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

Q14994 (NR1I3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Nuclear receptor subfamily 1 group I member 3
Alternative name(s):
Constitutive activator of retinoid response
Short name=Constitutive active response
Constitutive androstane receptor
Short name=CAR
Orphan nuclear receptor MB67
Gene names
Name:NR1I3
Synonyms:CAR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length352 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds and transactivates the retinoic acid response elements that control expression of the retinoic acid receptor beta 2 and alcohol dehydrogenase 3 genes. Transactivates both the phenobarbital responsive element module of the human CYP2B6 gene and the CYP3A4 xenobiotic response element.

Subunit structure

Interacts with ECT2 By similarity. Heterodimer of NR1I3 and RXR. Interacts with PSMC4. Directly interacts with DNAJC7. The DNAJC7-NR1I3 complex may also include HSP90 By similarity. Ref.8 Ref.9

Subcellular location

Nucleus. Cytoplasm. Cytoplasmcytoskeleton. Note: Recruited to the cytoplasm by DNAJC7 By similarity. Ref.9 Ref.10

Tissue specificity

Predominantly expressed in liver.

Induction

By dexamethasone.

Domain

Composed by a short N-terminal domain followed by the DNA binding, hinge, and ligand binding/dimerization domains.

Post-translational modification

Phosphorylated at Thr-38 by PKC, dephosphorylation of Thr-38 is required for nuclear translocation and activation. Ref.10

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 componentCytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
Receptor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processandrogen receptor signaling pathway

Traceable author statement PubMed 9783588. Source: GOC

gene expression

Traceable author statement. Source: Reactome

intracellular receptor signaling pathway

Traceable author statement Ref.1. Source: GOC

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement PubMed 8020947PubMed 9783588. Source: ProtInc

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionDNA binding

Traceable author statement PubMed 9783588. Source: ProtInc

androgen receptor activity

Traceable author statement PubMed 9783588. Source: ProtInc

ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity

Traceable author statement Ref.1. Source: ProtInc

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Traceable author statement PubMed 8020947Ref.1. Source: ProtInc

thyroid hormone receptor activity

Inferred from electronic annotation. Source: InterPro

transcription coactivator activity

Traceable author statement PubMed 9783588. Source: ProtInc

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 11 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14994-1)

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: Q14994-2)

The sequence of this isoform differs from the canonical sequence as follows:
     233-236: Missing.
Isoform 3 (identifier: Q14994-3)

The sequence of this isoform differs from the canonical sequence as follows:
     232-274: VSPTVGFQVEFLELLFHFHGTLRKLQLQEPEYVLLAAMALFSP → APYLT
Isoform 4 (identifier: Q14994-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: MASREDELRNCVVCGDQATGYHFNALTCEGCKGFF → MLPKRS
     232-274: Missing.
Isoform 5 (identifier: Q14994-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: MASREDELRNCVVCGDQATGYHFNALTCEGCKGFF → MLPKRS
     233-236: Missing.
Isoform 6 (identifier: Q14994-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: MASREDELRNCVVCGDQATGYHFNALTCEGCKGFF → MLPKRS
     233-236: Missing.
     274-274: P → PAPYLT
Isoform 7 (identifier: Q14994-7)

The sequence of this isoform differs from the canonical sequence as follows:
     232-274: Missing.
Isoform 8 (identifier: Q14994-8)

The sequence of this isoform differs from the canonical sequence as follows:
     274-274: P → PAPYLT
Isoform 9 (identifier: Q14994-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: MASREDELRNCVVCGDQATGYHFNALTCEGCKGFF → MLPKRS
     233-236: Missing.
     311-352: FLYAKLLGLLAELRSINEAYGYQIQHIQGLSAMMPLLQEICS → SPGTPWIHWSGKMLGPKIGPGSKGAQWLQ
Isoform 10 (identifier: Q14994-10)

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: MASREDELRNCVVCGDQATGYHFNALTCEGCKGFF → MLPKRS
     233-236: Missing.
     274-274: P → PAPYLT
     311-352: FLYAKLLGLLAELRSINEAYGYQIQHIQGLSAMMPLLQEICS → SPGTPWIHWSGKMLGPKIGPGSKGAQWLQ
Isoform 11 (identifier: Q14994-11)

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: MASREDELRNCVVCGDQATGYHFNALTCEGCKGFF → MLPKRS
     274-274: P → PAPYLT
     311-352: FLYAKLLGLLAELRSINEAYGYQIQHIQGLSAMMPLLQEICS → SPGTPWIHWSGKMLGPKIGPGSKGAQWLQ

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 352352Nuclear receptor subfamily 1 group I member 3
PRO_0000053552

Regions

DNA binding8 – 8376Nuclear receptor
Zinc finger11 – 3121NR C4-type
Zinc finger47 – 7125NR C4-type

Amino acid modifications

Modified residue381Phosphothreonine; by PKC Ref.10

Natural variations

Alternative sequence1 – 3535MASRE…CKGFF → MLPKRS in isoform 4, isoform 5, isoform 6, isoform 9, isoform 10 and isoform 11.
VSP_043730
Alternative sequence232 – 27443VSPTV…ALFSP → APYLT in isoform 3.
VSP_043144
Alternative sequence232 – 27443Missing in isoform 4 and isoform 7.
VSP_043731
Alternative sequence233 – 2364Missing in isoform 2, isoform 5, isoform 6, isoform 9 and isoform 10.
VSP_010634
Alternative sequence2741P → PAPYLT in isoform 6, isoform 8, isoform 10 and isoform 11.
VSP_043732
Alternative sequence311 – 35242FLYAK…QEICS → SPGTPWIHWSGKMLGPKIGP GSKGAQWLQ in isoform 9, isoform 10 and isoform 11.
VSP_046144
Natural variant1331V → G. Ref.12
VAR_018344

Secondary structure

.................................... 352
Helix Strand Turn

Details...

Sequences

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

Last modified June 21, 2004. Version 2.
Checksum: 73B060FE4950D519

FASTA35239,942
        10         20         30         40         50         60 
MASREDELRN CVVCGDQATG YHFNALTCEG CKGFFRRTVS KSIGPTCPFA GSCEVSKTQR 

        70         80         90        100        110        120 
RHCPACRLQK CLDAGMRKDM ILSAEALALR RAKQAQRRAQ QTPVQLSKEQ EELIRTLLGA 

       130        140        150        160        170        180 
HTRHMGTMFE QFVQFRPPAH LFIHHQPLPT LAPVLPLVTH FADINTFMVL QVIKFTKDLP 

       190        200        210        220        230        240 
VFRSLPIEDQ ISLLKGAAVE ICHIVLNTTF CLQTQNFLCG PLRYTIEDGA RVSPTVGFQV 

       250        260        270        280        290        300 
EFLELLFHFH GTLRKLQLQE PEYVLLAAMA LFSPDRPGVT QRDEIDQLQE EMALTLQSYI 

       310        320        330        340        350 
KGQQRRPRDR FLYAKLLGLL AELRSINEAY GYQIQHIQGL SAMMPLLQEI CS 

« Hide

Isoform 2 [UniParc].

Checksum: 92EAAD07D7DCB9DA
Show »

FASTA34839,558
Isoform 3 [UniParc].

Checksum: EE9F842EF2B19A2E
Show »

FASTA31435,588
Isoform 4 [UniParc].

Checksum: 7F3BFA4F60A16FB1
Show »

FASTA28031,900
Isoform 5 [UniParc].

Checksum: C41CFFC814E96E46
Show »

FASTA31936,416
Isoform 6 [UniParc].

Checksum: 32245F1A8C523B1E
Show »

FASTA32436,961
Isoform 7 [UniParc].

Checksum: 47BDCF4FC3777574
Show »

FASTA30935,043
Isoform 8 [UniParc].

Checksum: 1AF956D0A2759781
Show »

FASTA35740,488
Isoform 9 [UniParc].

Checksum: EA8397560E3A2AC1
Show »

FASTA30634,778
Isoform 10 [UniParc].

Checksum: 88A1BD387DDFFF8B
Show »

FASTA31135,323
Isoform 11 [UniParc].

Checksum: A90FF3A0E39D1305
Show »

FASTA31535,708

References

« Hide 'large scale' references
[1]"A new orphan member of the nuclear hormone receptor superfamily that interacts with a subset of retinoic acid response elements."
Baes M., Gulick T., Choi H.S., Martinoli M.G., Simha D., Moore D.D.
Mol. Cell. Biol. 14:1544-1552(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Liver.
[2]"Expression of constitutive androstane receptor splice variants in human tissues and their functional consequences."
Lamba J.K., Lamba V., Yasuda K., Lin Y.S., Assem M., Thompson E., Strom S., Schuetz E.G.
J. Pharmacol. Exp. Ther. 311:811-821(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5; 6 AND 7), NUCLEOTIDE SEQUENCE [MRNA] OF 1-288 (ISOFORM 9), NUCLEOTIDE SEQUENCE [MRNA] OF 1-293 (ISOFORM 10), NUCLEOTIDE SEQUENCE [MRNA] OF 1-297 (ISOFORM 11), ALTERNATIVE SPLICING.
[3]Zhou G., Nong W., Li H., Ke R., Shen C., Zhong G., Zheng Z., Liang M., Huang B., Lin L., Yang S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8).
[4]"Isolation of cDNA coding for multiple human nuclear receptor clones."
Kaighin V.A., Martin A.L., Aronstam R.S.
Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 7).
Tissue: Eye and Small intestine.
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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; 3 AND 7).
[8]"A component of the 26S proteasome binds on orphan member of the nuclear hormone receptor superfamily."
Choi H.S., Seol W., Moore D.D.
J. Steroid Biochem. Mol. Biol. 56:23-30(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PSMC4.
[9]"Cytoplasmic accumulation of the nuclear receptor CAR by a tetratricopeptide repeat protein in HepG2 cells."
Kobayashi K., Sueyoshi T., Inoue K., Moore R., Negishi M.
Mol. Pharmacol. 64:1069-1075(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DNAJC7, SUBCELLULAR LOCATION.
[10]"Dephosphorylation of threonine 38 is required for nuclear translocation and activation of human xenobiotic receptor CAR (NR1I3)."
Mutoh S., Osabe M., Inoue K., Moore R., Pedersen L., Perera L., Rebolloso Y., Sueyoshi T., Negishi M.
J. Biol. Chem. 284:34785-34792(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-38, SUBCELLULAR LOCATION.
[11]"A structural basis for constitutive activity in the human CAR/RXRalpha heterodimer."
Xu R.X., Lambert M.H., Wisely B.B., Warren E.N., Weinert E.E., Waitt G.M., Williams J.D., Collins J.L., Moore L.B., Willson T.M., Moore J.T.
Mol. Cell 16:919-928(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 103-352.
[12]"Twenty-six novel single nucleotide polymorphisms and their frequencies of the NR1I3 (CAR) gene in a Japanese population."
Ikeda S., Kurose K., Ozawa S., Sai K., Hasegawa R., Komamura K., Ueno K., Kamakura S., Kitakaze M., Tomoike H., Nakajima T., Matsumoto K., Saito H., Goto Y., Kimura H., Katoh M., Sugai K., Minami N. expand/collapse author list , Shirao K., Tamura T., Yamamoto N., Minami H., Ohtsu A., Yoshida T., Saijo N., Saito Y., Sawada J.
Drug Metab. Pharmacokinet. 18:413-418(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLY-133.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z30425 mRNA. Translation: CAA83016.1.
AY572808 mRNA. Translation: AAT47161.1.
AY572810 mRNA. Translation: AAT47163.1.
AY572811 mRNA. Translation: AAT47164.1.
AY572812 mRNA. Translation: AAT47165.1.
AY572817 mRNA. Translation: AAT47170.1.
AY572818 mRNA. Translation: AAT47171.1.
AY572827 mRNA. Translation: AAT47180.1.
DQ022681 mRNA. Translation: AAY56401.1.
HQ692838 mRNA. Translation: ADZ17349.1.
HQ692839 mRNA. Translation: ADZ17350.1.
HQ692840 mRNA. Translation: ADZ17351.1.
HQ692841 mRNA. Translation: ADZ17352.1.
AL590714 Genomic DNA. Translation: CAH72153.1.
AL590714 Genomic DNA. Translation: CAH72154.1.
CH471121 Genomic DNA. Translation: EAW52608.1.
CH471121 Genomic DNA. Translation: EAW52609.1.
BC069626 mRNA. Translation: AAH69626.1.
BC121120 mRNA. Translation: AAI21121.1.
BC121121 mRNA. Translation: AAI21122.1.
PIRA56197.
RefSeqNP_001070938.1. NM_001077470.2.
NP_001070939.1. NM_001077471.2.
NP_001070940.1. NM_001077472.2.
NP_001070941.1. NM_001077473.2.
NP_001070944.1. NM_001077476.2.
NP_001070945.1. NM_001077477.2.
NP_001070947.1. NM_001077479.2.
NP_001070948.1. NM_001077480.2.
NP_001070949.1. NM_001077481.2.
NP_001070950.1. NM_001077482.2.
NP_005113.1. NM_005122.4.
UniGeneHs.349642.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XV9X-ray2.70B/D103-352[»]
1XVPX-ray2.60B/D103-352[»]
ProteinModelPortalQ14994.
SMRQ14994. Positions 11-352.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115295. 14 interactions.
IntActQ14994. 7 interactions.
STRING9606.ENSP00000356959.

Chemistry

BindingDBQ14994.
ChEMBLCHEMBL5503.
GuidetoPHARMACOLOGY607.

PTM databases

PhosphoSiteQ14994.

Polymorphism databases

DMDM49066046.

Proteomic databases

PaxDbQ14994.
PRIDEQ14994.

Protocols and materials databases

DNASU9970.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367979; ENSP00000356958; ENSG00000143257. [Q14994-8]
ENST00000367980; ENSP00000356959; ENSG00000143257. [Q14994-8]
ENST00000367981; ENSP00000356960; ENSG00000143257. [Q14994-6]
ENST00000367982; ENSP00000356961; ENSG00000143257. [Q14994-1]
ENST00000367983; ENSP00000356962; ENSG00000143257. [Q14994-2]
ENST00000367984; ENSP00000356963; ENSG00000143257. [Q14994-7]
ENST00000367985; ENSP00000356965; ENSG00000143257. [Q14994-3]
ENST00000412844; ENSP00000399361; ENSG00000143257. [Q14994-11]
ENST00000437437; ENSP00000407446; ENSG00000143257. [Q14994-9]
ENST00000504010; ENSP00000424345; ENSG00000143257. [Q14994-4]
ENST00000508740; ENSP00000423666; ENSG00000143257. [Q14994-10]
ENST00000511676; ENSP00000427175; ENSG00000143257. [Q14994-5]
GeneID9970.
KEGGhsa:9970.
UCSCuc001fzh.3. human. [Q14994-6]
uc001fzj.3. human. [Q14994-5]
uc001fzl.3. human. [Q14994-4]
uc001fzp.3. human.
uc001fzx.3. human. [Q14994-1]
uc001fzy.3. human. [Q14994-2]
uc001fzz.3. human. [Q14994-3]
uc001gab.3. human. [Q14994-7]

Organism-specific databases

CTD9970.
GeneCardsGC01M161199.
HGNCHGNC:7969. NR1I3.
HPAHPA051365.
MIM603881. gene.
neXtProtNX_Q14994.
PharmGKBPA391.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG251788.
HOGENOMHOG000220844.
HOVERGENHBG108655.
KOK08541.
OMAPRDRFLY.
PhylomeDBQ14994.
TreeFamTF316304.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.
SignaLinkQ14994.

Gene expression databases

ArrayExpressQ14994.
BgeeQ14994.
CleanExHS_NR1I3.
GenevestigatorQ14994.

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

EvolutionaryTraceQ14994.
GeneWikiConstitutive_androstane_receptor.
GenomeRNAi9970.
NextBio37626.
PROQ14994.
SOURCESearch...

Entry information

Entry nameNR1I3_HUMAN
AccessionPrimary (citable) accession number: Q14994
Secondary accession number(s): E9PGH6 expand/collapse secondary AC list , E9PH10, E9PHN4, F1D8Q0, F1D8Q1, Q0VAC9, Q4U0F0, Q5VTW5, Q5VTW6, Q6GZ68, Q6GZ77, Q6GZ78, Q6GZ83, Q6GZ84, Q6GZ85, Q6GZ87
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 21, 2004
Last modified: April 16, 2014
This is version 143 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM