Protein:PTK2B |
Protein Summary |
 Gene summary |
| Gene name: PTK2B | ASpdb.0 ID: 2185 | Gene | Gene symbol | PTK2B | Gene ID | 2185 |
| Gene name | protein tyrosine kinase 2 beta |
| Synonyms | CADTK|CAKB|FADK2|FAK2|PKB|PTK|PYK2|RAFTK |
| Cytomap | 8p21.2 |
| Type of gene | protein-coding |
| Description | protein-tyrosine kinase 2-betaCAK-betaFADK 2PTK2B protein tyrosine kinase 2 betacalcium-dependent tyrosine kinasecalcium-regulated non-receptor proline-rich tyrosine kinasecell adhesion kinase betafocal adhesion kinase 2proline-rich tyrosine kinas |
| Modification date | 20240416 |
| UniProtAcc | Q14289 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | PTK2B | GO:0004715 | non-membrane spanning protein tyrosine kinase activity | 7544443|10518561 |
| Gene | PTK2B | GO:0005634 | nucleus | 19880522 |
| Gene | PTK2B | GO:0005925 | focal adhesion | 18765415 |
| Gene | PTK2B | GO:0010595 | positive regulation of endothelial cell migration | 21245381 |
| Gene | PTK2B | GO:0018108 | peptidyl-tyrosine phosphorylation | 7544443 |
| Gene | PTK2B | GO:0030027 | lamellipodium | 18765415 |
| Gene | PTK2B | GO:0038083 | peptidyl-tyrosine autophosphorylation | 9545257 |
| Gene | PTK2B | GO:0043267 | negative regulation of potassium ion transport | 7544443 |
| Gene | PTK2B | GO:0048471 | perinuclear region of cytoplasm | 18765415 |
| Gene | PTK2B | GO:2000058 | regulation of ubiquitin-dependent protein catabolic process | 19880522 |
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 |
| Q14289-1 | Q14289-1_4eku_A.pdb | 4EKU | X-ray | 3.25 | A | 21 | 366 |
| 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 |
| Q14289 | PTK2B | Q14289-1 | Q14289-2 | 1009 | 967 | 739 | 780 | Deletion | none | none | 738 | 738 |
| Multiple sequence alignment of our canonical and alternatively spliced PTK2B |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of PTK2B |
| UniProt-id | ENSG | ENST | ENSP |
| Q14289-1 | ENSG00000120899.18 | ENST00000346049.10 | ENSP00000332816.6 |
| Q14289-1 | ENSG00000120899.18 | ENST00000397501.5 | ENSP00000380638.1 |
| Q14289-2 | ENSG00000120899.18 | ENST00000420218.3 | ENSP00000391995.2 |
| Q14289-2 | ENSG00000120899.18 | ENST00000517339.5 | ENSP00000427931.1 |
| UniProt-id | NM ID | NP ID |
| Q14289-1 | NM_004103.4 | NP_004094.3 |
| Q14289-1 | NM_173174.2 | NP_775266.1 |
| Q14289-1 | NM_173176.2 | NP_775268.1 |
| Q14289-1 | XM_005273447.4 | XP_005273504.1 |
| Q14289-1 | XM_011544441.2 | XP_011542743.1 |
| Q14289-1 | XM_017013214.1 | XP_016868703.1 |
| Q14289-2 | NM_173175.2 | NP_775267.1 |
| Amino acid sequences of our canonical and alternatively spliced PTK2B |
| accession_id | Protein sequence |
| Q14289-1 | MSGVSEPLSRVKLGTLRRPEGPAEPMVVVPVDVEKEDVRILKVCFYSNSFNPGKNFKLVKCTVQTEIREIITSILLSGRIGPNIRLAECY GLRLKHMKSDEIHWLHPQMTVGEVQDKYECLHVEAEWRYDLQIRYLPEDFMESLKEDRTTLLYFYQQLRNDYMQRYASKVSEGMALQLGC LELRRFFKDMPHNALDKKSNFELLEKEVGLDLFFPKQMQENLKPKQFRKMIQQTFQQYASLREEECVMKFFNTLAGFANIDQETYRCELI QGWNITVDLVIGPKGIRQLTSQDAKPTCLAEFKQIRSIRCLPLEEGQAVLQLGIEGAPQALSIKTSSLAEAENMADLIDGYCRLQGEHQG SLIIHPRKDGEKRNSLPQIPMLNLEARRSHLSESCSIESDIYAEIPDETLRRPGGPQYGIAREDVVLNRILGEGFFGEVYEGVYTNHKGE KINVAVKTCKKDCTLDNKEKFMSEAVIMKNLDHPHIVKLIGIIEEEPTWIIMELYPYGELGHYLERNKNSLKVLTLVLYSLQICKAMAYL ESINCVHRDIAVRNILVASPECVKLGDFGLSRYIEDEDYYKASVTRLPIKWMSPESINFRRFTTASDVWMFAVCMWEILSFGKQPFFWLE NKDVIGVLEKGDRLPKPDLCPPVLYTLMTRCWDYDPSDRPRFTELVCSLSDVYQMEKDIAMEQERNARYRTPKILEPTAFQEPPPKPSRP KYRPPPQTNLLAPKLQFQVPEGLCASSPTLTSPMEYPSPVNSLHTPPLHRHNVFKRHSMREEDFIQPSSREEAQQLWEAEKVKMRQILDK QQKQMVEDYQWLRQEEKSLDPMVYMNDKSPLTPEKEVGYLEFTGPPQKPPRLGAQSIQPTANLDRTDDLVYLNVMELVRAVLELKNELCQ LPPEGYVVVVKNVGLTLRKLIGSVDDLLPSLPSSSRTEIEGTQKLLNKDLAELINKMRLAQQNAVTSLSEECKRQMLTASHTLAVDAKNL |
| Q14289-2 | MSGVSEPLSRVKLGTLRRPEGPAEPMVVVPVDVEKEDVRILKVCFYSNSFNPGKNFKLVKCTVQTEIREIITSILLSGRIGPNIRLAECY GLRLKHMKSDEIHWLHPQMTVGEVQDKYECLHVEAEWRYDLQIRYLPEDFMESLKEDRTTLLYFYQQLRNDYMQRYASKVSEGMALQLGC LELRRFFKDMPHNALDKKSNFELLEKEVGLDLFFPKQMQENLKPKQFRKMIQQTFQQYASLREEECVMKFFNTLAGFANIDQETYRCELI QGWNITVDLVIGPKGIRQLTSQDAKPTCLAEFKQIRSIRCLPLEEGQAVLQLGIEGAPQALSIKTSSLAEAENMADLIDGYCRLQGEHQG SLIIHPRKDGEKRNSLPQIPMLNLEARRSHLSESCSIESDIYAEIPDETLRRPGGPQYGIAREDVVLNRILGEGFFGEVYEGVYTNHKGE KINVAVKTCKKDCTLDNKEKFMSEAVIMKNLDHPHIVKLIGIIEEEPTWIIMELYPYGELGHYLERNKNSLKVLTLVLYSLQICKAMAYL ESINCVHRDIAVRNILVASPECVKLGDFGLSRYIEDEDYYKASVTRLPIKWMSPESINFRRFTTASDVWMFAVCMWEILSFGKQPFFWLE NKDVIGVLEKGDRLPKPDLCPPVLYTLMTRCWDYDPSDRPRFTELVCSLSDVYQMEKDIAMEQERNARYRTPKILEPTAFQEPPPKPSRP KYRPPPQTNLLAPKLQFQEEDFIQPSSREEAQQLWEAEKVKMRQILDKQQKQMVEDYQWLRQEEKSLDPMVYMNDKSPLTPEKEVGYLEF TGPPQKPPRLGAQSIQPTANLDRTDDLVYLNVMELVRAVLELKNELCQLPPEGYVVVVKNVGLTLRKLIGSVDDLLPSLPSSSRTEIEGT |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| PTK2B (go to UniProt):Q14289 |
| 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 |
Gene Isoform Structures and Expression Levels for PTK2B |
| Gene structures of our canonical and alternative spliced genes of PTK2B * 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 Q14289-1 |
| 3D view using mol* of Q14289-2 |
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 Q14289-1 |
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| pLDDT distribution across the protein length of Q14289-2 |
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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 Q14289-1 |
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| Ramachandran plot of Q14289-2 |
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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 |
| Q14289-1 | 1.081 | 98 | 1.072 | 302.526 | 0.427 | 0.83 | 1.092 | 1.025 | 1.094 | 0.938 | 0.68 | 93,102,104,132,133,134,136,154,157,158,161,162,165 ,166,254,258,259,260,261,262,263,281,282,347,351 |
| Q14289-2 | 1.052 | 115 | 1.094 | 227.066 | 0.513 | 0.725 | 0.962 | 0.801 | 0.863 | 0.928 | 1.133 | 103,104,105,106,108,109,113,117,118,309,310,311,32 1,338,339,342,343,345,346,361,363,364,365,366 |
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 Q14289-1_Q14289-1_4eku_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 Q14289-1_4eku_A_Q14289-2.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q14289-1_Q14289-2.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/Q14289-1_vs_Q14289-2.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/Q14289-1_vs_Q14289-2.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 PTK2B |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
| Q14289 | PTK2B | DB01645 | Genistein | investigational | |
| Q14289 | PTK2B | DB12010 | Fostamatinib | approved, investigational | inhibitor |
| Q14289 | PTK2B | DB01097 | Leflunomide | approved, investigational | antagonist |
| Q14289 | PTK2B | DB08341 | 4-{[4-{[(1R,2R)-2-(dimethylamino)cyclopentyl]amino}-5-(trifluoromethyl)pyrimidin-2-yl]amino}-N-methylbenzenesulfonamide | experimental |
Related Diseases to PTK2B |
| Previous studies relating to the alternative splicing of PTK2B and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| PTK2B | 14961028 | p210BCR/ABL-induced alteration of pre-mRNA splicing in primary human CD34+ hematopoietic progenitor cells. | Chronic myelogenous leukemia (CML) is a malignancy of the human hematopoietic stem cell (HSC) caused by the p210BCR/ABL oncoprotein. Although alternative splicing of pre-mRNA is a critical determinant of a cell's protein repertoire, it has not been associated with CML pathogenesis. We identified a BCR/ABL-dependent increase in expression of multiple genes involved in pre-mRNA splicing (eg SRPK1, RNA Helicase II/Gu, and hnRNPA2/B1) by subtractive hybridization of cDNA from p210BCR/ABL-eGFP vs eGFP-transduced umbilical cord blood CD34+ cells. beta1-integrin signaling is important to HSC maintenance and proliferation/differentiation, and is abnormal in CML. As an example of how changes in pre-mRNA processing might contribute to CML pathogenesis, we observed alternative splicing of a gene for a beta1-integrin-responsive nonreceptor tyrosine kinase (PYK2), resulting in increased expression of full-length Pyk2 in BCR/ABL-containing cells. Treatment of p210BCR/ABL-positive cells with the Abl-specific tyrosine kinase inhibitor STI571 reverted PYK2 splicing to a configuration more consistent with normal cells, and correlated with decreased expression of BCR/ABL-induced proteins involved in pre-mRNA processing. Whether altered PYK2 splicing contributes to CML pathogenesis remains undetermined; however, we propose that generic changes in pre-mRNA splicing as a result of p210BCR/ABL kinase activity may contribute to CML pathogenesis. | D015464 | Leukemia, Myelogenous, Chronic, BCR-ABL Positive |
| PTK2B | 14961028 | p210BCR/ABL-induced alteration of pre-mRNA splicing in primary human CD34+ hematopoietic progenitor cells. | Chronic myelogenous leukemia (CML) is a malignancy of the human hematopoietic stem cell (HSC) caused by the p210BCR/ABL oncoprotein. Although alternative splicing of pre-mRNA is a critical determinant of a cell's protein repertoire, it has not been associated with CML pathogenesis. We identified a BCR/ABL-dependent increase in expression of multiple genes involved in pre-mRNA splicing (eg SRPK1, RNA Helicase II/Gu, and hnRNPA2/B1) by subtractive hybridization of cDNA from p210BCR/ABL-eGFP vs eGFP-transduced umbilical cord blood CD34+ cells. beta1-integrin signaling is important to HSC maintenance and proliferation/differentiation, and is abnormal in CML. As an example of how changes in pre-mRNA processing might contribute to CML pathogenesis, we observed alternative splicing of a gene for a beta1-integrin-responsive nonreceptor tyrosine kinase (PYK2), resulting in increased expression of full-length Pyk2 in BCR/ABL-containing cells. Treatment of p210BCR/ABL-positive cells with the Abl-specific tyrosine kinase inhibitor STI571 reverted PYK2 splicing to a configuration more consistent with normal cells, and correlated with decreased expression of BCR/ABL-induced proteins involved in pre-mRNA processing. Whether altered PYK2 splicing contributes to CML pathogenesis remains undetermined; however, we propose that generic changes in pre-mRNA splicing as a result of p210BCR/ABL kinase activity may contribute to CML pathogenesis. | D015466 | Leukemia, Myeloid, Chronic-Phase |
Clinically important variants in PTK2B |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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