Protein:CAMK2B |
Protein Summary |
Gene summary |
| Gene name: CAMK2B | ASpdb.0 ID: 816 | Gene | Gene symbol | CAMK2B | Gene ID | 816 |
| Gene name | calcium/calmodulin dependent protein kinase II beta |
| Synonyms | CAM2|CAMK2|CAMKB|CaMKIIbeta|MRD54 |
| Cytomap | 7p13 |
| Type of gene | protein-coding |
| Description | calcium/calmodulin-dependent protein kinase type II subunit betaCaM kinase II beta subunitCaM-kinase II beta chaincaMK-II subunit betaproline rich calmodulin-dependent protein kinase |
| Modification date | 20240407 |
| UniProtAcc | Q13554 |
Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | CAMK2B | GO:0005954 | calcium- and calmodulin-dependent protein kinase complex | 20668654 |
| Gene | CAMK2B | GO:0009931 | calcium-dependent protein serine/threonine kinase activity | 31930741 |
| Gene | CAMK2B | GO:0018105 | peptidyl-serine phosphorylation | 31930741 |
| Gene | CAMK2B | GO:0046777 | protein autophosphorylation | 18817731 |
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 |
| Q13554-1 | Q13554-1_3bhh_A.pdb | 3BHH | X-ray | 2.4 | A | 11 | 301 |
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 |
| Q13554 | CAMK2B | Q13554-1 | Q13554-2 | 666 | 542 | 410 | 533 | Deletion | none | none | 409 | 409 |
| Q13554 | CAMK2B | Q13554-1 | Q13554-3 | 666 | 503 | 316 | 316 | Substitution | V | A | 316 | 316 |
| Q13554 | CAMK2B | Q13554-1 | Q13554-3 | 666 | 503 | 317 | 340 | Deletion | none | none | 316 | 316 |
| Q13554 | CAMK2B | Q13554-1 | Q13554-3 | 666 | 503 | 379 | 393 | Deletion | none | none | 354 | 354 |
| Q13554 | CAMK2B | Q13554-1 | Q13554-3 | 666 | 503 | 410 | 533 | Deletion | none | none | 370 | 370 |
| Q13554 | CAMK2B | Q13554-1 | Q13554-4 | 666 | 479 | 316 | 316 | Substitution | V | A | 316 | 316 |
| Q13554 | CAMK2B | Q13554-1 | Q13554-4 | 666 | 479 | 317 | 340 | Deletion | none | none | 316 | 316 |
| Q13554 | CAMK2B | Q13554-1 | Q13554-4 | 666 | 479 | 354 | 392 | Deletion | none | none | 329 | 329 |
| Q13554 | CAMK2B | Q13554-1 | Q13554-4 | 666 | 479 | 410 | 533 | Deletion | none | none | 346 | 346 |
| Q13554 | CAMK2B | Q13554-1 | Q13554-5 | 666 | 518 | 316 | 316 | Substitution | V | A | 316 | 316 |
| Q13554 | CAMK2B | Q13554-1 | Q13554-5 | 666 | 518 | 317 | 340 | Deletion | none | none | 316 | 316 |
| Q13554 | CAMK2B | Q13554-1 | Q13554-5 | 666 | 518 | 410 | 533 | Deletion | none | none | 385 | 385 |
| Q13554 | CAMK2B | Q13554-1 | Q13554-6 | 666 | 492 | 354 | 377 | Deletion | none | none | 353 | 353 |
| Q13554 | CAMK2B | Q13554-1 | Q13554-6 | 666 | 492 | 410 | 533 | Deletion | none | none | 385 | 385 |
| Q13554 | CAMK2B | Q13554-1 | Q13554-6 | 666 | 492 | 559 | 584 | Deletion | none | none | 410 | 410 |
| Q13554 | CAMK2B | Q13554-1 | Q13554-7 | 666 | 449 | 316 | 316 | Substitution | V | A | 316 | 316 |
| Q13554 | CAMK2B | Q13554-1 | Q13554-7 | 666 | 449 | 317 | 533 | Deletion | none | none | 316 | 316 |
| Q13554 | CAMK2B | Q13554-1 | Q13554-8 | 666 | 517 | 316 | 340 | Deletion | none | none | 315 | 315 |
| Q13554 | CAMK2B | Q13554-1 | Q13554-8 | 666 | 517 | 410 | 533 | Deletion | none | none | 384 | 384 |
Multiple sequence alignment of our canonical and alternatively spliced CAMK2B |
Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of CAMK2B |
| UniProt-id | ENSG | ENST | ENSP |
| Q13554-1 | ENSG00000058404.21 | ENST00000395749.7 | ENSP00000379098.2 |
| Q13554-2 | ENSG00000058404.21 | ENST00000350811.7 | ENSP00000326375.5 |
| Q13554-2 | ENSG00000058404.21 | ENST00000440254.6 | ENSP00000397937.2 |
| Q13554-2 | ENSG00000058404.21 | ENST00000700285.1 | ENSP00000514918.1 |
| Q13554-3 | ENSG00000058404.21 | ENST00000358707.7 | ENSP00000351542.3 |
| Q13554-4 | ENSG00000058404.21 | ENST00000353625.8 | ENSP00000326427.5 |
| Q13554-5 | ENSG00000058404.21 | ENST00000395747.6 | ENSP00000379096.2 |
| Q13554-6 | ENSG00000058404.21 | ENST00000347193.8 | ENSP00000326544.6 |
| Q13554-7 | ENSG00000058404.21 | ENST00000346990.8 | ENSP00000326518.5 |
| Q13554-8 | ENSG00000058404.21 | ENST00000258682.10 | ENSP00000258682.6 |
| UniProt-id | NM ID | NP ID |
| Q13554-1 | NM_001220.4 | NP_001211.3 |
| Q13554-2 | NM_001293170.1 | NP_001280099.1 |
| Q13554-2 | NM_172078.2 | NP_742075.1 |
| Q13554-3 | NM_172081.2 | NP_742078.1 |
| Q13554-4 | NM_172083.2 | NP_742080.1 |
| Q13554-5 | NM_172079.2 | NP_742076.1 |
| Q13554-6 | NM_172082.2 | NP_742079.1 |
| Q13554-7 | NM_172084.2 | NP_742081.1 |
| Q13554-8 | NM_172080.2 | NP_742077.1 |
Amino acid sequences of our canonical and alternatively spliced CAMK2B |
| accession_id | Protein sequence |
| Q13554-1 | MATTVTCTRFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVF DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGY LSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHP WVCQRSTVASMMHRQETVECLKKFNARRKLKGAILTTMLATRNFSVGRQTTAPATMSTAASGTTMGLVEQAKSLLNKKADGVKPQTNSTK NSAAATSPKGTLPPAALEPQTTVIHNPVDGIKESSDSANTTIEDEDAKAPRVPDILSSVRRGSGAPEAEGPLPCPSPAPFSPLPAPSPRI SDILNSVRRGSGTPEAEGPLSAGPPPCLSPALLGPLSSPSPRISDILNSVRRGSGTPEAEGPSPVGPPPCPSPTIPGPLPTPSRKQEIIK TTEQLIEAVNNGDFEAYAKICDPGLTSFEPEALGNLVEGMDFHRFYFENLLAKNSKPIHTTILNPHVHVIGEDAACIAYIRLTQYIDGQG |
| Q13554-2 | MATTVTCTRFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVF DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGY LSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHP WVCQRSTVASMMHRQETVECLKKFNARRKLKGAILTTMLATRNFSVGRQTTAPATMSTAASGTTMGLVEQAKSLLNKKADGVKPQTNSTK NSAAATSPKGTLPPAALEPQTTVIHNPVDGIKESSDSANTTIEDEDAKARKQEIIKTTEQLIEAVNNGDFEAYAKICDPGLTSFEPEALG NLVEGMDFHRFYFENLLAKNSKPIHTTILNPHVHVIGEDAACIAYIRLTQYIDGQGRPRTSQSEETRVWHRRDGKWQNVHFHCSGAPVAP |
| Q13554-3 | MATTVTCTRFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVF DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGY LSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHP WVCQRSTVASMMHRQETVECLKKFNARRKLKGAILTTMLATRNFSAAKSLLNKKADGVKPQTNSTKNSAAATSPKGTLPPAALESSDSAN TTIEDEDAKARKQEIIKTTEQLIEAVNNGDFEAYAKICDPGLTSFEPEALGNLVEGMDFHRFYFENLLAKNSKPIHTTILNPHVHVIGED |
| Q13554-4 | MATTVTCTRFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVF DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGY LSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHP WVCQRSTVASMMHRQETVECLKKFNARRKLKGAILTTMLATRNFSAAKSLLNKKADGVKESSDSANTTIEDEDAKARKQEIIKTTEQLIE AVNNGDFEAYAKICDPGLTSFEPEALGNLVEGMDFHRFYFENLLAKNSKPIHTTILNPHVHVIGEDAACIAYIRLTQYIDGQGRPRTSQS |
| Q13554-5 | MATTVTCTRFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVF DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGY LSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHP WVCQRSTVASMMHRQETVECLKKFNARRKLKGAILTTMLATRNFSAAKSLLNKKADGVKPQTNSTKNSAAATSPKGTLPPAALEPQTTVI HNPVDGIKESSDSANTTIEDEDAKARKQEIIKTTEQLIEAVNNGDFEAYAKICDPGLTSFEPEALGNLVEGMDFHRFYFENLLAKNSKPI |
| Q13554-6 | MATTVTCTRFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVF DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGY LSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHP WVCQRSTVASMMHRQETVECLKKFNARRKLKGAILTTMLATRNFSVGRQTTAPATMSTAASGTTMGLVEQAKSLLNKKADGVKEPQTTVI HNPVDGIKESSDSANTTIEDEDAKARKQEIIKTTEQLIEAVNNGDFEAYAFYFENLLAKNSKPIHTTILNPHVHVIGEDAACIAYIRLTQ |
| Q13554-7 | MATTVTCTRFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVF DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGY LSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHP WVCQRSTVASMMHRQETVECLKKFNARRKLKGAILTTMLATRNFSARKQEIIKTTEQLIEAVNNGDFEAYAKICDPGLTSFEPEALGNLV |
| Q13554-8 | MATTVTCTRFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVF DLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGY LSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHP WVCQRSTVASMMHRQETVECLKKFNARRKLKGAILTTMLATRNFSAKSLLNKKADGVKPQTNSTKNSAAATSPKGTLPPAALEPQTTVIH NPVDGIKESSDSANTTIEDEDAKARKQEIIKTTEQLIEAVNNGDFEAYAKICDPGLTSFEPEALGNLVEGMDFHRFYFENLLAKNSKPIH |
Protein Functional Features |
Main function of this protein. (from UniProt) |
| CAMK2B (go to UniProt):Q13554 |
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 |
| Q13554 | Region | 349 | 534 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=410;End=533 |
| Q13554 | Region | 349 | 534 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=379;End=393 |
| Q13554 | Region | 349 | 534 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=410;End=533 |
| Q13554 | Region | 349 | 534 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=354;End=392 |
| Q13554 | Region | 349 | 534 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=410;End=533 |
| Q13554 | Region | 349 | 534 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=410;End=533 |
| Q13554 | Region | 349 | 534 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=354;End=377 |
| Q13554 | Region | 349 | 534 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=410;End=533 |
| Q13554 | Region | 349 | 534 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=317;End=533 |
| Q13554 | Region | 349 | 534 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=410;End=533 |
| Q13554 | Compositional bias | 350 | 368 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=354;End=392 |
| Q13554 | Compositional bias | 350 | 368 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=354;End=377 |
| Q13554 | Compositional bias | 350 | 368 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=317;End=533 |
| Q13554 | Compositional bias | 430 | 446 | Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=410;End=533 |
| Q13554 | Compositional bias | 430 | 446 | Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=410;End=533 |
| Q13554 | Compositional bias | 430 | 446 | Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=410;End=533 |
| Q13554 | Compositional bias | 430 | 446 | Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=410;End=533 |
| Q13554 | Compositional bias | 430 | 446 | Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=410;End=533 |
| Q13554 | Compositional bias | 430 | 446 | Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=317;End=533 |
| Q13554 | Compositional bias | 430 | 446 | Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=410;End=533 |
| Q13554 | Compositional bias | 511 | 530 | Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=410;End=533 |
| Q13554 | Compositional bias | 511 | 530 | Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=410;End=533 |
| Q13554 | Compositional bias | 511 | 530 | Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=410;End=533 |
| Q13554 | Compositional bias | 511 | 530 | Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=410;End=533 |
| Q13554 | Compositional bias | 511 | 530 | Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=410;End=533 |
| Q13554 | Compositional bias | 511 | 530 | Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=317;End=533 |
| Q13554 | Compositional bias | 511 | 530 | Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=410;End=533 |
Gene Isoform Structures and Expression Levels for CAMK2B |
Gene structures of our canonical and alternative spliced genes of CAMK2B* 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. |
Expression levels of gene isoforms across TCGA. |
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 Q13554-1 |
| 3D view using mol* of Q13554-2 |
| 3D view using mol* of Q13554-3 |
| 3D view using mol* of Q13554-4 |
| 3D view using mol* of Q13554-5 |
| 3D view using mol* of Q13554-6 |
| 3D view using mol* of Q13554-7 |
| 3D view using mol* of Q13554-8 |
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. |
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 Q13554-1 |
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| Ramachandran plot of Q13554-2 |
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| Ramachandran plot of Q13554-5 |
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| Ramachandran plot of Q13554-6 |
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| Ramachandran plot of Q13554-7 |
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| Ramachandran plot of Q13554-8 |
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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 |
| Q13554-1 | 1.121 | 120 | 1.163 | 536.452 | 0.542 | 0.812 | 0.996 | 1.352 | 0.809 | 1.67 | 0.698 | 20,23,24,25,26,28,41,43,45,50,54,57,58,60,61,65,74 ,90,92,93,94,96,143,156,157,158,159,160 |
| Q13554-2 | 1.084 | 62 | 1.08 | 93.296 | 0.319 | 0.973 | 1.263 | 2.917 | 0.75 | 3.888 | 0.828 | 421,425,433,445,447,458,459,462,463,466,467,497,51 5,517,531,538,539 |
| Q13554-3 | 1.068 | 61 | 1.05 | 97.412 | 0.358 | 0.981 | 1.148 | 2.71 | 0.837 | 3.239 | 1.052 | 382,386,394,406,408,419,420,423,424,427,428,458,47 6,478,492,499,500 |
| Q13554-4 | 1.075 | 168 | 1.106 | 347.116 | 0.533 | 0.774 | 0.934 | 1.172 | 0.916 | 1.28 | 0.828 | 362,363,370,382,384,396,399,400,403,404,406,407,40 9,410,411,434,436,438,439,440,441,442,446,452,454, 468,475,476,477,478,479 |
| Q13554-5 | 1.082 | 266 | 1.126 | 1199.471 | 0.583 | 0.759 | 0.93 | 1.057 | 0.828 | 1.277 | 0.913 | 20,21,23,24,25,26,28,41,43,45,50,53,54,57,58,60,61 ,65,74,90,91,92,93,94,96,97,138,140,141,143,156,15 7,158,159,160,161,177,178,179,180,202,206,211,212, 214,215,216,217,219,222,290,293,294,297,298,299,30 1,302,303,304,305,306,309,355 |
| Q13554-6 | 1.055 | 187 | 1.104 | 670.222 | 0.628 | 0.714 | 0.854 | 0.869 | 0.811 | 1.071 | 1.017 | 20,22,23,24,25,26,27,28,41,43,44,45,46,49,50,54,57 ,58,61,65,74,85,90,91,92,93,94,96,140,141,143,156, 157,158,159,306,309,310,313 |
| Q13554-7 | 1.082 | 256 | 1.122 | 971.376 | 0.564 | 0.764 | 0.931 | 1.195 | 0.846 | 1.411 | 0.852 | 20,23,24,25,26,28,41,43,45,50,53,54,57,58,60,61,74 ,90,91,93,94,95,96,97,135,138,139,140,141,143,156, 157,158,159,160,171,172,173,175,177,178,179,180,19 1,202,206,212,213,214,215,216,217,218,219,222,294, 297,298,299,301,302,303,305,306,309,310,313 |
| Q13554-8 | 1.085 | 324 | 1.132 | 1443.344 | 0.571 | 0.756 | 0.93 | 1.188 | 0.801 | 1.483 | 0.764 | 20,21,23,24,25,26,28,41,43,45,49,50,51,54,57,58,61 ,74,88,90,91,92,93,94,96,134,136,138,140,141,143,1 56,157,158,159,160,161,177,178,179,180,202,206,210 ,211,212,213,214,215,216,217,218,219,222,290,293,2 94,297,298,299,301,302,303,304,305,306,308,309,312 ,313,316,317,320,353,358,359 |
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 Q13554-1_Q13554-1_3bhh_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 Q13554-1_3bhh_A_Q13554-2.pdb |
| 3D view using mol* of Q13554-1_3bhh_A_Q13554-3.pdb |
| 3D view using mol* of Q13554-1_3bhh_A_Q13554-4.pdb |
| 3D view using mol* of Q13554-1_3bhh_A_Q13554-5.pdb |
| 3D view using mol* of Q13554-1_3bhh_A_Q13554-6.pdb |
| 3D view using mol* of Q13554-1_3bhh_A_Q13554-7.pdb |
| 3D view using mol* of Q13554-1_3bhh_A_Q13554-8.pdb |
Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q13554-1_Q13554-2.pdb |
| 3D view using mol* of Q13554-1_Q13554-3.pdb |
| 3D view using mol* of Q13554-1_Q13554-4.pdb |
| 3D view using mol* of Q13554-1_Q13554-5.pdb |
| 3D view using mol* of Q13554-1_Q13554-6.pdb |
| 3D view using mol* of Q13554-1_Q13554-7.pdb |
| 3D view using mol* of Q13554-1_Q13554-8.pdb |
Protein Feature Comparison of the protein sequendary structures among the protiens. |
Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
Protein-Protein Interaction |
Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to CAMK2B |
Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
| Q13554 | CAMK2B | DB12010 | Fostamatinib | approved, investigational | inhibitor |
| Q13554 | CAMK2B | DB07168 | [4-({4-[(5-cyclopropyl-1H-pyrazol-3-yl)amino]-6-(methylamino)pyrimidin-2-yl}amino)phenyl]acetonitrile | experimental |
Related Diseases to CAMK2B |
Previous studies relating to the alternative splicing of CAMK2B and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| CAMK2B | 7758473 | Characterization and expression of multiple alternatively spliced transcripts of the Goodpasture antigen gene region. Goodpasture antibodies recognize recombinant proteins representing the autoantigen and one of its alternative forms. | Collagen IV, the major component of basement membranes, is composed of six distinct alpha chains (alpha 1-alpha 6). Atypically among the collagen IV genes, the exons encoding the carboxyl-terminal region of the human alpha 3(IV) chain undergo alternative splicing. This region has been designated as the Goodpasture antigen because of its reactivity in the kidney and lung with the pathogenic autoantibodies causing Goodpasture syndrome. The data presented in this report demonstrate that, in human kidney, the gene region encompassing the Goodpasture antigen generates at least six alternatively spliced transcripts predicting five distinct proteins that differ in their carboxyl-terminus and retain, except in one case, the exon that harbors the characteristic amino-terminus of the antigen. Goodpasture antibodies specifically recognize recombinant proteins representing the antigen and the alternative form that retains the amino-half of the antigen, suggesting that this moiety could be involved in the in vivo binding of the pathogenic antibodies. Furthermore, the sera of control individuals contain autoantibodies against the antigen that can be differentiated from those causing the syndrome based on their specific reactivities, suggesting that the binding of the pathogenic autoantibodies to a specific determinant likely trigger a distinct and unique cascade of events causing the disease. | D019867 | Anti-Glomerular Basement Membrane Disease |
Clinically important variants in CAMK2B |
(ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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