UniProt Accession

 SRPK2_HUMAN; P78362; A8MVX2; O75220; O75221; Q6NUL0; Q6V1X2; Q8IYQ3 

Genbank Protein ID

 U88666; AC005070; AC005070; AC004884; AC073138; CH471070; BC035214; BC068547; BE781215; AY354201 

Genbank Nucleotide ID

 AAC05299.1; AAC29140.1; AAC29141.1; EAW83359.1; AAH35214.1; AAH68547.1; AAQ63886.1 

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

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
179	HLLKWIIKSNYQGLP	ubiquitination	[1]
209	DYLHSKCKIIHTDIK	ubiquitination	[2]
216	KIIHTDIKPENILMC	ubiquitination	[2]
241	AEATEWQKAGAPPPS	ubiquitination	[2]
300	LEREAERKIIEENIT	ubiquitination	[2]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] 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] 

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. 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. 

Sequence Annotation

 DOMAIN 81 684 Protein kinase.
 NP_BIND 87 95 ATP (By similarity).
 ACT_SITE 214 214 Proton acceptor (By similarity).
 BINDING 110 110 ATP (By similarity).
 MOD_RES 52 52 Phosphoserine; by CK2 (By similarity).
 MOD_RES 380 380 Phosphoserine.
 MOD_RES 492 492 Phosphothreonine; by PKB/AKT1.
 MOD_RES 494 494 Phosphoserine.
 MOD_RES 497 497 Phosphoserine.
 MOD_RES 588 588 Phosphoserine; by CK2 (By similarity).  

Keyword

 3D-structure; Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; Differentiation; Kinase; mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 688 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0071889; F:14-3-3 protein binding; ISS: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; ISS:BHF-UCL.
 GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
 GO:0045087; P:innate immune response; IC:BHF-UCL.
 GO:0007243; P:intracellular protein kinase cascade; IDA:UniProtKB.
 GO:0045071; P:negative regulation of viral genome replication; IDA:BHF-UCL.
 GO:0035063; P:nuclear speck organization; ISS:BHF-UCL.
 GO:0045787; P:positive regulation of cell cycle; ISS:BHF-UCL.
 GO:0008284; P:positive regulation of cell proliferation; IDA:BHF-UCL.
 GO:0010628; P:positive regulation of gene expression; ISS:BHF-UCL.
 GO:0043525; P:positive regulation of neuron apoptotic process; ISS:BHF-UCL.
 GO:0045070; P:positive regulation of viral genome replication; IDA:BHF-UCL.
 GO:0048024; P:regulation of mRNA splicing, via spliceosome; TAS:UniProtKB.
 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