| UniProt ID | KKCC2_MOUSE | |
|---|---|---|
| UniProt AC | Q8C078 | |
| Protein Name | Calcium/calmodulin-dependent protein kinase kinase 2 | |
| Gene Name | Camkk2 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 588 | |
| Subcellular Localization | Nucleus. Cytoplasm. Cell projection. Predominantly nuclear in unstimulated cells. Found in the cytoplasm and neurites after forskolin induction.. | |
| Protein Description | Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Phosphorylates CAMK1, CAMK4 and CAMK1D (By similarity). Efficiently phosphorylates 5'-AMP-activated protein kinase (AMPK) trimer, including that consisting of PRKAA1, PRKAB1 and PRKAG1. This phosphorylation is stimulated in response to Ca(2+) signals (By similarity). May play a role in neurite growth. Isoform 2 may promote neurite elongation, while isoform 1 may promoter neurite branching (By similarity). May be involved in hippocampal activation of CREB1.. | |
| Protein Sequence | MSSCVSSQPTSDRVAPQDELGSGGGSREGQKPCEALRGLSSLSIHLGMESFIVVTECEPGRGVDLNLARDQPPEADGQELPLEASDPESRSPLSGRKMSLQEPSQGGPASSSNSLDMNGRCICPSLSYSPASSPQSSPRMPRRPTVESHHVSITGLQDCVQLNQYTLKDEIGKGSYGVVKLAYNENDNTYYAMKVLSKKKLIRQAGFPRRPPPRGARPAPGGCIQPRGPIEQVYQEIAILKKLDHPNVVKLVEVLDDPNEDHLYMVFELVNQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDIKPSNLLVGEDGHIKIADFGVSNEFKGSDALLSNTVGTPAFMAPESLSETRKIFSGKALDVWAMGVTLYCFVFGQCPFMDERIMCLHSKIKSQALEFPDQPDIAEDLKDLITRMLDKNPESRIVVPEIKLHPWVTRHGAEPLPSEDENCTLVEVTEEEVENSVKHIPSLATVILVKTMIRKRSFGNPFEGSRREERSLSAPGNLLTKKPTREWEPLSEPKEARQRRQPPGPRAGPCGGGGSALVKGGPCVESWGAPAPGSPPRMPPLQPEEVMEPE | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MSSCVSSQP ------CCCCCCCCC | 32.23 | - | |
| 85 | Phosphorylation | QELPLEASDPESRSP CCCCCCCCCCCCCCC | 44.30 | 21082442 | |
| 89 | Phosphorylation | LEASDPESRSPLSGR CCCCCCCCCCCCCCC | 43.37 | 26824392 | |
| 91 | Phosphorylation | ASDPESRSPLSGRKM CCCCCCCCCCCCCCC | 39.20 | 25521595 | |
| 94 | Phosphorylation | PESRSPLSGRKMSLQ CCCCCCCCCCCCCCC | 39.68 | 25619855 | |
| 99 | Phosphorylation | PLSGRKMSLQEPSQG CCCCCCCCCCCCCCC | 29.90 | 25521595 | |
| 104 | Phosphorylation | KMSLQEPSQGGPASS CCCCCCCCCCCCCCC | 40.48 | 25619855 | |
| 110 | Phosphorylation | PSQGGPASSSNSLDM CCCCCCCCCCCCCCC | 37.12 | 25619855 | |
| 111 | Phosphorylation | SQGGPASSSNSLDMN CCCCCCCCCCCCCCC | 35.33 | 25619855 | |
| 112 | Phosphorylation | QGGPASSSNSLDMNG CCCCCCCCCCCCCCC | 28.13 | 25619855 | |
| 114 | Phosphorylation | GPASSSNSLDMNGRC CCCCCCCCCCCCCEE | 27.91 | 25619855 | |
| 125 | Phosphorylation | NGRCICPSLSYSPAS CCEEECCCCCCCCCC | 26.07 | 26643407 | |
| 127 | Phosphorylation | RCICPSLSYSPASSP EEECCCCCCCCCCCC | 28.09 | 26745281 | |
| 128 | Phosphorylation | CICPSLSYSPASSPQ EECCCCCCCCCCCCC | 24.78 | 26745281 | |
| 129 | Phosphorylation | ICPSLSYSPASSPQS ECCCCCCCCCCCCCC | 15.60 | 21082442 | |
| 132 | Phosphorylation | SLSYSPASSPQSSPR CCCCCCCCCCCCCCC | 46.03 | 21082442 | |
| 133 | Phosphorylation | LSYSPASSPQSSPRM CCCCCCCCCCCCCCC | 29.12 | 25521595 | |
| 136 | Phosphorylation | SPASSPQSSPRMPRR CCCCCCCCCCCCCCC | 45.77 | 25168779 | |
| 137 | Phosphorylation | PASSPQSSPRMPRRP CCCCCCCCCCCCCCC | 15.98 | 21082442 | |
| 154 | Phosphorylation | ESHHVSITGLQDCVQ CCCCCEEECHHHHHH | 25.08 | 29899451 | |
| 176 | Phosphorylation | DEIGKGSYGVVKLAY CCCCCCCCEEEEEEE | 23.70 | - | |
| 190 | Phosphorylation | YNENDNTYYAMKVLS EECCCCCEEEEHHHC | 8.76 | - | |
| 191 | Phosphorylation | NENDNTYYAMKVLSK ECCCCCEEEEHHHCH | 9.74 | - | |
| 223 | Glutathionylation | ARPAPGGCIQPRGPI CCCCCCCCCCCCCHH | 3.02 | 24333276 | |
| 456 | Phosphorylation | HGAEPLPSEDENCTL CCCCCCCCCCCCCEE | 66.42 | - | |
| 462 | Phosphorylation | PSEDENCTLVEVTEE CCCCCCCEEEECCHH | 45.48 | 29899451 | |
| 474 | Phosphorylation | TEEEVENSVKHIPSL CHHHHHHHHCCCCHH | 21.02 | - | |
| 483 | Phosphorylation | KHIPSLATVILVKTM CCCCHHHHHHHHHHH | 17.24 | 21183079 | |
| 489 | Phosphorylation | ATVILVKTMIRKRSF HHHHHHHHHHHHHCC | 15.45 | - | |
| 495 | Phosphorylation | KTMIRKRSFGNPFEG HHHHHHHCCCCCCCC | 40.31 | 25521595 | |
| 503 | Phosphorylation | FGNPFEGSRREERSL CCCCCCCCCCHHHCC | 22.44 | 28833060 | |
| 509 | Phosphorylation | GSRREERSLSAPGNL CCCCHHHCCCCCCCC | 29.92 | 22324799 | |
| 511 | Phosphorylation | RREERSLSAPGNLLT CCHHHCCCCCCCCCC | 33.39 | 22942356 | |
| 511 (in isoform 2) | Phosphorylation | - | 33.39 | 27566939 | |
| 518 | Phosphorylation | SAPGNLLTKKPTREW CCCCCCCCCCCCCCC | 39.94 | 28833060 | |
| 522 | Phosphorylation | NLLTKKPTREWEPLS CCCCCCCCCCCCCCC | 50.53 | 24719451 | |
| 522 (in isoform 2) | Phosphorylation | - | 50.53 | 25266776 | |
| 525 (in isoform 2) | Phosphorylation | - | 14.82 | 30635358 | |
| 564 | Phosphorylation | KGGPCVESWGAPAPG ECCCCCCCCCCCCCC | 15.48 | 25619855 | |
| 572 | Phosphorylation | WGAPAPGSPPRMPPL CCCCCCCCCCCCCCC | 30.58 | 25521595 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of KKCC2_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KKCC2_MOUSE !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of KKCC2_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of KKCC2_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129 AND SER-133, ANDMASS SPECTROMETRY. | |
| "Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, AND MASSSPECTROMETRY. | |