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Q9UH73 (COE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor COE1

Short name=O/E-1
Short name=OE-1
Alternative name(s):
Early B-cell factor
Gene names
Name:EBF1
Synonyms:COE1, EBF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length591 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional activator which recognizes variations of the palindromic sequence 5'-ATTCCCNNGGGAATT-3' By similarity.

Subunit structure

Forms either a homodimer or a heterodimer with a related family member By similarity. Interacts with ZNF423 and ZNF521, leading to prevent EBF1 to bind DNA and activate target genes. Ref.3

Subcellular location

Nucleus Potential.

Sequence similarities

Belongs to the COE family.

Contains 1 IPT/TIG domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UH73-1)

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: Q9UH73-2)

The sequence of this isoform differs from the canonical sequence as follows:
     162-184: Missing.
     252-259: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 591591Transcription factor COE1
PRO_0000107825

Regions

Domain262 – 34584IPT/TIG
Zinc finger151 – 17020C5-type Potential
Region63 – 664Interaction with DNA By similarity
Region197 – 2048Interaction with DNA By similarity
Region236 – 2394Interaction with DNA By similarity
Compositional bias462 – 55089Pro/Ser/Thr-rich

Sites

Site1631Interaction with DNA By similarity
Site1721Interaction with DNA By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.4

Natural variations

Alternative sequence162 – 18423Missing in isoform 2.
VSP_012304
Alternative sequence252 – 2598Missing in isoform 2.
VSP_012305

Experimental info

Sequence conflict1121L → I in AAF19643. Ref.2
Sequence conflict1471N → S in AAF19643. Ref.2
Sequence conflict228 – 2292VS → AP in AAF19643. Ref.2
Sequence conflict305 – 3062IT → TG in AAF19643. Ref.2
Sequence conflict3091A → S in AAF19643. Ref.2
Sequence conflict3471L → R in AAF19643. Ref.2

Secondary structure

............................................................ 591
Helix Strand Turn

Details...

Sequences

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

Last modified May 10, 2004. Version 2.
Checksum: E47797B6FC1E5071

FASTA59164,464
        10         20         30         40         50         60 
MFGIQESIQR SGSSMKEEPL GSGMNAVRTW MQGAGVLDAN TAAQSGVGLA RAHFEKQPPS 

        70         80         90        100        110        120 
NLRKSNFFHF VLALYDRQGQ PVEIERTAFV GFVEKEKEAN SEKTNNGIHY RLQLLYSNGI 

       130        140        150        160        170        180 
RTEQDFYVRL IDSMTKQAIV YEGQDKNPEM CRVLLTHEIM CSRCCDKKSC GNRNETPSDP 

       190        200        210        220        230        240 
VIIDRFFLKF FLKCNQNCLK NAGNPRDMRR FQVVVSTTVN VDGHVLAVSD NMFVHNNSKH 

       250        260        270        280        290        300 
GRRARRLDPS EGTPSYLEHA TPCIKAISPS EGWTTGGATV IIIGDNFFDG LQVIFGTMLV 

       310        320        330        340        350        360 
WSELITPHAI RVQTPPRHIP GVVEVTLSYK SKQFCKGTPG RFIYTALNEP TIDYGFQRLQ 

       370        380        390        400        410        420 
KVIPRHPGDP ERLPKEVILK RAADLVEALY GMPHNNQEII LKRAADIAEA LYSVPRNHNQ 

       430        440        450        460        470        480 
LPALANTSVH AGMMGVNSFS GQLAVNVSEA SQATNQGFTR NSSSVSPHGY VPSTTPQQTN 

       490        500        510        520        530        540 
YNSVTTSMNG YGSAAMSNLG GSPTFLNGSA ANSPYAIVPS SPTMASSTSL PSNCSSSSGI 

       550        560        570        580        590 
FSFSPANMVS AVKQKSAFAP VVRPQTSPPP TCTSTNGNSL QAISGMIVPP M 

« Hide

Isoform 2 [UniParc].

Checksum: 5D199E23BDD2E2F6
Show »

FASTA56061,059

References

« Hide 'large scale' references
[1]"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] (ISOFORMS 1 AND 2).
Tissue: Testis.
[2]"Cloning of human early B-cell factor and identification of target genes suggest a conserved role in B-cell development in man and mouse."
Gisler R., Jacobsen S.E., Sigvardsson M.
Blood 96:1457-1464(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-591 (ISOFORM 1).
[3]"Early hematopoietic zinc finger protein (EHZF), the human homolog to mouse Evi3, is highly expressed in primitive human hematopoietic cells."
Bond H.M., Mesuraca M., Carbone E., Bonelli P., Agosti V., Amodio N., De Rosa G., Di Nicola M., Gianni A.M., Moore M.A., Hata A., Grieco M., Morrone G., Venuta S.
Blood 103:2062-2070(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZNF521.
[4]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[5]"Structural determination of functional domains in early B-cell factor (EBF) family of transcription factors reveals similarities to Rel DNA-binding proteins and a novel dimerization motif."
Siponen M.I., Wisniewska M., Lehtio L., Johansson I., Svensson L., Raszewski G., Nilsson L., Sigvardsson M., Berglund H.
J. Biol. Chem. 285:25875-25879(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 10-351 IN COMPLEX WITH ZINC IONS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC038805 mRNA. Translation: AAH38805.1.
BC041178 mRNA. Translation: AAH41178.1.
AF208502 mRNA. Translation: AAF19643.1.
CCDSCCDS4343.1. [Q9UH73-1]
RefSeqNP_076870.1. NM_024007.3. [Q9UH73-1]
NP_874367.1. NM_182708.1. [Q9UH73-2]
UniGeneHs.573143.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LYRX-ray2.51A10-250[»]
3MQIX-ray2.30A/B/C258-351[»]
ProteinModelPortalQ9UH73.
SMRQ9UH73. Positions 35-413.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108211. 4 interactions.
IntActQ9UH73. 1 interaction.
STRING9606.ENSP00000322898.

PTM databases

PhosphoSiteQ9UH73.

Polymorphism databases

DMDM47117917.

Proteomic databases

MaxQBQ9UH73.
PaxDbQ9UH73.
PRIDEQ9UH73.

Protocols and materials databases

DNASU1879.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000313708; ENSP00000322898; ENSG00000164330. [Q9UH73-1]
ENST00000380654; ENSP00000370029; ENSG00000164330. [Q9UH73-2]
GeneID1879.
KEGGhsa:1879.
UCSCuc003lxl.5. human. [Q9UH73-2]
uc010jip.3. human. [Q9UH73-1]

Organism-specific databases

CTD1879.
GeneCardsGC05M158123.
HGNCHGNC:3126. EBF1.
MIM164343. gene.
neXtProtNX_Q9UH73.
PharmGKBPA162384225.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG259050.
HOGENOMHOG000092311.
HOVERGENHBG005108.
InParanoidQ9UH73.
KOK09103.
OMAHAATPCI.
OrthoDBEOG7J446V.
PhylomeDBQ9UH73.
TreeFamTF313391.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.

Gene expression databases

ArrayExpressQ9UH73.
BgeeQ9UH73.
CleanExHS_EBF1.
GenevestigatorQ9UH73.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
InterProIPR011598. bHLH_dom.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR003523. Transcription_factor_COE.
IPR018350. Transcription_factor_COE_CS.
[Graphical view]
PANTHERPTHR10747. PTHR10747. 1 hit.
PfamPF01833. TIG. 1 hit.
[Graphical view]
SMARTSM00353. HLH. 1 hit.
SM00429. IPT. 1 hit.
[Graphical view]
SUPFAMSSF81296. SSF81296. 1 hit.
PROSITEPS01345. COE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEBF1. human.
EvolutionaryTraceQ9UH73.
GeneWikiEBF1.
GenomeRNAi1879.
NextBio7685.
PROQ9UH73.
SOURCESearch...

Entry information

Entry nameCOE1_HUMAN
AccessionPrimary (citable) accession number: Q9UH73
Secondary accession number(s): Q8IW11
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: May 10, 2004
Last modified: July 9, 2014
This is version 119 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM