Protein:CAMKK2 |
Protein Summary |
Gene summary |
| Gene name: CAMKK2 | ASpdb.0 ID: 10645 | Gene | Gene symbol | CAMKK2 | Gene ID | 10645 |
| Gene name | calcium/calmodulin dependent protein kinase kinase 2 |
| Synonyms | CAMKK|CAMKKB |
| Cytomap | 12q24.31 |
| Type of gene | protein-coding |
| Description | calcium/calmodulin-dependent protein kinase kinase 2CAMKK beta proteincaM-KK 2caM-KK betacaM-kinase kinase 2caM-kinase kinase betacalcium/calmodulin-dependent protein kinase betacalcium/calmodulin-dependent protein kinase kinase 2, beta |
| Modification date | 20240403 |
| UniProtAcc | Q96RR4 |
Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | CAMKK2 | GO:0005509 | calcium ion binding | 11395482 |
| Gene | CAMKK2 | GO:0005829 | cytosol | - |
| Gene | CAMKK2 | GO:0006468 | protein phosphorylation | 11395482 |
| Gene | CAMKK2 | GO:0046777 | protein autophosphorylation | 11395482 |
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 |
| Q96RR4-1 | Q96RR4-1_6cmj_A.pdb | 6CMJ | X-ray | 2.4 | A | 161 | 463 |
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 |
| Q96RR4 | CAMKK2 | Q96RR4-1 | Q96RR4-2 | 588 | 533 | 533 | 533 | Substitution | E | T | 533 | 533 |
| Q96RR4 | CAMKK2 | Q96RR4-1 | Q96RR4-2 | 588 | 533 | 534 | 554 | Deletion | none | none | 533 | 533 |
| Q96RR4 | CAMKK2 | Q96RR4-1 | Q96RR4-2 | 588 | 533 | 555 | 588 | Deletion | none | none | 533 | 533 |
| Q96RR4 | CAMKK2 | Q96RR4-1 | Q96RR4-3 | 588 | 541 | 520 | 532 | Substitution | KPTRECESLSELK | QGSEDNLQGTDPP | 520 | 532 |
| Q96RR4 | CAMKK2 | Q96RR4-1 | Q96RR4-3 | 588 | 541 | 533 | 541 | Substitution | EARQRRQPP | PVGEEEVLL | 533 | 541 |
| Q96RR4 | CAMKK2 | Q96RR4-1 | Q96RR4-3 | 588 | 541 | 542 | 554 | Deletion | none | none | 541 | 541 |
| Q96RR4 | CAMKK2 | Q96RR4-1 | Q96RR4-3 | 588 | 541 | 555 | 588 | Deletion | none | none | 541 | 541 |
| Q96RR4 | CAMKK2 | Q96RR4-1 | Q96RR4-4 | 588 | 545 | 442 | 484 | Deletion | none | none | 441 | 441 |
| Q96RR4 | CAMKK2 | Q96RR4-1 | Q96RR4-5 | 588 | 498 | 442 | 484 | Deletion | none | none | 441 | 441 |
| Q96RR4 | CAMKK2 | Q96RR4-1 | Q96RR4-5 | 588 | 498 | 520 | 532 | Substitution | KPTRECESLSELK | QGSEDNLQGTDPP | 477 | 489 |
| Q96RR4 | CAMKK2 | Q96RR4-1 | Q96RR4-5 | 588 | 498 | 533 | 541 | Substitution | EARQRRQPP | PVGEEEVLL | 490 | 498 |
| Q96RR4 | CAMKK2 | Q96RR4-1 | Q96RR4-5 | 588 | 498 | 542 | 554 | Deletion | none | none | 498 | 498 |
| Q96RR4 | CAMKK2 | Q96RR4-1 | Q96RR4-5 | 588 | 498 | 555 | 588 | Deletion | none | none | 498 | 498 |
| Q96RR4 | CAMKK2 | Q96RR4-1 | Q96RR4-6 | 588 | 490 | 442 | 484 | Deletion | none | none | 441 | 441 |
| Q96RR4 | CAMKK2 | Q96RR4-1 | Q96RR4-6 | 588 | 490 | 533 | 533 | Substitution | E | T | 490 | 490 |
| Q96RR4 | CAMKK2 | Q96RR4-1 | Q96RR4-6 | 588 | 490 | 534 | 554 | Deletion | none | none | 490 | 490 |
| Q96RR4 | CAMKK2 | Q96RR4-1 | Q96RR4-6 | 588 | 490 | 555 | 588 | Deletion | none | none | 490 | 490 |
| Q96RR4 | CAMKK2 | Q96RR4-1 | Q96RR4-7 | 588 | 556 | 533 | 554 | Substitution | EARQRRQPPGHRPAPRGGGGSA | GTKKKKGLDSMTSTVAAGWLDRRV | 533 | 556 |
| Q96RR4 | CAMKK2 | Q96RR4-1 | Q96RR4-7 | 588 | 556 | 555 | 588 | Deletion | none | none | 556 | 556 |
Multiple sequence alignment of our canonical and alternatively spliced CAMKK2 |
Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of CAMKK2 |
| UniProt-id | ENSG | ENST | ENSP |
| Q96RR4-1 | ENSG00000110931.19 | ENST00000324774.9 | ENSP00000312741.5 |
| Q96RR4-1 | ENSG00000110931.19 | ENST00000402834.8 | ENSP00000384591.4 |
| Q96RR4-1 | ENSG00000110931.19 | ENST00000404169.8 | ENSP00000384600.3 |
| Q96RR4-1 | ENSG00000110931.19 | ENST00000652382.1 | ENSP00000498824.1 |
| Q96RR4-2 | ENSG00000110931.19 | ENST00000392473.2 | ENSP00000376265.2 |
| Q96RR4-3 | ENSG00000110931.19 | ENST00000337174.7 | ENSP00000336634.3 |
| Q96RR4-3 | ENSG00000110931.19 | ENST00000412367.6 | ENSP00000388368.2 |
| Q96RR4-4 | ENSG00000110931.19 | ENST00000347034.6 | ENSP00000321230.3 |
| Q96RR4-5 | ENSG00000110931.19 | ENST00000538733.5 | ENSP00000445944.1 |
| Q96RR4-6 | ENSG00000110931.19 | ENST00000446440.6 | ENSP00000388273.2 |
| Q96RR4-7 | ENSG00000110931.19 | ENST00000392474.6 | ENSP00000376266.2 |
| UniProt-id | NM ID | NP ID |
| Q96RR4-1 | NM_001270485.1 | NP_001257414.1 |
| Q96RR4-1 | NM_006549.3 | NP_006540.3 |
| Q96RR4-2 | NM_172214.2 | NP_757363.1 |
| Q96RR4-2 | XM_005253823.1 | XP_005253880.1 |
| Q96RR4-3 | NM_153499.2 | NP_705719.2 |
| Q96RR4-3 | NM_172226.2 | NP_757380.1 |
| Q96RR4-4 | NM_172216.1 | NP_757365.1 |
| Q96RR4-4 | XM_005253822.3 | XP_005253879.1 |
| Q96RR4-5 | NM_153500.1 | NP_705720.1 |
| Q96RR4-5 | XM_005253824.3 | XP_005253881.1 |
| Q96RR4-6 | NM_172215.2 | NP_757364.1 |
| Q96RR4-7 | NM_001270486.1 | NP_001257415.1 |
| Q96RR4-7 | XM_011537763.1 | XP_011536065.1 |
| Q96RR4-7 | XM_017018702.1 | XP_016874191.1 |
Amino acid sequences of our canonical and alternatively spliced CAMKK2 |
| accession_id | Protein sequence |
| Q96RR4-1 | MSSCVSSQPSSNRAAPQDELGGRGSSSSESQKPCEALRGLSSLSIHLGMESFIVVTECEPGCAVDLGLARDRPLEADGQEVPLDTSGSQA RPHLSGRKLSLQERSQGGLAAGGSLDMNGRCICPSLPYSPVSSPQSSPRLPRRPTVESHHVSITGMQDCVQLNQYTLKDEIGKGSYGVVK LAYNENDNTYYAMKVLSKKKLIRQAGFPRRPPPRGTRPAPGGCIQPRGPIEQVYQEIAILKKLDHPNVVKLVEVLDDPNEDHLYMVFELV NQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDIKPSNLLVGEDGHIKIADFGVSNEFKGSDALLSNTVGTPAFMAPESLS ETRKIFSGKALDVWAMGVTLYCFVFGQCPFMDERIMCLHSKIKSQALEFPDQPDIAEDLKDLITRMLDKNPESRIVVPEIKLHPWVTRHG AEPLPSEDENCTLVEVTEEEVENSVKHIPSLATVILVKTMIRKRSFGNPFEGSRREERSLSAPGNLLTKKPTRECESLSELKEARQRRQP |
| Q96RR4-2 | MSSCVSSQPSSNRAAPQDELGGRGSSSSESQKPCEALRGLSSLSIHLGMESFIVVTECEPGCAVDLGLARDRPLEADGQEVPLDTSGSQA RPHLSGRKLSLQERSQGGLAAGGSLDMNGRCICPSLPYSPVSSPQSSPRLPRRPTVESHHVSITGMQDCVQLNQYTLKDEIGKGSYGVVK LAYNENDNTYYAMKVLSKKKLIRQAGFPRRPPPRGTRPAPGGCIQPRGPIEQVYQEIAILKKLDHPNVVKLVEVLDDPNEDHLYMVFELV NQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDIKPSNLLVGEDGHIKIADFGVSNEFKGSDALLSNTVGTPAFMAPESLS ETRKIFSGKALDVWAMGVTLYCFVFGQCPFMDERIMCLHSKIKSQALEFPDQPDIAEDLKDLITRMLDKNPESRIVVPEIKLHPWVTRHG |
| Q96RR4-3 | MSSCVSSQPSSNRAAPQDELGGRGSSSSESQKPCEALRGLSSLSIHLGMESFIVVTECEPGCAVDLGLARDRPLEADGQEVPLDTSGSQA RPHLSGRKLSLQERSQGGLAAGGSLDMNGRCICPSLPYSPVSSPQSSPRLPRRPTVESHHVSITGMQDCVQLNQYTLKDEIGKGSYGVVK LAYNENDNTYYAMKVLSKKKLIRQAGFPRRPPPRGTRPAPGGCIQPRGPIEQVYQEIAILKKLDHPNVVKLVEVLDDPNEDHLYMVFELV NQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDIKPSNLLVGEDGHIKIADFGVSNEFKGSDALLSNTVGTPAFMAPESLS ETRKIFSGKALDVWAMGVTLYCFVFGQCPFMDERIMCLHSKIKSQALEFPDQPDIAEDLKDLITRMLDKNPESRIVVPEIKLHPWVTRHG AEPLPSEDENCTLVEVTEEEVENSVKHIPSLATVILVKTMIRKRSFGNPFEGSRREERSLSAPGNLLTKQGSEDNLQGTDPPPVGEEEVL |
| Q96RR4-4 | MSSCVSSQPSSNRAAPQDELGGRGSSSSESQKPCEALRGLSSLSIHLGMESFIVVTECEPGCAVDLGLARDRPLEADGQEVPLDTSGSQA RPHLSGRKLSLQERSQGGLAAGGSLDMNGRCICPSLPYSPVSSPQSSPRLPRRPTVESHHVSITGMQDCVQLNQYTLKDEIGKGSYGVVK LAYNENDNTYYAMKVLSKKKLIRQAGFPRRPPPRGTRPAPGGCIQPRGPIEQVYQEIAILKKLDHPNVVKLVEVLDDPNEDHLYMVFELV NQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDIKPSNLLVGEDGHIKIADFGVSNEFKGSDALLSNTVGTPAFMAPESLS ETRKIFSGKALDVWAMGVTLYCFVFGQCPFMDERIMCLHSKIKSQALEFPDQPDIAEDLKDLITRMLDKNPESRIVVPEIKILVKTMIRK RSFGNPFEGSRREERSLSAPGNLLTKKPTRECESLSELKEARQRRQPPGHRPAPRGGGGSALVRGSPCVESCWAPAPGSPARMHPLRPEE |
| Q96RR4-5 | MSSCVSSQPSSNRAAPQDELGGRGSSSSESQKPCEALRGLSSLSIHLGMESFIVVTECEPGCAVDLGLARDRPLEADGQEVPLDTSGSQA RPHLSGRKLSLQERSQGGLAAGGSLDMNGRCICPSLPYSPVSSPQSSPRLPRRPTVESHHVSITGMQDCVQLNQYTLKDEIGKGSYGVVK LAYNENDNTYYAMKVLSKKKLIRQAGFPRRPPPRGTRPAPGGCIQPRGPIEQVYQEIAILKKLDHPNVVKLVEVLDDPNEDHLYMVFELV NQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDIKPSNLLVGEDGHIKIADFGVSNEFKGSDALLSNTVGTPAFMAPESLS ETRKIFSGKALDVWAMGVTLYCFVFGQCPFMDERIMCLHSKIKSQALEFPDQPDIAEDLKDLITRMLDKNPESRIVVPEIKILVKTMIRK |
| Q96RR4-6 | MSSCVSSQPSSNRAAPQDELGGRGSSSSESQKPCEALRGLSSLSIHLGMESFIVVTECEPGCAVDLGLARDRPLEADGQEVPLDTSGSQA RPHLSGRKLSLQERSQGGLAAGGSLDMNGRCICPSLPYSPVSSPQSSPRLPRRPTVESHHVSITGMQDCVQLNQYTLKDEIGKGSYGVVK LAYNENDNTYYAMKVLSKKKLIRQAGFPRRPPPRGTRPAPGGCIQPRGPIEQVYQEIAILKKLDHPNVVKLVEVLDDPNEDHLYMVFELV NQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDIKPSNLLVGEDGHIKIADFGVSNEFKGSDALLSNTVGTPAFMAPESLS ETRKIFSGKALDVWAMGVTLYCFVFGQCPFMDERIMCLHSKIKSQALEFPDQPDIAEDLKDLITRMLDKNPESRIVVPEIKILVKTMIRK |
| Q96RR4-7 | MSSCVSSQPSSNRAAPQDELGGRGSSSSESQKPCEALRGLSSLSIHLGMESFIVVTECEPGCAVDLGLARDRPLEADGQEVPLDTSGSQA RPHLSGRKLSLQERSQGGLAAGGSLDMNGRCICPSLPYSPVSSPQSSPRLPRRPTVESHHVSITGMQDCVQLNQYTLKDEIGKGSYGVVK LAYNENDNTYYAMKVLSKKKLIRQAGFPRRPPPRGTRPAPGGCIQPRGPIEQVYQEIAILKKLDHPNVVKLVEVLDDPNEDHLYMVFELV NQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDIKPSNLLVGEDGHIKIADFGVSNEFKGSDALLSNTVGTPAFMAPESLS ETRKIFSGKALDVWAMGVTLYCFVFGQCPFMDERIMCLHSKIKSQALEFPDQPDIAEDLKDLITRMLDKNPESRIVVPEIKLHPWVTRHG AEPLPSEDENCTLVEVTEEEVENSVKHIPSLATVILVKTMIRKRSFGNPFEGSRREERSLSAPGNLLTKKPTRECESLSELKGTKKKKGL |
Protein Functional Features |
Main function of this protein. (from UniProt) |
| CAMKK2 (go to UniProt):Q96RR4 |
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 |
| Q96RR4 | Domain | 165 | 446 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Deletion;Start=442;End=484 |
| Q96RR4 | Domain | 165 | 446 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Deletion;Start=442;End=484 |
| Q96RR4 | Domain | 165 | 446 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Deletion;Start=442;End=484 |
| Q96RR4 | Region | 472 | 477 | Note=Autoinhibitory domain;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=442;End=484 |
| Q96RR4 | Region | 472 | 477 | Note=Autoinhibitory domain;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=442;End=484 |
| Q96RR4 | Region | 472 | 477 | Note=Autoinhibitory domain;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=442;End=484 |
| Q96RR4 | Region | 475 | 500 | Note=Calmodulin-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=442;End=484 |
| Q96RR4 | Region | 475 | 500 | Note=Calmodulin-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=442;End=484 |
| Q96RR4 | Region | 475 | 500 | Note=Calmodulin-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 | Type=Deletion;Start=442;End=484 |
| Q96RR4 | Region | 497 | 588 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=533;End=533 |
| Q96RR4 | Region | 497 | 588 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=534;End=554 |
| Q96RR4 | Region | 497 | 588 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=555;End=588 |
| Q96RR4 | Region | 497 | 588 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=520;End=532 |
| Q96RR4 | Region | 497 | 588 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=533;End=541 |
| Q96RR4 | Region | 497 | 588 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=542;End=554 |
| Q96RR4 | Region | 497 | 588 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=555;End=588 |
| Q96RR4 | Region | 497 | 588 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=520;End=532 |
| Q96RR4 | Region | 497 | 588 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=533;End=541 |
| Q96RR4 | Region | 497 | 588 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=542;End=554 |
| Q96RR4 | Region | 497 | 588 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=555;End=588 |
| Q96RR4 | Region | 497 | 588 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=533;End=533 |
| Q96RR4 | Region | 497 | 588 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=534;End=554 |
| Q96RR4 | Region | 497 | 588 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=555;End=588 |
| Q96RR4 | Region | 497 | 588 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=533;End=554 |
| Q96RR4 | Region | 497 | 588 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=555;End=588 |
| Q96RR4 | Compositional bias | 523 | 540 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=533;End=533 |
| Q96RR4 | Compositional bias | 523 | 540 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=534;End=554 |
| Q96RR4 | Compositional bias | 523 | 540 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=520;End=532 |
| Q96RR4 | Compositional bias | 523 | 540 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=533;End=541 |
| Q96RR4 | Compositional bias | 523 | 540 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=520;End=532 |
| Q96RR4 | Compositional bias | 523 | 540 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=533;End=541 |
| Q96RR4 | Compositional bias | 523 | 540 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=533;End=533 |
| Q96RR4 | Compositional bias | 523 | 540 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=534;End=554 |
| Q96RR4 | Compositional bias | 523 | 540 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=533;End=554 |
Gene Isoform Structures and Expression Levels for CAMKK2 |
Gene structures of our canonical and alternative spliced genes of CAMKK2* 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 Q96RR4-1 |
| 3D view using mol* of Q96RR4-2 |
| 3D view using mol* of Q96RR4-3 |
| 3D view using mol* of Q96RR4-4 |
| 3D view using mol* of Q96RR4-5 |
| 3D view using mol* of Q96RR4-6 |
| 3D view using mol* of Q96RR4-7 |
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 Q96RR4-1 |
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| Ramachandran plot of Q96RR4-2 |
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| Ramachandran plot of Q96RR4-5 |
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| Ramachandran plot of Q96RR4-6 |
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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 |
| Q96RR4-1 | 1.14 | 215 | 1.176 | 351.918 | 0.356 | 0.85 | 1.122 | 1.905 | 0.842 | 2.263 | 0.735 | 49,50,51,53,54,55,56,58,169,170,171,172,173,174,17 5,176,177,178,179,181,192,194,196,233,236,240,249, 250,267,268,269,270,271,273,274,310,312,314,316,31 7,319,327,329,330,331,332,333,334,350 |
| Q96RR4-2 | 1.146 | 226 | 1.182 | 410.228 | 0.394 | 0.858 | 1.121 | 1.736 | 0.835 | 2.079 | 0.854 | 48,49,50,51,53,54,55,56,58,169,170,171,172,173,174 ,175,176,177,178,179,181,192,194,196,232,236,240,2 49,250,267,268,269,270,271,273,274,310,312,314,316 ,317,319,329,330,331,332,333,334 |
| Q96RR4-3 | 1.131 | 163 | 1.198 | 348.488 | 0.486 | 0.777 | 0.965 | 1.84 | 0.637 | 2.887 | 0.984 | 51,53,54,55,56,57,58,169,170,171,172,173,174,175,1 76,177,179,181,192,194,196,236,240,249,267,269,270 ,271,272,273,274,276,277,319,329,330,331 |
| Q96RR4-4 | 1.028 | 503 | 1.063 | 1410.759 | 0.604 | 0.705 | 0.891 | 0.744 | 0.92 | 0.808 | 0.947 | 43,44,45,46,47,48,49,50,51,52,53,54,55,56,58,169,1 70,171,172,173,174,175,176,177,178,179,181,192,194 ,196,201,202,204,205,206,207,208,223,224,225,226,2 27,228,229,232,233,235,236,238,239,240,249,250,267 ,268,269,270,271,273,274,277,278,279,311,312,314,3 15,316,319,327,329,330,331,332,333,334,335,336,337 ,338,341,342,343,344,345,346,347,348,349,350,351,3 52,353,354,357,360,361,362,363,364,366,387,388,391 ,392,393,394,395,398 |
| Q96RR4-5 | 1.179 | 161 | 1.23 | 318.647 | 0.383 | 0.873 | 1.147 | 2.215 | 0.717 | 3.09 | 1.144 | 49,51,52,53,55,56,58,169,171,172,173,174,175,176,1 77,178,179,181,190,192,194,236,240,249,267,269,270 ,271,273,274,312,314,317,319,329,330,331,332,333 |
| Q96RR4-6 | 1.035 | 448 | 1.06 | 1284.878 | 0.57 | 0.733 | 0.937 | 0.904 | 0.981 | 0.921 | 0.996 | 45,46,47,48,49,50,51,52,53,54,55,56,58,169,171,172 ,173,174,175,176,177,179,181,192,194,196,201,202,2 03,204,205,206,207,208,221,222,223,224,226,227,228 ,229,232,233,235,236,240,249,250,267,268,269,270,2 71,273,274,277,278,311,312,314,315,316,317,319,329 ,330,331,332,333,334,335,336,337,338,341,342,343,3 44,345,346,347,348,349,350,351,352,353,354,358,360 ,362,363,364,366,391,392,393,394,395,398,399 |
| Q96RR4-7 | 1.127 | 148 | 1.195 | 315.56 | 0.505 | 0.772 | 1.012 | 1.932 | 0.638 | 3.027 | 1.206 | 51,53,54,55,56,58,169,170,171,172,173,174,176,177, 179,181,192,194,196,236,240,249,250,267,268,269,27 0,271,273,274,319,329,330,331,332 |
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 Q96RR4-1_Q96RR4-1_6cmj_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 Q96RR4-1_6cmj_A_Q96RR4-2.pdb |
| 3D view using mol* of Q96RR4-1_6cmj_A_Q96RR4-3.pdb |
| 3D view using mol* of Q96RR4-1_6cmj_A_Q96RR4-4.pdb |
| 3D view using mol* of Q96RR4-1_6cmj_A_Q96RR4-5.pdb |
| 3D view using mol* of Q96RR4-1_6cmj_A_Q96RR4-6.pdb |
| 3D view using mol* of Q96RR4-1_6cmj_A_Q96RR4-7.pdb |
Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q96RR4-1_Q96RR4-2.pdb |
| 3D view using mol* of Q96RR4-1_Q96RR4-3.pdb |
| 3D view using mol* of Q96RR4-1_Q96RR4-4.pdb |
| 3D view using mol* of Q96RR4-1_Q96RR4-5.pdb |
| 3D view using mol* of Q96RR4-1_Q96RR4-6.pdb |
| 3D view using mol* of Q96RR4-1_Q96RR4-7.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 CAMKK2 |
Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
| Q96RR4 | CAMKK2 | DB12010 | Fostamatinib | approved, investigational | inhibitor |
Related Diseases to CAMKK2 |
Previous studies relating to the alternative splicing of CAMKK2 and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| CAMKK2 | 9662074 | Cloning, expression and chromosomal localization of human Ca2+/calmodulin-dependent protein kinase kinase. | A human cDNA clone encoding the calcium/calmodulin-dependent protein kinase kinase (CaMKK) was isolated by RT-PCR amplification of the fragment corresponding to the conserved kinase catalytic domain followed by rapid amplification of cDNA ends and cDNA library screening. Compilation of nucleotide sequencing data yielded a consensus cDNA sequence of 1.9 kb with an open reading frame of 1,251 nucleotides in length which translates to a polypeptide of 417 amino acids (47 kd). It showed significant homology to the rat brain CaMKK isozymes. The human CaMKK, which was expressed as a Flag-tagged protein in human non-small cell lung cancer H- 1299 cells followed by immunoprecipitation with anti-Flag antibody, was shown to phosphorylate recombinant human CaMK I in a calcium/CaM-dependent fashion. Northern blot analysis revealed that human CaMKK is ubiquitously expressed, with brain showing the highest level of expression. The CaMKK gene is localized to human chromosome 12. The presence of cDNA clones with divergent 3' terminal sequences suggests a family of CaMKK variants which may arise from alternative splicing. | D002289 | Carcinoma, Non-Small-Cell Lung |
| CAMKK2 | 9662074 | Cloning, expression and chromosomal localization of human Ca2+/calmodulin-dependent protein kinase kinase. | A human cDNA clone encoding the calcium/calmodulin-dependent protein kinase kinase (CaMKK) was isolated by RT-PCR amplification of the fragment corresponding to the conserved kinase catalytic domain followed by rapid amplification of cDNA ends and cDNA library screening. Compilation of nucleotide sequencing data yielded a consensus cDNA sequence of 1.9 kb with an open reading frame of 1,251 nucleotides in length which translates to a polypeptide of 417 amino acids (47 kd). It showed significant homology to the rat brain CaMKK isozymes. The human CaMKK, which was expressed as a Flag-tagged protein in human non-small cell lung cancer H- 1299 cells followed by immunoprecipitation with anti-Flag antibody, was shown to phosphorylate recombinant human CaMK I in a calcium/CaM-dependent fashion. Northern blot analysis revealed that human CaMKK is ubiquitously expressed, with brain showing the highest level of expression. The CaMKK gene is localized to human chromosome 12. The presence of cDNA clones with divergent 3' terminal sequences suggests a family of CaMKK variants which may arise from alternative splicing. | D008175 | Lung Neoplasms |
| CAMKK2 | 21957496 | Differential effects of PKA-controlled CaMKK2 variants on neuronal differentiation. | Regulation between protein kinases is critical for the establishment of signaling pathways/networks to 'orchestrate' cellular processes. Besides posttranslational phosphorylation, alternative pre-mRNA splicing is another way to control kinase properties, but splicing regulation between two kinases and the effect of resulting variants on cells has barely been explored. Here we examined the effect of the protein kinase A (PKA) pathway on the alternative splicing and variant properties of the Ca²âº/calmodulin-dependent protein kinase kinase 2 (CaMKK2) gene in B35 neuroblastoma cells. Inclusion of the exon 16 of CaMKK2 was significantly reduced by H89, a PKA selective inhibitor. Consistently, overexpressed PKA strongly promoted the exon inclusion in a CaMKK2 sequence-dependent way in splicing reporter assays. In vitro, purified CaMKKβ1 variant proteins were found to be kinase-active. In cells, they were differentially phosphorylated by PKA. In RNA interference assays, CaMKKβ1 was found to be essential for forskolin-induced neurite growth. Interestingly, overexpression of the variant without exon 16 (-E16) promoted neurite elongation while the other one (+E16) promoted neurite branching; in contrast, reduction of the latter one enhanced neurite elongation. Moreover, the variants are differentially expressed and the exon 16-containing transcripts highly enriched in the brain, particularly the cerebellum and hippocampus. Thus, PKA regulates the alternative splicing of CaMKK2 to produce variants that differentially modulate neuronal differentiation. Taken together with the many distinct variants of kinases, alternative splicing regulation likely adds another layer of modulation between protein kinases in cellular signaling networks. | D009447 | Neuroblastoma |
Clinically important variants in CAMKK2 |
(ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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