RA Maki R.A., Ely K.R.;
RT "A new pattern for helix-turn-helix recognition revealed by the PU.1 ETS-
RT domain-DNA complex.";
RL Nature 380:456-460(1996).
CC -!- FUNCTION: Binds to the PU-box, a purine-rich DNA sequence (5'-GAGGAA-
CC 3') that can act as a lymphoid-specific enhancer. This protein is a
CC transcriptional activator that may be specifically involved in the
CC differentiation or activation of macrophages or B-cells. Also binds RNA
CC and may modulate pre-mRNA splicing. {ECO:0000269|PubMed:8626664}.
CC -!- SUBUNIT: Binds DNA as a monomer. Interacts with RUNX1 and SPIB (By
CC similarity). Interacts with CEBPD and NONO. Interacts with GFI1; the
CC interaction represses SPI1 transcriptional activity. Interacts with
CC CEBPE (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P17947,
CC ECO:0000269|PubMed:17197705, ECO:0000269|PubMed:7594592,
CC ECO:0000269|PubMed:8626664}.
CC -!- INTERACTION:
CC P17433; P70338: Gfi1; NbExp=2; IntAct=EBI-607588, EBI-3954754;
CC P17433; Q99K48: Nono; NbExp=3; IntAct=EBI-607588, EBI-607499;
CC P17433; Q99684: GFI1; Xeno; NbExp=2; IntAct=EBI-607588, EBI-949368;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DISEASE: Note=Involved in murine acute Friend erythroleukemia. It is a
CC target region for SFFV proviral insertion.
CC {ECO:0000269|PubMed:2594367}.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB59699.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA35502.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X17463; CAA35502.1; ALT_INIT; mRNA.
DR EMBL; L03215; AAB59699.1; ALT_INIT; mRNA.
DR EMBL; M32370; AAA40024.1; -; mRNA.
DR EMBL; M38252; AAA40110.1; -; mRNA.
DR EMBL; BC003815; AAH03815.1; -; mRNA.
DR CCDS; CCDS16425.1; -.
DR PIR; A34693; A34693.
DR RefSeq; NP_035485.1; NM_011355.2.
DR PDB; 1PUE; X-ray; 2.10 A; E/F=171-259.
DR PDB; 5W3G; NMR; -; A=167-272.
DR PDBsum; 1PUE; -.
DR PDBsum; 5W3G; -.
DR AlphaFoldDB; P17433; -.
DR SMR; P17433; -.
DR BioGRID; 203184; 16.
DR CORUM; P17433; -.
DR IntAct; P17433; 8.
DR STRING; 10090.ENSMUSP00000002180; -.
DR iPTMnet; P17433; -.
DR PhosphoSitePlus; P17433; -.
DR PaxDb; P17433; -.
DR PeptideAtlas; P17433; -.
DR PRIDE; P17433; -.
DR ProteomicsDB; 257319; -.
DR Antibodypedia; 26734; 556 antibodies from 44 providers.
DR DNASU; 20375; -.
DR Ensembl; ENSMUST00000002180; ENSMUSP00000002180; ENSMUSG00000002111.
DR GeneID; 20375; -.
DR KEGG; mmu:20375; -.
DR UCSC; uc008kuj.1; mouse.
DR CTD; 6688; -.
DR MGI; MGI:98282; Spi1.
DR VEuPathDB; HostDB:ENSMUSG00000002111; -.
DR eggNOG; KOG3805; Eukaryota.
DR GeneTree; ENSGT00940000159754; -.
DR HOGENOM; CLU_066451_0_0_1; -.
DR InParanoid; P17433; -.
DR OMA; SYLPRMY; -.
DR OrthoDB; 1272250at2759; -.
DR PhylomeDB; P17433; -.
DR TreeFam; TF352494; -.
DR BioGRID-ORCS; 20375; 9 hits in 76 CRISPR screens.
DR ChiTaRS; Spi1; mouse.
DR EvolutionaryTrace; P17433; -.
DR PRO; PR:P17433; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P17433; protein.
DR Bgee; ENSMUSG00000002111; Expressed in granulocyte and 148 other tissues.
DR ExpressionAtlas; P17433; baseline and differential.
DR Genevisible; P17433; MM.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0005667; C:transcription regulator complex; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IMP:ARUK-UCL.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:ARUK-UCL.
DR GO; GO:0003677; F:DNA binding; IDA:BHF-UCL.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; ISO:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:ARUK-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:ARUK-UCL.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; ISO:MGI.
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; IPI:ARUK-UCL.
DR GO; GO:0051525; F:NFAT protein binding; IPI:BHF-UCL.
DR GO; GO:0140311; F:protein sequestering activity; IMP:ARUK-UCL.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0097677; F:STAT family protein binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0060033; P:anatomical structure regression; IMP:MGI.
DR GO; GO:1902262; P:apoptotic process involved in blood vessel morphogenesis; IMP:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0002357; P:defense response to tumor cell; ISO:MGI.
DR GO; GO:0098508; P:endothelial to hematopoietic transition; IEP:ARUK-UCL.
DR GO; GO:0030218; P:erythrocyte differentiation; IMP:MGI.
DR GO; GO:0002316; P:follicular B cell differentiation; IGI:ARUK-UCL.
DR GO; GO:0002314; P:germinal center B cell differentiation; IGI:ARUK-UCL.
DR GO; GO:0030851; P:granulocyte differentiation; IDA:MGI.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:MGI.
DR GO; GO:0044027; P:hypermethylation of CpG island; ISO:MGI.
DR GO; GO:0002327; P:immature B cell differentiation; IGI:ARUK-UCL.
DR GO; GO:0070102; P:interleukin-6-mediated signaling pathway; ISO:MGI.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IMP:ARUK-UCL.
DR GO; GO:0030098; P:lymphocyte differentiation; IDA:MGI.
DR GO; GO:0002320; P:lymphoid progenitor cell differentiation; IMP:MGI.
DR GO; GO:0030225; P:macrophage differentiation; IDA:MGI.
DR GO; GO:0043011; P:myeloid dendritic cell differentiation; IMP:MGI.
DR GO; GO:0002573; P:myeloid leukocyte differentiation; IMP:MGI.
DR GO; GO:1904178; P:negative regulation of adipose tissue development; IMP:ARUK-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; ISO:MGI.
DR GO; GO:0090241; P:negative regulation of histone H4 acetylation; ISO:MGI.
DR GO; GO:0045347; P:negative regulation of MHC class II biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0043314; P:negative regulation of neutrophil degranulation; IMP:ARUK-UCL.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0120186; P:negative regulation of protein localization to chromatin; IMP:ARUK-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:ARUK-UCL.
DR GO; GO:0090402; P:oncogene-induced cell senescence; IDA:ARUK-UCL.
DR GO; GO:1904238; P:pericyte cell differentiation; IMP:ARUK-UCL.
DR GO; GO:1905036; P:positive regulation of antifungal innate immune response; IMP:ARUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:1904151; P:positive regulation of microglial cell mediated cytotoxicity; IMP:ARUK-UCL.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IDA:BHF-UCL.
DR GO; GO:2000529; P:positive regulation of myeloid dendritic cell chemotaxis; IMP:ARUK-UCL.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; IDA:ARUK-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0002572; P:pro-T cell differentiation; IMP:ARUK-UCL.
DR GO; GO:0051090; P:regulation of DNA-binding transcription factor activity; IMP:ARUK-UCL.
DR GO; GO:0045646; P:regulation of erythrocyte differentiation; ISO:MGI.
DR GO; GO:1901674; P:regulation of histone H3-K27 acetylation; IDA:ARUK-UCL.
DR GO; GO:1905453; P:regulation of myeloid progenitor cell differentiation; IMP:ARUK-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IDA:MGI.
DR GO; GO:0036462; P:TRAIL-activated apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:ARUK-UCL.
DR GO; GO:0001944; P:vasculature development; IMP:MGI.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000418; Ets_dom.
DR InterPro; IPR046328; ETS_fam.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11849; PTHR11849; 1.
DR Pfam; PF00178; Ets; 1.
DR PRINTS; PR00454; ETSDOMAIN.
DR SMART; SM00413; ETS; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR PROSITE; PS50061; ETS_DOMAIN_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Nucleus; Phosphoprotein;
KW Proto-oncogene; Reference proteome; RNA-binding; Transcription;
KW Transcription regulation.
FT CHAIN 1..272
FT /note="Transcription factor PU.1"
FT /id="PRO_0000204133"
FT DNA_BIND 172..255
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 126..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17947"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:1PUE"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:1PUE"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:1PUE"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:1PUE"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:1PUE"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:1PUE"
FT HELIX 208..219
FT /evidence="ECO:0007829|PDB:1PUE"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:5W3G"
FT HELIX 227..240
FT /evidence="ECO:0007829|PDB:1PUE"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:1PUE"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:1PUE"
FT HELIX 256..260
FT /evidence="ECO:0007829|PDB:5W3G"
SQ SEQUENCE 272 AA; 31349 MW; 765E9CC2F374EB6E CRC64;
MLQACKMEGF SLTAPPSDDL VTYDSELYQR PMHDYYSFVG SDGESHSDHY WDFSAHHVHN
NEFENFPENH FTELQSVQPP QLQQLYRHME LEQMHVLDTP MVPPHTGLSH QVSYMPRMCF
PYQTLSPAHQ QSSDEEEGER QSPPLEVSDG EADGLEPGPG LLHGETGSKK KIRLYQFLLD
LLRSGDMKDS IWWVDKDKGT FQFSSKHKEA LAHRWGIQKG NRKKMTYQKM ARALRNYGKT
GEVKKVKKKL TYQFSGEVLG RGGLAERRLP PH
