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Q13557

- KCC2D_HUMAN

UniProt

Q13557 - KCC2D_HUMAN

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Protein
Calcium/calmodulin-dependent protein kinase type II subunit delta
Gene
CAMK2D, CAMKD
Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei43 – 431ATP By similarity
Active sitei136 – 1361Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi20 – 289ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calmodulin-dependent protein kinase activity Source: BHF-UCL
  3. ion channel binding Source: BHF-UCL
  4. titin binding Source: BHF-UCL

GO - Biological processi

  1. G1/S transition of mitotic cell cycle Source: Ensembl
  2. calcium ion transport Source: Ensembl
  3. cardiac muscle cell contraction Source: BHF-UCL
  4. cellular response to calcium ion Source: BHF-UCL
  5. cytokine-mediated signaling pathway Source: Reactome
  6. interferon-gamma-mediated signaling pathway Source: Reactome
  7. peptidyl-serine phosphorylation Source: BHF-UCL
  8. peptidyl-threonine phosphorylation Source: BHF-UCL
  9. positive regulation of cardiac muscle hypertrophy Source: UniProtKB
  10. protein autophosphorylation Source: Ensembl
  11. protein phosphorylation Source: UniProtKB
  12. regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: UniProtKB
  13. regulation of cell growth Source: UniProtKB
  14. regulation of cellular localization Source: UniProtKB
  15. regulation of heart contraction Source: UniProtKB
  16. regulation of histone deacetylase activity Source: BHF-UCL
  17. regulation of relaxation of cardiac muscle Source: BHF-UCL
  18. regulation of ryanodine-sensitive calcium-release channel activity Source: UniProtKB
  19. regulation of sodium ion transport Source: Ensembl
  20. regulation of the force of heart contraction Source: BHF-UCL
  21. regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  22. relaxation of cardiac muscle Source: BHF-UCL
  23. synaptic transmission Source: Reactome
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. 2681.
ReactomeiREACT_18307. Trafficking of AMPA receptors.
REACT_200775. HSF1-dependent transactivation.
REACT_20546. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_20568. CREB phosphorylation through the activation of Ras.
REACT_20594. Unblocking of NMDA receptor, glutamate binding and activation.
REACT_20642. CREB phosphorylation through the activation of CaMKII.
REACT_25078. Interferon gamma signaling.
SignaLinkiQ13557.

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
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:1462. CAMK2D.

Subcellular locationi

GO - Cellular componenti

  1. T-tubule Source: Ensembl
  2. axon initial segment Source: Ensembl
  3. calcium channel complex Source: Ensembl
  4. calcium- and calmodulin-dependent protein kinase complex Source: UniProtKB
  5. cytoplasm Source: BHF-UCL
  6. cytosol Source: Reactome
  7. endocytic vesicle membrane Source: Reactome
  8. intercalated disc Source: Ensembl
  9. neuromuscular junction Source: Ensembl
  10. neuronal cell body Source: Ensembl
  11. nucleoplasm Source: Reactome
  12. nucleus Source: BHF-UCL
  13. plasma membrane Source: Reactome
  14. sarcoplasmic reticulum membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Sarcoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA92.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 499498Calcium/calmodulin-dependent protein kinase type II subunit delta
PRO_0000086099Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei287 – 2871Phosphothreonine; by autocatalysis1 Publication
Modified residuei306 – 3061Phosphothreonine; by autocatalysis Inferred
Modified residuei307 – 3071Phosphothreonine; by autocatalysis Inferred
Modified residuei318 – 3181N6-acetyllysine By similarity
Modified residuei319 – 3191Phosphoserine1 Publication
Modified residuei330 – 3301Phosphoserine By similarity
Modified residuei337 – 3371Phosphothreonine By similarity
Modified residuei404 – 4041Phosphoserine1 Publication
Modified residuei490 – 4901Phosphoserine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ13557.
PaxDbiQ13557.
PRIDEiQ13557.

PTM databases

PhosphoSiteiQ13557.

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.2 Publications

Gene expression databases

ArrayExpressiQ13557.
BgeeiQ13557.
CleanExiHS_CAMK2D.
GenevestigatoriQ13557.

Organism-specific databases

HPAiHPA026281.

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.1 Publication

Protein-protein interaction databases

BioGridi107267. 19 interactions.
DIPiDIP-33129N.
IntActiQ13557. 15 interactions.
MINTiMINT-3028061.
STRINGi9606.ENSP00000339740.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 2310
Beta strandi26 – 338
Turni34 – 363
Beta strandi39 – 468
Helixi47 – 493
Helixi52 – 6716
Beta strandi76 – 827
Beta strandi85 – 906
Helixi98 – 1058
Helixi110 – 12920
Helixi139 – 1413
Beta strandi142 – 1487
Beta strandi153 – 1553
Helixi158 – 1603
Helixi178 – 1803
Helixi183 – 1864
Helixi194 – 20916
Helixi219 – 22810
Turni235 – 2406
Helixi243 – 25210
Turni257 – 2593
Helixi263 – 2664
Helixi270 – 2734
Helixi275 – 2784
Helixi296 – 31015
Helixi340 – 36324
Helixi366 – 3727
Beta strandi373 – 3808
Helixi382 – 3843
Beta strandi389 – 3924
Helixi393 – 4019
Beta strandi410 – 42112
Beta strandi426 – 43813
Beta strandi444 – 45815
Beta strandi461 – 47010

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 8-474.

Miscellaneous databases

EvolutionaryTraceiQ13557.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 272259Protein kinase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni283 – 29210Autoinhibitory domain By similarity
Regioni291 – 30111Calmodulin-binding By similarity
Add
BLAST

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
HOVERGENiHBG108055.
InParanoidiQ13557.
KOiK04515.
OrthoDBiEOG7ZD1VM.
PhylomeDBiQ13557.
TreeFamiTF315229.

Family and domain databases

InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR013543. Ca/CaM-dep_prot_kinase-assoc.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
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]
SUPFAMiSSF56112. 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. Align

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

MASTTTCTRF TDEYQLFEEL GKGAFSVVRR CMKIPTGQEY AAKIINTKKL    50
SARDHQKLER EARICRLLKH PNIVRLHDSI SEEGFHYLVF DLVTGGELFE 100
DIVAREYYSE ADASHCIQQI LESVNHCHLN GIVHRDLKPE NLLLASKSKG 150
AAVKLADFGL AIEVQGDQQA WFGFAGTPGY LSPEVLRKDP YGKPVDMWAC 200
GVILYILLVG YPPFWDEDQH RLYQQIKAGA YDFPSPEWDT VTPEAKDLIN 250
KMLTINPAKR ITASEALKHP WICQRSTVAS MMHRQETVDC LKKFNARRKL 300
KGAILTTMLA TRNFSAAKSL LKKPDGVKES TESSNTTIED EDVKARKQEI 350
IKVTEQLIEA INNGDFEAYT KICDPGLTAF EPEALGNLVE GMDFHRFYFE 400
NALSKSNKPI HTIILNPHVH LVGDDAACIA YIRLTQYMDG SGMPKTMQSE 450
ETRVWHRRDG KWQNVHFHRS GSPTVPIKPP CIPNGKENFS GGTSLWQNI 499
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 BAD92525.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti167 – 1671D → E.1 Publication
Corresponds to variant rs35367671 [ dbSNP | Ensembl ].
VAR_040602
Natural varianti463 – 4631Q → E.
Corresponds to variant rs1053668 [ dbSNP | Ensembl ].
VAR_028196
Natural varianti493 – 4931T → I.1 Publication
Corresponds to variant rs35765784 [ dbSNP | Ensembl ].
VAR_040603

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei328 – 3281K → KKRKSSSSVQMMEPQTTVIH NPDGNK in isoform Delta 11.
VSP_023095
Alternative sequencei328 – 3281K → KKRKSSSSVQMM in isoform Delta 3 and isoform Delta 7.
VSP_023096
Alternative sequencei328 – 3281K → KINNKANVVTSPKENIPTPA L in isoform Delta 4 and isoform Delta 8.
VSP_023097
Alternative sequencei329 – 3291E → EPQTTVIHNPDGNKE in isoform Delta 9 and isoform Delta 10.
VSP_023098
Alternative sequencei478 – 4781K → N in isoform Delta 12.
VSP_041820
Alternative sequencei479 – 49921Missing in isoform Delta 6, isoform Delta 7, isoform Delta 8, isoform Delta 10 and isoform Delta 12.
VSP_023099Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti39 – 391E → G in AAD20442. 1 Publication
Sequence conflicti272 – 2721I → T in AAX88806. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_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_005263312.1. XM_005263255.2. [Q13557-6]
XP_006714392.1. XM_006714329.1. [Q13557-10]
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]
ENST00000394526; ENSP00000378034; ENSG00000145349. [Q13557-3]
ENST00000418639; ENSP00000406131; ENSG00000145349. [Q13557-6]
ENST00000429180; ENSP00000415707; ENSG00000145349. [Q13557-4]
ENST00000454265; ENSP00000415248; ENSG00000145349. [Q13557-11]
ENST00000508738; ENSP00000422566; ENSG00000145349. [Q13557-9]
ENST00000515496; ENSP00000423482; ENSG00000145349. [Q13557-3]
GeneIDi817.
KEGGihsa:817.
UCSCiuc003ibi.3. human. [Q13557-1]
uc003ibj.3. human. [Q13557-12]
uc003ibm.2. human. [Q13557-10]
uc003ibn.2. human. [Q13557-9]

Polymorphism databases

DMDMi116242602.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS3703.1. [Q13557-1 ]
CCDS3704.1. [Q13557-8 ]
CCDS43263.1. [Q13557-12 ]
CCDS47127.1. [Q13557-10 ]
CCDS54797.1. [Q13557-9 ]
RefSeqi NP_001212.2. NM_001221.3. [Q13557-1 ]
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_005263312.1. XM_005263255.2. [Q13557-6 ]
XP_006714392.1. XM_006714329.1. [Q13557-10 ]
UniGenei Hs.144114.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2VN9 X-ray 2.30 A/B 11-309 [» ]
2W2C X-ray 2.70 A/B/C/D/E/F/G/H/I/J/K/L/M/N 334-475 [» ]
2WEL X-ray 1.90 A 11-335 [» ]
3GP2 X-ray 1.46 B 294-311 [» ]
ProteinModelPortali Q13557.
SMRi Q13557. Positions 8-474.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107267. 19 interactions.
DIPi DIP-33129N.
IntActi Q13557. 15 interactions.
MINTi MINT-3028061.
STRINGi 9606.ENSP00000339740.

Chemistry

BindingDBi Q13557.
ChEMBLi CHEMBL2801.
GuidetoPHARMACOLOGYi 1558.

PTM databases

PhosphoSitei Q13557.

Polymorphism databases

DMDMi 116242602.

Proteomic databases

MaxQBi Q13557.
PaxDbi Q13557.
PRIDEi Q13557.

Protocols and materials databases

DNASUi 817.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000296402 ; ENSP00000296402 ; ENSG00000145349 . [Q13557-8 ]
ENST00000342666 ; ENSP00000339740 ; ENSG00000145349 . [Q13557-1 ]
ENST00000379773 ; ENSP00000369098 ; ENSG00000145349 . [Q13557-8 ]
ENST00000394522 ; ENSP00000378030 ; ENSG00000145349 . [Q13557-10 ]
ENST00000394524 ; ENSP00000378032 ; ENSG00000145349 . [Q13557-12 ]
ENST00000394526 ; ENSP00000378034 ; ENSG00000145349 . [Q13557-3 ]
ENST00000418639 ; ENSP00000406131 ; ENSG00000145349 . [Q13557-6 ]
ENST00000429180 ; ENSP00000415707 ; ENSG00000145349 . [Q13557-4 ]
ENST00000454265 ; ENSP00000415248 ; ENSG00000145349 . [Q13557-11 ]
ENST00000508738 ; ENSP00000422566 ; ENSG00000145349 . [Q13557-9 ]
ENST00000515496 ; ENSP00000423482 ; ENSG00000145349 . [Q13557-3 ]
GeneIDi 817.
KEGGi hsa:817.
UCSCi uc003ibi.3. human. [Q13557-1 ]
uc003ibj.3. human. [Q13557-12 ]
uc003ibm.2. human. [Q13557-10 ]
uc003ibn.2. human. [Q13557-9 ]

Organism-specific databases

CTDi 817.
GeneCardsi GC04M114372.
HGNCi HGNC:1462. CAMK2D.
HPAi HPA026281.
MIMi 607708. gene.
neXtProti NX_Q13557.
PharmGKBi PA92.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOVERGENi HBG108055.
InParanoidi Q13557.
KOi K04515.
OrthoDBi EOG7ZD1VM.
PhylomeDBi Q13557.
TreeFami TF315229.

Enzyme and pathway databases

BRENDAi 2.7.11.17. 2681.
Reactomei REACT_18307. Trafficking of AMPA receptors.
REACT_200775. HSF1-dependent transactivation.
REACT_20546. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_20568. CREB phosphorylation through the activation of Ras.
REACT_20594. Unblocking of NMDA receptor, glutamate binding and activation.
REACT_20642. CREB phosphorylation through the activation of CaMKII.
REACT_25078. Interferon gamma signaling.
SignaLinki Q13557.

Miscellaneous databases

ChiTaRSi CAMK2D. human.
EvolutionaryTracei Q13557.
GeneWikii CAMK2D.
GenomeRNAii 817.
NextBioi 3330.
PROi Q13557.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13557.
Bgeei Q13557.
CleanExi HS_CAMK2D.
Genevestigatori Q13557.

Family and domain databases

InterProi IPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR013543. Ca/CaM-dep_prot_kinase-assoc.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
PANTHERi PTHR24347. PTHR24347. 1 hit.
Pfami PF08332. CaMKII_AD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and expression of delta-isoforms of the multifunctional Ca2+/calmodulin-dependent protein kinase in failing and nonfailing human myocardium."
    Hoch B., Meyer R., Hetzer R., Krause E.-G., Karczewski P.
    Circ. Res. 84:713-721(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA 2), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
    Tissue: Myocardium.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DELTA 12).
  3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DELTA 10).
    Tissue: Brain.
  4. Zhou G., Nong W., Li H., Ke R., Li M., Zheng Z., Zhong G., Shen C., Liang M., Lin L., Yang S.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DELTA 7).
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 6).
  7. "Cloning and quantitative determination of the human Ca2+/calmodulin-dependent protein kinase II (CaMK II) isoforms in human beta cells."
    Rochlitz H., Voigt A., Lankat-Buttgereit B., Goeke B., Heimberg H., Nauck M.A., Schiemann U., Schatz H., Pfeiffer A.F.
    Diabetologia 43:465-473(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-243, ALTERNATIVE SPLICING.
    Tissue: Insulinoma.
  8. "Identification of novel human tumor cell-specific CaMK-II variants."
    Tombes R.M., Krystal G.W.
    Biochim. Biophys. Acta 1355:281-292(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 302-417, ALTERNATIVE SPLICING.
  9. "Comparative analyses of the three-dimensional structures and enzymatic properties of alpha, beta, gamma and delta isoforms of Ca2+-calmodulin-dependent protein kinase II."
    Gaertner T.R., Kolodziej S.J., Wang D., Kobayashi R., Koomen J.M., Stoops J.K., Waxham M.N.
    J. Biol. Chem. 279:12484-12494(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, SUBUNIT, AUTOPHOSPHORYLATION.
  10. "Ca2+-calmodulin-dependent protein kinase expression and signalling in skeletal muscle during exercise."
    Rose A.J., Kiens B., Richter E.A.
    J. Physiol. (Lond.) 574:889-903(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SKELETAL MUSCLE, PHOSPHORYLATION AT THR-287, FUNCTION IN PHOSPHORYLATION OF PLN, TISSUE SPECIFICITY, INDUCTION.
  11. "Nuclear calcium/calmodulin-dependent protein kinase IIdelta preferentially transmits signals to histone deacetylase 4 in cardiac cells."
    Little G.H., Bai Y., Williams T., Poizat C.
    J. Biol. Chem. 282:7219-7231(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF HDAC4.
  12. "Role of Ca2+/calmodulin-dependent protein kinase (CaMK) in excitation-contraction coupling in the heart."
    Maier L.S., Bers D.M.
    Cardiovasc. Res. 73:631-640(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON INVOLVEMENT IN EXCITATION-CONTRACTION COUPLING IN HEART.
  13. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Cardiac ryanodine receptor phosphorylation by CaM Kinase II: keeping the balance right."
    Currie S.
    Front. Biosci. 14:5134-5156(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON PHOSPHORYLATION OF RYR2.
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319; SER-404 AND SER-490, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  18. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Role of CaMKII in cardiovascular health, disease, and arrhythmia."
    Mohler P.J., Hund T.J.
    Heart Rhythm 8:142-144(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation."
    Rellos P., Pike A.C., Niesen F.H., Salah E., Lee W.H., von Delft F., Knapp S.
    PLoS Biol. 8:E1000426-E1000426(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 11-335 IN COMPLEX AND INHIBITORS.
  23. "Calmodulin bound to peptide from calmodulin kinase II (CaMKII)."
    Ng H.L., Alber T.A., Wand A.J.
    Submitted (MAR-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) OF 294-311 IN COMPLEX WITH CALMODULIN.
  24. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLU-167 AND ILE-493.

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: September 3, 2014
This is version 155 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 1 Publication.

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

External Data

Dasty 3

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