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P17433 (SPI1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor PU.1
Alternative name(s):
31 kDa-transforming protein
SFFV proviral integration 1 protein
Gene names
Name:Spi1
Synonyms:Sfpi-1, Sfpi1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length272 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to the PU-box, a purine-rich DNA sequence (5'-GAGGAA-3') that can act as a lymphoid-specific enhancer. This protein is a transcriptional activator that may be specifically involved in the differentiation or activation of macrophages or B-cells. Also binds RNA and may modulate pre-mRNA splicing. Ref.7

Subunit structure

Binds DNA as a monomer. Interacts with RUNX1 and SPIB By similarity. Interacts with CEBPD and NONO. Interacts with GFI1; the interaction represses SPI1 transcriptional activity. Ref.6 Ref.7 Ref.8

Subcellular location

Nucleus.

Involvement in disease

Involved in murine acute Friend erythroleukemia. It is a target region for SFFV proviral insertion.

Sequence similarities

Belongs to the ETS family.

Contains 1 ETS DNA-binding domain.

Sequence caution

The sequence AAB59699.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAA35502.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DiseaseProto-oncogene
   LigandDNA-binding
RNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanatomical structure regression

Inferred from mutant phenotype PubMed 16163358. Source: MGI

apoptotic process involved in patterning of blood vessels

Inferred from mutant phenotype PubMed 16163358. Source: MGI

erythrocyte differentiation

Inferred from mutant phenotype PubMed 9133423. Source: MGI

granulocyte differentiation

Inferred from direct assay PubMed 11980719. Source: MGI

histone H3 acetylation

Inferred from electronic annotation. Source: Ensembl

hypermethylation of CpG island

Inferred from electronic annotation. Source: Ensembl

lymphocyte differentiation

Inferred from direct assay PubMed 11980719. Source: MGI

lymphoid progenitor cell differentiation

Inferred from mutant phenotype PubMed 9133423. Source: MGI

macrophage differentiation

Inferred from direct assay PubMed 11980719. Source: MGI

myeloid dendritic cell differentiation

Inferred from mutant phenotype PubMed 10648399. Source: MGI

myeloid leukocyte differentiation

Inferred from mutant phenotype PubMed 9133423. Source: MGI

negative regulation of MHC class II biosynthetic process

Inferred from direct assay PubMed 7592651. Source: BHF-UCL

negative regulation of gene expression, epigenetic

Inferred from electronic annotation. Source: Ensembl

negative regulation of histone H4 acetylation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 15304486. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15100295. Source: MGI

regulation of erythrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 19796622. Source: MGI

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 11980719PubMed 14962908. Source: MGI

somatic stem cell maintenance

Inferred from direct assay PubMed 19379700. Source: MGI

transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 15304486. Source: GOC

vasculature development

Inferred from mutant phenotype PubMed 16163358. Source: MGI

   Cellular_componentnuclear chromatin

Inferred from direct assay PubMed 15187136. Source: BHF-UCL

nucleus

Inferred from direct assay PubMed 15304486. Source: BHF-UCL

transcription factor complex

Inferred by curator PubMed 11980719. Source: MGI

   Molecular_functionDNA binding

Inferred from physical interaction PubMed 7592651. Source: BHF-UCL

NFAT protein binding

Inferred from physical interaction PubMed 15304486. Source: BHF-UCL

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA polymerase II distal enhancer sequence-specific DNA binding

Inferred from direct assay PubMed 15304486. Source: BHF-UCL

RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 15304486. Source: BHF-UCL

RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from direct assay PubMed 15304486. Source: BHF-UCL

RNA polymerase II transcription factor binding

Inferred from physical interaction PubMed 15304486PubMed 18063754. Source: BHF-UCL

core promoter binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding

Inferred from direct assay PubMed 1409581. Source: MGI

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 11980719PubMed 14962908. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GFI1Q996842EBI-607588,EBI-949368From a different organism.
Gfi1P703382EBI-607588,EBI-3954754
NonoQ99K483EBI-607588,EBI-607499

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 272272Transcription factor PU.1
PRO_0000204133

Regions

DNA binding172 – 25584ETS

Amino acid modifications

Modified residue1481Phosphoserine Ref.9

Secondary structure

................ 272
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17433 [UniParc].

Last modified February 1, 2005. Version 2.
Checksum: 765E9CC2F374EB6E

FASTA27231,349
        10         20         30         40         50         60 
MLQACKMEGF SLTAPPSDDL VTYDSELYQR PMHDYYSFVG SDGESHSDHY WDFSAHHVHN 

        70         80         90        100        110        120 
NEFENFPENH FTELQSVQPP QLQQLYRHME LEQMHVLDTP MVPPHTGLSH QVSYMPRMCF 

       130        140        150        160        170        180 
PYQTLSPAHQ QSSDEEEGER QSPPLEVSDG EADGLEPGPG LLHGETGSKK KIRLYQFLLD 

       190        200        210        220        230        240 
LLRSGDMKDS IWWVDKDKGT FQFSSKHKEA LAHRWGIQKG NRKKMTYQKM ARALRNYGKT 

       250        260        270 
GEVKKVKKKL TYQFSGEVLG RGGLAERRLP PH 

« Hide

References

« Hide 'large scale' references
[1]"The putative oncogene Spi-1: murine chromosomal localization and transcriptional activation in murine acute erythroleukemias."
Moreau-Gachelin F., Ray D., Mattei M.-G., Tambourin P., Tavitian A.
Oncogene 4:1449-1456(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ICFW.
[2]Erratum
Moreau-Gachelin F., Ray D., Mattei M.-G., Tambourin P., Tavitian A.
Oncogene 5:941-941(1990)
Cited for: SEQUENCE REVISION.
[3]"The macrophage and B cell-specific transcription factor PU.1 is related to the ets oncogene."
Klemsz M.J., McKercher S.R., Celada A., van Beveren C., Maki R.A.
Cell 61:113-124(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"The Sfpi-1 proviral integration site of Friend erythroleukemia encodes the ets-related transcription factor Pu.1."
Paul R., Schuetze S., Kozak S.L., Kozak C.A., Kabat D.
J. Virol. 65:464-467(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary tumor.
[6]"Multiple proteins physically interact with PU.1. Transcriptional synergy with NF-IL6 beta (C/EBP delta, CRP3)."
Nagulapalli S., Pongubala J.M., Atchison M.L.
J. Immunol. 155:4330-4338(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CEBPD.
[7]"The transcription factor Spi-1/PU.1 binds RNA and interferes with the RNA-binding protein p54nrb."
Hallier M., Tavitian A., Moreau-Gachelin F.
J. Biol. Chem. 271:11177-11181(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA-BINDING, FUNCTION, INTERACTION WITH NONO.
[8]"The transcriptional repressor GFI-1 antagonizes PU.1 activity through protein-protein interaction."
Dahl R., Iyer S.R., Owens K.S., Cuylear D.D., Simon M.C.
J. Biol. Chem. 282:6473-6483(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GFI1.
[9]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"A new pattern for helix-turn-helix recognition revealed by the PU.1 ETS-domain-DNA complex."
Kodandapani R., Pio F., Ni C.-Z., Piccialli G., Klemsz M., McKercher S., Maki R.A., Ely K.R.
Nature 380:456-460(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 171-259.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X17463 mRNA. Translation: CAA35502.1. Different initiation.
L03215 mRNA. Translation: AAB59699.1. Different initiation.
M32370 mRNA. Translation: AAA40024.1.
M38252 mRNA. Translation: AAA40110.1.
BC003815 mRNA. Translation: AAH03815.1.
PIRA34693.
RefSeqNP_035485.1. NM_011355.1.
UniGeneMm.1302.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PUEX-ray2.10E/F171-259[»]
ProteinModelPortalP17433.
SMRP17433. Positions 171-259.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203184. 14 interactions.
IntActP17433. 5 interactions.
MINTMINT-94708.

PTM databases

PhosphoSiteP17433.

Proteomic databases

PRIDEP17433.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000002180; ENSMUSP00000002180; ENSMUSG00000002111.
GeneID20375.
KEGGmmu:20375.
UCSCuc008kuj.1. mouse.

Organism-specific databases

CTD6688.
MGIMGI:98282. Spi1.

Phylogenomic databases

eggNOGNOG237824.
HOGENOMHOG000095520.
HOVERGENHBG002474.
InParanoidP17433.
KOK09438.
OMAPRMCLPY.
PhylomeDBP17433.
TreeFamTF352494.

Gene expression databases

ArrayExpressP17433.
BgeeP17433.
CleanExMM_SFPI1.
GenevestigatorP17433.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR000418. Ets_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00178. Ets. 1 hit.
[Graphical view]
PRINTSPR00454. ETSDOMAIN.
SMARTSM00413. ETS. 1 hit.
[Graphical view]
PROSITEPS00345. ETS_DOMAIN_1. 1 hit.
PS00346. ETS_DOMAIN_2. 1 hit.
PS50061. ETS_DOMAIN_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP17433.
NextBio298282.
PROP17433.
SOURCESearch...

Entry information

Entry nameSPI1_MOUSE
AccessionPrimary (citable) accession number: P17433
Secondary accession number(s): Q99L57
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: February 1, 2005
Last modified: April 16, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot