MAPRE3

MAPRE3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1WYO, 3CO1, 3JAK, 3JAL, 3JAR, 3TQ7
Identifiers
Aliases	MAPRE3, EB3, EBF3, EBF3-S, RP3, microtubule associated protein RP/EB family member 3
External IDs	OMIM: 605788; MGI: 2140967; HomoloGene: 56565; GeneCards: MAPRE3; OMA:MAPRE3 - orthologs
Gene location (Human) Chr. Chromosome 2 (human)[1] Band 2p23.3 Start 26,970,637 bp[1] End 27,027,219 bp[1]
Gene location (Mouse) Chr. Chromosome 5 (mouse)[2] Band 5|5 B1 Start 30,971,985 bp[2] End 31,023,450 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Brodmann area 10 right hemisphere of cerebellum right frontal lobe right uterine tube middle frontal gyrus paraflocculus of cerebellum frontal pole cingulate gyrus anterior cingulate cortex anterior pituitary Top expressed in neural layer of retina superior frontal gyrus primary visual cortex dentate gyrus of hippocampal formation granule cell muscle of thigh perirhinal cortex cerebellar cortex CA3 field spermatid entorhinal cortex More reference expression data BioGPS More reference expression data
Gene ontology Molecular function microtubule binding protein binding identical protein binding protein C-terminus binding protein kinase binding microtubule plus-end binding Cellular component microtubule cytoskeleton microtubule plus-end perinuclear region of cytoplasm cytoplasmic microtubule midbody microtubule cytoskeleton cytoplasm microtubule organizing center spindle midzone mitotic spindle astral microtubule end Biological process positive regulation of transcription, DNA-templated cell cycle positive regulation of microtubule plus-end binding positive regulation of cyclin-dependent protein serine/threonine kinase activity cell division protein localization regulation of microtubule polymerization or depolymerization protein localization to microtubule positive regulation of protein kinase activity spindle assembly protein localization to microtubule plus-end Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 22924 100732 Ensembl ENSG00000084764 ENSMUSG00000029166 UniProt Q9UPY8 Q6PER3 RefSeq (mRNA) NM_001303050 NM_012326 NM_133350 NM_001310516 RefSeq (protein) NP_001289979 NP_036458 NP_001297445 NP_579928 Location (UCSC) Chr 2: 26.97 – 27.03 Mb Chr 5: 30.97 – 31.02 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Microtubule-associated protein RP/EB family member 3 is a protein that in humans is encoded by the MAPRE3 gene.[5][6]

The protein encoded by this gene is a member of the RP/EB family of genes. The protein localizes to the cytoplasmic microtubule network and binds APCL, a homolog of the adenomatous polyposis coli tumor suppressor gene.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000084764 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000029166 – 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. Renner C, Pfitzenmeier JP, Gerlach K, Held G, Ohnesorge S, Sahin U, Bauer S, Pfreundschuh M (Aug 1997). "RP1, a new member of the adenomatous polyposis coli-binding EB1-like gene family, is differentially expressed in activated T cells". J Immunol. 159 (3): 1276–83. doi:10.4049/jimmunol.159.3.1276. PMID 9233623. S2CID 23797920.
6. "Entrez Gene: MAPRE3 microtubule-associated protein, RP/EB family, member 3".

Further reading

• Juwana JP, Henderikx P, Mischo A, et al. (1999). "EB/RP gene family encodes tubulin binding proteins". Int. J. Cancer. 81 (2): 275–84. doi:10.1002/(SICI)1097-0215(19990412)81:2<275::AID-IJC18>3.0.CO;2-Z. PMID 10188731. S2CID 33232892.
• Nakagawa H, Koyama K, Murata Y, et al. (2000). "EB3, a novel member of the EB1 family preferentially expressed in the central nervous system, binds to a CNS-specific APC homologue". Oncogene. 19 (2): 210–6. doi:10.1038/sj.onc.1203308. PMID 10644998. S2CID 2284265.
• Su LK, Qi Y (2001). "Characterization of human MAPRE genes and their proteins". Genomics. 71 (2): 142–9. doi:10.1006/geno.2000.6428. PMID 11161807.
• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Bu W, Su LK (2004). "Characterization of functional domains of human EB1 family proteins". J. Biol. Chem. 278 (50): 49721–31. doi:10.1074/jbc.M306194200. PMID 14514668.
• Douglas MW, Diefenbach RJ, Homa FL, et al. (2004). "Herpes simplex virus type 1 capsid protein VP26 interacts with dynein light chains RP3 and Tctex1 and plays a role in retrograde cellular transport". J. Biol. Chem. 279 (27): 28522–30. doi:10.1074/jbc.M311671200. PMID 15117959.
• 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:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Mimori-Kiyosue Y, Grigoriev I, Lansbergen G, et al. (2005). "CLASP1 and CLASP2 bind to EB1 and regulate microtubule plus-end dynamics at the cell cortex". J. Cell Biol. 168 (1): 141–53. doi:10.1083/jcb.200405094. PMC 2171674. PMID 15631994.
• Yeh TY, Chuang JZ, Sung CH (2005). "Dynein light chain rp3 acts as a nuclear matrix-associated transcriptional modulator in a dynein-independent pathway". J. Cell Sci. 118 (Pt 15): 3431–43. doi:10.1242/jcs.02472. PMID 16079286.
• 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.