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Protein

Calcium/calmodulin-dependent protein kinase type II subunit delta

Gene

Camk2d

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Calcium/calmodulin-dependent protein kinase involved in the regulation of Ca2+ homeostatis and excitation-contraction coupling (ECC) in heart by targeting ion channels, transporters and accessory proteins involved in Ca2+ influx into the myocyte, Ca2+ release from the sarcoplasmic reticulum (SR), SR Ca2+ 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 Ca2+ release via direct phosphorylation of RYR2 Ca2+ 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 Ca2+ influx to myocytes by binding and phosphorylating the L-type Ca2+ channel subunit beta-2 CACNB2. In addition to Ca2+ 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 Ca2+ 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 Ca2+ transport through phosphorylation of PLN/PLB and triadin, a ryanodine receptor-coupling factor.7 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by Ca2+/calmodulin. Binding of calmodulin results in conformational change that relieves intrasteric autoinhibition and allows autophosphorylation of Thr-287 which turns the kinase in a constitutively active form and confers to the kinase a Ca2+-independent activity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei43 – 431ATPPROSITE-ProRule annotation
Active sitei136 – 1361Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi20 – 289ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calmodulin binding Source: MGI
  • calmodulin-dependent protein kinase activity Source: BHF-UCL
  • ion channel binding Source: BHF-UCL
  • protein homodimerization activity Source: MGI
  • protein serine/threonine kinase activity Source: MGI
  • sodium channel inhibitor activity Source: MGI
  • titin binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.17. 3474.
ReactomeiR-MMU-3371571. HSF1-dependent transactivation.
R-MMU-399719. Trafficking of AMPA receptors.
R-MMU-438066. Unblocking of NMDA receptor, glutamate binding and activation.
R-MMU-442729. CREB phosphorylation through the activation of CaMKII.
R-MMU-442742. CREB phosphorylation through the activation of Ras.
R-MMU-442982. Ras activation uopn Ca2+ infux through NMDA receptor.
R-MMU-5576892. Phase 0 - rapid depolarisation.
R-MMU-5578775. Ion homeostasis.
R-MMU-5673001. RAF/MAP kinase cascade.
R-MMU-877300. Interferon gamma signaling.
R-MMU-936837. Ion transport by P-type ATPases.

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium/calmodulin-dependent protein kinase type II subunit delta (EC:2.7.11.17)
Short name:
CaM kinase II subunit delta
Short name:
CaMK-II subunit delta
Gene namesi
Name:Camk2d
Synonyms:Kiaa4163
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1341265. Camk2d.

Subcellular locationi

GO - Cellular componenti

  • axon initial segment Source: MGI
  • calcium channel complex Source: Ensembl
  • cytoplasm Source: MGI
  • cytosol Source: Ensembl
  • intercalated disc Source: MGI
  • membrane Source: MGI
  • neuromuscular junction Source: MGI
  • neuronal cell body Source: MGI
  • nucleus Source: MGI
  • perinuclear region of cytoplasm Source: Ensembl
  • sarcoplasmic reticulum Source: MGI
  • sarcoplasmic reticulum membrane Source: UniProtKB-SubCell
  • T-tubule Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Sarcoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 499498Calcium/calmodulin-dependent protein kinase type II subunit deltaPRO_0000277817Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei287 – 2871Phosphothreonine; by autocatalysisCurated
Modified residuei306 – 3061Phosphothreonine; by autocatalysisBy similarity
Modified residuei307 – 3071Phosphothreonine; by autocatalysisBy similarity
Modified residuei315 – 3151PhosphoserineBy similarity
Modified residuei318 – 3181N6-acetyllysineCombined sources
Modified residuei319 – 3191PhosphoserineBy similarity
Modified residuei330 – 3301PhosphoserineCombined sources
Modified residuei331 – 3311PhosphothreonineBy similarity
Modified residuei333 – 3331PhosphoserineCombined sources
Modified residuei336 – 3361PhosphothreonineCombined sources
Modified residuei337 – 3371PhosphothreonineCombined sources
Modified residuei404 – 4041PhosphoserineBy similarity
Modified residuei490 – 4901PhosphoserineBy similarity
Modified residuei494 – 4941PhosphoserineCombined sources

Post-translational modificationi

Autophosphorylation of Thr-287 following activation by Ca2+/calmodulin. Phosphorylation of Thr-287 locks the kinase into an activated state (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ6PHZ2.
MaxQBiQ6PHZ2.
PeptideAtlasiQ6PHZ2.
PRIDEiQ6PHZ2.

PTM databases

iPTMnetiQ6PHZ2.
PhosphoSiteiQ6PHZ2.
SwissPalmiQ6PHZ2.

Expressioni

Tissue specificityi

Expressed in cardiac muscle and skeletal muscle. Isoform Delta 2, isoform Delta 6, isoform Delta 6 and isoform Delta 10 are expressed in cardiac muscle. Isoform Delta 2 is expressed in skeletal muscle.1 Publication

Gene expression databases

BgeeiQ6PHZ2.
ExpressionAtlasiQ6PHZ2. baseline and differential.
GenevisibleiQ6PHZ2. MM.

Interactioni

Subunit structurei

CAMK2 is composed of 4 different chains: alpha (CAMK2A), beta (CAMK2B), gamma (CAMK2G), and delta (CAMK2D). The different isoforms assemble into homo- or heteromultimeric holoenzymes composed of 12 subunits with two hexameric rings stacked one on top of the other. Interacts with RRAD (By similarity). Interacts with CACNB2.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
FliiQ9JJ285EBI-2308458,EBI-7996161

GO - Molecular functioni

  • calmodulin binding Source: MGI
  • ion channel binding Source: BHF-UCL
  • protein homodimerization activity Source: MGI
  • titin binding Source: MGI

Protein-protein interaction databases

BioGridi223798. 4 interactions.
DIPiDIP-47638N.
IntActiQ6PHZ2. 13 interactions.
MINTiMINT-4391081.

Structurei

3D structure databases

ProteinModelPortaliQ6PHZ2.
SMRiQ6PHZ2. Positions 8-474.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 272259Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni283 – 29210Autoinhibitory domainBy similarity
Regioni291 – 30111Calmodulin-bindingBy similarityAdd
BLAST

Domaini

The CAMK2 protein kinases contain a unique C-terminal subunit association domain responsible for oligomerization.

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00760000118944.
HOGENOMiHOG000233016.
HOVERGENiHBG108055.
InParanoidiQ6PHZ2.
KOiK04515.
OrthoDBiEOG7ZD1VM.
PhylomeDBiQ6PHZ2.

Family and domain databases

Gene3Di3.10.450.50. 1 hit.
InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR013543. Ca/CaM-dep_prot_kinase-assoc.
IPR011009. Kinase-like_dom.
IPR032710. NTF2-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 1 hit.
PfamiPF08332. CaMKII_AD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF54427. SSF54427. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6PHZ2-1) [UniParc]FASTAAdd to basket

Also known as: Delta 2

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASTTTCTRF TDEYQLFEEL GKGAFSVVRR CMKIPTGQEY AAKIINTKKL
60 70 80 90 100
SARDHQKLER EARICRLLKH PNIVRLHDSI SEEGFHYLVF DLVTGGELFE
110 120 130 140 150
DIVAREYYSE ADASHCIQQI LESVNHCHLN GIVHRDLKPE NLLLASKSKG
160 170 180 190 200
AAVKLADFGL AIEVQGDQQA WFGFAGTPGY LSPEVLRKDP YGKPVDMWAC
210 220 230 240 250
GVILYILLVG YPPFWDEDQH RLYQQIKAGA YDFPSPEWDT VTPEAKDLIN
260 270 280 290 300
KMLTINPAKR ITASEALKHP WICQRSTVAS MMHRQETVDC LKKFNARRKL
310 320 330 340 350
KGAILTTMLA TRNFSAAKSL LKKPDGVKES TESSNTTIED EDVKARKQEI
360 370 380 390 400
IKVTEQLIEA INNGDFEAYT KICDPGLTAF EPEALGNLVE GMDFHRFYFE
410 420 430 440 450
NALSKSNKPI HTIILNPHVH LVGDDAACIA YIRLTQYMDG SGMPKTMQSE
460 470 480 490
ETRVWHRRDG KWQNVHFHRS GSPTVPIKPP CIPNGKENFS GGTSLWQNI
Length:499
Mass (Da):56,369
Last modified:July 5, 2004 - v1
Checksum:i62999FBAB98120CE
GO
Isoform 2 (identifier: Q6PHZ2-2) [UniParc]FASTAAdd to basket

Also known as: Delta 6

The sequence of this isoform differs from the canonical sequence as follows:
     478-478: K → N
     479-499: Missing.

Show »
Length:478
Mass (Da):54,114
Checksum:i506DA27C914E4F7E
GO
Isoform 3 (identifier: Q6PHZ2-4) [UniParc]FASTAAdd to basket

Also known as: Delta 10

The sequence of this isoform differs from the canonical sequence as follows:
     329-329: E → EPQTTVIHNPDGNKE
     478-478: K → N
     479-499: Missing.

Show »
Length:492
Mass (Da):55,645
Checksum:iE0FD0E736590F908
GO
Isoform 4 (identifier: Q6PHZ2-5) [UniParc]FASTAAdd to basket

Also known as: Delta 5

The sequence of this isoform differs from the canonical sequence as follows:
     328-328: K → KINNKANVVTSPKENIPTPALEPQTTVIHNPDGNK
     478-478: K → N
     479-499: Missing.

Show »
Length:512
Mass (Da):57,748
Checksum:i7DA5645FB35B3EAD
GO

Sequence cautioni

The sequence BAD90304.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti123 – 1253SVN → AVL in BAC30232 (PubMed:16141072).Curated
Sequence conflicti129 – 1324LNGI → QMGV in BAC30232 (PubMed:16141072).Curated
Sequence conflicti199 – 1991A → V in BAC30232 (PubMed:16141072).Curated
Isoform 2 (identifier: Q6PHZ2-2)
Sequence conflicti478 – 4781N → K in BAE25062 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei328 – 3281K → KINNKANVVTSPKENIPTPA LEPQTTVIHNPDGNK in isoform 4. 2 PublicationsVSP_023100
Alternative sequencei329 – 3291E → EPQTTVIHNPDGNKE in isoform 3. 1 PublicationVSP_023101
Alternative sequencei478 – 4781K → N in isoform 2, isoform 3 and isoform 4. 2 PublicationsVSP_023103
Alternative sequencei479 – 49921Missing in isoform 2, isoform 3 and isoform 4. 2 PublicationsVSP_023102Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK039076 mRNA. Translation: BAC30232.1.
AK012702 mRNA. Translation: BAB28422.1.
AK142435 mRNA. Translation: BAE25062.1.
AK148840 mRNA. Translation: BAE28674.1.
AK220516 mRNA. Translation: BAD90304.1. Different initiation.
BC052894 mRNA. Translation: AAH52894.1.
CCDSiCCDS17823.1. [Q6PHZ2-1]
CCDS51065.1. [Q6PHZ2-2]
CCDS80015.1. [Q6PHZ2-5]
CCDS80016.1. [Q6PHZ2-4]
RefSeqiNP_001020609.1. NM_001025438.2. [Q6PHZ2-1]
NP_001020610.1. NM_001025439.2.
NP_001280592.1. NM_001293663.1. [Q6PHZ2-5]
NP_001280593.1. NM_001293664.1. [Q6PHZ2-4]
NP_076302.1. NM_023813.4. [Q6PHZ2-2]
UniGeneiMm.255822.
Mm.442379.

Genome annotation databases

EnsembliENSMUST00000066466; ENSMUSP00000063359; ENSMUSG00000053819. [Q6PHZ2-4]
ENSMUST00000106400; ENSMUSP00000102008; ENSMUSG00000053819. [Q6PHZ2-2]
ENSMUST00000106402; ENSMUSP00000102010; ENSMUSG00000053819. [Q6PHZ2-5]
ENSMUST00000199300; ENSMUSP00000143504; ENSMUSG00000053819. [Q6PHZ2-1]
GeneIDi108058.
KEGGimmu:108058.
UCSCiuc008rgh.2. mouse. [Q6PHZ2-1]
uc008rgl.2. mouse. [Q6PHZ2-2]
uc008rgn.2. mouse. [Q6PHZ2-5]
uc008rgo.2. mouse. [Q6PHZ2-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK039076 mRNA. Translation: BAC30232.1.
AK012702 mRNA. Translation: BAB28422.1.
AK142435 mRNA. Translation: BAE25062.1.
AK148840 mRNA. Translation: BAE28674.1.
AK220516 mRNA. Translation: BAD90304.1. Different initiation.
BC052894 mRNA. Translation: AAH52894.1.
CCDSiCCDS17823.1. [Q6PHZ2-1]
CCDS51065.1. [Q6PHZ2-2]
CCDS80015.1. [Q6PHZ2-5]
CCDS80016.1. [Q6PHZ2-4]
RefSeqiNP_001020609.1. NM_001025438.2. [Q6PHZ2-1]
NP_001020610.1. NM_001025439.2.
NP_001280592.1. NM_001293663.1. [Q6PHZ2-5]
NP_001280593.1. NM_001293664.1. [Q6PHZ2-4]
NP_076302.1. NM_023813.4. [Q6PHZ2-2]
UniGeneiMm.255822.
Mm.442379.

3D structure databases

ProteinModelPortaliQ6PHZ2.
SMRiQ6PHZ2. Positions 8-474.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi223798. 4 interactions.
DIPiDIP-47638N.
IntActiQ6PHZ2. 13 interactions.
MINTiMINT-4391081.

PTM databases

iPTMnetiQ6PHZ2.
PhosphoSiteiQ6PHZ2.
SwissPalmiQ6PHZ2.

Proteomic databases

EPDiQ6PHZ2.
MaxQBiQ6PHZ2.
PeptideAtlasiQ6PHZ2.
PRIDEiQ6PHZ2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000066466; ENSMUSP00000063359; ENSMUSG00000053819. [Q6PHZ2-4]
ENSMUST00000106400; ENSMUSP00000102008; ENSMUSG00000053819. [Q6PHZ2-2]
ENSMUST00000106402; ENSMUSP00000102010; ENSMUSG00000053819. [Q6PHZ2-5]
ENSMUST00000199300; ENSMUSP00000143504; ENSMUSG00000053819. [Q6PHZ2-1]
GeneIDi108058.
KEGGimmu:108058.
UCSCiuc008rgh.2. mouse. [Q6PHZ2-1]
uc008rgl.2. mouse. [Q6PHZ2-2]
uc008rgn.2. mouse. [Q6PHZ2-5]
uc008rgo.2. mouse. [Q6PHZ2-4]

Organism-specific databases

CTDi817.
MGIiMGI:1341265. Camk2d.
RougeiSearch...

Phylogenomic databases

GeneTreeiENSGT00760000118944.
HOGENOMiHOG000233016.
HOVERGENiHBG108055.
InParanoidiQ6PHZ2.
KOiK04515.
OrthoDBiEOG7ZD1VM.
PhylomeDBiQ6PHZ2.

Enzyme and pathway databases

BRENDAi2.7.11.17. 3474.
ReactomeiR-MMU-3371571. HSF1-dependent transactivation.
R-MMU-399719. Trafficking of AMPA receptors.
R-MMU-438066. Unblocking of NMDA receptor, glutamate binding and activation.
R-MMU-442729. CREB phosphorylation through the activation of CaMKII.
R-MMU-442742. CREB phosphorylation through the activation of Ras.
R-MMU-442982. Ras activation uopn Ca2+ infux through NMDA receptor.
R-MMU-5576892. Phase 0 - rapid depolarisation.
R-MMU-5578775. Ion homeostasis.
R-MMU-5673001. RAF/MAP kinase cascade.
R-MMU-877300. Interferon gamma signaling.
R-MMU-936837. Ion transport by P-type ATPases.

Miscellaneous databases

PROiQ6PHZ2.
SOURCEiSearch...

Gene expression databases

BgeeiQ6PHZ2.
ExpressionAtlasiQ6PHZ2. baseline and differential.
GenevisibleiQ6PHZ2. MM.

Family and domain databases

Gene3Di3.10.450.50. 1 hit.
InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR013543. Ca/CaM-dep_prot_kinase-assoc.
IPR011009. Kinase-like_dom.
IPR032710. NTF2-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 1 hit.
PfamiPF08332. CaMKII_AD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF54427. SSF54427. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
    Strain: C57BL/6J.
    Tissue: Hypothalamus, Stomach and Sympathetic ganglion.
  2. "Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Fetal brain.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C3H/He.
    Tissue: Osteoblast.
  4. "delta-Ca(2+)/calmodulin-dependent protein kinase II expression pattern in adult mouse heart and cardiogenic differentiation of embryonic stem cells."
    Hoch B., Wobus A.M., Krause E.G., Karczewski P.
    J. Cell. Biochem. 79:293-300(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. "The deltaC isoform of CaMKII is activated in cardiac hypertrophy and induces dilated cardiomyopathy and heart failure."
    Zhang T., Maier L.S., Dalton N.D., Miyamoto S., Ross J. Jr., Bers D.M., Brown J.H.
    Circ. Res. 92:912-919(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CARDIAC HYPERTROPHY.
  6. Cited for: FUNCTION IN PHOSPHORYLATION OF POTASSIUM CHANNEL.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330 AND THR-337, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; THR-336; THR-337 AND SER-494, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen and Testis.
  10. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-318, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  11. Cited for: FUNCTION IN MYOCARDIAL REMODELING.
  12. Cited for: FUNCTION IN PHOSPHORYLATION OF SODIUM CHANNEL.
  13. "Requirement for Ca2+/calmodulin-dependent kinase II in the transition from pressure overload-induced cardiac hypertrophy to heart failure in mice."
    Ling H., Zhang T., Pereira L., Means C.K., Cheng H., Gu Y., Dalton N.D., Peterson K.L., Chen J., Bers D., Heller Brown J.
    J. Clin. Invest. 119:1230-1240(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CARDIAC HYPERTROPHIC CARDIOMYOPATHY.
  14. "The delta isoform of CaM kinase II is required for pathological cardiac hypertrophy and remodeling after pressure overload."
    Backs J., Backs T., Neef S., Kreusser M.M., Lehmann L.H., Patrick D.M., Grueter C.E., Qi X., Richardson J.A., Hill J.A., Katus H.A., Bassel-Duby R., Maier L.S., Olson E.N.
    Proc. Natl. Acad. Sci. U.S.A. 106:2342-2347(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CARDIAC HYPERTROPHY AND REMODELING.
  15. Cited for: FUNCTION IN PHOSPHORYLATION OF L-TYPE CALCIUM CHANNEL, INTERACTION WITH CACNB2.

Entry informationi

Entry nameiKCC2D_MOUSE
AccessioniPrimary (citable) accession number: Q6PHZ2
Secondary accession number(s): Q3UF87
, Q3UQH9, Q5DTK4, Q8CAC5, Q9CZE2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: July 5, 2004
Last modified: July 6, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Mice overexpressing CaMK2D develop a dilated cardiomyopathy, enlarged myocytes with reduced contractility and altered Ca2+ handling, and die prematurely in PubMed:12676814.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.