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Q6PHZ2 (KCC2D_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calcium/calmodulin-dependent protein kinase type II subunit delta
Short name=CaM kinase II subunit delta
Short name=CaMK-II subunit delta
EC=2.7.11.17
Gene names
Name:Camk2d
Synonyms:Kiaa4163
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length499 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.6 Ref.7 Ref.8 Ref.13 Ref.14 Ref.15

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

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.

Subunit structure

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. Ref.15

Subcellular location

Cell membrane › sarcolemma; Peripheral membrane protein; Cytoplasmic side Probable. Sarcoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Probable.

Tissue specificity

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. Ref.4

Domain

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

Post-translational modification

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

Miscellaneous

Mice overexpressing CaMK2D develop a dilated cardiomyopathy, enlarged myocytes with reduced contractility and altered Ca2+ handling, and die prematurely in Ref.5.

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily.

Contains 1 protein kinase domain.

Sequence caution

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

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
Sarcoplasmic reticulum
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Calmodulin-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 12660151. Source: MGI

calcium ion transport

Inferred from direct assay PubMed 15652482. Source: MGI

cardiac muscle contraction

Inferred from direct assay PubMed 15652482. Source: MGI

peptidyl-serine phosphorylation

Inferred from direct assay PubMed 20877009. Source: MGI

positive regulation of cardiac muscle hypertrophy

Inferred from sequence or structural similarity. Source: UniProtKB

protein autophosphorylation

Inferred from mutant phenotype PubMed 12660151. Source: MGI

regulation of cellular localization

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of sodium ion transport

Inferred from direct assay PubMed 20877009. Source: MGI

   Cellular_componentT-tubule

Inferred from direct assay PubMed 15652482. Source: MGI

axon initial segment

Inferred from direct assay PubMed 20877009. Source: MGI

calcium- and calmodulin-dependent protein kinase complex

Traceable author statement PubMed 11264466. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 15652482. Source: MGI

intercalated disc

Inferred from direct assay PubMed 20877009. Source: MGI

neuromuscular junction

Inferred from direct assay PubMed 17873280. Source: MGI

neuronal cell body

Inferred from direct assay PubMed 20877009. Source: MGI

nucleus

Inferred from direct assay PubMed 15652482. Source: MGI

sarcoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

calmodulin-dependent protein kinase activity

Inferred from electronic annotation. Source: EC

protein serine/threonine kinase activity

Inferred from direct assay PubMed 20877009. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6PHZ2-1)

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.
Isoform 2 (identifier: Q6PHZ2-2)

Also known as: Delta 6;

The sequence of this isoform differs from the canonical sequence as follows:
     478-478: K → N
     479-499: Missing.
Isoform 3 (identifier: Q6PHZ2-4)

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.
Isoform 4 (identifier: Q6PHZ2-5)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 499498Calcium/calmodulin-dependent protein kinase type II subunit delta
PRO_0000277817

Regions

Domain14 – 272259Protein kinase
Nucleotide binding20 – 289ATP By similarity
Region283 – 29210Autoinhibitory domain By similarity
Region291 – 30111Calmodulin-binding By similarity

Sites

Active site1361Proton acceptor By similarity
Binding site431ATP By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue2311Phosphotyrosine Ref.10
Modified residue2871Phosphothreonine; by autocatalysis Probable
Modified residue3061Phosphothreonine; by autocatalysis By similarity
Modified residue3071Phosphothreonine; by autocatalysis By similarity
Modified residue3191Phosphoserine By similarity
Modified residue3301Phosphoserine Ref.12
Modified residue3371Phosphothreonine Ref.11 Ref.12
Modified residue4041Phosphoserine By similarity
Modified residue4901Phosphoserine By similarity

Natural variations

Alternative sequence3281K → KINNKANVVTSPKENIPTPA LEPQTTVIHNPDGNK in isoform 4.
VSP_023100
Alternative sequence3291E → EPQTTVIHNPDGNKE in isoform 3.
VSP_023101
Alternative sequence4781K → N in isoform 2, isoform 3 and isoform 4.
VSP_023103
Alternative sequence479 – 49921Missing in isoform 2, isoform 3 and isoform 4.
VSP_023102

Experimental info

Sequence conflict123 – 1253SVN → AVL in BAC30232. Ref.1
Sequence conflict129 – 1324LNGI → QMGV in BAC30232. Ref.1
Sequence conflict1991A → V in BAC30232. Ref.1
Isoform 2:
Sequence conflict4781N → K in BAE25062. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Delta 2) [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 62999FBAB98120CE

FASTA49956,369
        10         20         30         40         50         60 
MASTTTCTRF TDEYQLFEEL GKGAFSVVRR CMKIPTGQEY AAKIINTKKL SARDHQKLER 

        70         80         90        100        110        120 
EARICRLLKH PNIVRLHDSI SEEGFHYLVF DLVTGGELFE DIVAREYYSE ADASHCIQQI 

       130        140        150        160        170        180 
LESVNHCHLN GIVHRDLKPE NLLLASKSKG AAVKLADFGL AIEVQGDQQA WFGFAGTPGY 

       190        200        210        220        230        240 
LSPEVLRKDP YGKPVDMWAC GVILYILLVG YPPFWDEDQH RLYQQIKAGA YDFPSPEWDT 

       250        260        270        280        290        300 
VTPEAKDLIN KMLTINPAKR ITASEALKHP WICQRSTVAS MMHRQETVDC LKKFNARRKL 

       310        320        330        340        350        360 
KGAILTTMLA TRNFSAAKSL LKKPDGVKES TESSNTTIED EDVKARKQEI IKVTEQLIEA 

       370        380        390        400        410        420 
INNGDFEAYT KICDPGLTAF EPEALGNLVE GMDFHRFYFE NALSKSNKPI HTIILNPHVH 

       430        440        450        460        470        480 
LVGDDAACIA YIRLTQYMDG SGMPKTMQSE ETRVWHRRDG KWQNVHFHRS GSPTVPIKPP 

       490 
CIPNGKENFS GGTSLWQNI

« Hide

Isoform 2 (Delta 6) [UniParc].

Checksum: 506DA27C914E4F7E
Show »

FASTA47854,114
Isoform 3 (Delta 10) [UniParc].

Checksum: E0FD0E736590F908
Show »

FASTA49255,645
Isoform 4 (Delta 5) [UniParc].

Checksum: 7DA5645FB35B3EAD
Show »

FASTA51257,748

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Regulation of Kv4.3 currents by Ca2+/calmodulin-dependent protein kinase II."
Sergeant G.P., Ohya S., Reihill J.A., Perrino B.A., Amberg G.C., Imaizumi Y., Horowitz B., Sanders K.M., Koh S.D.
Am. J. Physiol. 288:C304-C313(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF POTASSIUM CHANNEL.
[7]"Calmodulin kinase II inhibition protects against structural heart disease."
Zhang R., Khoo M.S., Wu Y., Yang Y., Grueter C.E., Ni G., Price E.E. Jr., Thiel W., Guatimosim S., Song L.S., Madu E.C., Shah A.N., Vishnivetskaya T.A., Atkinson J.B., Gurevich V.V., Salama G., Lederer W.J., Colbran R.J., Anderson M.E.
Nat. Med. 11:409-417(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MYOCARDIAL REMODELING.
[8]"Ca2+/calmodulin-dependent protein kinase II regulates cardiac Na+ channels."
Wagner S., Dybkova N., Rasenack E.C., Jacobshagen C., Fabritz L., Kirchhof P., Maier S.K., Zhang T., Hasenfuss G., Brown J.H., Bers D.M., Maier L.S.
J. Clin. Invest. 116:3127-3138(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF SODIUM CHANNEL.
[9]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287, MASS SPECTROMETRY.
Tissue: Brain.
[10]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-231, MASS SPECTROMETRY.
Tissue: Brain.
[11]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-337, MASS SPECTROMETRY.
Tissue: Liver.
[12]"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, MASS SPECTROMETRY.
Tissue: Embryonic fibroblast.
[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]"CaV1.2 beta-subunit coordinates CaMKII-triggered cardiomyocyte death and afterdepolarizations."
Koval O.M., Guan X., Wu Y., Joiner M.L., Gao Z., Chen B., Grumbach I.M., Luczak E.D., Colbran R.J., Song L.S., Hund T.J., Mohler P.J., Anderson M.E.
Proc. Natl. Acad. Sci. U.S.A. 107:4996-5000(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF L-TYPE CALCIUM CHANNEL, INTERACTION WITH CACNB2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00112584.
IPI00828919.
IPI00987787.
IPI01016213.
RefSeqNP_001020609.1. NM_001025438.1.
NP_001020610.1. NM_001025439.1.
NP_076302.1. NM_023813.3.
UniGeneMm.255822.

3D structure databases

ProteinModelPortalQ6PHZ2.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-47638N.
IntActQ6PHZ2. 2 interactions.
MINTMINT-4391081.
STRING10090.ENSMUSP00000102012.

PTM databases

PhosphoSiteQ6PHZ2.

Proteomic databases

PaxDbQ6PHZ2.
PRIDEQ6PHZ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000066466; ENSMUSP00000063359; ENSMUSG00000053819.
ENSMUST00000106400; ENSMUSP00000102008; ENSMUSG00000053819.
ENSMUST00000106402; ENSMUSP00000102010; ENSMUSG00000053819.
ENSMUST00000169051; ENSMUSP00000132554; ENSMUSG00000053819.
GeneID108058.
KEGGmmu:108058.
UCSCuc008rgh.1. mouse.
uc008rgl.1. mouse.
uc008rgn.1. mouse.
uc008rgo.1. mouse.

Organism-specific databases

CTD817.
MGIMGI:1341265. Camk2d.
RougeSearch...

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00680000099653.
HOGENOMHOG000233016.
HOVERGENHBG108055.
KOK04515.
OrthoDBEOG42JNR7.

Gene expression databases

ArrayExpressQ6PHZ2.
BgeeQ6PHZ2.
GenevestigatorQ6PHZ2.

Family and domain databases

InterProIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR013543. Ca/CaM-dep_prot_kinase-assoc.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERPTHR24347. PTHR24347. 1 hit.
PfamPF08332. CaMKII_AD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. Kinase_like. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBQ6PHZ2.
NextBio359953.
SOURCESearch...

Entry information

Entry nameKCC2D_MOUSE
AccessionPrimary (citable) accession number: Q6PHZ2
Secondary accession number(s): Q3UF87 expand/collapse secondary AC list , Q3UQH9, Q5DTK4, Q8CAC5, Q9CZE2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: July 5, 2004
Last modified: May 29, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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