PARD3
From Wikipedia, the free encyclopedia
Par-3 partitioning defective 3 homolog (C. elegans)
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Identifiers | ||||||||||||||
Symbol(s) | PARD3; ASIP; PAR3; Baz; Bazooka; FLJ21015; PAR3alpha; PARD3A; SE2-5L16; SE2-5LT1; SE2-5T2 | |||||||||||||
External IDs | OMIM: 606745 MGI: 2135608 HomoloGene: 10489 | |||||||||||||
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RNA expression pattern | ||||||||||||||
Orthologs | ||||||||||||||
Human | Mouse | |||||||||||||
Entrez | 56288 | 93742 | ||||||||||||
Ensembl | ENSG00000148498 | ENSMUSG00000025812 | ||||||||||||
Uniprot | Q8TEW0 | Q4JJC0 | ||||||||||||
Refseq | NM_019619 (mRNA) NP_062565 (protein) |
NM_001013580 (mRNA) NP_001013598 (protein) |
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Location | Chr 10: 34.44 - 35.14 Mb | Chr 8: 129.95 - 130.5 Mb | ||||||||||||
Pubmed search | [1] | [2] |
Par-3 partitioning defective 3 homolog (C. elegans), also known as PARD3, is a human gene.[1]
PARD proteins, which were first identified in C. elegans, are essential for asymmetric cell division and polarized growth, whereas CDC42 (MIM 116952) mediates the establishment of cell polarity. The CDC42 GTPase, which is controlled by nucleotide exchange factors (GEFs; see MIM 606057) and GTPase-activating proteins (GAPs; see MIM 604980), interacts with a large set of effector proteins that typically contain a CDC42/RAC (MIM 602048)-interactive binding (CRIB) domain.[supplied by OMIM][1]
[edit] References
[edit] Further reading
- Joberty G, Petersen C, Gao L, Macara IG (2000). "The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42.". Nat. Cell Biol. 2 (8): 531–9. doi: . PMID 10934474.
- Johansson A, Driessens M, Aspenström P (2000). "The mammalian homologue of the Caenorhabditis elegans polarity protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and Rac1.". J. Cell. Sci. 113 ( Pt 18): 3267–75. PMID 10954424.
- Eichmuller S, Usener D, Dummer R, et al. (2001). "Serological detection of cutaneous T-cell lymphoma-associated antigens.". Proc. Natl. Acad. Sci. U.S.A. 98 (2): 629–34. doi: . PMID 11149944.
- Suzuki A, Yamanaka T, Hirose T, et al. (2001). "Atypical protein kinase C is involved in the evolutionarily conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures.". J. Cell Biol. 152 (6): 1183–96. PMID 11257119.
- Noda Y, Takeya R, Ohno S, et al. (2001). "Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C.". Genes Cells 6 (2): 107–19. PMID 11260256.
- Ebnet K, Suzuki A, Horikoshi Y, et al. (2001). "The cell polarity protein ASIP/PAR-3 directly associates with junctional adhesion molecule (JAM).". EMBO J. 20 (14): 3738–48. doi: . PMID 11447115.
- Fang CM, Xu YH (2002). "Down-regulated expression of atypical PKC-binding domain deleted asip isoforms in human hepatocellular carcinomas.". Cell Res. 11 (3): 223–9. doi: . PMID 11642408.
- Gao L, Macara IG, Joberty G (2003). "Multiple splice variants of Par3 and of a novel related gene, Par3L, produce proteins with different binding properties.". Gene 294 (1-2): 99–107. PMID 12234671.
- Kohjima M, Noda Y, Takeya R, et al. (2003). "PAR3beta, a novel homologue of the cell polarity protein PAR3, localizes to tight junctions.". Biochem. Biophys. Res. Commun. 299 (4): 641–6. PMID 12459187.
- 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: . PMID 12477932.
- Takekuni K, Ikeda W, Fujito T, et al. (2003). "Direct binding of cell polarity protein PAR-3 to cell-cell adhesion molecule nectin at neuroepithelial cells of developing mouse.". J. Biol. Chem. 278 (8): 5497–500. doi: . PMID 12515806.
- Warner DR, Pisano MM, Roberts EA, Greene RM (2003). "Identification of three novel Smad binding proteins involved in cell polarity.". FEBS Lett. 539 (1-3): 167–73. PMID 12650946.
- Brajenovic M, Joberty G, Küster B, et al. (2004). "Comprehensive proteomic analysis of human Par protein complexes reveals an interconnected protein network.". J. Biol. Chem. 279 (13): 12804–11. doi: . PMID 14676191.
- 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: . PMID 14702039.
- Navarro-Lérida I, Martínez Moreno M, Roncal F, et al. (2004). "Proteomic identification of brain proteins that interact with dynein light chain LC8.". Proteomics 4 (2): 339–46. doi: . PMID 14760703.
- Brill LM, Salomon AR, Ficarro SB, et al. (2004). "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry.". Anal. Chem. 76 (10): 2763–72. doi: . PMID 15144186.
- Liu XF, Ishida H, Raziuddin R, Miki T (2004). "Nucleotide exchange factor ECT2 interacts with the polarity protein complex Par6/Par3/protein kinase Czeta (PKCzeta) and regulates PKCzeta activity.". Mol. Cell. Biol. 24 (15): 6665–75. doi: . PMID 15254234.
- Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins.". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi: . PMID 15302935.
- Jin J, Smith FD, Stark C, et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization.". Curr. Biol. 14 (16): 1436–50. doi: . PMID 15324660.
- 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: . PMID 15489334.