Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Transcription factor COE1

Gene

EBF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei163 – 1631Interaction with DNABy similarity
Sitei172 – 1721Interaction with DNABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri151 – 17020C5-typeSequence AnalysisAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_27161. Transcriptional regulation of white adipocyte differentiation.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor COE1
Short name:
O/E-1
Short name:
OE-1
Alternative name(s):
Early B-cell factor
Gene namesi
Name:EBF1
Synonyms:COE1, EBF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:3126. EBF1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162384225.

Polymorphism and mutation databases

BioMutaiEBF1.
DMDMi47117917.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 591591Transcription factor COE1PRO_0000107825Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9UH73.
PaxDbiQ9UH73.
PRIDEiQ9UH73.

PTM databases

PhosphoSiteiQ9UH73.

Expressioni

Gene expression databases

BgeeiQ9UH73.
CleanExiHS_EBF1.
ExpressionAtlasiQ9UH73. baseline and differential.
GenevisibleiQ9UH73. HS.

Interactioni

Subunit structurei

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.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATPAF2Q8N5M13EBI-765426,EBI-1166928
HOMEZQ8IX15-33EBI-765426,EBI-10172004

Protein-protein interaction databases

BioGridi108211. 6 interactions.
IntActiQ9UH73. 3 interactions.
STRINGi9606.ENSP00000322898.

Structurei

Secondary structure

1
591
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi25 – 317Combined sources
Beta strandi36 – 383Combined sources
Helixi39 – 435Combined sources
Turni44 – 463Combined sources
Beta strandi49 – 568Combined sources
Beta strandi60 – 634Combined sources
Beta strandi66 – 7611Combined sources
Beta strandi83 – 9311Combined sources
Helixi95 – 973Combined sources
Helixi99 – 1013Combined sources
Beta strandi108 – 1158Combined sources
Beta strandi121 – 13212Combined sources
Turni133 – 1353Combined sources
Beta strandi152 – 1554Combined sources
Helixi158 – 1603Combined sources
Helixi162 – 1654Combined sources
Turni171 – 1755Combined sources
Beta strandi181 – 1833Combined sources
Turni184 – 1863Combined sources
Beta strandi187 – 1948Combined sources
Beta strandi211 – 2199Combined sources
Beta strandi223 – 2286Combined sources
Beta strandi232 – 2354Combined sources
Beta strandi263 – 2686Combined sources
Beta strandi271 – 2733Combined sources
Beta strandi279 – 2868Combined sources
Beta strandi292 – 2954Combined sources
Beta strandi298 – 3003Combined sources
Beta strandi302 – 3065Combined sources
Beta strandi309 – 3135Combined sources
Beta strandi321 – 3299Combined sources
Beta strandi340 – 3456Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LYRX-ray2.51A10-250[»]
3MQIX-ray2.30A/B/C258-351[»]
ProteinModelPortaliQ9UH73.
SMRiQ9UH73. Positions 35-413.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UH73.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini262 – 34584IPT/TIGAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni63 – 664Interaction with DNABy similarity
Regioni197 – 2048Interaction with DNABy similarity
Regioni236 – 2394Interaction with DNABy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi462 – 55089Pro/Ser/Thr-richAdd
BLAST

Sequence similaritiesi

Belongs to the COE family.Curated
Contains 1 IPT/TIG domain.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri151 – 17020C5-typeSequence AnalysisAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG259050.
GeneTreeiENSGT00390000014051.
HOGENOMiHOG000092311.
HOVERGENiHBG005108.
InParanoidiQ9UH73.
OMAiHAATPCI.
OrthoDBiEOG7J446V.
PhylomeDBiQ9UH73.
TreeFamiTF313391.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR011598. bHLH_dom.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR003523. Transcription_factor_COE.
IPR018350. Transcription_factor_COE_CS.
[Graphical view]
PANTHERiPTHR10747. PTHR10747. 1 hit.
PfamiPF01833. TIG. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
SM00429. IPT. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 1 hit.
PROSITEiPS01345. COE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UH73-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MFGIQESIQR SGSSMKEEPL GSGMNAVRTW MQGAGVLDAN TAAQSGVGLA
60 70 80 90 100
RAHFEKQPPS NLRKSNFFHF VLALYDRQGQ PVEIERTAFV GFVEKEKEAN
110 120 130 140 150
SEKTNNGIHY RLQLLYSNGI RTEQDFYVRL IDSMTKQAIV YEGQDKNPEM
160 170 180 190 200
CRVLLTHEIM CSRCCDKKSC GNRNETPSDP VIIDRFFLKF FLKCNQNCLK
210 220 230 240 250
NAGNPRDMRR FQVVVSTTVN VDGHVLAVSD NMFVHNNSKH GRRARRLDPS
260 270 280 290 300
EGTPSYLEHA TPCIKAISPS EGWTTGGATV IIIGDNFFDG LQVIFGTMLV
310 320 330 340 350
WSELITPHAI RVQTPPRHIP GVVEVTLSYK SKQFCKGTPG RFIYTALNEP
360 370 380 390 400
TIDYGFQRLQ KVIPRHPGDP ERLPKEVILK RAADLVEALY GMPHNNQEII
410 420 430 440 450
LKRAADIAEA LYSVPRNHNQ LPALANTSVH AGMMGVNSFS GQLAVNVSEA
460 470 480 490 500
SQATNQGFTR NSSSVSPHGY VPSTTPQQTN YNSVTTSMNG YGSAAMSNLG
510 520 530 540 550
GSPTFLNGSA ANSPYAIVPS SPTMASSTSL PSNCSSSSGI FSFSPANMVS
560 570 580 590
AVKQKSAFAP VVRPQTSPPP TCTSTNGNSL QAISGMIVPP M
Length:591
Mass (Da):64,464
Last modified:May 10, 2004 - v2
Checksum:iE47797B6FC1E5071
GO
Isoform 2 (identifier: Q9UH73-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     162-184: Missing.
     252-259: Missing.

Note: No experimental confirmation available.
Show »
Length:560
Mass (Da):61,059
Checksum:i5D199E23BDD2E2F6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti112 – 1121L → I in AAF19643 (PubMed:10942392).Curated
Sequence conflicti147 – 1471N → S in AAF19643 (PubMed:10942392).Curated
Sequence conflicti228 – 2292VS → AP in AAF19643 (PubMed:10942392).Curated
Sequence conflicti305 – 3062IT → TG in AAF19643 (PubMed:10942392).Curated
Sequence conflicti309 – 3091A → S in AAF19643 (PubMed:10942392).Curated
Sequence conflicti347 – 3471L → R in AAF19643 (PubMed:10942392).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei162 – 18423Missing in isoform 2. 1 PublicationVSP_012304Add
BLAST
Alternative sequencei252 – 2598Missing in isoform 2. 1 PublicationVSP_012305

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC038805 mRNA. Translation: AAH38805.1.
BC041178 mRNA. Translation: AAH41178.1.
AF208502 mRNA. Translation: AAF19643.1.
CCDSiCCDS4343.1. [Q9UH73-1]
CCDS78081.1. [Q9UH73-2]
RefSeqiNP_076870.1. NM_024007.3. [Q9UH73-1]
NP_874367.1. NM_182708.1. [Q9UH73-2]
UniGeneiHs.573143.

Genome annotation databases

EnsembliENST00000313708; ENSP00000322898; ENSG00000164330.
ENST00000380654; ENSP00000370029; ENSG00000164330. [Q9UH73-2]
GeneIDi1879.
UCSCiuc003lxl.5. human. [Q9UH73-2]
uc010jip.3. human. [Q9UH73-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC038805 mRNA. Translation: AAH38805.1.
BC041178 mRNA. Translation: AAH41178.1.
AF208502 mRNA. Translation: AAF19643.1.
CCDSiCCDS4343.1. [Q9UH73-1]
CCDS78081.1. [Q9UH73-2]
RefSeqiNP_076870.1. NM_024007.3. [Q9UH73-1]
NP_874367.1. NM_182708.1. [Q9UH73-2]
UniGeneiHs.573143.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LYRX-ray2.51A10-250[»]
3MQIX-ray2.30A/B/C258-351[»]
ProteinModelPortaliQ9UH73.
SMRiQ9UH73. Positions 35-413.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108211. 6 interactions.
IntActiQ9UH73. 3 interactions.
STRINGi9606.ENSP00000322898.

PTM databases

PhosphoSiteiQ9UH73.

Polymorphism and mutation databases

BioMutaiEBF1.
DMDMi47117917.

Proteomic databases

MaxQBiQ9UH73.
PaxDbiQ9UH73.
PRIDEiQ9UH73.

Protocols and materials databases

DNASUi1879.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000313708; ENSP00000322898; ENSG00000164330.
ENST00000380654; ENSP00000370029; ENSG00000164330. [Q9UH73-2]
GeneIDi1879.
UCSCiuc003lxl.5. human. [Q9UH73-2]
uc010jip.3. human. [Q9UH73-1]

Organism-specific databases

CTDi1879.
GeneCardsiGC05M158126.
HGNCiHGNC:3126. EBF1.
MIMi164343. gene.
neXtProtiNX_Q9UH73.
PharmGKBiPA162384225.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG259050.
GeneTreeiENSGT00390000014051.
HOGENOMiHOG000092311.
HOVERGENiHBG005108.
InParanoidiQ9UH73.
OMAiHAATPCI.
OrthoDBiEOG7J446V.
PhylomeDBiQ9UH73.
TreeFamiTF313391.

Enzyme and pathway databases

ReactomeiREACT_27161. Transcriptional regulation of white adipocyte differentiation.

Miscellaneous databases

ChiTaRSiEBF1. human.
EvolutionaryTraceiQ9UH73.
GeneWikiiEBF1.
GenomeRNAii1879.
NextBioi7685.
PROiQ9UH73.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UH73.
CleanExiHS_EBF1.
ExpressionAtlasiQ9UH73. baseline and differential.
GenevisibleiQ9UH73. HS.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR011598. bHLH_dom.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR003523. Transcription_factor_COE.
IPR018350. Transcription_factor_COE_CS.
[Graphical view]
PANTHERiPTHR10747. PTHR10747. 1 hit.
PfamiPF01833. TIG. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
SM00429. IPT. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 1 hit.
PROSITEiPS01345. COE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiCOE1_HUMAN
AccessioniPrimary (citable) accession number: Q9UH73
Secondary accession number(s): Q8IW11
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: May 10, 2004
Last modified: July 22, 2015
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.