Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P37242 (THB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thyroid hormone receptor beta
Alternative name(s):
Nuclear receptor subfamily 1 group A member 2
c-erbA-2
c-erbA-beta
Gene names
Name:Thrb
Synonyms:Erba2, Nr1a2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Nuclear hormone receptor that can act as a repressor or activator of transcription. High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine.

Subunit structure

Binds DNA as a dimer; homodimer and heterodimer with RXRB. Interacts with the coactivators NCOA1/SRC1, NCOA2/GRIP1, NCOA7 and MED1/TRAP220 in a ligand-inducible manner. Interacts with the corepressor NCOR1 in absence of ligand By similarity. Interacts with C1D. Interacts with NR2F6; the interaction impairs the binding of the THRB homodimer and THRB:RXRB heterodimer to T3 response elements. Interacts with PRMT2 and THRSP By similarity. Ref.5

Subcellular location

Nucleus.

Domain

Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.

Sequence similarities

Belongs to the nuclear hormone receptor family. NR1 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionReceptor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processType I pneumocyte differentiation

Inferred from genetic interaction PubMed 22001906. Source: MGI

female courtship behavior

Inferred from mutant phenotype PubMed 10769387. Source: MGI

intracellular receptor signaling pathway

Inferred from sequence or structural similarity. Source: GOC

negative regulation of female receptivity

Inferred from mutant phenotype PubMed 10769387. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction PubMed 22001906PubMed 7566114. Source: MGI

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15062575. Source: MGI

organ morphogenesis

Inferred from mutant phenotype PubMed 9927422. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction PubMed 12407160. Source: MGI

regulation of heart contraction

Inferred from mutant phenotype PubMed 9832432. Source: MGI

regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction PubMed 19052228. Source: MGI

regulation of transcription, DNA-templated

Traceable author statement PubMed 9927422. Source: MGI

sensory perception of sound

Inferred from mutant phenotype PubMed 8673137. Source: MGI

   Cellular_componentnucleus

Inferred from direct assay PubMed 17952069. Source: MGI

   Molecular_functionchromatin DNA binding

Inferred from direct assay PubMed 17952069. Source: MGI

protein binding

Inferred from physical interaction PubMed 16936638. Source: IntAct

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Traceable author statement PubMed 9927422. Source: MGI

steroid hormone receptor activity

Inferred from electronic annotation. Source: InterPro

thyroid hormone binding

Inferred from sequence or structural similarity. Source: UniProtKB

thyroid hormone receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AipO089152EBI-6935043,EBI-6935014

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Beta-1 (identifier: P37242-1)

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 Beta-2 (identifier: P37242-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-93: MTPNSMTENG...QTFQTEEKKC → MNYCMPEVHE...QVQSPPHSQK

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 461461Thyroid hormone receptor beta
PRO_0000053448

Regions

DNA binding107 – 18175Nuclear receptor
Zinc finger107 – 12721NR C4-type
Zinc finger145 – 16925NR C4-type
Region1 – 106106Modulating
Region244 – 461218Interaction with NR2F6 By similarity
Region244 – 461218Ligand-binding

Sites

Binding site2821Thyroid hormone By similarity
Binding site3201Thyroid hormone By similarity
Binding site3311Thyroid hormone; via amide nitrogen By similarity
Binding site4351Thyroid hormone By similarity

Natural variations

Alternative sequence1 – 9393MTPNS…EEKKC → MNYCMPEVHEVCPAASSNCY MQVTDYLAYLEDSPALSGRD VQAVPSSSIYMEQAWAVNQP YTCSYPGNLFKSKDSDLDMA LSQSSQPAHLPEEKPFPQVQ SPPHSQK in isoform Beta-2.
VSP_031078

Experimental info

Sequence conflict4451E → G in BAE34683. Ref.3

Sequences

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

Last modified October 1, 1994. Version 1.
Checksum: 99089194FC3E6B33

FASTA46152,630
        10         20         30         40         50         60 
MTPNSMTENG LPAWDKQKPR PDRGQDWKLV GMSEACLHRK SHVERRGALK NEQTSPHLIQ 

        70         80         90        100        110        120 
ATWTSSIFHL DPDDVNDQSI SSAQTFQTEE KKCKGYIPSY LDKDELCVVC GDKATGYHYR 

       130        140        150        160        170        180 
CITCEGCKGF FRRTIQKSLH PSYSCKYEGK CIIDKVTRNQ CQECRFKKCI YVGMATDLVL 

       190        200        210        220        230        240 
DDSKRLAKRK LIEENREKRR REELQKSIGH KPEPTDEEWE LIKTVTEAHV ATNAQGSHWK 

       250        260        270        280        290        300 
QKRKFLPEDI GQAPIVNAPE GGKVDLEAFS HFTKIITPAI TRVVDFAKKL PMFCELPCED 

       310        320        330        340        350        360 
QIILLKGCCM EIMSLRAAVR YDPDSETLTL NGEMAVTRGQ LKNGGLGVVS DAIFDLGMSL 

       370        380        390        400        410        420 
SSFNLDDTEV ALLQAVLLMS SDRPGLACVE RIEKYQDSFL LAFEHYINYR KHHVTHFWPK 

       430        440        450        460 
LLMKVTDLRM IGACHASRFL HMKVECPTEL FPPLFLEVFE D 

« Hide

Isoform Beta-2 [UniParc] [UniParc].

Checksum: 0ED4FF2D92F889DE
Show »

FASTA47553,916

References

« Hide 'large scale' references
[1]"Isolation and characterization of mouse complementary DNAs encoding alpha and beta thyroid hormone receptors from thyrotrope cells: the mouse pituitary-specific beta 2 isoform differs at the amino terminus from the corresponding species from rat pituitary tumor cells."
Wood W.M., Ocran K.W., Gordon D.F., Ridgway E.C.
Mol. Endocrinol. 5:1049-1061(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-1 AND BETA-2).
Tissue: Thyroid.
[2]"Structural and functional characterization of the genomic locus encoding the murine beta 2 thyroid hormone receptor."
Wood W.M., Dowding J.M., Haugen B.R., Bright T.M., Gordon D.F., Ridgway E.C.
Mol. Endocrinol. 8:1605-1617(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DBA/2J.
Tissue: Liver.
[3]"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. expand/collapse author list , 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] (ISOFORM BETA-1).
Strain: C57BL/6J.
Tissue: Visual cortex.
[4]"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] (ISOFORM BETA-2).
Strain: C57BL/6.
Tissue: Eye.
[5]"Cloning and characterization of a corepressor and potential component of the nuclear hormone receptor repression complex."
Zamir I., Dawson J., Lavinsky R.M., Glass C.K., Rosenfeld M.G., Lazar M.A.
Proc. Natl. Acad. Sci. U.S.A. 94:14400-14405(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH C1D.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S62756 mRNA. Translation: AAB20226.1.
S62758 mRNA. Translation: AAB20227.1.
U15548 expand/collapse EMBL AC list , U15542, U15543, U15544, U15545, U15546, U15547 Genomic DNA. Translation: AAA86957.1.
AK158826 mRNA. Translation: BAE34683.1.
BC089035 mRNA. Translation: AAH89035.1.
BC119552 mRNA. Translation: AAI19553.1.
BC119553 mRNA. Translation: AAI19554.1.
CCDSCCDS26835.1. [P37242-2]
CCDS49404.1. [P37242-1]
PIRA40377.
A57035.
RefSeqNP_001106888.1. NM_001113417.1. [P37242-1]
NP_033406.1. NM_009380.3. [P37242-2]
XP_006518029.1. XM_006517966.1. [P37242-1]
XP_006518030.1. XM_006517967.1. [P37242-1]
XP_006518031.1. XM_006517968.1. [P37242-1]
XP_006518032.1. XM_006517969.1. [P37242-1]
XP_006518033.1. XM_006517970.1. [P37242-1]
XP_006518034.1. XM_006517971.1. [P37242-1]
XP_006518035.1. XM_006517972.1. [P37242-1]
UniGeneMm.32563.
Mm.491616.

3D structure databases

ProteinModelPortalP37242.
SMRP37242. Positions 105-461.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204184. 9 interactions.
IntActP37242. 2 interactions.
MINTMINT-3374177.

Chemistry

GuidetoPHARMACOLOGY589.

PTM databases

PhosphoSiteP37242.

Proteomic databases

PRIDEP37242.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022303; ENSMUSP00000022303; ENSMUSG00000021779. [P37242-1]
ENSMUST00000022304; ENSMUSP00000022304; ENSMUSG00000021779. [P37242-2]
ENSMUST00000091471; ENSMUSP00000089053; ENSMUSG00000021779. [P37242-1]
GeneID21834.
KEGGmmu:21834.
UCSCuc007shk.2. mouse. [P37242-1]
uc007sho.2. mouse. [P37242-2]

Organism-specific databases

CTD7068.
MGIMGI:98743. Thrb.

Phylogenomic databases

eggNOGNOG272726.
GeneTreeENSGT00740000114969.
HOGENOMHOG000010313.
HOVERGENHBG005606.
KOK08362.
OMACSNILES.
OrthoDBEOG7TBC2V.
PhylomeDBP37242.
TreeFamTF328382.

Gene expression databases

BgeeP37242.
CleanExMM_THRB.
GenevestigatorP37242.

Family and domain databases

Gene3D1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProIPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001723. Str_hrmn_rcpt.
IPR001728. ThyrH_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSPR00398. STRDHORMONER.
PR00047. STROIDFINGER.
PR00546. THYROIDHORMR.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 1 hit.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio301286.
PROP37242.
SOURCESearch...

Entry information

Entry nameTHB_MOUSE
AccessionPrimary (citable) accession number: P37242
Secondary accession number(s): P37244, Q0VDR8, Q3TY80
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: July 9, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot