| Tag | Content |
|---|
| EKPD ID | EKS-MUM-00506 |
| Classification | | Group/Family | Score | E-Value | Start | End | Domain Length |
|---|
| CAMK/CAMK2 | 588.2 | 4.2E-177 | 14 | 272 | 259 |
|
| Status | Reviewed |
| Ensembl Protein | ENSMUSP00000133019 |
| UniProt Accession | Q6PHZ2; Q3UF87; Q3UQH9; Q5DTK4; Q8CAC5; Q9CZE2; |
| Protein Name | Calcium/calmodulin-dependent protein kinase type II subunit delta |
| Protein Synonyms/Alias | CaM kinase II subunit delta; CaMK-II subunit delta; |
| Gene Name | Camk2d |
| Gene Synonyms/Alias | Camk2d; Kiaa4163; |
| Ensembl Information | |
| Organism | Mus musculus |
| Functional Description | Calcium/calmodulin-dependent protein kinase involved inthe regulation of Ca(2+) homeostatis and excitation-contraction coupling (ECC) in heart by targeting ion channels, transporters and accessory proteins involved in Ca(2+) influx into the myocyte, Ca(2+) release from the sarcoplasmic reticulum (SR), SR Ca(2+) uptake and Na(+) and K(+) channel transport. Targets also transcription factors and signaling molecules to regulate heart function. In its activated form, is involved in the pathogenesis of dilated cardiomyopathy and heart failure. Contributes to cardiac decompensation and heart failure by regulating SR Ca(2+) release via direct phosphorylation of RYR2 Ca(2+) channel on 'Ser- 2808'. In the nucleus, phosphorylates the MEF2 repressor HDAC4, promoting its nuclear export and binding to 14-3-3 protein, and expression of MEF2 and genes involved in the hypertrophic program. Is essential for left ventricular remodeling responses to myocardial infarction. In pathological myocardial remodeling acts downstream of the beta adrenergic receptor signaling cascade to regulate key proteins involved in ECC. Regulates Ca(2+) influx to myocytes by binding and phosphorylating the L-type Ca(2+) channel subunit beta-2 CACNB2. In addition to Ca(2+) channels, can target and regulate the cardiac sarcolemmal Na(+) channel Nav1.5/SCN5A and the K+ channel Kv4.3/KCND3, which contribute to arrhythmogenesis in heart failure. Phosphorylates phospholamban (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2, contributing to the enhancement of SR Ca(2+) uptake that may be important in frequency-dependent acceleration of relaxation (FDAR) and maintenance of contractile function during acidosis. May participate in the modulation of skeletal muscle function in response to exercise, by regulating SR Ca(2+) transport through phosphorylation of PLN/PLB and triadin, a ryanodine receptor- coupling factor. |
| Protein Length | 361 |
Protein Sequence
(FASTA) | | MASTTTCTRF TDEYQLFEEL GKGAFSVVRR CMKIPTGQEY AAKIINTKKL SARDHQKLER 60 | | EARICRLLKH PNIVRLHDSI SEEGFHYLVF DLVTGGELFE DIVAREYYSE ADASHCIQQI 120 | | LESVNHCHLN GIVHRDLKPE NLLLASKSKG AAVKLADFGL AIEVQGDQQA WFGFAGTPGY 180 | | LSPEVLRKDP YGKPVDMWAC GVILYILLVG YPPFWDEDQH RLYQQIKAGA YDFPSPEWDT 240 | | VTPEAKDLIN KMLTINPAKR ITASEALKHP WICQRSTVAS MMHRQETVDC LKKFNARRKL 300 | | KGAILTTMLA TRNFSAAKSL LKKPDGVKES TESSNTTIED EDVKATVCRA CRCMPQCLST 360 | | S 361 |
|
Nucleotide Sequence
(FASTA) | | ATGGCTTCGA CCACCACCTG CACCCGGTTC ACCGACGAGT ATCAGCTCTT TGAGGAGCTC 60 | | GGAAAGGGGG CGTTCTCAGT GGTGAGAAGA TGTATGAAAA TCCCTACTGG ACAAGAGTAT 120 | | GCTGCCAAAA TTATCAACAC CAAAAAGCTT TCTGCTAGGG ACCATCAGAA ACTGGAAAGG 180 | | GAAGCTAGAA TCTGCCGTCT CTTGAAGCAC CCCAATATTG TGAGACTTCA CGACAGTATA 240 | | TCGGAGGAGG GCTTCCATTA CTTGGTGTTT GACTTAGTGA CTGGTGGCGA ACTGTTTGAA 300 | | GACATAGTGG CAAGAGAATA TTACAGTGAA GCTGATGCCA GTCATTGTAT ACAACAGATT 360 | | CTAGAGAGTG TAAATCATTG TCACCTAAAT GGCATAGTTC ACAGGGACCT GAAGCCTGAG 420 | | AATTTGCTTT TAGCTAGCAA GTCCAAAGGA GCAGCTGTGA AGCTGGCAGA CTTCGGCTTA 480 | | GCCATAGAAG TTCAAGGCGA CCAGCAGGCA TGGTTTGGTT TTGCTGGCAC ACCTGGGTAT 540 | | CTTTCTCCAG AAGTCCTGCG TAAAGATCCT TATGGAAAAC CAGTGGATAT GTGGGCATGC 600 | | GGTGTCATCC TCTACATCTT GCTGGTGGGA TACCCACCCT TCTGGGATGA AGATCAGCAT 660 | | AGACTGTATC AGCAGATCAA GGCCGGAGCT TACGATTTTC CGTCACCAGA ATGGGATACA 720 | | GTGACACCTG AAGCCAAAGA CCTCATCAAC AAAATGCTGA CCATCAACCC TGCCAAACGT 780 | | ATCACAGCCT CTGAGGCCCT GAAACACCCA TGGATCTGTC AACGCTCTAC TGTTGCCTCC 840 | | ATGATGCACA GGCAGGAGAC TGTAGACTGC TTGAAGAAAT TTAATGCTAG ACGGAAACTG 900 | | AAGGGCGCCA TCTTGACAAC TATGCTGGCT ACGAGAAATT TTTCAGCAGC CAAGAGTTTA 960 | | TTGAAGAAAC CAGATGGGGT AAAGGAGTCA ACTGAGAGCT CAAACACCAC CATTGAGGAT 1020 | | GAAGACGTGA AAGCCACGGT TTGCAGGGCC TGTCGCTGTA TGCCACAATG CCTCTCCACC 1080 | | TCCTAA 1086 |
|
| Domain Profile | S: 1 yqlfeelgkgafsvvrrcvkvttgqeyaakiintkklsardhqklerearicrllkhpni 60 | yqlfeelgkgafsvvrrc+k+ tgqeyaakiintkklsardhqklerearicrllkhpni | Q: 14 YQLFEELGKGAFSVVRRCMKIPTGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNI 73 | 9*********************************************************** |
| S: 61 vrlhdsiseegfhylvfdlvtggelfedivareyyseadashciqqilesvlhihqngvv 120 | vrlhdsiseegfhylvfdlvtggelfedivareyyseadashciqqilesv+h+h ng+v | Q: 74 VRLHDSISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILESVNHCHLNGIV 133 | ************************************************************ |
| S: 121 hrdlkpenlllaskakgaavkladfglaievqgdqqawfgfagtpgylspevlrkdpygk 180 | hrdlkpenlllask+kgaavkladfglaievqgdqqawfgfagtpgylspevlrkdpygk | Q: 134 HRDLKPENLLLASKSKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKDPYGK 193 | ************************************************************ |
| S: 181 pvdlwacgvilyillvgyppfwdedqhrlyqqikagaydfpspewdtvtpeakdlinkml 240 | pvd+wacgvilyillvgyppfwdedqhrlyqqikagaydfpspewdtvtpeakdlinkml | Q: 194 PVDMWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKML 253 | ************************************************************ |
| S: 241 tinpakritadealkhpwi 259 | tinpakrita+ealkhpwi | Q: 254 TINPAKRITASEALKHPWI 272 | ******************8 |
|
Domain Sequence
(FASTA) | | YQLFEELGKG AFSVVRRCMK IPTGQEYAAK IINTKKLSAR DHQKLEREAR ICRLLKHPNI 60 | | VRLHDSISEE GFHYLVFDLV TGGELFEDIV AREYYSEADA SHCIQQILES VNHCHLNGIV 120 | | HRDLKPENLL LASKSKGAAV KLADFGLAIE VQGDQQAWFG FAGTPGYLSP EVLRKDPYGK 180 | | PVDMWACGVI LYILLVGYPP FWDEDQHRLY QQIKAGAYDF PSPEWDTVTP EAKDLINKML 240 | | TINPAKRITA SEALKHPWI 259 |
|
| Keyword | Acetylation; Alternative splicing; ATP-binding; Calmodulin-binding; Cell membrane; Complete proteome; Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Sarcoplasmic reticulum; Serine/threonine-protein kinase; Transferase. |
| Sequence Source | Ensembl |
| Orthology | |
| Gene Ontology | |
| KEGG | |
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| Created Date | 20-Feb-2013 |