ID   SPI1_HUMAN              Reviewed;         270 AA.
AC   P17947;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   05-OCT-2010, entry version 112.
DE   RecName: Full=Transcription factor PU.1;
DE   AltName: Full=31 kDa-transforming protein;
GN   Name=SPI1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=90265606; PubMed=1693183;
RA   Ray D., Culine S., Tavitian A., Moreau-Gachelin F.;
RT   "The human homologue of the putative proto-oncogene Spi-1:
RT   characterization and expression in tumors.";
RL   Oncogene 5:663-668(1990).
RN   [2]
RP   ERRATUM, AND SEQUENCE REVISION.
RA   Ray D., Culine S., Tavitian A., Moreau-Gachelin F.;
RL   Oncogene 5:1611-1612(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Fetal liver;
RA   Li W.B., Gruber C., Jessee J., Polayes D.;
RT   "Full-length cDNA libraries and normalization.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA   Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA   FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA   Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA   Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA   Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [5]
RP   INTERACTION WITH SPIB.
RX   MEDLINE=99214189; PubMed=10196196; DOI=10.1074/jbc.274.16.11115;
RA   Rao S., Matsumura A., Yoon J., Simon M.C.;
RT   "SPI-B activates transcription via a unique proline, serine, and
RT   threonine domain and exhibits DNA binding affinity differences from
RT   PU.1.";
RL   J. Biol. Chem. 274:11115-11124(1999).
RN   [6]
RP   INTERACTION WITH RUNX1.
RX   MEDLINE=99223592; PubMed=10207087;
RA   Mao S., Frank R.C., Zhang J., Miyazaki Y., Nimer S.D.;
RT   "Functional and physical interactions between AML1 proteins and an ETS
RT   protein, MEF: implications for the pathogenesis of t(8;21)-positive
RT   leukemias.";
RL   Mol. Cell. Biol. 19:3635-3644(1999).
CC   -!- FUNCTION: Binds to the PU-box, a purine-rich DNA sequence (5'-
CC       GAGGAA-3') that can act as a lymphoid-specific enhancer. This
CC       protein is a transcriptional activator that may be specifically
CC       involved in the differentiation or activation of macrophages or B-
CC       cells. Also binds RNA and may modulate pre-mRNA splicing (By
CC       similarity).
CC   -!- SUBUNIT: Binds DNA as a monomer. Interacts with RUNX1 and SPIB.
CC       Interacts with CEBPD and NONO (By similarity).
CC   -!- INTERACTION:
CC       P31260:HOXA10; NbExp=2; IntAct=EBI-2293548, EBI-2293516;
CC       Q15156:PML-RAR; NbExp=2; IntAct=EBI-2293548, EBI-867256;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P17947-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P17947-2; Sequence=VSP_038690;
CC   -!- INDUCTION: Highly expressed in both FV-P and FV-A-induced erythro-
CC       leukemia cell lines that have undergone rearrangements of the Spi-
CC       1 gene due to the insertion of SFFV.
CC   -!- SIMILARITY: Belongs to the ETS family.
CC   -!- SIMILARITY: Contains 1 ETS DNA-binding domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA36281.1; Type=Erroneous initiation;
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/SPI1ID269.html";
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DR   EMBL; X52056; CAA36281.1; ALT_INIT; mRNA.
DR   EMBL; AL532058; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC090559; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC090582; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00018333; -.
DR   IPI; IPI00827738; -.
DR   PIR; S60367; S60367.
DR   RefSeq; NP_001074016.1; -.
DR   RefSeq; NP_003111.2; -.
DR   UniGene; Hs.502511; -.
DR   ProteinModelPortal; P17947; -.
DR   SMR; P17947; 169-257.
DR   DIP; DIP-953N; -.
DR   IntAct; P17947; 30.
DR   STRING; P17947; -.
DR   PhosphoSite; P17947; -.
DR   PRIDE; P17947; -.
DR   Ensembl; ENST00000378538; ENSP00000367799; ENSG00000066336.
DR   GeneID; 6688; -.
DR   UCSC; uc001nfb.1; human.
DR   CTD; 6688; -.
DR   GeneCards; GC11M047332; -.
DR   H-InvDB; HIX0035922; -.
DR   HGNC; HGNC:11241; SPI1.
DR   HPA; CAB004079; -.
DR   MIM; 165170; gene.
DR   PharmGKB; PA36071; -.
DR   eggNOG; prNOG05218; -.
DR   HOVERGEN; HBG002474; -.
DR   InParanoid; P17947; -.
DR   OMA; PRMCLPY; -.
DR   Pathway_Interaction_DB; il4_2pathway; IL4-mediated signaling events.
DR   NextBio; 26063; -.
DR   ArrayExpress; P17947; -.
DR   Bgee; P17947; -.
DR   CleanEx; HS_SPI1; -.
DR   Genevestigator; P17947; -.
DR   GermOnline; ENSG00000066336; Homo sapiens.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:transcription factor activity; IDA:BHF-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription from R...; TAS:ProtInc.
DR   GO; GO:0043193; P:positive regulation of gene-specific transc...; IDA:BHF-UCL.
DR   GO; GO:0045646; P:regulation of erythrocyte differentiation; IMP:BHF-UCL.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR000418; Ets.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF00178; Ets; 1.
DR   PRINTS; PR00454; ETSDOMAIN.
DR   SMART; SM00413; ETS; 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   Activator; Alternative splicing; Complete proteome; DNA-binding;
KW   Nucleus; Phosphoprotein; Proto-oncogene; RNA-binding; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    270       Transcription factor PU.1.
FT                                /FTId=PRO_0000204132.
FT   DNA_BIND    170    253       ETS.
FT   MOD_RES     146    146       Phosphoserine (By similarity).
FT   VAR_SEQ      15     15       P -> PQ (in isoform 2).
FT                                /FTId=VSP_038690.
SQ   SEQUENCE   270 AA;  31083 MW;  9592DAA1D85053ED CRC64;
     MLQACKMEGF PLVPPPSEDL VPYDTDLYQR QTHEYYPYLS SDGESHSDHY WDFHPHHVHS
     EFESFAENNF TELQSVQPPQ LQQLYRHMEL EQMHVLDTPM VPPHPSLGHQ VSYLPRMCLQ
     YPSLSPAQPS SDEEEGERQS PPLEVSDGEA DGLEPGPGLL PGETGSKKKI RLYQFLLDLL
     RSGDMKDSIW WVDKDKGTFQ FSSKHKEALA HRWGIQKGNR KKMTYQKMAR ALRNYGKTGE
     VKKVKKKLTY QFSGEVLGRG GLAERRHPPH
//