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Protein

Calcium/calmodulin-dependent protein kinase type II subunit delta

Gene

Camk2d

Organism
Rattus norvegicus (Rat)
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 (By similarity).By similarity2 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-dependent protein kinase activity Source: BHF-UCL
  • ion channel binding Source: BHF-UCL
  • nitric-oxide synthase binding Source: RGD
  • protein kinase activity Source: CACAO
  • sodium channel inhibitor activity Source: Ensembl

GO - Biological processi

  • calcium ion transport Source: Ensembl
  • cardiac muscle cell contraction Source: BHF-UCL
  • cell growth involved in cardiac muscle cell development Source: RGD
  • cellular potassium ion homeostasis Source: RGD
  • endoplasmic reticulum calcium ion homeostasis Source: BHF-UCL
  • G1/S transition of mitotic cell cycle Source: Ensembl
  • negative regulation of sodium ion transmembrane transporter activity Source: Ensembl
  • peptidyl-serine phosphorylation Source: BHF-UCL
  • peptidyl-threonine phosphorylation Source: BHF-UCL
  • positive regulation of cardiac muscle cell apoptotic process Source: BHF-UCL
  • positive regulation of cardiac muscle hypertrophy Source: UniProtKB
  • positive regulation of ERK1 and ERK2 cascade Source: RGD
  • positive regulation of Rac protein signal transduction Source: RGD
  • positive regulation of smooth muscle cell migration Source: RGD
  • positive regulation of smooth muscle cell proliferation Source: RGD
  • protein autophosphorylation Source: RGD
  • protein oligomerization Source: Ensembl
  • protein phosphorylation Source: UniProtKB
  • regulation of cardiac muscle cell action potential Source: BHF-UCL
  • regulation of cardiac muscle cell action potential involved in regulation of contraction Source: BHF-UCL
  • regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: BHF-UCL
  • regulation of cell communication by electrical coupling Source: BHF-UCL
  • regulation of cell communication by electrical coupling involved in cardiac conduction Source: BHF-UCL
  • regulation of cellular localization Source: UniProtKB
  • regulation of G2/M transition of mitotic cell cycle Source: RGD
  • regulation of generation of L-type calcium current Source: BHF-UCL
  • regulation of membrane depolarization Source: Ensembl
  • regulation of relaxation of cardiac muscle Source: BHF-UCL
  • regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
  • relaxation of cardiac muscle Source: BHF-UCL
  • response to hypoxia Source: RGD
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. 5301.
ReactomeiR-RNO-3371571. HSF1-dependent transactivation.
R-RNO-399719. Trafficking of AMPA receptors.
R-RNO-438066. Unblocking of NMDA receptor, glutamate binding and activation.
R-RNO-442729. CREB phosphorylation through the activation of CaMKII.
R-RNO-442742. CREB phosphorylation through the activation of Ras.
R-RNO-442982. Ras activation uopn Ca2+ infux through NMDA receptor.
R-RNO-5576892. Phase 0 - rapid depolarisation.
R-RNO-5578775. Ion homeostasis.
R-RNO-5673001. RAF/MAP kinase cascade.
R-RNO-877300. Interferon gamma signaling.
R-RNO-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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi2263. Camk2d.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane, Nucleus, Sarcoplasmic reticulum

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2111382.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 533532Calcium/calmodulin-dependent protein kinase type II subunit deltaPRO_0000086100Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei287 – 2871Phosphothreonine; by autocatalysisBy similarity
Modified residuei306 – 3061Phosphothreonine; by autocatalysisBy similarity
Modified residuei307 – 3071Phosphothreonine; by autocatalysisBy similarity
Modified residuei315 – 3151PhosphoserineBy similarity
Modified residuei318 – 3181N6-acetyllysineBy similarity
Modified residuei319 – 3191PhosphoserineBy similarity
Modified residuei364 – 3641PhosphoserineBy similarity
Modified residuei365 – 3651PhosphothreonineBy similarity
Modified residuei367 – 3671PhosphoserineCombined sources
Modified residuei370 – 3701PhosphothreonineBy similarity
Modified residuei371 – 3711PhosphothreonineCombined sources
Modified residuei524 – 5241PhosphoserineBy similarity
Modified residuei528 – 5281PhosphoserineBy similarity

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

PaxDbiP15791.
PRIDEiP15791.

PTM databases

iPTMnetiP15791.
PhosphoSiteiP15791.

Expressioni

Tissue specificityi

Isoform Delta 1 is the predominant form in the brain, isoform Delta 2 and isoform Delta 3 predominate in the aorta and isoform Delta 4 in skeletal muscle.

Inductioni

By cocaine in cardiomyocytes.1 Publication

Gene expression databases

GenevisibleiP15791. RN.

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 and CACNB2.1 Publication

GO - Molecular functioni

  • ion channel binding Source: BHF-UCL
  • nitric-oxide synthase binding Source: RGD

Protein-protein interaction databases

BioGridi246431. 5 interactions.
IntActiP15791. 4 interactions.
MINTiMINT-1892750.
STRINGi10116.ENSRNOP00000016026.

Structurei

3D structure databases

ProteinModelPortaliP15791.
SMRiP15791. Positions 11-309, 370-508.
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

eggNOGiKOG0033. Eukaryota.
ENOG410XNRX. LUCA.
GeneTreeiENSGT00760000118944.
HOVERGENiHBG108055.
InParanoidiP15791.
KOiK04515.
OMAiHNPTDGN.
OrthoDBiEOG7ZD1VM.
PhylomeDBiP15791.

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. 2 hits.
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 (7)i

Sequence statusi: Complete.

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

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Delta 1 (identifier: P15791-1) [UniParc]FASTAAdd to basket

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 LKKPDGVKIN NKANVVTSPK ENIPTPALEP
360 370 380 390 400
QTTVIHNPDG NKESTESSNT TIEDEDVKAR KQEIIKVTEQ LIEAINNGDF
410 420 430 440 450
EAYTKICDPG LTAFEPEALG NLVEGMDFHR FYFENALPKI NKPIHTIILN
460 470 480 490 500
PHVHLVGDDA ACIAYIRLTQ YMDGNGMPKT MQSEETRVWH RRDGKWQNIH
510 520 530
FHRSGSPTVP IKPPCIPNGK ENFSGGTSLW QNI
Length:533
Mass (Da):60,081
Last modified:April 1, 1990 - v1
Checksum:iE41BCB2B5A00E7CA
GO
Isoform Delta 2 (identifier: P15791-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     329-362: Missing.

Show »
Length:499
Mass (Da):56,447
Checksum:iA200989BB0E857D6
GO
Isoform Delta 3 (identifier: P15791-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     329-335: INNKANV → KRKSSSV
     337-359: Missing.
     360-362: GNK → QMM

Show »
Length:510
Mass (Da):57,709
Checksum:iD21D28E2314C20AB
GO
Isoform Delta 4 (identifier: P15791-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     349-362: Missing.

Show »
Length:519
Mass (Da):58,549
Checksum:iD8D44571AB08AE3B
GO
Isoform Delta 5 (identifier: P15791-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     329-362: Missing.
     512-533: KPPCIPNGKENFSGGTSLWQNI → N

Show »
Length:478
Mass (Da):54,191
Checksum:iD58353ACB0B7CEBF
GO
Isoform Delta 6 (identifier: P15791-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     512-533: KPPCIPNGKENFSGGTSLWQNI → N

Show »
Length:512
Mass (Da):57,825
Checksum:iF84B958F92A2BF6C
GO
Isoform Delta 7 (identifier: P15791-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     349-362: Missing.
     512-533: KPPCIPNGKENFSGGTSLWQNI → N

Show »
Length:498
Mass (Da):56,293
Checksum:iBC7AC4EE329AC27A
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei329 – 36234Missing in isoform Delta 2 and isoform Delta 5. 2 PublicationsVSP_004784Add
BLAST
Alternative sequencei329 – 3357INNKANV → KRKSSSV in isoform Delta 3. 1 PublicationVSP_004785
Alternative sequencei337 – 35923Missing in isoform Delta 3. 1 PublicationVSP_004786Add
BLAST
Alternative sequencei349 – 36214Missing in isoform Delta 4 and isoform Delta 7. 1 PublicationVSP_004788Add
BLAST
Alternative sequencei360 – 3623GNK → QMM in isoform Delta 3. 1 PublicationVSP_004787
Alternative sequencei512 – 53322KPPCI…LWQNI → N in isoform Delta 5, isoform Delta 6 and isoform Delta 7. CuratedVSP_012043Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05072 mRNA. Translation: AAA40866.1.
BC107562 mRNA. Translation: AAI07563.1.
L13406 mRNA. Translation: AAA41479.1.
L13407 mRNA. Translation: AAA41480.1.
L13408 mRNA. Translation: AAA41481.1.
X77192 Genomic DNA. Translation: CAA54412.1.
X77193 Genomic DNA. Translation: CAA54413.1.
X77194 Genomic DNA. Translation: CAA54414.1.
X77195 Genomic DNA. Translation: CAA54415.1.
X75774 Genomic DNA. Translation: CAA53395.1.
PIRiA34366.
RefSeqiNP_036651.1. NM_012519.2. [P15791-1]
UniGeneiRn.87208.

Genome annotation databases

EnsembliENSRNOT00000015564; ENSRNOP00000015559; ENSRNOG00000011589. [P15791-2]
ENSRNOT00000016026; ENSRNOP00000016026; ENSRNOG00000011589. [P15791-1]
ENSRNOT00000068198; ENSRNOP00000062625; ENSRNOG00000011589. [P15791-1]
GeneIDi24246.
KEGGirno:24246.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05072 mRNA. Translation: AAA40866.1.
BC107562 mRNA. Translation: AAI07563.1.
L13406 mRNA. Translation: AAA41479.1.
L13407 mRNA. Translation: AAA41480.1.
L13408 mRNA. Translation: AAA41481.1.
X77192 Genomic DNA. Translation: CAA54412.1.
X77193 Genomic DNA. Translation: CAA54413.1.
X77194 Genomic DNA. Translation: CAA54414.1.
X77195 Genomic DNA. Translation: CAA54415.1.
X75774 Genomic DNA. Translation: CAA53395.1.
PIRiA34366.
RefSeqiNP_036651.1. NM_012519.2. [P15791-1]
UniGeneiRn.87208.

3D structure databases

ProteinModelPortaliP15791.
SMRiP15791. Positions 11-309, 370-508.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246431. 5 interactions.
IntActiP15791. 4 interactions.
MINTiMINT-1892750.
STRINGi10116.ENSRNOP00000016026.

Chemistry

ChEMBLiCHEMBL2111382.

PTM databases

iPTMnetiP15791.
PhosphoSiteiP15791.

Proteomic databases

PaxDbiP15791.
PRIDEiP15791.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000015564; ENSRNOP00000015559; ENSRNOG00000011589. [P15791-2]
ENSRNOT00000016026; ENSRNOP00000016026; ENSRNOG00000011589. [P15791-1]
ENSRNOT00000068198; ENSRNOP00000062625; ENSRNOG00000011589. [P15791-1]
GeneIDi24246.
KEGGirno:24246.

Organism-specific databases

CTDi817.
RGDi2263. Camk2d.

Phylogenomic databases

eggNOGiKOG0033. Eukaryota.
ENOG410XNRX. LUCA.
GeneTreeiENSGT00760000118944.
HOVERGENiHBG108055.
InParanoidiP15791.
KOiK04515.
OMAiHNPTDGN.
OrthoDBiEOG7ZD1VM.
PhylomeDBiP15791.

Enzyme and pathway databases

BRENDAi2.7.11.17. 5301.
ReactomeiR-RNO-3371571. HSF1-dependent transactivation.
R-RNO-399719. Trafficking of AMPA receptors.
R-RNO-438066. Unblocking of NMDA receptor, glutamate binding and activation.
R-RNO-442729. CREB phosphorylation through the activation of CaMKII.
R-RNO-442742. CREB phosphorylation through the activation of Ras.
R-RNO-442982. Ras activation uopn Ca2+ infux through NMDA receptor.
R-RNO-5576892. Phase 0 - rapid depolarisation.
R-RNO-5578775. Ion homeostasis.
R-RNO-5673001. RAF/MAP kinase cascade.
R-RNO-877300. Interferon gamma signaling.
R-RNO-936837. Ion transport by P-type ATPases.

Miscellaneous databases

NextBioi602745.
PROiP15791.

Gene expression databases

GenevisibleiP15791. RN.

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. 2 hits.
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. "Tissue-specific expression of four types of rat calmodulin-dependent protein kinase II mRNAs."
    Tobimatsu T., Fujisawa H.
    J. Biol. Chem. 264:17907-17912(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA 1).
  2. "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 DELTA 2).
    Tissue: Prostate.
  3. "Identification of novel isoforms of the delta subunit of Ca2+/calmodulin-dependent protein kinase II. Differential expression in rat brain and aorta."
    Schworer C.M., Rothblum L.I., Thekkumkara T.J., Singer H.A.
    J. Biol. Chem. 268:14443-14449(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 314-533 (ISOFORMS DELTA 2; DELTA 3 AND DELTA 4).
    Strain: Sprague-Dawley.
    Tissue: Aorta and Skeletal muscle.
  4. "New isoforms of multifunctional calcium/calmodulin-dependent protein kinase II."
    Mayer P., Moehlig M., Schatz H., Pfeiffer A.
    FEBS Lett. 333:315-318(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 307-533 (ISOFORMS DELTA 1; DELTA 2; DELTA 4; DELTA 5; DELTA 6 AND DELTA 7).
  5. "Frequency-encoding Thr17 phospholamban phosphorylation is independent of Ser16 phosphorylation in cardiac myocytes."
    Hagemann D., Kuschel M., Kuramochi T., Zhu W., Cheng H., Xiao R.P.
    J. Biol. Chem. 275:22532-22536(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF PLN/PLB.
  6. "Cocaine activates calcium/calmodulin kinase II and causes cardiomyocyte hypertrophy."
    Henning R.J., Cuevas J.
    J. Cardiovasc. Pharmacol. 48:802-813(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY COCAINE.
  7. Cited for: INTERACTION WITH RRAD.
  8. "CaMKIIdelta isoforms differentially affect calcium handling but similarly regulate HDAC/MEF2 transcriptional responses."
    Zhang T., Kohlhaas M., Backs J., Mishra S., Phillips W., Dybkova N., Chang S., Ling H., Bers D.M., Maier L.S., Olson E.N., Brown J.H.
    J. Biol. Chem. 282:35078-35087(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF HDAC4 AND RYR2.
  9. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367 AND THR-371, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKCC2D_RAT
AccessioniPrimary (citable) accession number: P15791
Secondary accession number(s): P97915
, P97916, Q3B7L0, Q63904, Q63905, Q63906, Q63907, Q63908
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: May 11, 2016
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.