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Q3MHJ9 (KCC2B_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Calcium/calmodulin-dependent protein kinase type II subunit beta

Short name=CaM kinase II subunit beta
Short name=CaMK-II subunit beta
EC=2.7.11.17
Gene names
Name:CAMK2B
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length542 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca2+/calmodulin-binding and autophosphorylation, and is involved in dendritic spine and synapse formation, neuronal plasticity and regulation of sarcoplamic reticulum Ca2+ transport in skeletal muscle. In neurons, plays an essential structural role in the reorganization of the actin cytoskeleton during plasticity by binding and bundling actin filaments in a kinase-independent manner. This structural function is required for correct targeting of CaMK2A, which acts downstream of NMDAR to promote dendritic spine and synapse formation and maintain synaptic plasticity which enables long-term potentiation (LTP) and hippocampus-dependent learning. In developing hippocampal neurons, promotes arborization of the dendritic tree and in mature neurons, promotes dendritic remodeling. Participates in the modulation of skeletal muscle function in response to exercise. In slow-twitch muscles, is involved in regulation of sarcoplamic reticulum (SR) Ca2+ transport and in fast-twitch muscle participates in the control of Ca2+ release from the SR through phosphorylation of triadin, a ryanodine receptor-coupling factor, and phospholamban (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2 By similarity.

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 By similarity.

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 SYNGAP1, CAMK2N2 and MPDZ By similarity.

Subcellular location

Cytoplasmcytoskeleton. Cytoplasmcytoskeletoncentrosome. Sarcoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity.

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.

Sequence similarities

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

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 542542Calcium/calmodulin-dependent protein kinase type II subunit beta
PRO_0000260268

Regions

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

Sites

Active site1361Proton acceptor By similarity
Binding site431ATP By similarity

Amino acid modifications

Modified residue171Phosphotyrosine By similarity
Modified residue2871Phosphothreonine; by autocatalysis By similarity
Modified residue3061Phosphothreonine; by autocatalysis By similarity
Modified residue3071Phosphothreonine; by autocatalysis By similarity
Modified residue3151Phosphoserine By similarity
Modified residue3581Phosphoserine By similarity
Modified residue3671Phosphoserine By similarity
Modified residue3971Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3MHJ9 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: 29C877521DEC4FD1

FASTA54260,482
        10         20         30         40         50         60 
MATTVTCTRF TDEYQLYEDI GKGAFSVVRR CVKLCTGHEY AAKIINTKKL SARDHQKLER 

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

       130        140        150        160        170        180 
LEAVLHCHQM GVVHRDLKPE NLLLASKCKG AAVKLADFGL AIEVQGDQQA WFGFAGTPGY 

       190        200        210        220        230        240 
LSPEVLRKEA YGKPVDIWAC GVILYILLVG YPPFWDEDQH KLYQQIKAGA YDFPSPEWDT 

       250        260        270        280        290        300 
VTPEAKNLIN QMLTINPAKR IMAHEALKHP WVCQRSTVAS MMHRQETVEC LKKFNARRKL 

       310        320        330        340        350        360 
KGAILTTMLA TRNFSVGRQT TAPATMSTAA SGATMGLVEQ AKSLLNKKAD GVKPQTNSTK 

       370        380        390        400        410        420 
NSAAATSPKG TLPPAALEPQ TTVIHNPVDG IKESSDSTHT TIEDEDTKAR KQEIIKITEQ 

       430        440        450        460        470        480 
LIEAVNNGDF EAYAKICDPG LTSFEPEALG NLVEGMDFHR FYFENLLAKN SKPIHTTILN 

       490        500        510        520        530        540 
PHVHVIGEDA ACIAYIRLTQ YIDGQGRPRT SQSEETRVWH RRDGKWQNVH FHCSGAPVAP 


LQ 

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References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Hypothalamus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC105210 mRNA. Translation: AAI05211.1.
IPIIPI00688192.
RefSeqNP_001030434.1. NM_001035357.1.
UniGeneBt.91448.

3D structure databases

HSSPHSSP built from PDB template 2BDW based on UniProtKB Q9NG91.
ProteinModelPortalQ3MHJ9.
SMRQ3MHJ9. Positions 11-301, 403-536.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3MHJ9.

Proteomic databases

PRIDEQ3MHJ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000016813; ENSBTAP00000016813; ENSBTAG00000012653.
GeneID525416.
KEGGbta:525416.

Organism-specific databases

CTD816.

Phylogenomic databases

eggNOGmaNOG12460.
GeneTreeENSGT00550000074354.
HOVERGENHBG108055.
InParanoidQ3MHJ9.
OMACPSPAPF.
OrthoDBEOG42JNR7.
PhylomeDBQ3MHJ9.

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.
IPR017442. Se/Thr_kinase-like_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR002290. Ser/Thr_kinase_dom.
[Graphical view]
KOK04515.
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...

Entry information

Entry nameKCC2B_BOVIN
AccessionPrimary (citable) accession number: Q3MHJ9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: October 25, 2005
Last modified: January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families