Nuclear receptor subfamily 0 group B member 2

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P97947 (NR0B2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 93. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Nuclear receptor subfamily 0 group B member 2

Alternative name(s):
Orphan nuclear receptor SHP
Small heterodimer partner

Gene names

Name:	Nr0b2
Synonyms:	Shp

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	260 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as a transcriptional regulator. Acts as a negative regulator of receptor-dependent signaling pathways. Specifically inhibits transactivation of the nuclear receptor with whom it interacts. Inhibits transcriptional activity of NEUROD1 on E-box-containing promoter by interfering with the coactivation function of the p300/CBP-mediated trancription complex for NEUROD1.
Subunit structure	Heterodimer; efficient DNA binding requires dimerization with another bHLH protein. Interacts (via N-terminus) with NEUROD1 (via N-terminus an C-terminus). Interacts with ID2. Interacts with NR1I3 and EID1 By similarity. Interacts with RARA, RXRA, THRB, NR5A1, NR5A2, PPARA and PPARG. May also interact with HNF4A. Ref.1
Subcellular location	Cytoplasm By similarity. Nucleus Probable. Note: Colocalizes with NEUROD1 in the nucleus By similarity.
Tissue specificity	Detected in kidney, testis, heart and liver. Ref.1
Sequence similarities	Belongs to the nuclear hormone receptor family. NR0 subfamily.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Molecular function	Receptor Repressor
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of sequence-specific DNA binding transcription factor activity Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 15860571. Source: RGD organ regeneration Inferred from expression pattern PubMed 15904869. Source: RGD positive regulation of insulin secretion Inferred from mutant phenotype PubMed 17259388. Source: RGD response to glucose stimulus Inferred from mutant phenotype PubMed 17259388. Source: RGD transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB protein complex Inferred from direct assay PubMed 10648597 PubMed 15860571. Source: RGD
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro protein complex binding Inferred from direct assay PubMed 10648597. Source: RGD sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro steroid hormone receptor activity Inferred from electronic annotation. Source: InterPro transcription corepressor activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 260

260

Nuclear receptor subfamily 0 group B member 2

PRO_0000232757

Regions

Region

60 – 231

172

Ligand-binding By similarity

Secondary structure

260

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P97947 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 71C1E09C8B912A79
Show »

FASTA

260

28,750

        10         20         30         40         50         60 
MSSSQSGVCP CQGSASHPTI LYTLLSPGPR TRPMAPASRS HCLCQQHRPV RLCAPHRTCR 

        70         80         90        100        110        120 
EALDVLGKTV AFLRNLPSFC LLPHEDQRRL LEGCWGPLFL LGLAQDTVTF EVAEAPVPSI 

       130        140        150        160        170        180 
LKKILLEEPN SGAQGAQPPD PPQPSLAAVQ WLQHCLESFW SLELGPKEYA YLKGTILFNP 

       190        200        210        220        230        240 
DVPGLHASCH IAHLQQEAHW ALCEVLEPWY PASQGRLARI LLMASTLKNI SCTLLVDLFF 

       250        260 
RPVIGDVDIT ELLEDMLLLR

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"An orphan nuclear receptor lacking a zinc-finger DNA-binding domain: interaction with several nuclear receptors." Masuda N., Yasumo H., Tamura T., Hashiguchi N., Furusawa T., Tsukamoto T., Sadano H., Osumi T. Biochim. Biophys. Acta 1350:27-32(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], INTERACTION WITH HNF4A; RARA; RXRA; PPARA AND THRB, TISSUE SPECIFICITY. Strain: Fischer 344-Jcl and Sprague-Dawley. Tissue: Liver.
[2]	"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: Liver.
[3]	"Crystallographic identification and functional characterization of phospholipids as ligands for the orphan nuclear receptor steroidogenic factor-1." Li Y., Choi M., Cavey G., Daugherty J., Suino K., Kovach A., Bingham N.C., Kliewer S.A., Xu H.E. Mol. Cell 17:491-502(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 17-28 IN COMPLEX WITH NR5A1.
[4]	"Structural and biochemical basis for selective repression of the orphan nuclear receptor liver receptor homolog 1 by small heterodimer partner." Li Y., Choi M., Suino K., Kovach A., Daugherty J., Kliewer S.A., Xu H.E. Proc. Natl. Acad. Sci. U.S.A. 102:9505-9510(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 16-26 IN COMPLEX WITH NR5A2 AND OF 115-131 IN COMPLEX WITH PPARG.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D86839 Genomic DNA. Translation: BAA13171.1.
D86580 mRNA. Translation: BAA13127.1.
BC088117 mRNA. Translation: AAH88117.1.

IPI

IPI00209708.

RefSeq

NP_476474.1. NM_057133.1.

UniGene

Rn.10712.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YP0	X-ray	1.50	B	17-28	[»]
1ZGY	X-ray	1.80	B	115-131	[»]
1ZH7	X-ray	2.50	C/D	16-26	[»]

ProteinModelPortal

P97947.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46314N.

STRING

10116.ENSRNOP00000009683.

PTM databases

PhosphoSite

P97947.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000009683; ENSRNOP00000009683; ENSRNOG00000007229.

GeneID

117274.

KEGG

rno:117274.

UCSC

RGD:621032. rat.

Organism-specific databases

CTD

8431.

RGD

621032. Nr0b2.

Phylogenomic databases

eggNOG

NOG235713.

GeneTree

ENSGT00390000015719.

HOGENOM

HOG000231151.

HOVERGEN

HBG008136.

InParanoid

P97947.

K08563.

OMA

HRTCREA.

OrthoDB

EOG4FXR8J.

Gene expression databases

Genevestigator

P97947.

GermOnline

ENSRNOG00000007229. Rattus norvegicus.

Family and domain databases

Gene3D

1.10.565.10. 1 hit.

InterPro

IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001723. Str_hrmn_rcpt.
[Graphical view]

Pfam

PF00104. Hormone_recep. 1 hit.
[Graphical view]

PRINTS

PR00398. STRDHORMONER.

SMART

SM00430. HOLI. 1 hit.
[Graphical view]

SUPFAM

SSF48508. Str_ncl_receptor. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P97947.

NextBio

620203.

Entry information

Entry name

NR0B2_RAT

Accession

Primary (citable) accession number: P97947

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 18, 2006
Last sequence update:	May 1, 1997
Last modified:	April 3, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents