ERH (gene)

ERH
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1W9G, 2NML
Identifiers
Aliases	ERH, DROER, enhancer of rudimentary homolog (Drosophila)
External IDs	MGI: 108089 HomoloGene: 3274 GeneCards: ERH
Gene ontology Molecular function • methyl-CpG binding • poly(A) RNA binding • protein binding Cellular component • methylosome • midbody • membrane Biological process • pyrimidine nucleoside metabolic process • cell cycle • nucleobase-containing compound metabolic process • pyrimidine nucleotide biosynthetic process • osteoblast differentiation • positive regulation of Notch signaling pathway 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	NM_007951
RefSeq (protein)	NP_004441.1	NP_031977.1
Location (UCSC)	Chr 14: 69.38 – 69.4 Mb	Chr 12: 80.63 – 80.64 Mb
PubMed search	[1]	[2]
Wikidata

View/Edit Human

View/Edit Mouse

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; PDBj PDBsum structure summary

In molecular biology, Enhancer of rudimentary homolog is a protein that in humans is encoded by the ERH gene.^[3][4][5]

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.^[6]

From an evolutionary point of view, enhancer of rudimentary is highly conserved and has been found to exist in probably all multicellular eukaryotic organisms.^[4] It has been proposed that this protein plays a role in the cell cycle.

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Isomura M, Okui K, Fujiwara T, Shin S, Nakamura Y (Sep 1996). "Cloning and mapping of a novel human cDNA homologous to DROER, the enhancer of the Drosophila melanogaster rudimentary gene". Genomics. 32 (1): 125–7. doi:10.1006/geno.1996.0086. PMID 8786099.
4. Gelsthorpe M, Pulumati M, McCallum C, Dang-Vu K, Tsubota SI (Apr 1997). "The putative cell cycle gene, enhancer of rudimentary, encodes a highly conserved protein found in plants and animals". Gene. 186 (2): 189–95. doi:10.1016/S0378-1119(96)00701-9. PMID 9074495.
5. "Entrez Gene: ERH enhancer of rudimentary homolog (Drosophila)".
6. Wojcik, E.; Murphy, A. M.; Fares, H.; Dang-Vu, K.; Tsubota, S. I. (1994). "Enhancer of rudimentaryp1, e(r)p1, a highly conserved enhancer of the rudimentary gene". Genetics. 138 (4): 1163–1170. PMC 1206255. PMID 7896098.

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.
• 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.
• 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.
• 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