Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Calcium/calmodulin-dependent protein kinase type II subunit delta

Gene

CAMK2D

Organism
Homo sapiens (Human)
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.2 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.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei43ATPPROSITE-ProRule annotation1
Active sitei136Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi20 – 28ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calmodulin binding Source: BHF-UCL
  • calmodulin-dependent protein kinase activity Source: BHF-UCL
  • ion channel binding Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL
  • protein serine/threonine kinase activity Source: BHF-UCL
  • Ras guanyl-nucleotide exchange factor activity Source: Reactome
  • sodium channel inhibitor activity Source: BHF-UCL
  • titin binding Source: BHF-UCL

GO - Biological processi

  • calcium ion transport Source: Ensembl
  • cardiac muscle cell contraction Source: BHF-UCL
  • cell growth involved in cardiac muscle cell development Source: Ensembl
  • cellular potassium ion homeostasis Source: Ensembl
  • cellular response to calcium ion Source: BHF-UCL
  • endoplasmic reticulum calcium ion homeostasis Source: BHF-UCL
  • G1/S transition of mitotic cell cycle Source: Ensembl
  • interferon-gamma-mediated signaling pathway Source: Reactome
  • MAPK cascade Source: Reactome
  • negative regulation of sodium ion transmembrane transport Source: BHF-UCL
  • negative regulation of sodium ion transmembrane transporter activity Source: BHF-UCL
  • 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: Ensembl
  • positive regulation of Rac protein signal transduction Source: Ensembl
  • positive regulation of smooth muscle cell migration Source: Ensembl
  • positive regulation of smooth muscle cell proliferation Source: Ensembl
  • protein autophosphorylation Source: BHF-UCL
  • protein oligomerization Source: BHF-UCL
  • protein phosphorylation Source: UniProtKB
  • regulation of calcium ion transmembrane transport via high voltage-gated calcium channel Source: BHF-UCL
  • 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: UniProtKB
  • 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 cell growth Source: UniProtKB
  • regulation of cellular localization Source: UniProtKB
  • regulation of cellular response to heat Source: Reactome
  • regulation of G2/M transition of mitotic cell cycle Source: Ensembl
  • regulation of heart contraction Source: UniProtKB
  • regulation of heart rate by cardiac conduction Source: BHF-UCL
  • regulation of histone deacetylase activity Source: BHF-UCL
  • regulation of membrane depolarization Source: BHF-UCL
  • regulation of relaxation of cardiac muscle Source: BHF-UCL
  • regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
  • regulation of ryanodine-sensitive calcium-release channel activity Source: UniProtKB
  • regulation of the force of heart contraction Source: BHF-UCL
  • regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • relaxation of cardiac muscle Source: BHF-UCL
  • response to hypoxia Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS07247-MONOMER.
BRENDAi2.7.11.17. 2681.
ReactomeiR-HSA-3371571. HSF1-dependent transactivation.
R-HSA-399719. Trafficking of AMPA receptors.
R-HSA-438066. Unblocking of NMDA receptor, glutamate binding and activation.
R-HSA-442729. CREB phosphorylation through the activation of CaMKII.
R-HSA-442742. CREB phosphorylation through the activation of Ras.
R-HSA-442982. Ras activation uopn Ca2+ infux through NMDA receptor.
R-HSA-5576892. Phase 0 - rapid depolarisation.
R-HSA-5578775. Ion homeostasis.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-877300. Interferon gamma signaling.
R-HSA-936837. Ion transport by P-type ATPases.
SignaLinkiQ13557.
SIGNORiQ13557.

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:CAMKD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:1462. CAMK2D.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane, Sarcoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

DisGeNETi817.
OpenTargetsiENSG00000145349.
PharmGKBiPA92.

Chemistry databases

ChEMBLiCHEMBL2801.
GuidetoPHARMACOLOGYi1558.

Polymorphism and mutation databases

BioMutaiCAMK2D.
DMDMi116242602.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000860992 – 499Calcium/calmodulin-dependent protein kinase type II subunit deltaAdd BLAST498

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei287Phosphothreonine; by autocatalysis1 Publication1
Modified residuei306Phosphothreonine; by autocatalysisCurated1
Modified residuei307Phosphothreonine; by autocatalysisCurated1
Modified residuei315PhosphoserineCombined sources1
Modified residuei318N6-acetyllysineBy similarity1
Modified residuei319PhosphoserineCombined sources1
Modified residuei330PhosphoserineCombined sources1
Modified residuei331PhosphothreonineCombined sources1
Modified residuei333PhosphoserineBy similarity1
Modified residuei336PhosphothreonineBy similarity1
Modified residuei337PhosphothreonineCombined sources1
Modified residuei404PhosphoserineCombined sources1
Modified residuei490PhosphoserineCombined sources1
Modified residuei494PhosphoserineBy similarity1

Post-translational modificationi

Autophosphorylation of Thr-287 following activation by Ca2+/calmodulin. Phosphorylation of Thr-287 locks the kinase into an activated state.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ13557.
MaxQBiQ13557.
PaxDbiQ13557.
PeptideAtlasiQ13557.
PRIDEiQ13557.

PTM databases

iPTMnetiQ13557.
PhosphoSitePlusiQ13557.
SwissPalmiQ13557.

Expressioni

Tissue specificityi

Expressed in cardiac muscle and skeletal muscle. Isoform Delta 3, isoform Delta 2, isoform Delta 8 and isoform Delta 9 are expressed in cardiac muscle. Isoform Delta 11 is expressed in skeletal muscle.2 Publications

Inductioni

Activity is induced in skeletal muscle during exercise.1 Publication

Gene expression databases

BgeeiENSG00000145349.
CleanExiHS_CAMK2D.
ExpressionAtlasiQ13557. baseline and differential.
GenevisibleiQ13557. HS.

Organism-specific databases

HPAiHPA026281.
HPA051783.
HPA051785.
HPA053973.

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 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
BANPQ8N9N53EBI-351018,EBI-744695
CAMK2GQ13555-54EBI-11534483,EBI-12020154
DNAL4O960153EBI-351018,EBI-742362
EPHA10Q5JZY3-33EBI-351018,EBI-10244652
FKBP1BP681063EBI-351018,EBI-6693977
FNDC3BQ53EP0-33EBI-351018,EBI-10242151
FXR2P511163EBI-351018,EBI-740459
MOAP1Q96BY23EBI-351018,EBI-739825
MRPL11Q9Y3B73EBI-351018,EBI-5453723
SCN5AQ1452416EBI-351018,EBI-726858
TNPO2O147873EBI-351018,EBI-431907
TTC5Q8N0Z63EBI-351018,EBI-9526213

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi107267. 80 interactors.
DIPiDIP-33129N.
IntActiQ13557. 35 interactors.
MINTiMINT-3028061.
STRINGi9606.ENSP00000339740.

Chemistry databases

BindingDBiQ13557.

Structurei

Secondary structure

1499
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi14 – 23Combined sources10
Beta strandi26 – 33Combined sources8
Turni34 – 36Combined sources3
Beta strandi39 – 46Combined sources8
Helixi47 – 49Combined sources3
Helixi52 – 67Combined sources16
Beta strandi76 – 82Combined sources7
Beta strandi85 – 90Combined sources6
Helixi98 – 105Combined sources8
Helixi110 – 129Combined sources20
Helixi139 – 141Combined sources3
Beta strandi142 – 148Combined sources7
Beta strandi153 – 155Combined sources3
Helixi158 – 160Combined sources3
Helixi178 – 180Combined sources3
Helixi183 – 186Combined sources4
Helixi194 – 209Combined sources16
Helixi219 – 228Combined sources10
Turni235 – 240Combined sources6
Helixi243 – 252Combined sources10
Turni257 – 259Combined sources3
Helixi263 – 266Combined sources4
Helixi270 – 273Combined sources4
Helixi275 – 278Combined sources4
Helixi296 – 310Combined sources15
Helixi340 – 363Combined sources24
Helixi366 – 372Combined sources7
Beta strandi373 – 380Combined sources8
Helixi382 – 384Combined sources3
Beta strandi389 – 392Combined sources4
Helixi393 – 401Combined sources9
Beta strandi410 – 421Combined sources12
Beta strandi426 – 438Combined sources13
Beta strandi444 – 458Combined sources15
Beta strandi461 – 470Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VN9X-ray2.30A/B11-309[»]
2W2CX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L/M/N334-475[»]
2WELX-ray1.90A11-335[»]
3GP2X-ray1.46B294-311[»]
ProteinModelPortaliQ13557.
SMRiQ13557.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13557.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 272Protein kinasePROSITE-ProRule annotationAdd BLAST259

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni283 – 292Autoinhibitory domainBy similarity10
Regioni291 – 301Calmodulin-bindingBy similarityAdd BLAST11

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.
InParanoidiQ13557.
KOiK04515.
PhylomeDBiQ13557.
TreeFamiTF315229.

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 (10)i

Sequence statusi: Complete.

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

This entry describes 10 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Delta 2 (identifier: Q13557-1) [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 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:October 17, 2006 - v3
Checksum:i62999FBAB98120CE
GO
Isoform Delta 3 (identifier: Q13557-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     328-328: K → KKRKSSSSVQMM

Show »
Length:510
Mass (Da):57,620
Checksum:i0F312AC0E5938A07
GO
Isoform Delta 4 (identifier: Q13557-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     328-328: K → KINNKANVVTSPKENIPTPAL

Show »
Length:519
Mass (Da):58,472
Checksum:i184D4250A261D923
GO
Isoform Delta 6 (identifier: Q13557-8) [UniParc]FASTAAdd to basket

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

Show »
Length:478
Mass (Da):54,128
Checksum:i571DA27C914E4F7E
GO
Isoform Delta 7 (identifier: Q13557-9) [UniParc]FASTAAdd to basket

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

Show »
Length:489
Mass (Da):55,378
Checksum:iA45841A7EBFBFA5E
GO
Isoform Delta 8 (identifier: Q13557-5) [UniParc]FASTAAdd to basket

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

Show »
Length:498
Mass (Da):56,230
Checksum:i3EE4353E136343BB
GO
Isoform Delta 9 (identifier: Q13557-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     329-329: E → EPQTTVIHNPDGNKE

Show »
Length:513
Mass (Da):57,901
Checksum:i79B81366F7E1C69B
GO
Isoform Delta 10 (identifier: Q13557-10) [UniParc]FASTAAdd to basket

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

Show »
Length:492
Mass (Da):55,660
Checksum:iE78D0E736590F908
GO
Isoform Delta 11 (identifier: Q13557-11) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     328-328: K → KKRKSSSSVQMMEPQTTVIHNPDGNK

Show »
Length:524
Mass (Da):59,152
Checksum:i3BFC4B5CAF9B3B88
GO
Isoform Delta 12 (identifier: Q13557-12) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:478
Mass (Da):54,114
Checksum:i506DA27C914E4F7E
GO

Sequence cautioni

The sequence BAD92525 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti39E → G in AAD20442 (PubMed:10189359).Curated1
Sequence conflicti272I → T in AAX88806 (Ref. 4) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_040602167D → E.1 PublicationCorresponds to variant rs35367671dbSNPEnsembl.1
Natural variantiVAR_028196463Q → E.Corresponds to variant rs1053668dbSNPEnsembl.1
Natural variantiVAR_040603493T → I.1 PublicationCorresponds to variant rs35765784dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_023095328K → KKRKSSSSVQMMEPQTTVIH NPDGNK in isoform Delta 11. Curated1
Alternative sequenceiVSP_023096328K → KKRKSSSSVQMM in isoform Delta 3 and isoform Delta 7. 1 Publication1
Alternative sequenceiVSP_023097328K → KINNKANVVTSPKENIPTPA L in isoform Delta 4 and isoform Delta 8. Curated1
Alternative sequenceiVSP_023098329E → EPQTTVIHNPDGNKE in isoform Delta 9 and isoform Delta 10. 1 Publication1
Alternative sequenceiVSP_041820478K → N in isoform Delta 12. 1 Publication1
Alternative sequenceiVSP_023099479 – 499Missing in isoform Delta 6, isoform Delta 7, isoform Delta 8, isoform Delta 10 and isoform Delta 12. 4 PublicationsAdd BLAST21

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF071569 mRNA. Translation: AAD20442.1.
AK055642 mRNA. Translation: BAG51545.1.
AB209288 mRNA. Translation: BAD92525.1. Different initiation.
AY987011 mRNA. Translation: AAX88806.1.
AC004056 Genomic DNA. No translation available.
AC004168 Genomic DNA. No translation available.
AC093900 Genomic DNA. No translation available.
AC107386 Genomic DNA. No translation available.
BC032784 mRNA. Translation: AAH32784.1.
AJ252239 mRNA. Translation: CAB65123.1.
U50361 mRNA. Translation: AAB16866.1.
CCDSiCCDS3703.1. [Q13557-1]
CCDS3704.1. [Q13557-8]
CCDS43263.1. [Q13557-12]
CCDS47127.1. [Q13557-10]
CCDS54797.1. [Q13557-9]
RefSeqiNP_001212.2. NM_001221.3. [Q13557-1]
NP_001308495.1. NM_001321566.1. [Q13557-6]
NP_001308502.1. NM_001321573.1. [Q13557-11]
NP_001308509.1. NM_001321580.1. [Q13557-4]
NP_001308518.1. NM_001321589.1. [Q13557-10]
NP_742112.1. NM_172114.1. [Q13557-10]
NP_742113.1. NM_172115.2. [Q13557-8]
NP_742125.1. NM_172127.2. [Q13557-8]
NP_742126.1. NM_172128.2. [Q13557-12]
NP_742127.1. NM_172129.1. [Q13557-9]
XP_011530591.1. XM_011532289.1. [Q13557-3]
XP_011530593.1. XM_011532291.1. [Q13557-9]
UniGeneiHs.144114.

Genome annotation databases

EnsembliENST00000296402; ENSP00000296402; ENSG00000145349. [Q13557-8]
ENST00000342666; ENSP00000339740; ENSG00000145349. [Q13557-1]
ENST00000379773; ENSP00000369098; ENSG00000145349. [Q13557-8]
ENST00000394522; ENSP00000378030; ENSG00000145349. [Q13557-10]
ENST00000394524; ENSP00000378032; ENSG00000145349. [Q13557-12]
ENST00000508738; ENSP00000422566; ENSG00000145349. [Q13557-9]
ENST00000515496; ENSP00000423482; ENSG00000145349. [Q13557-3]
GeneIDi817.
KEGGihsa:817.
UCSCiuc003ibi.4. human. [Q13557-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF071569 mRNA. Translation: AAD20442.1.
AK055642 mRNA. Translation: BAG51545.1.
AB209288 mRNA. Translation: BAD92525.1. Different initiation.
AY987011 mRNA. Translation: AAX88806.1.
AC004056 Genomic DNA. No translation available.
AC004168 Genomic DNA. No translation available.
AC093900 Genomic DNA. No translation available.
AC107386 Genomic DNA. No translation available.
BC032784 mRNA. Translation: AAH32784.1.
AJ252239 mRNA. Translation: CAB65123.1.
U50361 mRNA. Translation: AAB16866.1.
CCDSiCCDS3703.1. [Q13557-1]
CCDS3704.1. [Q13557-8]
CCDS43263.1. [Q13557-12]
CCDS47127.1. [Q13557-10]
CCDS54797.1. [Q13557-9]
RefSeqiNP_001212.2. NM_001221.3. [Q13557-1]
NP_001308495.1. NM_001321566.1. [Q13557-6]
NP_001308502.1. NM_001321573.1. [Q13557-11]
NP_001308509.1. NM_001321580.1. [Q13557-4]
NP_001308518.1. NM_001321589.1. [Q13557-10]
NP_742112.1. NM_172114.1. [Q13557-10]
NP_742113.1. NM_172115.2. [Q13557-8]
NP_742125.1. NM_172127.2. [Q13557-8]
NP_742126.1. NM_172128.2. [Q13557-12]
NP_742127.1. NM_172129.1. [Q13557-9]
XP_011530591.1. XM_011532289.1. [Q13557-3]
XP_011530593.1. XM_011532291.1. [Q13557-9]
UniGeneiHs.144114.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VN9X-ray2.30A/B11-309[»]
2W2CX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L/M/N334-475[»]
2WELX-ray1.90A11-335[»]
3GP2X-ray1.46B294-311[»]
ProteinModelPortaliQ13557.
SMRiQ13557.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107267. 80 interactors.
DIPiDIP-33129N.
IntActiQ13557. 35 interactors.
MINTiMINT-3028061.
STRINGi9606.ENSP00000339740.

Chemistry databases

BindingDBiQ13557.
ChEMBLiCHEMBL2801.
GuidetoPHARMACOLOGYi1558.

PTM databases

iPTMnetiQ13557.
PhosphoSitePlusiQ13557.
SwissPalmiQ13557.

Polymorphism and mutation databases

BioMutaiCAMK2D.
DMDMi116242602.

Proteomic databases

EPDiQ13557.
MaxQBiQ13557.
PaxDbiQ13557.
PeptideAtlasiQ13557.
PRIDEiQ13557.

Protocols and materials databases

DNASUi817.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296402; ENSP00000296402; ENSG00000145349. [Q13557-8]
ENST00000342666; ENSP00000339740; ENSG00000145349. [Q13557-1]
ENST00000379773; ENSP00000369098; ENSG00000145349. [Q13557-8]
ENST00000394522; ENSP00000378030; ENSG00000145349. [Q13557-10]
ENST00000394524; ENSP00000378032; ENSG00000145349. [Q13557-12]
ENST00000508738; ENSP00000422566; ENSG00000145349. [Q13557-9]
ENST00000515496; ENSP00000423482; ENSG00000145349. [Q13557-3]
GeneIDi817.
KEGGihsa:817.
UCSCiuc003ibi.4. human. [Q13557-1]

Organism-specific databases

CTDi817.
DisGeNETi817.
GeneCardsiCAMK2D.
HGNCiHGNC:1462. CAMK2D.
HPAiHPA026281.
HPA051783.
HPA051785.
HPA053973.
MIMi607708. gene.
neXtProtiNX_Q13557.
OpenTargetsiENSG00000145349.
PharmGKBiPA92.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0033. Eukaryota.
ENOG410XNRX. LUCA.
GeneTreeiENSGT00760000118944.
HOVERGENiHBG108055.
InParanoidiQ13557.
KOiK04515.
PhylomeDBiQ13557.
TreeFamiTF315229.

Enzyme and pathway databases

BioCyciZFISH:HS07247-MONOMER.
BRENDAi2.7.11.17. 2681.
ReactomeiR-HSA-3371571. HSF1-dependent transactivation.
R-HSA-399719. Trafficking of AMPA receptors.
R-HSA-438066. Unblocking of NMDA receptor, glutamate binding and activation.
R-HSA-442729. CREB phosphorylation through the activation of CaMKII.
R-HSA-442742. CREB phosphorylation through the activation of Ras.
R-HSA-442982. Ras activation uopn Ca2+ infux through NMDA receptor.
R-HSA-5576892. Phase 0 - rapid depolarisation.
R-HSA-5578775. Ion homeostasis.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-877300. Interferon gamma signaling.
R-HSA-936837. Ion transport by P-type ATPases.
SignaLinkiQ13557.
SIGNORiQ13557.

Miscellaneous databases

ChiTaRSiCAMK2D. human.
EvolutionaryTraceiQ13557.
GeneWikiiCAMK2D.
GenomeRNAii817.
PROiQ13557.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000145349.
CleanExiHS_CAMK2D.
ExpressionAtlasiQ13557. baseline and differential.
GenevisibleiQ13557. HS.

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...

Entry informationi

Entry nameiKCC2D_HUMAN
AccessioniPrimary (citable) accession number: Q13557
Secondary accession number(s): A8MVS8
, Q52PK4, Q59G21, Q8N553, Q9UGH6, Q9UQE9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 17, 2006
Last modified: November 30, 2016
This is version 181 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Expression of CAMK2D is significantly increased in patients suffering from dilated cardiomyopathy in PubMed:10189359.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. 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.