PRPF40A

From Wikipedia, the free encyclopedia

PRP40 pre-mRNA processing factor 40 homolog A (S. cerevisiae)

PDB rendering based on 1uzc.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1UZC, 1YWI, 1YWJ, 1ZR7, 2CQN, 2DYF, 2KZG, 2L5F, 2L9V, 2LKS

Identifiers

Symbols

PRPF40A; FBP-11; FBP11; FLAF1; FNBP3; HIP-10; HIP10; HYPA; NY-REN-6; Prp40

External IDs

OMIM: 612941 MGI: 1860512 HomoloGene: 6377 GeneCards: PRPF40A Gene

Gene Ontology
Molecular function	• protein binding • proline-rich region binding
Cellular component	• nucleus • nucleolus • nuclear matrix • nuclear speck
Biological process	• mRNA processing • cytoskeleton organization • cell cycle • regulation of cell shape • RNA splicing • cell migration • regulation of cytokinesis • cell division
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 2:
153.51 – 153.57 Mb

Chr 2:
53.13 – 53.19 Mb

PubMed search

Pre-mRNA-processing factor 40 homolog A is a protein that in humans is encoded by the PRPF40A gene.^[1]^[2]^[3]

Interactions

PRPF40A has been shown to interact with Huntingtin.^[4]

References

↑ Bedford MT, Reed R, Leder P (Sep 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. doi:10.1073/pnas.95.18.10602. PMC 27941. PMID 9724750.
↑ Wiesner S, Stier G, Sattler M, Macias MJ (Dec 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.
↑ "Entrez Gene: PRPF40A PRP40 pre-mRNA processing factor 40 homolog A (S. cerevisiae)".
↑ Faber, P W; Barnes G T, Srinidhi J, Chen J, Gusella J F, MacDonald M E (Sep 1998). "Huntingtin interacts with a family of WW domain proteins". Hum. Mol. Genet. (ENGLAND) 7 (9): 1463–74. doi:10.1093/hmg/7.9.1463. ISSN 0964-6906. PMID 9700202. Cite uses deprecated parameters (help)

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. 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.
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.
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. 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. 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. doi:10.1038/nature02082. PMID 14603323.
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. 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. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
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.

PDB gallery

1uzc: THE STRUCTURE OF AN FF DOMAIN FROM HUMAN HYPA/FBP11

1ywi: Structure of the FBP11WW1 domain complexed to the peptide APPTPPPLPP

1ywj: Structure of the FBP11WW1 domain

1zr7: Solution structure of the first WW domain of FBP11

2cqn: Solution structure of the FF domain of human Formin-binding protein 3

2dyf: Solution structure of the first WW domain of FBP11 / HYPA (FBP11 WW1) complexed with a PL (PPLP) motif peptide ligand

v t e Post-transcriptional modification

Nuclear	Precursor mRNA 5′ cap formation Polyadenylation CPSF CstF PAP PAB2 CFI CFII Poly(A)-binding protein RNA splicing: intron/exon snRNP spliceosome minor spliceosome U1 alternative splicing pre-mRNA processing factor PLRG1 PRPF3 PRPF4 PRPF4B PRPF6 PRPF8 PRPF18 PRPF19 PRPF31 PRPF38A PRPF38B PRPF39 PRPF40A PRPF40B RNA editing Polyuridylation

Cytosolic	5′ cap methylation Messenger RNA decapping: DCP1A DCP1B DCP2 DCPS EDC3 EDC4

see also: disorders of transcription and post transcriptional modification, Transcription B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)

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PRPF40A

Interactions

References

Further reading