CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000821
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 SRSF protein kinase 2 
Protein Synonyms/Alias
 SFRS protein kinase 2; Serine/arginine-rich protein-specific kinase 2; SR-protein-specific kinase 2; SRSF protein kinase 2 N-terminal; SRSF protein kinase 2 C-terminal 
Gene Name
 Srpk2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
128LDEIKLLKCVRESDPubiquitination[1]
207DYLHSKCKIIHTDIKubiquitination[1]
214KIIHTDIKPENILMCubiquitination[1]
239AEATEWQKAGAPPPSubiquitination[1]
532GNACWVHKHFTEDIQacetylation[2]
611RHFALSGKYSREFFNubiquitination[1, 3]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965
Functional Description
 Serine/arginine-rich protein-specific kinase which 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. 
Sequence Annotation
 DOMAIN 79 681 Protein kinase.
 NP_BIND 85 93 ATP (By similarity).
 ACT_SITE 212 212 Proton acceptor (By similarity).
 BINDING 108 108 ATP (By similarity).
 MOD_RES 50 50 Phosphoserine; by CK2 (By similarity).
 MOD_RES 378 378 Phosphoserine (By similarity).
 MOD_RES 485 485 Phosphothreonine; by PKB/AKT1 (By
 MOD_RES 487 487 Phosphoserine (By similarity).
 MOD_RES 490 490 Phosphoserine (By similarity).
 MOD_RES 581 581 Phosphoserine; by CK2 (By similarity).  
Keyword
 ATP-binding; Complete proteome; Cytoplasm; Differentiation; Kinase; mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 681 AA 
Protein Sequence
MSVNSEKSSS SERPEPQQKA PLVPPPPPPP PPPPLPDPAP PEPEEEILGS DDEEQEDPAD 60
YCKGGYHPVK IGDLFNGRYH VIRKLGWGHF STVWLCWDMQ GKRFVAMKVV KSAQHYTETA 120
LDEIKLLKCV RESDPSDPNK DMVVQLIDDF KISGMNGIHV CMVFEVLGHH LLKWIIKSNY 180
QGLPVRCVKS IIRQVLQGLD YLHSKCKIIH TDIKPENILM CVDDAYVRRM AAEATEWQKA 240
GAPPPSGSAV STAPQQKPIG KISKNKKKKL KKKQKRQAEL LEKRLQEIEE LEREAERKIL 300
EENITSAEAS GEQDGEYQPE VTLKAADLED TTEEETAKDN GEVEDQEEKE DAEKENAEKD 360
EDDVEQELAN LDPTWVESPK ANGHIENGPF SLEQQLEDEE DDEDDCANPE EYNLDEPNAE 420
SDYTYSSSYE QFNGELPNGQ HKTSEFPTPL FSGPLEPVAC GSVISEGSPL TEQEESSPSH 480
DRSRTVSASS TGDLPKTKTR AADLLVNPLD PRNADKIRVK IADLGNACWV HKHFTEDIQT 540
RQYRSIEVLI GAGYSTPADI WSTACMAFEL ATGDYLFEPH SGEDYSRDED HIAHIIELLG 600
SIPRHFALSG KYSREFFNRR GELRHITKLK PWSLFDVLVE KYGWPHEDAA QFTDFLIPML 660
EMVPEKRASA GECLRHPWLN S 681 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IEA:Compara.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0071889; F:14-3-3 protein binding; IDA:BHF-UCL.
 GO:0005524; F:ATP binding; IDA:UniProtKB.
 GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
 GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
 GO:0001525; P:angiogenesis; IDA:BHF-UCL.
 GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
 GO:0007243; P:intracellular protein kinase cascade; IDA:UniProtKB.
 GO:0045071; P:negative regulation of viral genome replication; ISS:BHF-UCL.
 GO:0035063; P:nuclear speck organization; IDA:BHF-UCL.
 GO:0045787; P:positive regulation of cell cycle; IDA:BHF-UCL.
 GO:0008284; P:positive regulation of cell proliferation; IDA:BHF-UCL.
 GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL.
 GO:0043525; P:positive regulation of neuron apoptotic process; IDA:BHF-UCL.
 GO:0045070; P:positive regulation of viral genome replication; ISS:BHF-UCL.
 GO:0000245; P:spliceosomal complex assembly; IDA:UniProtKB. 
Interpro
 IPR011009; Kinase-like_dom.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 IPR008271; Ser/Thr_kinase_AS. 
Pfam
 PF00069; Pkinase 
SMART
  
PROSITE
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST 
PRINTS