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Protein

Transcription factor PU.1

Gene

Spi1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi172 – 25584ETSPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • anatomical structure regression Source: MGI
  • apoptotic process involved in patterning of blood vessels Source: MGI
  • erythrocyte differentiation Source: MGI
  • granulocyte differentiation Source: MGI
  • histone H3 acetylation Source: MGI
  • hypermethylation of CpG island Source: MGI
  • lymphocyte differentiation Source: MGI
  • lymphoid progenitor cell differentiation Source: MGI
  • macrophage differentiation Source: MGI
  • myeloid dendritic cell differentiation Source: MGI
  • myeloid leukocyte differentiation Source: MGI
  • negative regulation of gene expression, epigenetic Source: MGI
  • negative regulation of histone H4 acetylation Source: MGI
  • negative regulation of MHC class II biosynthetic process Source: BHF-UCL
  • negative regulation of transcription, DNA-templated Source: MGI
  • negative regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
  • positive regulation of transcription, DNA-templated Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • regulation of erythrocyte differentiation Source: MGI
  • regulation of transcription, DNA-templated Source: MGI
  • regulation of transcription from RNA polymerase II promoter Source: MGI
  • somatic stem cell maintenance Source: MGI
  • transcription from RNA polymerase II promoter Source: GOC
  • vasculature development Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor PU.1
Alternative name(s):
31 kDa-transforming protein
SFFV proviral integration 1 protein
Gene namesi
Name:Spi1
Synonyms:Sfpi-1, Sfpi1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:98282. Spi1.

Subcellular locationi

GO - Cellular componenti

  • nuclear chromatin Source: BHF-UCL
  • nucleus Source: BHF-UCL
  • transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 272272Transcription factor PU.1PRO_0000204133Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei142 – 1421PhosphoserineBy similarity
Modified residuei148 – 1481Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP17433.

PTM databases

PhosphoSiteiP17433.

Expressioni

Gene expression databases

BgeeiP17433.
CleanExiMM_SFPI1.
ExpressionAtlasiP17433. baseline and differential.
GenevisibleiP17433. MM.

Interactioni

Subunit structurei

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.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GFI1Q996842EBI-607588,EBI-949368From a different organism.
Gfi1P703382EBI-607588,EBI-3954754
NonoQ99K483EBI-607588,EBI-607499

Protein-protein interaction databases

BioGridi203184. 16 interactions.
IntActiP17433. 5 interactions.
MINTiMINT-94708.
STRINGi10090.ENSMUSP00000002180.

Structurei

Secondary structure

1
272
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi174 – 18411Combined sources
Turni188 – 1903Combined sources
Beta strandi191 – 1955Combined sources
Turni196 – 1994Combined sources
Beta strandi200 – 2034Combined sources
Turni205 – 2073Combined sources
Helixi208 – 21912Combined sources
Helixi227 – 24014Combined sources
Beta strandi241 – 2455Combined sources
Beta strandi251 – 2544Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PUEX-ray2.10E/F171-259[»]
ProteinModelPortaliP17433.
SMRiP17433. Positions 171-259.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17433.

Family & Domainsi

Sequence similaritiesi

Belongs to the ETS family.Curated
Contains 1 ETS DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG237824.
HOGENOMiHOG000095520.
HOVERGENiHBG002474.
InParanoidiP17433.
KOiK09438.
OMAiPRMCLPY.
PhylomeDBiP17433.
TreeFamiTF352494.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR000418. Ets_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00178. Ets. 1 hit.
[Graphical view]
PRINTSiPR00454. ETSDOMAIN.
SMARTiSM00413. ETS. 1 hit.
[Graphical view]
PROSITEiPS00345. ETS_DOMAIN_1. 1 hit.
PS00346. ETS_DOMAIN_2. 1 hit.
PS50061. ETS_DOMAIN_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P17433-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLQACKMEGF SLTAPPSDDL VTYDSELYQR PMHDYYSFVG SDGESHSDHY
60 70 80 90 100
WDFSAHHVHN NEFENFPENH FTELQSVQPP QLQQLYRHME LEQMHVLDTP
110 120 130 140 150
MVPPHTGLSH QVSYMPRMCF PYQTLSPAHQ QSSDEEEGER QSPPLEVSDG
160 170 180 190 200
EADGLEPGPG LLHGETGSKK KIRLYQFLLD LLRSGDMKDS IWWVDKDKGT
210 220 230 240 250
FQFSSKHKEA LAHRWGIQKG NRKKMTYQKM ARALRNYGKT GEVKKVKKKL
260 270
TYQFSGEVLG RGGLAERRLP PH
Length:272
Mass (Da):31,349
Last modified:February 1, 2005 - v2
Checksum:i765E9CC2F374EB6E
GO

Sequence cautioni

The sequence AAB59699.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA35502.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS16425.1.
PIRiA34693.
RefSeqiNP_035485.1. NM_011355.1.
UniGeneiMm.1302.

Genome annotation databases

EnsembliENSMUST00000002180; ENSMUSP00000002180; ENSMUSG00000002111.
GeneIDi20375.
KEGGimmu:20375.
UCSCiuc008kuj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS16425.1.
PIRiA34693.
RefSeqiNP_035485.1. NM_011355.1.
UniGeneiMm.1302.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PUEX-ray2.10E/F171-259[»]
ProteinModelPortaliP17433.
SMRiP17433. Positions 171-259.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203184. 16 interactions.
IntActiP17433. 5 interactions.
MINTiMINT-94708.
STRINGi10090.ENSMUSP00000002180.

PTM databases

PhosphoSiteiP17433.

Proteomic databases

PRIDEiP17433.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000002180; ENSMUSP00000002180; ENSMUSG00000002111.
GeneIDi20375.
KEGGimmu:20375.
UCSCiuc008kuj.1. mouse.

Organism-specific databases

CTDi6688.
MGIiMGI:98282. Spi1.

Phylogenomic databases

eggNOGiNOG237824.
HOGENOMiHOG000095520.
HOVERGENiHBG002474.
InParanoidiP17433.
KOiK09438.
OMAiPRMCLPY.
PhylomeDBiP17433.
TreeFamiTF352494.

Miscellaneous databases

EvolutionaryTraceiP17433.
NextBioi298282.
PROiP17433.
SOURCEiSearch...

Gene expression databases

BgeeiP17433.
CleanExiMM_SFPI1.
ExpressionAtlasiP17433. baseline and differential.
GenevisibleiP17433. MM.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR000418. Ets_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00178. Ets. 1 hit.
[Graphical view]
PRINTSiPR00454. ETSDOMAIN.
SMARTiSM00413. ETS. 1 hit.
[Graphical view]
PROSITEiPS00345. ETS_DOMAIN_1. 1 hit.
PS00346. ETS_DOMAIN_2. 1 hit.
PS50061. ETS_DOMAIN_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiSPI1_MOUSE
AccessioniPrimary (citable) accession number: P17433
Secondary accession number(s): Q99L57
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: February 1, 2005
Last modified: June 24, 2015
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.