SRPK2

SRPK2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2X7G
Identifiers
Aliases	SRPK2, SFRSK2, SRSF protein kinase 2
External IDs	MGI: 1201408 HomoloGene: 101663 GeneCards: SRPK2
Genetically Related Diseases
myopia[1]
Gene ontology Molecular function • transferase activity • nucleotide binding • protein kinase activity • 14-3-3 protein binding • kinase activity • protein serine/threonine kinase activity • protein binding • poly(A) RNA binding • ATP binding • magnesium ion binding Cellular component • cytoplasm • nucleoplasm • nucleolus • nucleus Biological process • cell differentiation • intracellular signal transduction • nuclear speck organization • phosphorylation • mRNA processing • regulation of mRNA splicing, via spliceosome • protein phosphorylation • spliceosomal complex assembly • positive regulation of neuron apoptotic process • negative regulation of viral genome replication • positive regulation of gene expression • positive regulation of cell cycle • angiogenesis • RNA splicing • positive regulation of cell proliferation • positive regulation of viral genome replication • innate immune response Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	6733	20817
Ensembl	ENSG00000135250	ENSMUSG00000062604
UniProt	P78362	O54781
RefSeq (mRNA)	NM_001278273 NM_182691 NM_182692	NM_009274
RefSeq (protein)	NP_001265202.1 NP_872633.1 NP_872634.1	NP_033300.2
Location (UCSC)	Chr 7: 105.11 – 105.4 Mb	Chr 5: 23.5 – 23.68 Mb
PubMed search	[2]	[3]
Wikidata

View/Edit Human

View/Edit Mouse

Serine/threonine-protein kinase SRPK2 is an enzyme that in humans is encoded by the SRPK2 gene.^[4][5][6]

Interactions

SRPK2 has been shown to interact with:

• ASF/SF2^[5][7][8] and
• U2AF2.^[5][9]

References

1. "Diseases that are genetically associated with SRPK2 view/edit references on wikidata".
2. "Human PubMed Reference:".
3. "Mouse PubMed Reference:".
4. Gui JF, Lane WS, Fu XD (Jul 1994). "A serine kinase regulates intracellular localization of splicing factors in the cell cycle". Nature. 369 (6482): 678–82. doi:10.1038/369678a0. PMID 8208298.
5. Wang HY, Lin W, Dyck JA, Yeakley JM, Songyang Z, Cantley LC, Fu XD (Mar 1998). "SRPK2: a differentially expressed SR protein-specific kinase involved in mediating the interaction and localization of pre-mRNA splicing factors in mammalian cells". J Cell Biol. 140 (4): 737–50. doi:10.1083/jcb.140.4.737. PMC 2141757. PMID 9472028.
6. "Entrez Gene: SRPK2 SFRS protein kinase 2".
7. Umehara H, Nishii Y, Morishima M, Kakehi Y, Kioka N, Amachi T, Koizumi J, Hagiwara M, Ueda K (Feb 2003). "Effect of cisplatin treatment on speckled distribution of a serine/arginine-rich nuclear protein CROP/Luc7A". Biochem. Biophys. Res. Commun. 301 (2): 324–9. doi:10.1016/s0006-291x(02)03017-6. PMID 12565863.
8. Koizumi J, Okamoto Y, Onogi H, Mayeda A, Krainer AR, Hagiwara M (Apr 1999). "The subcellular localization of SF2/ASF is regulated by direct interaction with SR protein kinases (SRPKs)". J. Biol. Chem. 274 (16): 11125–31. doi:10.1074/jbc.274.16.11125. PMID 10196197.
9. Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.

Further reading

• 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.
• Kuroyanagi N, Onogi H, Wakabayashi T, Hagiwara M (1998). "Novel SR-protein-specific kinase, SRPK2, disassembles nuclear speckles.". Biochem. Biophys. Res. Commun. 242 (2): 357–64. doi:10.1006/bbrc.1997.7913. PMID 9446799.
• Koizumi J, Okamoto Y, Onogi H, Mayeda A, Krainer AR, Hagiwara M (1999). "The subcellular localization of SF2/ASF is regulated by direct interaction with SR protein kinases (SRPKs)". J. Biol. Chem. 274 (16): 11125–31. doi:10.1074/jbc.274.16.11125. PMID 10196197.
• Daub H, Blencke S, Habenberger P, Kurtenbach A, Dennenmoser J, Wissing J, Ullrich A, Cotten M (2002). "Identification of SRPK1 and SRPK2 as the major cellular protein kinases phosphorylating hepatitis B virus core protein". J. Virol. 76 (16): 8124–37. doi:10.1128/JVI.76.16.8124-8137.2002. PMC 155132. PMID 12134018.
• Brill LM, Salomon AR, Ficarro SB, Mukherji M, Stettler-Gill M, Peters EC (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:10.1021/ac035352d. PMID 15144186.
• Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455.
• Zheng Y, Fu XD, Ou JH (2005). "Suppression of hepatitis B virus replication by SRPK1 and SRPK2 via a pathway independent of the phosphorylation of the viral core protein". Virology. 342 (1): 150–8. doi:10.1016/j.virol.2005.07.030. PMID 16122776.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.