PAXIP1

PAX interacting (with transcription-activation domain) protein 1
Identifiers
Symbols	PAXIP1; CAGF29; FLJ41049; PACIP1; PAXIP1L; PTIP; TNRC2
External IDs	OMIM: 608254 MGI: 1890430 HomoloGene: 68995 GeneCards: PAXIP1 Gene
Gene Ontology Cellular component • intracellular • nucleus • nuclear matrix • histone methyltransferase complex Biological process • positive regulation of histone H3-K36 methylation • DNA repair • DNA recombination • regulation of transcription, DNA-dependent • response to ionizing radiation • DNA damage response, signal transduction by p53 class mediator • positive regulation of protein ubiquitination • positive regulation of histone acetylation • positive regulation of isotype switching • histone H3-K4 methylation • positive regulation of histone H3-K4 methylation • positive regulation of transcription initiation from RNA polymerase II promoter • positive regulation of transcription initiation from RNA polymerase II promoter Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	22976	55982
Ensembl	ENSG00000157212	ENSMUSG00000002221
UniProt	Q6ZW49	n/a
RefSeq (mRNA)	NM_007349	NM_018878.2
RefSeq (protein)	NP_031375	NP_061366.2
Location (UCSC)	Chr 7: 154.74 – 154.79 Mb	Chr 5: 28.07 – 28.12 Mb
PubMed search	[1]	[2]

PAX-interacting protein 1 is a protein that in humans is encoded by the PAXIP1 gene.^[1][2]

This gene is a member of the paired box (PAX) gene family and encodes a nuclear protein with six BRCT (breast cancer carboxy-terminal) domains. This protein plays a critical role in maintaining genome stability, condensation of chromatin and progression through mitosis.^[2]

Interactions

PAXIP1 has been shown to interact with PAX2^[3] and TP53BP1.^[4][5]

References

1. ^ Margolis RL, Abraham MR, Gatchell SB, Li SH, Kidwai AS, Breschel TS, Stine OC, Callahan C, McInnis MG, Ross CA (Jul 1997). "cDNAs with long CAG trinucleotide repeats from human brain". Hum Genet 100 (1): 114–22. doi:10.1007/s004390050476. PMID 9225980. 
2. ^ ^{a b} "Entrez Gene: PAXIP1 PAX interacting (with transcription-activation domain) protein 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=22976. 
3. ^ Lechner, M S; Levitan I, Dressler G R (Jul. 2000). "PTIP, a novel BRCT domain-containing protein interacts with Pax2 and is associated with active chromatin". Nucleic Acids Res. (ENGLAND) 28 (14): 2741–51. doi:10.1093/nar/28.14.2741. PMC 102659. PMID 10908331. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=102659. 
4. ^ Jowsey, Paul A; Doherty Aidan J, Rouse John (Dec. 2004). "Human PTIP facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation". J. Biol. Chem. (United States) 279 (53): 55562–9. doi:10.1074/jbc.M411021200. ISSN 0021-9258. PMID 15456759. 
5. ^ Manke, Isaac A; Lowery Drew M, Nguyen Anhco, Yaffe Michael B (Oct. 2003). "BRCT repeats as phosphopeptide-binding modules involved in protein targeting". Science (United States) 302 (5645): 636–9. doi:10.1126/science.1088877. PMID 14576432. 

Further reading

• "Toward a complete human genome sequence.". Genome Res. 8 (11): 1097–108. 1999. doi:10.1101/gr.8.11.1097. PMID 9847074. 
• Lechner MS, Levitan I, Dressler GR (2000). "PTIP, a novel BRCT domain-containing protein interacts with Pax2 and is associated with active chromatin.". Nucleic Acids Res. 28 (14): 2741–51. doi:10.1093/nar/28.14.2741. PMC 102659. PMID 10908331. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=102659. 
• Hoffmeister A, Ropolo A, Vasseur S, et al. (2002). "The HMG-I/Y-related protein p8 binds to p300 and Pax2 trans-activation domain-interacting protein to regulate the trans-activation activity of the Pax2A and Pax2B transcription factors on the glucagon gene promoter.". J. Biol. Chem. 277 (25): 22314–9. doi:10.1074/jbc.M201657200. PMID 11940591. 
• 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. 
• Cho EA, Prindle MJ, Dressler GR (2003). "BRCT domain-containing protein PTIP is essential for progression through mitosis.". Mol. Cell. Biol. 23 (5): 1666–73. doi:10.1128/MCB.23.5.1666-1673.2003. PMC 151700. PMID 12588986. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=151700. 
• Manke IA, Lowery DM, Nguyen A, Yaffe MB (2003). "BRCT repeats as phosphopeptide-binding modules involved in protein targeting.". Science 302 (5645): 636–9. doi:10.1126/science.1088877. PMID 14576432. 
• 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. 
• Jowsey PA, Doherty AJ, Rouse J (2005). "Human PTIP facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation.". J. Biol. Chem. 279 (53): 55562–9. doi:10.1074/jbc.M411021200. PMID 15456759. 
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
• Cho YW, Hong T, Hong S, et al. (2007). "PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex.". J. Biol. Chem. 282 (28): 20395–406. doi:10.1074/jbc.M701574200. PMC 2729684. PMID 17500065. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2729684. 
• Munoz IM, Jowsey PA, Toth R, Rouse J (2007). "Phospho-epitope binding by the BRCT domains of hPTIP controls multiple aspects of the cellular response to DNA damage.". Nucleic Acids Res. 35 (16): 5312–22. doi:10.1093/nar/gkm493. PMC 2018624. PMID 17690115. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2018624.