SRSF protein kinase 2

Details

Name
SRSF protein kinase 2
Synonyms
  • 2.7.11.1
  • Serine/arginine-rich protein-specific kinase 2
  • SFRS protein kinase 2
  • SR-protein-specific kinase 2
Gene Name
SRPK2
Organism
Humans
Amino acid sequence
>lcl|BSEQ0037279|SRSF protein kinase 2 MSVNSEKSSSSERPEPQQKAPLVPPPPPPPPPPPPPLPDPTPPEPEEEILGSDDEEQEDP ADYCKGGYHPVKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTE TALDEIKLLKCVRESDPSDPNKDMVVQLIDDFKISGMNGIHVCMVFEVLGHHLLKWIIKS NYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDAYVRRMAAEATEWQ KAGAPPPSGSAVSTAPQQKPIGKISKNKKKKLKKKQKRQAELLEKRLQEIEELEREAERK IIEENITSAAPSNDQDGEYCPEVKLKTTGLEEAAEAETAKDNGEAEDQEEKEDAEKENIE KDEDDVDQELANIDPTWIESPKTNGHIENGPFSLEQQLDDEDDDEEDCPNPEEYNLDEPN AESDYTYSSSYEQFNGELPNGRHKIPESQFPEFSTSLFSGSLEPVACGSVLSEGSPLTEQ EESSPSHDRSRTVSASSTGDLPKAKTRAADLLVNPLDPRNADKIRVKIADLGNACWVHKH FTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSGEDYSRDEDHIA HIIELLGSIPRHFALSGKYSREFFNRRGELRHITKLKPWSLFDVLVEKYGWPHEDAAQFT DFLIPMLEMVPEKRASAGECLRHPWLNS
Number of residues
688
分子量
77525.955
Theoretical pI
4.65
GO Classification
Functions
14-3-3 protein binding/ATP binding/magnesium ion binding/poly(A) RNA binding/protein serine/threonine kinase activity
Processes
angiogenesis/cell differentiation/innate immune response/intracellular signal transduction/negative regulation of viral genome replication/nuclear speck organization/positive regulation of cell cycle/positive regulation of cell proliferation/positive regulation of gene expression/positive regulation of neuron apoptotic process/positive regulation of viral genome replication/protein phosphorylation/regulation of mRNA splicing, via spliceosome/RNA splicing/spliceosomal complex assembly
Components
cytoplasm/nucleolus/nucleoplasm/nucleus
General Function
Protein serine/threonine kinase activity
Specific Function
丝氨酸/ arginine-rich蛋白特异性激酶specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Promotes neuronal apoptosis by up-regulating cyclin-D1 (CCND1) expression. This is done by the phosphorylation of SRSF2, leading to the suppression of p53/TP53 phosphorylation thereby relieving the repressive effect of p53/TP53 on cyclin-D1 (CCND1) expression. Phosphorylates ACIN1, and redistributes it from the nuclear speckles to the nucleoplasm, resulting in cyclin A1 but not cyclin A2 up-regulation. Plays an essential role in spliceosomal B complex formation via the phosphorylation of DDX23/PRP28. Can mediate hepatitis B virus (HBV) core protein phosphorylation. Plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>拼箱| BSEQ0019557 | SRSF蛋白激酶2 (SRPK2 ATG)TCAGTTAACTCTGAGAAGTCGTCCTCTTCAGAAAGGCCGGAGCCTCAACAGAAAGCT CCTTTAGTTCCTCCTCCTCCACCGCCACCACCACCACCACCGCCACCTTTGCCAGACCCC ACACCCCCGGAGCCAGAGGAGGAGATCCTGGGATCAGATGATGAGGAGCAAGAGGACCCT GCGGACTACTGCAAAGGTGGATATCATCCAGTGAAAATTGGAGACCTCTTCAATGGCCGG TATCATGTTATTAGAAAGCTTGGATGGGGGCACTTCTCTACTGTCTGGCTGTGCTGGGAT ATGCAGGGGAAAAGATTTGTTGCAATGAAAGTTGTAAAAAGTGCCCAGCATTATACGGAG ACAGCCTTGGATGAAATAAAATTGCTCAAATGTGTTCGAGAAAGTGATCCCAGTGACCCA AACAAAGACATGGTGGTCCAGCTCATTGACGACTTCAAGATTTCAGGCATGAATGGGATA CATGTCTGCATGGTCTTCGAAGTACTTGGCCACCATCTCCTCAAGTGGATCATCAAATCC AACTATCAAGGCCTCCCAGTACGTTGTGTGAAGAGTATCATTCGACAGGTCCTTCAAGGG TTAGATTACTTACACAGTAAGTGCAAGATCATTCATACTGACATAAAGCCGGAAAATATC TTGATGTGTGTGGATGATGCATATGTGAGAAGAATGGCAGCTGAGGCCACTGAGTGGCAG AAAGCAGGTGCTCCTCCTCCTTCAGGGTCTGCAGTGAGTACGGCTCCACAGCAGAAACCT ATAGGAAAAATATCTAAAAACAAAAAGAAAAAACTGAAAAAGAAACAGAAGAGGCAGGCT GAGTTATTGGAGAAGCGCCTGCAGGAGATAGAAGAATTGGAGCGAGAAGCTGAAAGGAAA ATAATAGAAGAAAACATCACCTCAGCTGCACCTTCCAATGACCAGGATGGCGAATACTGC CCAGAGGTGAAACTAAAAACAACAGGATTAGAGGAGGCGGCTGAGGCAGAGACTGCAAAG GACAATGGTGAAGCTGAGGACCAGGAAGAGAAAGAAGATGCTGAGAAAGAAAACATTGAA AAAGATGAAGATGATGTAGATCAGGAACTTGCGAACATAGACCCTACGTGGATAGAATCA CCTAAAACCAATGGCCATATTGAGAATGGCCCATTCTCACTGGAGCAGCAACTGGACGAT GAAGATGATGATGAAGAAGACTGCCCAAATCCTGAGGAATATAATCTTGATGAGCCAAAT GCAGAAAGTGATTACACATATAGCAGCTCCTATGAACAATTCAATGGTGAATTGCCAAAT GGACGACATAAAATTCCCGAGTCACAGTTCCCAGAGTTTTCCACCTCGTTGTTCTCTGGA TCCTTAGAACCTGTGGCCTGCGGCTCTGTGCTTTCTGAGGGATCACCACTTACTGAGCAA GAGGAGAGCAGTCCATCCCATGACAGAAGCAGAACGGTTTCAGCCTCCAGTACTGGGGAT TTGCCAAAAGCAAAAACCCGGGCAGCTGACTTGTTGGTGAATCCCCTGGATCCGCGGAAT GCAGATAAAATTAGAGTAAAAATTGCTGACCTGGGAAATGCTTGTTGGGTGCATAAACAC TTCACGGAAGACATCCAGACGCGTCAGTACCGCTCCATAGAGGTTTTAATAGGAGCGGGG TACAGCACCCCTGCGGACATCTGGAGCACGGCGTGTATGGCATTTGAGCTGGCAACGGGA GATTATTTGTTTGAACCACATTCTGGGGAAGACTATTCCAGAGACGAAGACCACATAGCC CACATCATAGAGCTGCTAGGCAGTATTCCAAGGCACTTTGCTCTATCTGGAAAATATTCT CGGGAATTCTTCAATCGCAGAGGAGAACTGCGACACATCACCAAGCTGAAGCCCTGGAGC CTCTTTGATGTACTTGTGGAAAAGTATGGCTGGCCCCATGAAGATGCTGCACAGTTTACA GATTTCCTGATCCCGATGTTAGAAATGGTTCCAGAAAAACGAGCCTCAGCTGGCGAATGC CTTCGGCATCCTTGGTTGAATTCTTAG
Chromosome Location
7
Locus
7q22-q31.1
External Identifiers
Resource Link
UniProtKB ID P78362
UniProtKB Entry Name SRPK2_HUMAN
GenBank Protein ID 1857944
GenBank Gene ID U88666
HGNC ID HGNC:11306
一般引用
  1. Wang HY, Lin W, Dyck JA, Yeakley JM, Songyang Z, Cantley LC, Fu XD: 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. 1998 Feb 23;140(4):737-50. [Article]
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  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  4. Daub H, Blencke S, Habenberger P, Kurtenbach A, Dennenmoser J, Wissing J, Ullrich A, Cotten M: Identification of SRPK1 and SRPK2 as the major cellular protein kinases phosphorylating hepatitis B virus core protein. J Virol. 2002 Aug;76(16):8124-37. [Article]
  5. Brill LM, Salomon AR, Ficarro SB, Mukherji M, Stettler-Gill M, Peters EC: Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry. Anal Chem. 2004 May 15;76(10):2763-72. [Article]
  6. Zheng Y, Fu XD, Ou JH: Suppression of hepatitis B virus replication by SRPK1 and SRPK2 via a pathway independent of the phosphorylation of the viral core protein. Virology. 2005 Nov 10;342(1):150-8. Epub 2005 Aug 24. [Article]
  7. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [Article]
  8. Jang SW, Yang SJ, Ehlen A, Dong S, Khoury H, Chen J, Persson JL, Ye K: Serine/arginine protein-specific kinase 2 promotes leukemia cell proliferation by phosphorylating acinus and regulating cyclin A1. Cancer Res. 2008 Jun 15;68(12):4559-70. doi: 10.1158/0008-5472.CAN-08-0021. [Article]
  9. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. [Article]
  10. Mathew R, Hartmuth K, Mohlmann S, Urlaub H, Ficner R, Luhrmann R: Phosphorylation of human PRP28 by SRPK2 is required for integration of the U4/U6-U5 tri-snRNP into the spliceosome. Nat Struct Mol Biol. 2008 May;15(5):435-43. doi: 10.1038/nsmb.1415. Epub 2008 Apr 20. [Article]
  11. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [Article]
  12. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [Article]
  13. Jang SW, Liu X, Fu H, Rees H, Yepes M, Levey A, Ye K: Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell cycle and cell death in neurons. J Biol Chem. 2009 Sep 4;284(36):24512-25. doi: 10.1074/jbc.M109.026237. Epub 2009 Jul 10. [Article]
  14. Mayya V,朗格DH、黄SI Rezaul K, L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [Article]
  15. Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475. [Article]
  16. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  17. Edmond V, Moysan E, Khochbin S, Matthias P, Brambilla C, Brambilla E, Gazzeri S, Eymin B: Acetylation and phosphorylation of SRSF2 control cell fate decision in response to cisplatin. EMBO J. 2011 Feb 2;30(3):510-23. doi: 10.1038/emboj.2010.333. Epub 2010 Dec 14. [Article]
  18. Giannakouros T, Nikolakaki E, Mylonis I, Georgatsou E: Serine-arginine protein kinases: a small protein kinase family with a large cellular presence. FEBS J. 2011 Feb;278(4):570-86. doi: 10.1111/j.1742-4658.2010.07987.x. Epub 2011 Jan 12. [Article]
  19. Hong Y, Jang SW, Ye K: The N-terminal fragment from caspase-cleaved serine/arginine protein-specific kinase2 (SRPK2) translocates into the nucleus and promotes apoptosis. J Biol Chem. 2011 Jan 7;286(1):777-86. doi: 10.1074/jbc.M110.193441. Epub 2010 Nov 5. [Article]
  20. Rigbolt KT, Prokhorova TA, Akimov V, Henningsen J, Johansen PT, Kratchmarova I, Kassem M, Mann M, Olsen JV, Blagoev B: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci Signal. 2011 Mar 15;4(164):rs3. doi: 10.1126/scisignal.2001570. [Article]
  21. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
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Drug Relations

Drug Relations
DrugBank ID Name Drug group Ph值armacological action? Actions Details
DB00173 Adenine approved, nutraceutical unknown Details
DB04395 Ph值osphoaminophosphonic Acid-Adenylate Ester experimental unknown Details
DB02733 Purvalanol experimental unknown Details