Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P17947 (SPI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor PU.1
Alternative name(s):
31 kDa-transforming protein
Gene names
Name:SPI1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length270 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 By similarity.

Subunit structure

Binds DNA as a monomer. Interacts with CEBPD and NONO By similarity. Interacts with RUNX1 and SPIB. Interacts with GFI1; the interaction represses SPI1 transcriptional activity. Ref.5 Ref.6 Ref.7

Subcellular location

Nucleus Ref.8.

Induction

Highly expressed in both FV-P and FV-A-induced erythro-leukemia cell lines that have undergone rearrangements of the SPI1 gene due to the insertion of SFFV. Negatively regulated by microRNA-155 (miR-155). Ref.8

Sequence similarities

Belongs to the ETS family.

Contains 1 ETS DNA-binding domain.

Sequence caution

The sequence CAA36281.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DiseaseProto-oncogene
   LigandDNA-binding
RNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanatomical structure regression

Inferred from electronic annotation. Source: Ensembl

apoptotic process involved in patterning of blood vessels

Inferred from electronic annotation. Source: Ensembl

erythrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

granulocyte differentiation

Inferred from electronic annotation. Source: Ensembl

histone H3 acetylation

Inferred from mutant phenotype PubMed 20139074. Source: UniProtKB

hypermethylation of CpG island

Inferred from direct assay PubMed 20139074. Source: UniProtKB

lymphocyte differentiation

Inferred from electronic annotation. Source: Ensembl

lymphoid progenitor cell differentiation

Inferred from electronic annotation. Source: Ensembl

macrophage differentiation

Inferred from electronic annotation. Source: Ensembl

myeloid dendritic cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of MHC class II biosynthetic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of gene expression, epigenetic

Inferred from direct assay PubMed 20139074. Source: UniProtKB

negative regulation of histone H4 acetylation

Inferred from mutant phenotype PubMed 20139074. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Traceable author statement PubMed 10867017. Source: ProtInc

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 20139074. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12833137. Source: BHF-UCL

regulation of erythrocyte differentiation

Inferred from mutant phenotype PubMed 12833137. Source: BHF-UCL

regulation of transcription from RNA polymerase II promoter

Inferred from Biological aspect of Ancestor. Source: RefGenome

somatic stem cell maintenance

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Inferred from Biological aspect of Ancestor. Source: GOC

   Cellular_componentnuclear chromatin

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

   Molecular_functionNFAT protein binding

Inferred from sequence or structural similarity. Source: BHF-UCL

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA polymerase II distal enhancer sequence-specific DNA binding

Inferred from sequence or structural similarity. Source: BHF-UCL

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

Inferred from sequence or structural similarity. Source: BHF-UCL

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

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II transcription factor binding

Inferred from sequence or structural similarity. Source: BHF-UCL

core promoter binding

Inferred from direct assay PubMed 20139074. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.6. Source: UniProtKB

sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 12833137. Source: BHF-UCL

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P17947-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P17947-2)

The sequence of this isoform differs from the canonical sequence as follows:
     15-15: P → PQ

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 270270Transcription factor PU.1
PRO_0000204132

Regions

DNA binding170 – 25384ETS

Amino acid modifications

Modified residue1461Phosphoserine By similarity

Natural variations

Alternative sequence151P → PQ in isoform 2.
VSP_038690

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 2005. Version 2.
Checksum: 9592DAA1D85053ED

FASTA27031,083
        10         20         30         40         50         60 
MLQACKMEGF PLVPPPSEDL VPYDTDLYQR QTHEYYPYLS SDGESHSDHY WDFHPHHVHS 

        70         80         90        100        110        120 
EFESFAENNF TELQSVQPPQ LQQLYRHMEL EQMHVLDTPM VPPHPSLGHQ VSYLPRMCLQ 

       130        140        150        160        170        180 
YPSLSPAQPS SDEEEGERQS PPLEVSDGEA DGLEPGPGLL PGETGSKKKI RLYQFLLDLL 

       190        200        210        220        230        240 
RSGDMKDSIW WVDKDKGTFQ FSSKHKEALA HRWGIQKGNR KKMTYQKMAR ALRNYGKTGE 

       250        260        270 
VKKVKKKLTY QFSGEVLGRG GLAERRHPPH 

« Hide

Isoform 2 [UniParc].

Checksum: F69ED4D4C3F77318
Show »

FASTA27131,211

References

« Hide 'large scale' references
[1]"The human homologue of the putative proto-oncogene Spi-1: characterization and expression in tumors."
Ray D., Culine S., Tavitian A., Moreau-Gachelin F.
Oncogene 5:663-668(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]Erratum
Ray D., Culine S., Tavitian A., Moreau-Gachelin F.
Oncogene 5:1611-1612(1990)
Cited for: SEQUENCE REVISION.
[3]"Full-length cDNA libraries and normalization."
Li W.B., Gruber C., Jessee J., Polayes D.
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Fetal liver.
[4]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"SPI-B activates transcription via a unique proline, serine, and threonine domain and exhibits DNA binding affinity differences from PU.1."
Rao S., Matsumura A., Yoon J., Simon M.C.
J. Biol. Chem. 274:11115-11124(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPIB.
[6]"Functional and physical interactions between AML1 proteins and an ETS protein, MEF: implications for the pathogenesis of t(8;21)-positive leukemias."
Mao S., Frank R.C., Zhang J., Miyazaki Y., Nimer S.D.
Mol. Cell. Biol. 19:3635-3644(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RUNX1.
[7]"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.
[8]"BCL6 positively regulates AID and germinal center gene expression via repression of miR-155."
Basso K., Schneider C., Shen Q., Holmes A.B., Setty M., Leslie C., Dalla-Favera R.
J. Exp. Med. 209:2455-2465(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52056 mRNA. Translation: CAA36281.1. Different initiation.
AL532058 mRNA. No translation available.
AC090559 Genomic DNA. No translation available.
AC090582 Genomic DNA. No translation available.
CCDSCCDS44591.1. [P17947-2]
CCDS7933.2. [P17947-1]
PIRS60367.
RefSeqNP_001074016.1. NM_001080547.1. [P17947-2]
NP_003111.2. NM_003120.2. [P17947-1]
UniGeneHs.502511.

3D structure databases

ProteinModelPortalP17947.
SMRP17947. Positions 169-257.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112566. 39 interactions.
DIPDIP-953N.
IntActP17947. 9 interactions.
STRING9606.ENSP00000227163.

PTM databases

PhosphoSiteP17947.

Polymorphism databases

DMDM60415923.

Proteomic databases

PaxDbP17947.
PRIDEP17947.

Protocols and materials databases

DNASU6688.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000227163; ENSP00000227163; ENSG00000066336. [P17947-2]
ENST00000378538; ENSP00000367799; ENSG00000066336. [P17947-1]
GeneID6688.
KEGGhsa:6688.
UCSCuc001nfb.1. human. [P17947-2]
uc001nfc.1. human. [P17947-1]

Organism-specific databases

CTD6688.
GeneCardsGC11M048800.
HGNCHGNC:11241. SPI1.
HPACAB004079.
HPA044653.
MIM165170. gene.
neXtProtNX_P17947.
PharmGKBPA36071.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG237824.
HOGENOMHOG000095520.
HOVERGENHBG002474.
InParanoidP17947.
KOK09438.
OMAPRMCLPY.
OrthoDBEOG78M02J.
PhylomeDBP17947.
TreeFamTF352494.

Enzyme and pathway databases

SignaLinkP17947.

Gene expression databases

ArrayExpressP17947.
BgeeP17947.
CleanExHS_SPI1.
GenevestigatorP17947.

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

GeneWikiSPI1.
GenomeRNAi6688.
NextBio26063.
PROP17947.
SOURCESearch...

Entry information

Entry nameSPI1_HUMAN
AccessionPrimary (citable) accession number: P17947
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: February 1, 2005
Last modified: July 9, 2014
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM