PAXIP1

PAXIP1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3SQD
Identifiers
Aliases	PAXIP1, CAGF29, PACIP1, PAXIP1L, PTIP, TNRC2, CAGF28, PAX interacting protein 1
External IDs	OMIM: 608254; MGI: 1890430; HomoloGene: 133914; GeneCards: PAXIP1; OMA:PAXIP1 - orthologs
Gene location (Human) Chr. Chromosome 7 (human) Band 7q36.2 Start 154,943,687 bp End 155,003,124 bp
Gene location (Mouse) Chr. Chromosome 5 (mouse) Band 5 B1|5 13.23 cM Start 27,945,078 bp End 27,996,689 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in secondary oocyte cerebellar hemisphere ventricular zone right hemisphere of cerebellum corpus epididymis thymus cerebellar vermis cartilage tissue embryo ganglionic eminence Top expressed in tail of embryo genital tubercle epiblast ventricular zone zygote islet of Langerhans thymus otic placode spermatid primitive streak More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding Cellular component nuclear matrix nucleoplasm MLL3/4 complex nucleus histone methyltransferase complex chromosome Biological process response to ionizing radiation positive regulation of histone H3-K36 methylation DNA recombination regulation of transcription, DNA-templated chorion development DNA damage response, signal transduction by p53 class mediator transcription, DNA-templated positive regulation of histone acetylation cellular response to DNA damage stimulus vasculogenesis positive regulation of isotype switching histone H3-K4 methylation positive regulation of histone H3-K4 methylation adipose tissue development double-strand break repair via nonhomologous end joining positive regulation of protein ubiquitination endothelial cell migration DNA repair positive regulation of transcription initiation from RNA polymerase II promoter regulation of cell cycle G2/M phase transition positive regulation of isotype switching to IgG isotypes positive regulation of response to DNA damage stimulus negative regulation of DNA-binding transcription factor activity Sources:Amigo / QuickGO
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: 27.95 – 28 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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

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.

Interactions

PAXIP1 has been shown to interact with PAX2 and TP53BP1.

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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• 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.