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PRPF40A
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1UZC, 1YWI, 1YWJ, 1ZR7, 2CQN, 2DYF, 2KZG, 2L5F, 2L9V, 2LKS
Identifiers
Aliases	PRPF40A, FBP-11, FBP11, FLAF1, FNBP3, HIP-10, HIP10, HYPA, NY-REN-6, Prp40, pre-mRNA processing factor 40 homolog A
External IDs	OMIM: 612941; MGI: 1860512; HomoloGene: 6377; GeneCards: PRPF40A; OMA:PRPF40A - orthologs
Gene location (Human) Chr. Chromosome 2 (human) Band 2q23.3 Start 152,651,593 bp End 152,718,012 bp
Gene location (Mouse) Chr. Chromosome 2 (mouse) Band 2|2 C1.1 Start 53,134,704 bp End 53,191,284 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in secondary oocyte caput epididymis corpus epididymis tail of epididymis Achilles tendon epithelium of nasopharynx trabecular bone mucosa of paranasal sinus oral cavity visceral pleura Top expressed in tail of embryo genital tubercle spermatid spermatocyte ventricular zone Rostral migratory stream zygote abdominal wall embryo epiblast More reference expression data BioGPS More reference expression data
Gene ontology Molecular function proline-rich region binding protein binding RNA binding Cellular component nuclear matrix U1 snRNP U2-type prespliceosome membrane nucleus nucleoplasm cytosol nuclear speck Biological process cell division cell cycle mRNA processing regulation of cytokinesis cell migration cytoskeleton organization RNA splicing regulation of cell shape mRNA splicing, via spliceosome mRNA cis splicing, via spliceosome Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 55660 56194 Ensembl ENSG00000196504 ENSMUSG00000061136 UniProt O75400 Q9R1C7 RefSeq (mRNA) NM_017892 NM_001354432 NM_001354431 NM_001365596 NM_001365597 NM_001365598 NM_001365599 NM_001365600 NM_001365601 NM_001365602 NM_001365603 NM_001365604 NM_001365605 NM_001395472 NM_001395473 NM_001395475 NM_001395476 NM_001395477 NM_001395478 NM_001395479 NM_001395480 NM_001395481 NM_001395482 NM_001395483 NM_001395488 NM_018785 RefSeq (protein) NP_060362 NP_001341361 NP_001341360 NP_001352525 NP_001352526 NP_001352527 NP_001352528 NP_001352529 NP_001352530 NP_001352531 NP_001352532 NP_001352533 NP_001352534 NP_061255 NP_001357944 NP_001357945 NP_001357946 NP_001357947 NP_001357948 NP_001357949 Location (UCSC) Chr 2: 152.65 – 152.72 Mb Chr 2: 53.13 – 53.19 Mb PubMed search
Wikidata
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Pre-mRNA-processing factor 40 homolog A is a protein that in humans is encoded by the PRPF40A gene.

Interactions

PRPF40A has been shown to interact with Huntingtin.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000196504 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000061136 – 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. Bedford MT, Reed R, Leder P (September 1998). "WW domain-mediated interactions reveal a spliceosome-associated protein that binds a third class of proline-rich motif: the proline glycine and methionine-rich motif". Proc Natl Acad Sci U S A. 95 (18): 10602–7. Bibcode:1998PNAS...9510602B. doi:10.1073/pnas.95.18.10602. PMC 27941. PMID 9724750.
6. Wiesner S, Stier G, Sattler M, Macias MJ (December 2002). "Solution structure and ligand recognition of the WW domain pair of the yeast splicing factor Prp40". J Mol Biol. 324 (4): 807–22. doi:10.1016/S0022-2836(02)01145-2. PMID 12460579.
7. "Entrez Gene: PRPF40A PRP40 pre-mRNA processing factor 40 homolog A (S. cerevisiae)".
8. Faber PW, Barnes G T, Srinidhi J, Chen J, Gusella J F, MacDonald M E (September 1998). "Huntingtin interacts with a family of WW domain proteins". Hum. Mol. Genet. 7 (9): 1463–74. doi:10.1093/hmg/7.9.1463. ISSN 0964-6906. PMID 9700202.

Further reading

• Chan DC, Bedford MT, Leder P (1996). "Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains". EMBO J. 15 (5): 1045–54. doi:10.1002/j.1460-2075.1996.tb00442.x. PMC 450002. PMID 8605874.
• Bedford MT, Chan DC, Leder P (1997). "FBP WW domains and the Abl SH3 domain bind to a specific class of proline-rich ligands". EMBO J. 16 (9): 2376–83. doi:10.1093/emboj/16.9.2376. PMC 1169838. PMID 9171351.
• Faber PW, Barnes GT, Srinidhi J, et al. (1998). "Huntingtin interacts with a family of WW domain proteins". Hum. Mol. Genet. 7 (9): 1463–74. doi:10.1093/hmg/7.9.1463. PMID 9700202.
• Scanlan MJ, Gordan JD, Williamson B, et al. (1999). "Antigens recognized by autologous antibody in patients with renal-cell carcinoma". Int. J. Cancer. 83 (4): 456–64. doi:10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5. PMID 10508479. S2CID 21839750.
• Bedford MT, Sarbassova D, Xu J, et al. (2000). "A novel pro-Arg motif recognized by WW domains". J. Biol. Chem. 275 (14): 10359–69. doi:10.1074/jbc.275.14.10359. PMID 10744724.
• Zhang QH, Ye M, Wu XY, et al. (2001). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Res. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152.
• Wenzel J, Sanzenbacher R, Ghadimi M, et al. (2002). "Multiple interactions of the cytosolic polyproline region of the CD95 ligand: hints for the reverse signal transduction capacity of a death factor". FEBS Lett. 509 (2): 255–62. doi:10.1016/S0014-5793(01)03174-X. PMID 11741599. S2CID 33084576.
• Allen M, Friedler A, Schon O, Bycroft M (2002). "The structure of an FF domain from human HYPA/FBP11". J. Mol. Biol. 323 (3): 411–6. doi:10.1016/S0022-2836(02)00968-3. PMID 12381297.
• 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.
• Katoh M, Katoh M (2004). "Identification and characterization of human FNBP3 gene in silico". Int. J. Mol. Med. 12 (4): 651–6. doi:10.3892/ijmm.12.4.651. PMID 12964049.
• Busino L, Donzelli M, Chiesa M, et al. (2003). "Degradation of Cdc25A by beta-TrCP during S phase and in response to DNA damage". Nature. 426 (6962): 87–91. Bibcode:2003Natur.426...87B. doi:10.1038/nature02082. PMID 14603323. S2CID 768783.
• Mizutani K, Suetsugu S, Takenawa T (2004). "FBP11 regulates nuclear localization of N-WASP and inhibits N-WASP-dependent microspike formation". Biochem. Biophys. Res. Commun. 313 (3): 468–74. doi:10.1016/j.bbrc.2003.11.139. PMID 14697212.
• 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.
• 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. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. 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. Bibcode:2004CBio...14.1436J. doi:10.1016/j.cub.2004.07.051. PMID 15324660. S2CID 2371325.
• Goehler H, Lalowski M, Stelzl U, et al. (2004). "A protein interaction network links GIT1, an enhancer of huntingtin aggregation, to Huntington's disease". Mol. Cell. 15 (6): 853–65. doi:10.1016/j.molcel.2004.09.016. PMID 15383276.
• Lin KT, Lu RM, Tarn WY (2004). "The WW domain-containing proteins interact with the early spliceosome and participate in pre-mRNA splicing in vivo". Mol. Cell. Biol. 24 (20): 9176–85. doi:10.1128/MCB.24.20.9176-9185.2004. PMC 517884. PMID 15456888.
• 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.

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