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Q99607 (ELF4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ETS-related transcription factor Elf-4
Alternative name(s):
E74-like factor 4
Myeloid Elf-1-like factor
Gene names
Name:ELF4
Synonyms:ELFR, MEF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length663 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional activator that binds to DNA sequences containing the consensus 5'-WGGA-3'. Transactivates promoters of the hematopoietic growth factor genes CSF2, IL3, IL8, and of the bovine lysozyme gene. Acts synergistically with RUNX1 to transactivate the IL3 promoter By similarity. Also transactivates the PRF1 promoter in natural killer (NK) cells. Plays a role in the development and function of NK and NK T-cells and in innate immunity. Controls the proliferation and homing of CD8+ T-cells via the Kruppel-like factors KLF4 and KLF2 By similarity. Controls cell senescence in a p53-dependent manner. Can also promote cellular transformation through inhibition of the p16 pathway. Ref.1 Ref.2 Ref.6 Ref.7 Ref.8 Ref.11 UniProtKB Q9Z2U4

Subunit structure

Interacts with RUNX1 (via the Runt domain); the interaction transactivates the IL3 promoter. Interacts (via its C-terminus) with PML; the interaction translocates ELF4 to PML nuclear bodies and enhances transactivation of LYZ. Ref.6 Ref.8

Subcellular location

NucleusPML body. Note: Accumulation into PML nuclear bodies is mediated by PML. Ref.8

Tissue specificity

Abundantly expressed in the placenta and in a variety of myeloid leukemia cell lines. Moderate levels of expression in heart, lung, spleen, thymus, peripheral blood lymphocytes, ovary and colon. Lower levels of expression in Jurkat T-cells and other T-cell lines and no expression in brain. Ref.1 Ref.2

Induction

By ponisterone A in erythroleukemia cells. Ref.7

Involvement in disease

A chromosomal aberration involving ELF4 has been found in a case of acute myeloid leukemia (AML). Translocation t(X;21)(q25-26;q22) with ERG.

Sequence similarities

Belongs to the ETS family.

Contains 1 ETS DNA-binding domain.

Sequence caution

The sequence AAC17452.1 differs from that shown. Reason: Frameshift at positions 334 and 412.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 663663ETS-related transcription factor Elf-4
PRO_0000204089

Regions

DNA binding209 – 29183ETS
Region87 – 206120RUNX1-binding Ref.6

Sites

Site25 – 262Breakpoint for translocation to form ELF4-ERG oncogene

Amino acid modifications

Modified residue1511Phosphoserine Ref.10
Modified residue6481Phosphoserine Ref.10 Ref.12 Ref.13

Experimental info

Sequence conflict293 – 2942MP → IA in AAC17452. Ref.2
Sequence conflict4991P → L in AAC17452. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q99607 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 1696085D31B09BC5

FASTA66370,730
        10         20         30         40         50         60 
MAITLQPSDL IFEFASNGMD DDIHQLEDPS VFPAVIVEQV PYPDLLHLYS GLELDDVHNG 

        70         80         90        100        110        120 
IITDGTLCMT QDQILEGSFL LTDDNEATSH TMSTAEVLLN MESPSDILDE KQIFSTSEML 

       130        140        150        160        170        180 
PDSDPAPAVT LPNYLFPASE PDALNRAGDT SDQEGHSLEE KASREESAKK TGKSKKRIRK 

       190        200        210        220        230        240 
TKGNRSTSPV TDPSIPIRKK SKDGKGSTIY LWEFLLALLQ DRNTCPKYIK WTQREKGIFK 

       250        260        270        280        290        300 
LVDSKAVSKL WGKQKNKPDM NYETMGRALR YYYQRGILAK VEGQRLVYQF KEMPKDLVVI 

       310        320        330        340        350        360 
EDEDESSEAT AAPPQASTAS VASASTTRRT SSRVSSRSAP QGKGSSSWEK PKIQHVGLQP 

       370        380        390        400        410        420 
SASLELGPSL DEEIPTTSTM LVSPAEGQVK LTKAVSASSV PSNIHLGVAP VGSGSALTLQ 

       430        440        450        460        470        480 
TIPLTTVLTN GPPASTTAPT QLVLQSVPAA STFKDTFTLQ ASFPLNASFQ DSQVAAPGAP 

       490        500        510        520        530        540 
LILSGLPQLL AGANRPTNPA PPTVTGAGPA GPSSQPPGTV IAAFIRTSGT TAAPRVKEGP 

       550        560        570        580        590        600 
LRSSSYVQGM VTGAPMEGLL VPEETLRELL RDQAHLQPLP TQVVSRGSHN PSLLGNQTLS 

       610        620        630        640        650        660 
PPSRPTVGLT PVAELELSSG SGSLLMAEPS VTTSGSLLTR SPTPAPFSPF NPTSLIKMEP 


HDI 

« Hide

References

« Hide 'large scale' references
[1]"MEF, a novel transcription factor with an Elf-1 like DNA binding domain but distinct transcriptional activating properties."
Miyazaki Y., Sun X., Uchida H., Zhang J., Nimer S.
Oncogene 13:1721-1729(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Tissue: Promyelocytic leukemia.
[2]"Cloning of a novel human ELF-1-related ETS transcription factor, ELFR, its characterization and chromosomal assignment relative to ELF-1."
Aryee D.N.T., Petermann R., Kos K., Henn T., Haas O.A., Kovar H.
Gene 210:71-78(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Tissue: Ewing sarcoma.
[3]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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].
Tissue: Placenta.
[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: FUNCTION, INTERACTION WITH RUNX1.
[7]"Myeloid ELF1-like factor is a potent activator of interleukin-8 expression in hematopoietic cells."
Hedvat C.V., Yao J., Sokolic R.A., Nimer S.D.
J. Biol. Chem. 279:6395-6400(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[8]"Myeloid Elf-1-like factor, an ETS transcription factor, up-regulates lysozyme transcription in epithelial cells through interaction with promyelocytic leukemia protein."
Suico M.A., Yoshida H., Seki Y., Uchikawa T., Lu Z., Shuto T., Matsuzaki K., Nakao M., Li J.-D., Kai H.
J. Biol. Chem. 279:19091-19098(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PML.
[9]"ELF4 is fused to ERG in a case of acute myeloid leukemia with a t(X;21)(q25-26;q22)."
Moore S.D., Offor O., Ferry J.A., Amrein P.C., Morton C.C., Dal Cin P.
Leuk. Res. 30:1037-1042(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH ERG.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151 AND SER-648, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"ELF4/MEF activates MDM2 expression and blocks oncogene-induced p16 activation to promote transformation."
Sashida G., Liu Y., Elf S., Miyata Y., Ohyashiki K., Izumi M., Menendez S., Nimer S.D.
Mol. Cell. Biol. 29:3687-3699(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-648, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-648, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U32645 mRNA. Translation: AAB53693.1.
AF000670 mRNA. Translation: AAC17452.1. Frameshift.
AL136450, Z81363 Genomic DNA. Translation: CAI42882.1.
Z81363, AL136450 Genomic DNA. Translation: CAI42371.1.
CH471107 Genomic DNA. Translation: EAX11813.1.
CH471107 Genomic DNA. Translation: EAX11814.1.
BC017194 mRNA. Translation: AAH17194.1.
CCDSCCDS14617.1.
RefSeqNP_001120669.1. NM_001127197.1.
NP_001412.1. NM_001421.3.
XP_005262446.1. XM_005262389.1.
UniGeneHs.271940.

3D structure databases

ProteinModelPortalQ99607.
SMRQ99607. Positions 209-290.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108315. 11 interactions.
IntActQ99607. 4 interactions.
STRING9606.ENSP00000311280.

PTM databases

PhosphoSiteQ99607.

Polymorphism databases

DMDM68052244.

Proteomic databases

MaxQBQ99607.
PaxDbQ99607.
PRIDEQ99607.

Protocols and materials databases

DNASU2000.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308167; ENSP00000311280; ENSG00000102034.
ENST00000335997; ENSP00000338608; ENSG00000102034.
GeneID2000.
KEGGhsa:2000.
UCSCuc004evd.4. human.

Organism-specific databases

CTD2000.
GeneCardsGC0XM129198.
HGNCHGNC:3319. ELF4.
HPAHPA058595.
MIM300775. gene.
neXtProtNX_Q99607.
Orphanet632. Short stature due to isolated growth hormone deficiency with X-linked hypogammaglobulinemia.
PharmGKBPA27747.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG291231.
HOGENOMHOG000049253.
HOVERGENHBG007183.
InParanoidQ99607.
KOK09428.
OMAYLFPVSE.
OrthoDBEOG73RBD1.
PhylomeDBQ99607.
TreeFamTF318679.

Gene expression databases

ArrayExpressQ99607.
BgeeQ99607.
CleanExHS_ELF4.
GenevestigatorQ99607.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR000418. Ets_dom.
IPR022084. TF_Elf_N.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF12310. Elf-1_N. 1 hit.
PF00178. 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

GeneWikiELF4.
GenomeRNAi2000.
NextBio8091.
PROQ99607.
SOURCESearch...

Entry information

Entry nameELF4_HUMAN
AccessionPrimary (citable) accession number: Q99607
Secondary accession number(s): D3DTG1, O60435
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 126 of the entry and version 1 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 X

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