PAXIP1

PAX interacting (with transcription-activation domain) protein 1
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 3SQD​
Identifiers
Symbols	PAXIP1 ; CAGF28; CAGF29; PACIP1; PAXIP1L; PTIP; TNRC2
External IDs	OMIM: 608254 MGI: 1890430 HomoloGene: 133914 GeneCards: PAXIP1 Gene
Gene ontology Molecular function • protein binding Cellular component • nucleus • nuclear matrix • histone methyltransferase complex Biological process • positive regulation of histone H3-K36 methylation • vasculogenesis • DNA repair • DNA recombination • transcription, DNA-templated • response to ionizing radiation • DNA damage response, signal transduction by p53 class mediator • positive regulation of protein ubiquitination • positive regulation of histone acetylation • endothelial cell migration • 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 • adipose tissue development • chorion development Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	22976	55982
Ensembl	ENSG00000157212	ENSMUSG00000002221
UniProt	Q6ZW49	Q6NZQ4
RefSeq (mRNA)	NM_007349	NM_018878
RefSeq (protein)	NP_031375	NP_061366
Location (UCSC)	Chr 7: 154.94 – 155 Mb	Chr 5: 27.74 – 27.79 Mb
PubMed search

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

Function

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 (July 1997). "cDNAs with long CAG trinucleotide repeats from human brain". Hum. Genet. 100 (1): 114–22. doi:10.1007/s004390050476. PMID 9225980.
2. "Entrez Gene: PAXIP1 PAX interacting (with transcription-activation domain) protein 1".
3. Lechner MS, Levitan I, Dressler GR (July 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.
4. Jowsey PA, Doherty AJ, Rouse J (December 2004). "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.
5. Manke IA, Lowery DM, Nguyen A, Yaffe MB (October 2003). "BRCT repeats as phosphopeptide-binding modules involved in protein targeting". Science 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. 1998. 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.
• Hoffmeister A, Ropolo A, Vasseur S, Mallo GV, Bodeker H, Ritz-Laser B, Dressler GR, Vaccaro MI, Dagorn JC, Moreno S, Iovanna JL (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.
• 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.
• 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.
• Jowsey PA, Doherty AJ, Rouse J (2004). "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, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (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, Guo H, Yu H, Kim D, Guszczynski T, Dressler GR, Copeland TD, Kalkum M, Ge K (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.
• 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.