ERH (gene)

Enhancer of rudimentary homolog (Drosophila)
PDB rendering based on 1w9g.
Available structures PDB 1W9G, 2NML
Identifiers
Symbols	ERH; DROER
External IDs	OMIM: 601191 MGI: 108089 HomoloGene: 3274 GeneCards: ERH Gene
Gene Ontology Molecular function • protein binding Cellular component • midbody Biological process • nucleobase-containing compound metabolic process • pyrimidine nucleoside metabolic process • cell cycle Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2079	13877
Ensembl	ENSG00000100632	ENSMUSG00000021131
UniProt	P84090	P84089
RefSeq (mRNA)	NM_004450.2	NM_007951.3
RefSeq (protein)	NP_004441.1	NP_031977.1
Location (UCSC)	Chr 14: 69.85 – 69.87 Mb	Chr 12: 81.74 – 81.75 Mb
PubMed search	[1]	[2]

Enhancer of rudimentary

crystal structure of enhancer of rudimentary homologue (erh)
Identifiers
Symbol	ER
Pfam	PF01133
InterPro	IPR000781
PROSITE	PDOC00732
SCOP	1j24
SUPERFAMILY	1j24
TCDB	3.A.16
Available protein structures: Pfam structures PDB RCSB PDB; PDBe PDBsum structure summary

In molecular biology, Enhancer of rudimentary homolog is a protein that in humans is encoded by the ERH gene.

The Drosophila protein enhancer of rudimentary protein is a small protein of 104 amino acids. It has been found to be an enhancer of the rudimentary gene, involved in pyrimidine biosynthesis.

From an evolutionary point of view, enhancer of rudimentary is highly conserved and has been found to exist in probably all multicellular eukaryotic organisms. It has been proposed that this protein plays a role in the cell cycle.

Further reading

• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics". Nature 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413. 
• Amente S, Napolitano G, Licciardo P, et al. (2005). "Identification of proteins interacting with the RNAPII FCP1 phosphatase: FCP1 forms a complex with arginine methyltransferase PRMT5 and it is a substrate for PRMT5-mediated methylation". FEBS Lett. 579 (3): 683–9. doi:10.1016/j.febslet.2004.12.045. PMID 15670829. 
• Wan C, Tempel W, Liu ZJ, et al. (2005). "Structure of the conserved transcriptional repressor enhancer of rudimentary homolog". Biochemistry 44 (13): 5017–23. doi:10.1021/bi047785w. PMID 15794639. 
• Stelzl U, Worm U, Lalowski M, et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070. 
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1847948. 
• Jin T, Guo F, Serebriiskii IG, et al. (2007). "A 1.55 A resolution X-ray crystal structure of HEF2/ERH and insights into its transcriptional and cell-cycle interaction networks". Proteins 68 (2): 427–37. doi:10.1002/prot.21343. PMID 17444515. 

This article incorporates text from the public domain Pfam and InterPro IPR000781