DNTTIP2

Deoxynucleotidyltransferase terminal-interacting protein 2 is an enzyme that in humans is encoded by the DNTTIP2 gene.[5][6]

DNTTIP2
Identifiers
Aliases	DNTTIP2, ERBP, FCF2, HSU15552, LPTS-RP2, TdIF2, deoxynucleotidyltransferase terminal interacting protein 2
External IDs	OMIM: 611199 MGI: 1923173 HomoloGene: 124162 GeneCards: DNTTIP2
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1p22.1 Start 93,866,284 bp[1] End 93,879,918 bp[1]
Gene location (Mouse) Chr. Chromosome 3 (mouse)[2] Band 3|3 G1 Start 122,274,388 bp[2] End 122,285,271 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • RNA binding Cellular component • cell nucleus • nucleolus Biological process • regulation of transcription, DNA-templated • transcription, DNA-templated Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	30836	99480
Ensembl	ENSG00000067334	ENSMUSG00000039756
UniProt	Q5QJE6	Q8R2M2
RefSeq (mRNA)	NM_014597	NM_153806
RefSeq (protein)	NP_055412	NP_722501
Location (UCSC)	Chr 1: 93.87 – 93.88 Mb	Chr 3: 122.27 – 122.29 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Interactions

DNTTIP2 has been shown to interact with Estrogen receptor alpha.[5]

References

1. GRCh38: Ensembl release 89: ENSG00000067334 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000039756 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Bu H, Kashireddy P, Chang J, Zhu YT, Zhang Z, Zheng W, Rao SM, Zhu YJ (Mar 2004). "ERBP, a novel estrogen receptor binding protein enhancing the activity of estrogen receptor". Biochem Biophys Res Commun. 317 (1): 54–9. doi:10.1016/j.bbrc.2004.02.179. PMID 15047147.
6. "Entrez Gene: DNTTIP2 deoxynucleotidyltransferase, terminal, interacting protein 2".

Further reading

• Soares-da-Silva P, Fernandes MH (1992). "Sodium-dependence and ouabain-sensitivity of the synthesis of dopamine in renal tissues of the rat". Br. J. Pharmacol. 105 (4): 811–6. doi:10.1111/j.1476-5381.1992.tb09062.x. PMC 1908707. PMID 1504714.
• Lim HD (1992). "Making an alternative occlusal splint". The Journal of Prosthetic Dentistry. 67 (4): 572–3. doi:10.1016/0022-3913(92)90094-Q. PMID 1507147.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• 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.
• Fujita K, Shimazaki N, Ohta Y, et al. (2004). "Terminal deoxynucleotidyltransferase forms a ternary complex with a novel chromatin remodeling protein with 82 kDa and core histone". Genes Cells. 8 (6): 559–71. doi:10.1046/j.1365-2443.2003.00656.x. PMID 12786946.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Rempola B, Karkusiewicz I, Piekarska I, Rytka J (2006). "Fcf1p and Fcf2p are novel nucleolar Saccharomyces cerevisiae proteins involved in pre-rRNA processing". Biochem. Biophys. Res. Commun. 346 (2): 546–54. doi:10.1016/j.bbrc.2006.05.140. PMID 16762320.