P17947 (SPI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription factor PU.1

Alternative name(s):
31 kDa-transforming protein

Gene names

Name:

SPI1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	270 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
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.
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 process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Disease	Proto-oncogene
Ligand	DNA-binding RNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	anatomical structure regression Inferred from electronic annotation. Source: Compara erythrocyte differentiation Inferred from electronic annotation. Source: Compara granulocyte differentiation Inferred from electronic annotation. Source: Compara histone H3 acetylation Inferred from mutant phenotype PubMed 20139074. Source: UniProtKB hypermethylation of CpG island Inferred from direct assay PubMed 20139074. Source: UniProtKB induction of apoptosis Inferred from electronic annotation. Source: Compara lymphocyte differentiation Inferred from electronic annotation. Source: Compara lymphoid progenitor cell differentiation Inferred from electronic annotation. Source: Compara macrophage differentiation Inferred from electronic annotation. Source: Compara myeloid dendritic cell differentiation Inferred from electronic annotation. Source: Compara negative regulation of MHC class II biosynthetic process Inferred from electronic annotation. Source: Compara 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 positive regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: BHF-UCL regulation of erythrocyte differentiation Inferred from mutant phenotype PubMed 12833137. Source: BHF-UCL somatic stem cell maintenance Inferred from electronic annotation. Source: Compara vasculature development Inferred from electronic annotation. Source: Compara
Cellular_component	nuclear chromatin Inferred from direct assay PubMed 15304486. Source: BHF-UCL
Molecular_function	NFAT 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: Compara 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HOXA10	P31260	2	EBI-2293548,EBI-2293516
PML-RAR	Q15156	20	EBI-2293548,EBI-867256
PRKDC	P78527	2	EBI-2293548,EBI-352053

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 270	270	Transcription factor PU.1		PRO_0000204132
Regions
	DNA binding	170 – 253	84	ETS
Amino acid modifications
	Modified residue	146	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	15	1	P → PQ in isoform 2.		VSP_038690

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 2005. Version 2. Checksum: 9592DAA1D85053ED	FASTA	270	31,083
	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
	Isoform 2 [UniParc]. Checksum: F69ED4D4C3F77318	FASTA	271	31,211
	10 20 30 40 50 60 MLQACKMEGF PLVPPQPSED LVPYDTDLYQ RQTHEYYPYL SSDGESHSDH YWDFHPHHVH 70 80 90 100 110 120 SEFESFAENN FTELQSVQPP QLQQLYRHME LEQMHVLDTP MVPPHPSLGH QVSYLPRMCL 130 140 150 160 170 180 QYPSLSPAQP SSDEEEGERQ SPPLEVSDGE ADGLEPGPGL LPGETGSKKK IRLYQFLLDL 190 200 210 220 230 240 LRSGDMKDSI WWVDKDKGTF QFSSKHKEAL AHRWGIQKGN RKKMTYQKMA RALRNYGKTG 250 260 270 EVKKVKKKLT YQFSGEVLGR GGLAERRHPP H

References

	« Hide 'large scale' referencesShow '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. , 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.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.
IPI	IPI00018333. IPI00827738.
PIR	S60367.
RefSeq	NP_001074016.1. NM_001080547.1. NP_003111.2. NM_003120.2.
UniGene	Hs.502511.
3D structure databases
ProteinModelPortal	P17947.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-953N.
IntAct	P17947. 9 interactions.
STRING	9606.ENSP00000227163.
PTM databases
PhosphoSite	P17947.
Polymorphism databases
DMDM	60415923.
Proteomic databases
PaxDb	P17947.
PRIDE	P17947.
Protocols and materials databases
DNASU	6688.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000227163; ENSP00000227163; ENSG00000066336. ENST00000378538; ENSP00000367799; ENSG00000066336.
GeneID	6688.
KEGG	hsa:6688.
UCSC	uc001nfb.1. human. uc001nfc.1. human.
Organism-specific databases
CTD	6688.
GeneCards	GC11M047430.
HGNC	HGNC:11241. SPI1.
HPA	CAB004079.
MIM	165170. gene.
neXtProt	NX_P17947.
PharmGKB	PA36071.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG237824.
HOGENOM	HOG000095520.
HOVERGEN	HBG002474.
InParanoid	P17947.
KO	K09438.
OMA	PRMCLPY.
OrthoDB	EOG4V9TRC.
Enzyme and pathway databases
Pathway_Interaction_DB	il4_2pathway. IL4-mediated signaling events.
Gene expression databases
ArrayExpress	P17947.
Bgee	P17947.
CleanEx	HS_SPI1.
Genevestigator	P17947.
GermOnline	ENSG00000066336. Homo sapiens.
Family and domain databases
Gene3D	1.10.10.10. 1 hit.
InterPro	IPR000418. Ets_dom. IPR011991. WHTH_DNA-bd_dom. [Graphical view]
Pfam	PF00178. Ets. 1 hit. [Graphical view]
PRINTS	PR00454. ETSDOMAIN.
SMART	SM00413. ETS. 1 hit. [Graphical view]
PROSITE	PS00345. ETS_DOMAIN_1. 1 hit. PS00346. ETS_DOMAIN_2. 1 hit. PS50061. ETS_DOMAIN_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	6688.
NextBio	26063.
SOURCE	Search...

Entry information

Entry name

SPI1_HUMAN

Accession

Primary (citable) accession number: P17947

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	February 1, 2005
Last modified:	May 1, 2013
This is version 139 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.