Protein:SRPK2 |
Protein Summary |
 Gene summary |
| Gene name: SRPK2 | ASpdb.0 ID: 6733 | Gene | Gene symbol | SRPK2 | Gene ID | 6733 |
| Gene name | SRSF protein kinase 2 |
| Synonyms | SFRSK2 |
| Cytomap | 7q22.3 |
| Type of gene | protein-coding |
| Description | SRSF protein kinase 2SFRS protein kinase 2SR protein kinase 2SR-protein-specific kinase 2serine kinase SRPK2serine/arginine-rich protein-specific kinase 2serine/arginine-rich splicing factor kinase 2serine/threonine-protein kinase SRPK2 |
| Modification date | 20240403 |
| UniProtAcc | P78362 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | SRPK2 | GO:0000245 | spliceosomal complex assembly | 9472028 |
| Gene | SRPK2 | GO:0000287 | magnesium ion binding | 9472028 |
| Gene | SRPK2 | GO:0000785 | chromatin | 28076779 |
| Gene | SRPK2 | GO:0004674 | protein serine/threonine kinase activity | 9472028 |
| Gene | SRPK2 | GO:0005524 | ATP binding | 9472028 |
| Gene | SRPK2 | GO:0005634 | nucleus | 9472028 |
| Gene | SRPK2 | GO:0005654 | nucleoplasm | 28076779 |
| Gene | SRPK2 | GO:0005730 | nucleolus | - |
| Gene | SRPK2 | GO:0005737 | cytoplasm | 9472028|28076779 |
| Gene | SRPK2 | GO:0005829 | cytosol | - |
| Gene | SRPK2 | GO:0006468 | protein phosphorylation | 9472028 |
| Gene | SRPK2 | GO:0008284 | positive regulation of cell population proliferation | 18559500 |
| Gene | SRPK2 | GO:0008380 | RNA splicing | 9472028 |
| Gene | SRPK2 | GO:0016607 | nuclear speck | 28076779 |
| Gene | SRPK2 | GO:0035556 | intracellular signal transduction | 9472028 |
| Gene | SRPK2 | GO:0045070 | positive regulation of viral genome replication | 20498328 |
| Gene | SRPK2 | GO:0045071 | negative regulation of viral genome replication | 12417631 |
| Gene | SRPK2 | GO:0062176 | R-loop processing | 28076779 |
AS Summary |
| Information of the canonical protein with experimentally identified structure from PDB (2023). |
| UniProt Acc | File name | PDB ID | Method | Resolution | Chain | Start | End |
| P78362-1 | P78362-1_5myv_A.pdb | 5MYV | X-ray | 2.9 | A | 68 | 688 |
| ASpdb's canonical and alternatively spliced isoform information. |
| accession_id | gene_name | canonical_id | alternative_id | canonical_length | alternative_length | canonical_start | canonical_end | type | originalSEQ | variationSEQ | alternative_start | alternative_end |
| P78362 | SRPK2 | P78362-1 | P78362-2 | 688 | 699 | 1 | 13 | Substitution | MSVNSEKSSSSER | MSSRKVLAIQARKRRPKREKHPKK | 1 | 24 |
| Multiple sequence alignment of our canonical and alternatively spliced SRPK2 |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of SRPK2 |
| UniProt-id | ENSG | ENST | ENSP |
| P78362-1 | ENSG00000135250.17 | ENST00000357311.7 | ENSP00000349863.3 |
| P78362-1 | ENSG00000135250.17 | ENST00000489828.5 | ENSP00000419791.1 |
| P78362-2 | ENSG00000135250.17 | ENST00000393651.8 | ENSP00000377262.3 |
| UniProt-id | NM ID | NP ID |
| P78362-1 | NM_001278273.1 | NP_001265202.1 |
| P78362-1 | NM_182691.2 | NP_872633.1 |
| P78362-2 | NM_182692.2 | NP_872634.1 |
| Amino acid sequences of our canonical and alternatively spliced SRPK2 |
| accession_id | Protein sequence |
| P78362-1 | MSVNSEKSSSSERPEPQQKAPLVPPPPPPPPPPPPPLPDPTPPEPEEEILGSDDEEQEDPADYCKGGYHPVKIGDLFNGRYHVIRKLGWG HFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNKDMVVQLIDDFKISGMNGIHVCMVFEVLGHHLLKWIIKS NYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDAYVRRMAAEATEWQKAGAPPPSGSAVSTAPQQKPIGKISKNKKK KLKKKQKRQAELLEKRLQEIEELEREAERKIIEENITSAAPSNDQDGEYCPEVKLKTTGLEEAAEAETAKDNGEAEDQEEKEDAEKENIE KDEDDVDQELANIDPTWIESPKTNGHIENGPFSLEQQLDDEDDDEEDCPNPEEYNLDEPNAESDYTYSSSYEQFNGELPNGRHKIPESQF PEFSTSLFSGSLEPVACGSVLSEGSPLTEQEESSPSHDRSRTVSASSTGDLPKAKTRAADLLVNPLDPRNADKIRVKIADLGNACWVHKH FTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSGEDYSRDEDHIAHIIELLGSIPRHFALSGKYSREFFNRRGEL |
| P78362-2 | MSSRKVLAIQARKRRPKREKHPKKPEPQQKAPLVPPPPPPPPPPPPPLPDPTPPEPEEEILGSDDEEQEDPADYCKGGYHPVKIGDLFNG RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNKDMVVQLIDDFKISGMNGIHVCMVFEVL GHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDAYVRRMAAEATEWQKAGAPPPSGSAVSTAPQQK PIGKISKNKKKKLKKKQKRQAELLEKRLQEIEELEREAERKIIEENITSAAPSNDQDGEYCPEVKLKTTGLEEAAEAETAKDNGEAEDQE EKEDAEKENIEKDEDDVDQELANIDPTWIESPKTNGHIENGPFSLEQQLDDEDDDEEDCPNPEEYNLDEPNAESDYTYSSSYEQFNGELP NGRHKIPESQFPEFSTSLFSGSLEPVACGSVLSEGSPLTEQEESSPSHDRSRTVSASSTGDLPKAKTRAADLLVNPLDPRNADKIRVKIA DLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSGEDYSRDEDHIAHIIELLGSIPRHFALSGKY |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| SRPK2 (go to UniProt):P78362 |
| Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at * Minus value of BPloci means that the break pointn is located before the CDS. |
| - Retained protein feature among the 13 regional features. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| P78362 | Region | 1 | 65 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=1;End=13 |
| P78362 | Compositional bias | 1 | 16 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=1;End=13 |
Gene Isoform Structures and Expression Levels for SRPK2 |
| Gene structures of our canonical and alternative spliced genes of SRPK2 * Click on the image to open the UCSC genome browser with custom track showing this image in a new window. |
| Expression levels of gene isoforms across GTEx. |
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| Expression levels of gene isoforms across TCGA. |
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Protein Structures |
| PDB and CIF files of the predicted protein structures * Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format. |
| 3D view using mol* of P78362-1 |
| 3D view using mol* of P78362-2 |
pLDDT Score Distribution |
| pLDDT score distribution of the predicted protein structures from AlphaFold2 * AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
| pLDDT distribution across the protein length of P78362-1 |
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| pLDDT distribution across the protein length of P78362-2 |
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Ramachandran Plot of Protein Structures |
| Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide. |
| Ramachandran plot of P78362-1 |
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Potential Active Site Information |
| The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite. |
| UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
| P78362-1 | 1.018 | 838 | 1.019 | 2797.165 | 0.545 | 0.726 | 0.91 | 0.483 | 1.092 | 0.443 | 1.039 | 46,48,49,50,51,52,53,54,56,58,59,62,68,85,86,87,88 ,89,90,91,92,93,95,108,110,112,117,118,120,121,122 ,124,125,128,129,146,164,166,167,168,169,170,171,1 72,174,175,176,177,178,179,181,182,213,214,216,218 ,219,221,222,228,231,232,235,238,239,247,248,250,2 51,426,427,428,429,430,431,432,433,434,435,436,437 ,438,507,508,509,512,514,529,530,531,532,533,534,5 35,540,541,542,543,544,545,546,547,548,549,550,551 ,555,556,558,560,561,575,576,581,582,583,584,585,5 86,587,588,594,595,597,600,601,604,605,618,619,623 ,633,634,635,636,637,639,644,648,649 |
| P78362-2 | 1.024 | 696 | 1.027 | 2241.848 | 0.55 | 0.734 | 0.931 | 0.479 | 1.086 | 0.442 | 0.83 | 1,4,57,58,59,60,61,62,63,64,65,66,96,97,98,99,100, 101,102,103,104,106,119,121,123,128,129,132,133,13 5,136,139,140,157,175,177,178,179,180,181,182,183, 185,186,187,189,190,192,193,224,225,227,229,230,23 2,239,243,246,250,257,258,259,260,261,262,437,438, 439,440,441,442,443,444,445,446,447,518,519,520,52 3,525,540,541,542,543,544,545,546,552,553,554,555, 556,557,558,559,560,561,562,565,566,567,569,571,57 2,593,596,597,598,599,605,606,630,634 |
Protein Structure and Feature Comparision |
| Protein Structure Comparision Using Template Modeling Scores (TM-score). |
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| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green) |
| 3D view using mol* of P78362-1_P78362-1_5myv_A.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of P78362-1_5myv_A_P78362-2.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of P78362-1_P78362-2.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/P78362-1_vs_P78362-2.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/P78362-1_vs_P78362-2.png |
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Protein-Protein Interaction |
| Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to SRPK2 |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
| P78362 | SRPK2 | DB04395 | Phosphoaminophosphonic Acid-Adenylate Ester | experimental | |
| P78362 | SRPK2 | DB02733 | Purvalanol | experimental | |
| P78362 | SRPK2 | DB00173 | Adenine | approved, nutraceutical |
Related Diseases to SRPK2 |
| Previous studies relating to the alternative splicing of SRPK2 and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| SRPK2 | 26853621 | Dysregulation of splicing proteins in head and neck squamous cell carcinoma. | Signaling plays an important role in regulating all cellular pathways. Altered signaling is one of the hallmarks of cancers. Phosphoproteomics enables interrogation of kinase mediated signaling pathways in biological systems. In cancers, this approach can be utilized to identify aberrantly activated pathways that potentially drive proliferation and tumorigenesis. To identify signaling alterations in head and neck squamous cell carcinoma (HNSCC), we carried out proteomic and phosphoproteomic analysis of HNSCC cell lines using a combination of tandem mass tag (TMT) labeling approach and titanium dioxide-based enrichment. We identified 4,920 phosphosites corresponding to 2,212 proteins in six HNSCC cell lines compared to a normal oral cell line. Our data indicated significant enrichment of proteins associated with splicing. We observed hyperphosphorylation of SRSF protein kinase 2 (SRPK2) and its downstream substrates in HNSCC cell lines. SRPK2 is a splicing kinase, known to phosphorylate serine/arginine (SR) rich domain proteins and regulate splicing process in eukaryotes. Although genome-wide studies have reported the contribution of alternative splicing events of several genes in the progression of cancer, the involvement of splicing kinases in HNSCC is not known. In this study, we studied the role of SRPK2 in HNSCC. Inhibition of SRPK2 resulted in significant decrease in colony forming and invasive ability in a panel of HNSCC cell lines. Our results indicate that phosphorylation of SRPK2 plays a crucial role in the regulation of splicing process in HNSCC and that splicing kinases can be developed as a new class of therapeutic target in HNSCC. | D063646 | Carcinogenesis |
| SRPK2 | 26853621 | Dysregulation of splicing proteins in head and neck squamous cell carcinoma. | Signaling plays an important role in regulating all cellular pathways. Altered signaling is one of the hallmarks of cancers. Phosphoproteomics enables interrogation of kinase mediated signaling pathways in biological systems. In cancers, this approach can be utilized to identify aberrantly activated pathways that potentially drive proliferation and tumorigenesis. To identify signaling alterations in head and neck squamous cell carcinoma (HNSCC), we carried out proteomic and phosphoproteomic analysis of HNSCC cell lines using a combination of tandem mass tag (TMT) labeling approach and titanium dioxide-based enrichment. We identified 4,920 phosphosites corresponding to 2,212 proteins in six HNSCC cell lines compared to a normal oral cell line. Our data indicated significant enrichment of proteins associated with splicing. We observed hyperphosphorylation of SRSF protein kinase 2 (SRPK2) and its downstream substrates in HNSCC cell lines. SRPK2 is a splicing kinase, known to phosphorylate serine/arginine (SR) rich domain proteins and regulate splicing process in eukaryotes. Although genome-wide studies have reported the contribution of alternative splicing events of several genes in the progression of cancer, the involvement of splicing kinases in HNSCC is not known. In this study, we studied the role of SRPK2 in HNSCC. Inhibition of SRPK2 resulted in significant decrease in colony forming and invasive ability in a panel of HNSCC cell lines. Our results indicate that phosphorylation of SRPK2 plays a crucial role in the regulation of splicing process in HNSCC and that splicing kinases can be developed as a new class of therapeutic target in HNSCC. | D002294 | Carcinoma, Squamous Cell |
| SRPK2 | 26853621 | Dysregulation of splicing proteins in head and neck squamous cell carcinoma. | Signaling plays an important role in regulating all cellular pathways. Altered signaling is one of the hallmarks of cancers. Phosphoproteomics enables interrogation of kinase mediated signaling pathways in biological systems. In cancers, this approach can be utilized to identify aberrantly activated pathways that potentially drive proliferation and tumorigenesis. To identify signaling alterations in head and neck squamous cell carcinoma (HNSCC), we carried out proteomic and phosphoproteomic analysis of HNSCC cell lines using a combination of tandem mass tag (TMT) labeling approach and titanium dioxide-based enrichment. We identified 4,920 phosphosites corresponding to 2,212 proteins in six HNSCC cell lines compared to a normal oral cell line. Our data indicated significant enrichment of proteins associated with splicing. We observed hyperphosphorylation of SRSF protein kinase 2 (SRPK2) and its downstream substrates in HNSCC cell lines. SRPK2 is a splicing kinase, known to phosphorylate serine/arginine (SR) rich domain proteins and regulate splicing process in eukaryotes. Although genome-wide studies have reported the contribution of alternative splicing events of several genes in the progression of cancer, the involvement of splicing kinases in HNSCC is not known. In this study, we studied the role of SRPK2 in HNSCC. Inhibition of SRPK2 resulted in significant decrease in colony forming and invasive ability in a panel of HNSCC cell lines. Our results indicate that phosphorylation of SRPK2 plays a crucial role in the regulation of splicing process in HNSCC and that splicing kinases can be developed as a new class of therapeutic target in HNSCC. | D006258 | Head and Neck Neoplasms |
| SRPK2 | 26853621 | Dysregulation of splicing proteins in head and neck squamous cell carcinoma. | Signaling plays an important role in regulating all cellular pathways. Altered signaling is one of the hallmarks of cancers. Phosphoproteomics enables interrogation of kinase mediated signaling pathways in biological systems. In cancers, this approach can be utilized to identify aberrantly activated pathways that potentially drive proliferation and tumorigenesis. To identify signaling alterations in head and neck squamous cell carcinoma (HNSCC), we carried out proteomic and phosphoproteomic analysis of HNSCC cell lines using a combination of tandem mass tag (TMT) labeling approach and titanium dioxide-based enrichment. We identified 4,920 phosphosites corresponding to 2,212 proteins in six HNSCC cell lines compared to a normal oral cell line. Our data indicated significant enrichment of proteins associated with splicing. We observed hyperphosphorylation of SRSF protein kinase 2 (SRPK2) and its downstream substrates in HNSCC cell lines. SRPK2 is a splicing kinase, known to phosphorylate serine/arginine (SR) rich domain proteins and regulate splicing process in eukaryotes. Although genome-wide studies have reported the contribution of alternative splicing events of several genes in the progression of cancer, the involvement of splicing kinases in HNSCC is not known. In this study, we studied the role of SRPK2 in HNSCC. Inhibition of SRPK2 resulted in significant decrease in colony forming and invasive ability in a panel of HNSCC cell lines. Our results indicate that phosphorylation of SRPK2 plays a crucial role in the regulation of splicing process in HNSCC and that splicing kinases can be developed as a new class of therapeutic target in HNSCC. | D000077195 | Squamous Cell Carcinoma of Head and Neck |
Clinically important variants in SRPK2 |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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