Protein Overview: gi|24987864, gi|...

General Information:
Name(s) found:	gi\|24987868 [NCBI NR] gi\|24987866 [NCBI NR] gi\|24987864 [NCBI NR] gi\|24987862 [NCBI NR] gi\|24987816 [NCBI NR] gi\|24987814 [NCBI NR] gi\|237640540 [NCBI NR] gi\|158429282 [NCBI NR] gi\|158429280 [NCBI NR] gi\|158429278 [NCBI NR]
Description(s) found: Found 20 descriptions. SHOW ALL	gi\|24987868\|pdb\|1MZN\|G Chain G, Crystal Structure At 1.9 Angstroems Resolution Of The Homodimer Of Human Rxr Alpha Ligand Binding Domain Bound To The Synthetic Agonist Compound Bms 649 And A Coactivator Peptide [NCBI NR] gi\|24987866\|pdb\|1MZN\|E Chain E, Crystal Structure At 1.9 Angstroems Resolution Of The Homodimer Of Human Rxr Alpha Ligand Binding Domain Bound To The Synthetic Agonist Compound Bms 649 And A Coactivator Peptide [NCBI NR] gi\|24987864\|pdb\|1MZN\|C Chain C, Crystal Structure At 1.9 Angstroems Resolution Of The Homodimer Of Human Rxr Alpha Ligand Binding Domain Bound To The Synthetic Agonist Compound Bms 649 And A Coactivator Peptide [NCBI NR] gi\|24987862\|pdb\|1MZN\|A Chain A, Crystal Structure At 1.9 Angstroems Resolution Of The Homodimer Of Human Rxr Alpha Ligand Binding Domain Bound To The Synthetic Agonist Compound Bms 649 And A Coactivator Peptide [NCBI NR] gi\|24987816\|pdb\|1MVC\|A Chain A, Crystal Structure Of The Human Rxr Alpha Ligand Binding Domain Bound To The Synthetic Agonist Compound Bms 649 And A Coactivator Peptide [NCBI NR] gi\|24987814\|pdb\|1MV9\|A Chain A, Crystal Structure Of The Human Rxr Alpha Ligand Binding Domain Bound To The Eicosanoid Dha (Docosa Hexaenoic Acid) And A Coactivator Peptide [NCBI NR] gi\|237640540\|pdb\|3FUG\|A Chain A, Crystal Structure Of The Retinoid X Receptor Ligand Binding Domain Bound To The Synthetic Agonist 3-[4-Hydroxy-3-(3,5, 5,8,8-Pentamethyl-5,6,7,8-Tetrahydronaphthalen-2-Yl)- Phenyl]acrylic Acid [NCBI NR] gi\|158429282\|pdb\|2P1V\|A Chain A, Crystal Structure Of The Ligand Binding Domain Of The Retinoid X Receptor Alpha In Complex With 3-(2'-Propoxy)- Tetrahydronaphtyl Cinnamic Acid And A Fragment Of The Coactivator Tif-2 [NCBI NR] gi\|158429280\|pdb\|2P1U\|A Chain A, Crystal Structure Of The Ligand Binding Domain Of The Retinoid X Receptor Alpha In Complex With 3-(2'-Ethoxy)- Tetrahydronaphtyl Cinnamic Acid And A Fragment Of The Coactivator Tif-2 [NCBI NR] gi\|158429278\|pdb\|2P1T\|A Chain A, Crystal Structure Of The Ligand Binding Domain Of The Retinoid X Receptor Alpha In Complex With 3-(2'-Methoxy)- Tetrahydronaphtyl Cinnamic Acid And A Fragment Of The Coactivator Tif-2 [NCBI NR]
Organism:	Homo sapiens
Length:	240 amino acids
Gene Ontology:
Cellular Component:	NONE FOUND
Biological Process:	NONE FOUND
Molecular Function:	NONE FOUND

Sequence:

Sequence:
[PDR BLAST]
[ProtParam]

      1          11         21         31         41         51         
      |          |          |          |          |          |          
    1 TSSANEDMPV ERILEAELAV EPKTETYVEA NMGLNPSSPN DPVTNICQAA DKQLFTLVEW  60
   61 AKRIPHFSEL PLDDQVILLR AGWNELLIAS FSHRSIAVKD GILLATGLHV HRNSAHSAGV 120
  121 GAIFDRVLTE LVSKMRDMQM DKTELGCLRA IVLFNPDSKG LSNPAEVEAL REKVYASLEA 180
  181 YCKHKYPEQP GRFAKLLLRL PALRSIGLKC LEHLFFFKLI GDTPIDTFLM EMLEAPHQMT 240
  241

Protein Complex Data

	PUBLICATION	TOPOLOGY	COCOMPLEXED PROTEINS
View Details	Noble WS, et al. (2009) Manuscript in preparation.		gi\|112491310 gi\|13786858 gi\|150261449 gi\|219109210, gi... gi\|24987864, gi\|... gi\|56554577 gi\|56966260, gi\|...

Mass Spectrometry Data

No mass spectrometry results found for this protein.

Yeast Two-Hybrid Data

The following interactions contain this protein:

NOT SHOWING SINGLE HITS. [ Show Single Hits ]

[View our yeast two-hybrid interpretation guidelines.]

No yeast two-hybrid interactions found for this protein.

Protein predicted to be:	GLOBULAR (No transmembrane regions or signal peptide)
Confidence of classification:	0.97

Protein Overview: gi|24987864, gi|...

Protein Complex Data

Mass Spectrometry Data

Yeast Two-Hybrid Data

Microscopy / Localization Data

Protein Structure Data

Philius Transmembrane Prediction: