PRPF4B

PRP4 pre-mRNA processing factor 4 homolog B (yeast)

Identifiers

PRPF4B; KIAA0536; PR4H; PRP4; PRP4H; PRP4K; dJ1013A10.1

External IDs

OMIM: 602338 MGI: 109584 HomoloGene: 8472 GeneCards: PRPF4B Gene

2.7.11.1

Gene Ontology
Molecular function	• nucleotide binding • protein kinase activity • protein serine/threonine kinase activity • protein binding • ATP binding
Cellular component	• nucleus • chromosome • nucleolus • catalytic step 2 spliceosome
Biological process	• nuclear mRNA splicing, via spliceosome • protein phosphorylation • RNA splicing
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 6:
4.02 – 4.07 Mb

Chr 13:
34.97 – 34.99 Mb

PubMed search

[1]

[2]

Serine/threonine-protein kinase PRP4 homolog is an enzyme that in humans is encoded by the PRPF4B gene.^[1]^[2]^[3]

Pre-mRNA splicing occurs in two sequential transesterification steps, and the protein encoded by this gene is thought to be involved in pre-mRNA splicing and in signal transduction. This protein belongs to a kinase family that includes serine/arginine-rich protein-specific kinases and cyclin-dependent kinases (CDKs). This protein is regarded as a CDK-like kinase (Clk) with homology to mitogen-activated protein kinases (MAPKs).^[3]

Interactions

PRPF4B has been shown to interact with Pinin.^[4]

References

^ Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (Aug 1998). "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Res 5 (1): 31–9. doi:10.1093/dnares/5.1.31. PMID 9628581.
^ Kojima T, Zama T, Wada K, Onogi H, Hagiwara M (Aug 2001). "Cloning of human PRP4 reveals interaction with Clk1". J Biol Chem 276 (34): 32247–56. doi:10.1074/jbc.M103790200. PMID 11418604.
^ ^a ^b "Entrez Gene: PRPF4B PRP4 pre-mRNA processing factor 4 homolog B (yeast)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8899.
^ Dellaire, Graham; Makarov Evgeny M, Cowger Jeff J M, Longman Dasa, Sutherland Heidi G E, Lührmann Reinhard, Torchia Joseph, Bickmore Wendy A (Jul. 2002). "Mammalian PRP4 Kinase Copurifies and Interacts with Components of Both the U5 snRNP and the N-CoR Deacetylase Complexes". Mol. Cell. Biol. (United States) 22 (14): 5141–56. doi:10.1128/MCB.22.14.5141-5156.2002. ISSN 0270-7306. PMC 139773. PMID 12077342. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139773.

Schultz SJ, Nigg EA (1994). "Identification of 21 novel human protein kinases, including 3 members of a family related to the cell cycle regulator nimA of Aspergillus nidulans". Cell Growth Differ. 4 (10): 821–30. PMID 8274451.
Gross T, Lützelberger M, Weigmann H, et al. (1997). "Functional analysis of the fission yeast Prp4 protein kinase involved in pre-mRNA splicing and isolation of a putative mammalian homologue". Nucleic Acids Res. 25 (5): 1028–35. doi:10.1093/nar/25.5.1028. PMC 146536. PMID 9102632. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=146536.
Huang Y, Deng T, Winston BW (2000). "Characterization of hPRP4 kinase activation: potential role in signaling". Biochem. Biophys. Res. Commun. 271 (2): 456–63. doi:10.1006/bbrc.2000.2651. PMID 10799319.
Jurica MS, Licklider LJ, Gygi SR, et al. (2002). "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis". RNA 8 (4): 426–39. doi:10.1017/S1355838202021088. PMC 1370266. PMID 11991638. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1370266.
Dellaire G, Makarov EM, Cowger JJ, et al. (2002). "Mammalian PRP4 Kinase Copurifies and Interacts with Components of Both the U5 snRNP and the N-CoR Deacetylase Complexes". Mol. Cell. Biol. 22 (14): 5141–56. doi:10.1128/MCB.22.14.5141-5156.2002. PMC 139773. PMID 12077342. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139773.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Brandenberger R, Wei H, Zhang S, et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=514446.
Bennett EM, Lever AM, Allen JF (2004). "Human Immunodeficiency Virus Type 2 Gag Interacts Specifically with PRP4, a Serine-Threonine Kinase, and Inhibits Phosphorylation of Splicing Factor SF2". J. Virol. 78 (20): 11303–12. doi:10.1128/JVI.78.20.11303-11312.2004. PMC 521795. PMID 15452250. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=521795.
Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455.
Zhang Y, Wolf-Yadlin A, Ross PL, et al. (2005). "Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules". Mol. Cell Proteomics 4 (9): 1240–50. doi:10.1074/mcp.M500089-MCP200. PMID 15951569.
Stelzl U, Worm U, Lalowski M, et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
Nousiainen M, Silljé HH, Sauer G, et al. (2006). "Phosphoproteome analysis of the human mitotic spindle". Proc. Natl. Acad. Sci. U.S.A. 103 (14): 5391–6. doi:10.1073/pnas.0507066103. PMC 1459365. PMID 16565220. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1459365.
Beausoleil SA, Villén J, Gerber SA, et al. (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243.
Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1847948.
Huang B, Ahn YT, McPherson L, et al. (2007). "Interaction of PRP4 with Krüppel-Like Factor 13 Regulates CCL5 Transcription". J. Immunol. 178 (11): 7081–7. PMC 2674583. PMID 17513757. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2674583.

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 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°)

PRPF4B

Interactions

References

Further reading