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Protein

Transcription factor COE2

Gene

Ebf2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcription factor that, in osteoblasts, activates the decoy receptor for RANKL, TNFRSF11B, which in turn regulates osteoclast differentiation. Acts in synergy with the Wnt-responsive LEF1/CTNNB1 pathway. Recognizes variations of the palindromic sequence 5'-ATTCCCNNGGGAATT-3'.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri150 – 16920C5-typeSequence analysisAdd
BLAST

GO - Molecular functioni

  • chromatin binding Source: MGI
  • DNA binding Source: MGI
  • metal ion binding Source: UniProtKB-KW
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: NTNU_SB

GO - Biological processi

  • adipose tissue development Source: MGI
  • brown fat cell differentiation Source: MGI
  • cell fate determination Source: MGI
  • positive regulation of chromatin binding Source: MGI
  • positive regulation of transcription, DNA-templated Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor COE2
Alternative name(s):
Early B-cell factor 2
Short name:
EBF-2
Metencephalon-mesencephalon-olfactory transcription factor 1
Short name:
MET-mesencephalon-olfactory TF1
Short name:
MET-mesencephalon-olfactory transcription factor 1
Olf-1/EBF-like 3
Short name:
O/E-3
Short name:
OE-3
Gene namesi
Name:Ebf2
Synonyms:Coe2, Mmot1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:894332. Ebf2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 575575Transcription factor COE2PRO_0000107829Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Cross-linki15 – 15Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki15 – 15Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiO08792.
PaxDbiO08792.
PeptideAtlasiO08792.
PRIDEiO08792.

PTM databases

iPTMnetiO08792.
PhosphoSiteiO08792.

Expressioni

Tissue specificityi

In adult expressed in olfactory epithelium and at a much lower level in Purkinje cells of the cerebellum. In embryo expressed in epithalamus, in cells near the ventricular zone of mesencephalon and on the ventral surface of rhombencephalon, in the developing vomeronasal organ, at a lower level in developing spinal cord. Not expressed in developing retina, inner ear, dorsal root ganglia, trigeminal ganglia and glossopharyngeal ganglia.

Developmental stagei

First detected at 9.0 dpc in the first and second archial arches. At 10.0 dpc and 10.5 dpc, expressed in somites, especially the forming sclerotomes. At 12.5 dpc, found in dorsal root ganglia. At 16.5 dpc, expressed in bone-forming areas and adipose tissues, as well as in specific neural tissues. In bone-forming areas, expressed along the mesenchymal condensation at 14.5 dpc, in the perichondrium and in cells invading the cartilagenous structures at 16.5 dpc. In 18.5 dpc tibias, scattered throughout the trabecular/cancellous bone area. In vitro, expression is induced during differentiation of immature osteoblasts, and then declines.1 Publication

Gene expression databases

BgeeiO08792.
CleanExiMM_EBF2.
GenevisibleiO08792. MM.

Interactioni

Subunit structurei

Forms either a homodimer or a heterodimer with a related family member.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei162 – 1621Interaction with DNABy similarity
Sitei171 – 1711Interaction with DNABy similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022637.

Structurei

3D structure databases

ProteinModelPortaliO08792.
SMRiO08792. Positions 35-384.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini253 – 33684IPT/TIGAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni62 – 654Interaction with DNABy similarity
Regioni196 – 2038Interaction with DNABy similarity
Regioni235 – 2384Interaction with DNABy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi453 – 53482Pro/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 fingeri150 – 16920C5-typeSequence analysisAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3836. Eukaryota.
ENOG410XQ9Z. LUCA.
GeneTreeiENSGT00390000014051.
HOGENOMiHOG000092311.
HOVERGENiHBG005108.
InParanoidiO08792.
KOiK09103.
OMAiSMMGINS.
OrthoDBiEOG7J446V.
PhylomeDBiO08792.
TreeFamiTF313391.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR032200. COE_DBD.
IPR032201. COE_HLH.
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.
PfamiPF16422. COE1_DBD. 1 hit.
PF16423. COE1_HLH. 1 hit.
PF01833. TIG. 1 hit.
[Graphical view]
SMARTiSM00429. IPT. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 1 hit.
PROSITEiPS01345. COE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O08792-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFGIQDTLGR GPALKDKSLG AEMDSVRSWV RNVGVVDANV AAQSGVALSR
60 70 80 90 100
AHFEKQPPSN LRKSNFFHFV LALYDRQGQP VEIERTAFVD FVENDKEQGN
110 120 130 140 150
EKTNNGTHYK LQLLYSNGVR TEQDLYVRLI DSVTKQPIAY EGQNKNPEMC
160 170 180 190 200
RVLLTHEVMC SRCCEKKSCG NRNETPSDPV IIDRFFLKFF LKCNQNCLKT
210 220 230 240 250
AGNPRDMRRF QVVLSTTVNV DGHVLAVSDN MFVHNNSKHG RRARRLDPSE
260 270 280 290 300
ATPCIKAISP SEGWTTGGAM VIIIGDNFFD GLQVVFGTML VWSELITPHA
310 320 330 340 350
IRVQTPPRHI PGVVEVTLSY KSKQFCKGAP GRFIYTALNE PTIDYGFQRL
360 370 380 390 400
QKVIPRHPGD PERLAKEMLL KRAADLVEAL YGTPHNNQDI ILKRAADIAE
410 420 430 440 450
ALYSVPRNPS QIPALSSSPA HSGMMGINSY GSQLGVSISE STQGNNQGYI
460 470 480 490 500
RNTSSISPRG YSSSSTPQQS NYSTSSNSMN GYSNVPMANL GVPGSPGFLN
510 520 530 540 550
GSPTGSPYGI MSSSPTVGSS STSSILPFSS SVFPAVKQKS AFAPVIRPQG
560 570
SPSPACSSGN GNGFRAMTGL VVPPM
Length:575
Mass (Da):62,606
Last modified:May 30, 2000 - v4
Checksum:iE8CDD6DAC7637449
GO

Sequence cautioni

The sequence AAB58423.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371D → V in AAC64322 (PubMed:9389446).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U71189 mRNA. Translation: AAB58423.1. Different initiation.
U92703 mRNA. Translation: AAB58323.1.
U82441 mRNA. Translation: AAC64322.1.
AK053013 mRNA. Translation: BAC35239.1.
AK139262 mRNA. Translation: BAE23936.1.
BC049188 mRNA. Translation: AAH49188.1.
BC050922 mRNA. Translation: AAH50922.1.
CCDSiCCDS27228.1.
RefSeqiNP_001263316.1. NM_001276387.1.
NP_034225.1. NM_010095.6.
XP_011243247.1. XM_011244945.1.
UniGeneiMm.319947.

Genome annotation databases

EnsembliENSMUST00000022637; ENSMUSP00000022637; ENSMUSG00000022053.
ENSMUST00000176029; ENSMUSP00000135782; ENSMUSG00000022053.
ENSMUST00000176161; ENSMUSP00000135500; ENSMUSG00000022053.
GeneIDi13592.
KEGGimmu:13592.
UCSCiuc007ukw.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U71189 mRNA. Translation: AAB58423.1. Different initiation.
U92703 mRNA. Translation: AAB58323.1.
U82441 mRNA. Translation: AAC64322.1.
AK053013 mRNA. Translation: BAC35239.1.
AK139262 mRNA. Translation: BAE23936.1.
BC049188 mRNA. Translation: AAH49188.1.
BC050922 mRNA. Translation: AAH50922.1.
CCDSiCCDS27228.1.
RefSeqiNP_001263316.1. NM_001276387.1.
NP_034225.1. NM_010095.6.
XP_011243247.1. XM_011244945.1.
UniGeneiMm.319947.

3D structure databases

ProteinModelPortaliO08792.
SMRiO08792. Positions 35-384.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022637.

PTM databases

iPTMnetiO08792.
PhosphoSiteiO08792.

Proteomic databases

MaxQBiO08792.
PaxDbiO08792.
PeptideAtlasiO08792.
PRIDEiO08792.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022637; ENSMUSP00000022637; ENSMUSG00000022053.
ENSMUST00000176029; ENSMUSP00000135782; ENSMUSG00000022053.
ENSMUST00000176161; ENSMUSP00000135500; ENSMUSG00000022053.
GeneIDi13592.
KEGGimmu:13592.
UCSCiuc007ukw.2. mouse.

Organism-specific databases

CTDi64641.
MGIiMGI:894332. Ebf2.

Phylogenomic databases

eggNOGiKOG3836. Eukaryota.
ENOG410XQ9Z. LUCA.
GeneTreeiENSGT00390000014051.
HOGENOMiHOG000092311.
HOVERGENiHBG005108.
InParanoidiO08792.
KOiK09103.
OMAiSMMGINS.
OrthoDBiEOG7J446V.
PhylomeDBiO08792.
TreeFamiTF313391.

Miscellaneous databases

ChiTaRSiEbf2. mouse.
PROiO08792.
SOURCEiSearch...

Gene expression databases

BgeeiO08792.
CleanExiMM_EBF2.
GenevisibleiO08792. MM.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR032200. COE_DBD.
IPR032201. COE_HLH.
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.
PfamiPF16422. COE1_DBD. 1 hit.
PF16423. COE1_HLH. 1 hit.
PF01833. TIG. 1 hit.
[Graphical view]
SMARTiSM00429. IPT. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 1 hit.
PROSITEiPS01345. COE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mmot1, a new helix-loop-helix transcription factor gene displaying a sharp expression boundary in the embryonic mouse brain."
    Malgaretti N., Pozzoli O., Bosetti A., Corradi A., Ciarmatori S., Panigada M., Bianchi M.E., Martinez S., Consalez G.G.
    J. Biol. Chem. 272:17632-17639(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    Tissue: Embryo.
  2. "The characterization of the Olf-1/EBF-like HLH transcription factor family: implications in olfactory gene regulation and neuronal development."
    Wang S.S., Tsai R.Y.L., Reed R.R.
    J. Neurosci. 17:4149-4158(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT.
    Strain: CD-1.
    Tissue: Embryo.
  3. "Family of Ebf/Olf-1-related genes potentially involved in neuronal differentiation and regional specification in the central nervous system."
    Garel S., Marin F., Mattei M.-G., Vesque C., Vincent A., Charnay P.
    Dev. Dyn. 210:191-205(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Embryo.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum and Embryonic head.
  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].
    Strain: C57BL/6J.
    Tissue: Brain and Olfactory epithelium.
  6. "EBF2 regulates osteoblast-dependent differentiation of osteoclasts."
    Kieslinger M., Folberth S., Dobreva G., Dorn T., Croci L., Erben R., Consalez G.G., Grosschedl R.
    Dev. Cell 9:757-767(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiCOE2_MOUSE
AccessioniPrimary (citable) accession number: O08792
Secondary accession number(s): Q543D5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: July 6, 2016
This is version 130 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.