Skip Header

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

Q13554

- KCC2B_HUMAN

UniProt

Q13554 - KCC2B_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Calcium/calmodulin-dependent protein kinase type II subunit beta

Gene

CAMK2B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 sarcoplasmic 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 sarcoplasmic 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/ATP2A2.1 Publication

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 – 431ATPPROSITE-ProRule annotation
Active sitei136 – 1361Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi20 – 289ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calmodulin-dependent protein kinase activity Source: UniProtKB-EC
  3. protein homodimerization activity Source: BHF-UCL

GO - Biological processi

  1. activation of meiosis involved in egg activation Source: Ensembl
  2. calcium ion transport Source: Ensembl
  3. cytokine-mediated signaling pathway Source: Reactome
  4. G1/S transition of mitotic cell cycle Source: Ensembl
  5. inhibitory G-protein coupled receptor phosphorylation Source: Ensembl
  6. interferon-gamma-mediated signaling pathway Source: Reactome
  7. neuromuscular process controlling balance Source: Ensembl
  8. peptidyl-serine phosphorylation Source: Ensembl
  9. positive regulation of apoptotic signaling pathway Source: Ensembl
  10. positive regulation of dendritic spine morphogenesis Source: UniProtKB
  11. positive regulation of neuron projection development Source: UniProtKB
  12. positive regulation of synapse maturation Source: UniProtKB
  13. protein autophosphorylation Source: UniProtKB
  14. protein phosphorylation Source: ProtInc
  15. regulation of calcium ion transport Source: UniProtKB
  16. regulation of dendritic spine development Source: UniProtKB
  17. regulation of long-term neuronal synaptic plasticity Source: UniProtKB
  18. regulation of skeletal muscle adaptation Source: UniProtKB
  19. regulation of synapse structural plasticity Source: UniProtKB
  20. regulation of synaptic transmission, cholinergic Source: Ensembl
  21. response to cadmium ion Source: Ensembl
  22. signal transduction Source: ProtInc
  23. synaptic transmission Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Differentiation, Neurogenesis

Keywords - Ligandi

Actin-binding, 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.
SignaLinkiQ13554.

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium/calmodulin-dependent protein kinase type II subunit beta (EC:2.7.11.17)
Short name:
CaM kinase II subunit beta
Short name:
CaMK-II subunit beta
Gene namesi
Name:CAMK2B
Synonyms:CAM2, CAMK2, CAMKB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:1461. CAMK2B.

Subcellular locationi

Cytoplasmcytoskeleton 1 Publication. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Sarcoplasmic reticulum membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication
Note: In slow-twitch muscle, evenly distributed between longitudinal SR and junctional SR.

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. endocytic vesicle membrane Source: Reactome
  3. nucleoplasm Source: Reactome
  4. plasma membrane Source: Reactome
  5. sarcoplasmic reticulum Source: UniProtKB-KW
  6. spindle midzone Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane, Sarcoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA91.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 666666Calcium/calmodulin-dependent protein kinase type II subunit betaPRO_0000086096Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171PhosphotyrosineBy similarity
Modified residuei287 – 2871Phosphothreonine; by autocatalysis1 Publication
Modified residuei306 – 3061Phosphothreonine; by autocatalysisBy similarity
Modified residuei307 – 3071Phosphothreonine; by autocatalysisBy similarity

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

Phosphoprotein

Proteomic databases

MaxQBiQ13554.
PaxDbiQ13554.
PRIDEiQ13554.

PTM databases

PhosphoSiteiQ13554.

Expressioni

Tissue specificityi

Widely expressed. Expressed in adult and fetal brain. Expression is slightly lower in fetal brain. Expressed in skeletal muscle.1 Publication

Inductioni

Activity is induced in skeletal muscle during exercise.1 Publication

Gene expression databases

BgeeiQ13554.
ExpressionAtlasiQ13554. baseline and differential.
GenevestigatoriQ13554.

Organism-specific databases

HPAiCAB006849.
HPA026307.
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 SYNGAP1 and CAMK2N2 (By similarity). Interacts with MPDZ.By similarity3 Publications

Protein-protein interaction databases

BioGridi107266. 20 interactions.
DIPiDIP-39770N.
IntActiQ13554. 4 interactions.

Structurei

Secondary structure

1
666
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 196
Beta strandi27 – 337
Turni34 – 363
Beta strandi39 – 468
Helixi52 – 6716
Beta strandi76 – 816
Beta strandi83 – 919
Beta strandi95 – 973
Helixi98 – 1025
Helixi110 – 12920
Helixi139 – 1413
Beta strandi142 – 1454
Beta strandi153 – 1553
Helixi178 – 1803
Helixi183 – 1864
Helixi194 – 20916
Helixi219 – 22810
Turni235 – 2384
Beta strandi239 – 2413
Helixi243 – 25210
Turni257 – 2593
Helixi263 – 2664
Helixi270 – 2734
Helixi275 – 2784
Helixi285 – 29814

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BHHX-ray2.40A/B/C/D11-303[»]
ProteinModelPortaliQ13554.
SMRiQ13554. Positions 10-396, 534-660.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13554.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 272259Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni283 – 29210Autoinhibitory domainBy similarity
Regioni291 – 30111Calmodulin-bindingAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118944.
HOVERGENiHBG108055.
InParanoidiQ13554.
KOiK04515.
OMAiQGPPPCL.
OrthoDBiEOG7ZD1VM.
PhylomeDBiQ13554.
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.
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 (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. Align

Note: The variable region of the CAMK2B protein is encoded by at least 7 exons (V1 to V7). Alternative splicing within this region gives rise to CAMK2B isoforms.

Isoform 4 (identifier: Q13554) [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
MATTVTCTRF TDEYQLYEDI GKGAFSVVRR CVKLCTGHEY AAKIINTKKL
60 70 80 90 100
SARDHQKLER EARICRLLKH SNIVRLHDSI SEEGFHYLVF DLVTGGELFE
110 120 130 140 150
DIVAREYYSE ADASHCIQQI LEAVLHCHQM GVVHRDLKPE NLLLASKCKG
160 170 180 190 200
AAVKLADFGL AIEVQGDQQA WFGFAGTPGY LSPEVLRKEA YGKPVDIWAC
210 220 230 240 250
GVILYILLVG YPPFWDEDQH KLYQQIKAGA YDFPSPEWDT VTPEAKNLIN
260 270 280 290 300
QMLTINPAKR ITAHEALKHP WVCQRSTVAS MMHRQETVEC LKKFNARRKL
310 320 330 340 350
KGAILTTMLA TRNFSVGRQT TAPATMSTAA SGTTMGLVEQ AKSLLNKKAD
360 370 380 390 400
GVKPQTNSTK NSAAATSPKG TLPPAALEPQ TTVIHNPVDG IKESSDSANT
410 420 430 440 450
TIEDEDAKAP RVPDILSSVR RGSGAPEAEG PLPCPSPAPF SPLPAPSPRI
460 470 480 490 500
SDILNSVRRG SGTPEAEGPL SAGPPPCLSP ALLGPLSSPS PRISDILNSV
510 520 530 540 550
RRGSGTPEAE GPSPVGPPPC PSPTIPGPLP TPSRKQEIIK TTEQLIEAVN
560 570 580 590 600
NGDFEAYAKI CDPGLTSFEP EALGNLVEGM DFHRFYFENL LAKNSKPIHT
610 620 630 640 650
TILNPHVHVI GEDAACIAYI RLTQYIDGQG RPRTSQSEET RVWHRRDGKW
660
QNVHFHCSGA PVAPLQ
Length:666
Mass (Da):72,678
Last modified:May 31, 2011 - v3
Checksum:i8CACFC3E392C3857
GO
Isoform 1 (identifier: Q13554-2) [UniParc]FASTAAdd to Basket

Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     410-533: Missing.

Show »
Length:542
Mass (Da):60,387
Checksum:i1F7AF874A78C9D26
GO
Isoform 2 (identifier: Q13554-3) [UniParc]FASTAAdd to Basket

Also known as: Beta1, Beta'E

The sequence of this isoform differs from the canonical sequence as follows:
     316-316: V → A
     317-340: Missing.
     379-393: Missing.
     410-533: Missing.

Show »
Length:503
Mass (Da):56,379
Checksum:i4389A566D66A9FE1
GO
Isoform 3 (identifier: Q13554-4) [UniParc]FASTAAdd to Basket

Also known as: Beta2

The sequence of this isoform differs from the canonical sequence as follows:
     316-316: V → A
     317-340: Missing.
     354-392: Missing.
     410-533: Missing.

Show »
Length:479
Mass (Da):54,074
Checksum:iE8A4B57BD6AA98AC
GO
Isoform 5 (identifier: Q13554-5) [UniParc]FASTAAdd to Basket

Also known as: Beta4, BetaE

The sequence of this isoform differs from the canonical sequence as follows:
     316-316: V → A
     317-340: Missing.
     410-533: Missing.

Show »
Length:518
Mass (Da):58,009
Checksum:i5853A731579E86D8
GO
Isoform 6 (identifier: Q13554-6) [UniParc]FASTAAdd to Basket

Also known as: Beta6

The sequence of this isoform differs from the canonical sequence as follows:
     354-377: Missing.
     410-533: Missing.
     559-584: Missing.

Show »
Length:492
Mass (Da):55,223
Checksum:i1102B7F9B979E307
GO
Isoform 7 (identifier: Q13554-7) [UniParc]FASTAAdd to Basket

Also known as: Beta7

The sequence of this isoform differs from the canonical sequence as follows:
     316-316: V → A
     317-533: Missing.

Show »
Length:449
Mass (Da):50,955
Checksum:i6EB6617646B54829
GO
Isoform 8 (identifier: Q13554-8) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     316-340: Missing.
     410-533: Missing.

Show »
Length:517
Mass (Da):57,938
Checksum:i1F4A8797FB7458A4
GO

Sequence cautioni

The sequence AAC99802.1 differs from that shown. Reason: Frameshift at positions 426, 433, 511 and 516.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681L → V in AAD03744. 1 PublicationCurated
Sequence conflicti68 – 681L → V in AAD03743. 1 PublicationCurated
Sequence conflicti535 – 5351K → N in AAB16863. (PubMed:9060999)Curated
Isoform 2 (identifier: Q13554-3)
Sequence conflicti316 – 3161A → V in AAD42036. (PubMed:10858498)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti489 – 4891P → L in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_045581
Natural varianti510 – 5101E → K.1 Publication
Corresponds to variant rs35452727 [ dbSNP | Ensembl ].
VAR_045582

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei316 – 34025Missing in isoform 8. CuratedVSP_041219Add
BLAST
Alternative sequencei316 – 3161V → A in isoform 2, isoform 3, isoform 5 and isoform 7. 6 PublicationsVSP_004770
Alternative sequencei317 – 533217Missing in isoform 7. 1 PublicationVSP_004772Add
BLAST
Alternative sequencei317 – 34024Missing in isoform 2, isoform 3 and isoform 5. 6 PublicationsVSP_004771Add
BLAST
Alternative sequencei354 – 39239Missing in isoform 3. 1 PublicationVSP_004774Add
BLAST
Alternative sequencei354 – 37724Missing in isoform 6. 1 PublicationVSP_004773Add
BLAST
Alternative sequencei379 – 39315Missing in isoform 2. 5 PublicationsVSP_004775Add
BLAST
Alternative sequencei410 – 533124Missing in isoform 1, isoform 2, isoform 3, isoform 5, isoform 6 and isoform 8. 6 PublicationsVSP_004776Add
BLAST
Alternative sequencei559 – 58426Missing in isoform 6. 1 PublicationVSP_004777Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF078803 mRNA. Translation: AAD42035.1.
AF081572 mRNA. Translation: AAD42036.1.
AF081924 mRNA. Translation: AAD42037.1.
AF083419 mRNA. Translation: AAD42038.1.
AF140350 mRNA. Translation: AAD42070.1.
U23460 mRNA. Translation: AAC99802.1. Frameshift.
AF112472 mRNA. Translation: AAD03744.1.
AF112471 mRNA. Translation: AAD03743.1.
AJ252236 mRNA. Translation: CAB65120.1.
AJ252237 mRNA. Translation: CAB65121.1.
AJ252238 mRNA. Translation: CAB65122.1.
AK290148 mRNA. Translation: BAF82837.1.
AK315663 mRNA. Translation: BAG38029.1.
CH236960 Genomic DNA. Translation: EAL23756.1.
CH236960 Genomic DNA. Translation: EAL23757.1.
CH236960 Genomic DNA. Translation: EAL23758.1.
CH236960 Genomic DNA. Translation: EAL23759.1.
CH236960 Genomic DNA. Translation: EAL23760.1.
CH236960 Genomic DNA. Translation: EAL23761.1.
CH236960 Genomic DNA. Translation: EAL23762.1.
BC019070 mRNA. Translation: AAH19070.1.
U50358 mRNA. Translation: AAB16863.1.
CCDSiCCDS43573.1. [Q13554-8]
CCDS5483.1. [Q13554-1]
CCDS5484.1. [Q13554-2]
CCDS5485.1. [Q13554-5]
CCDS5486.1. [Q13554-3]
CCDS5487.1. [Q13554-6]
CCDS5488.1. [Q13554-4]
CCDS5489.1. [Q13554-7]
RefSeqiNP_001211.3. NM_001220.4. [Q13554-1]
NP_001280099.1. NM_001293170.1. [Q13554-2]
NP_742075.1. NM_172078.2. [Q13554-2]
NP_742076.1. NM_172079.2. [Q13554-5]
NP_742077.1. NM_172080.2. [Q13554-8]
NP_742078.1. NM_172081.2. [Q13554-3]
NP_742079.1. NM_172082.2. [Q13554-6]
NP_742080.1. NM_172083.2. [Q13554-4]
NP_742081.1. NM_172084.2. [Q13554-7]
XP_006715839.1. XM_006715776.1. [Q13554-1]
UniGeneiHs.351887.

Genome annotation databases

EnsembliENST00000258682; ENSP00000258682; ENSG00000058404. [Q13554-8]
ENST00000346990; ENSP00000326518; ENSG00000058404. [Q13554-7]
ENST00000347193; ENSP00000326544; ENSG00000058404. [Q13554-6]
ENST00000350811; ENSP00000326375; ENSG00000058404. [Q13554-2]
ENST00000353625; ENSP00000326427; ENSG00000058404. [Q13554-4]
ENST00000358707; ENSP00000351542; ENSG00000058404. [Q13554-3]
ENST00000395747; ENSP00000379096; ENSG00000058404. [Q13554-5]
ENST00000395749; ENSP00000379098; ENSG00000058404. [Q13554-1]
ENST00000440254; ENSP00000397937; ENSG00000058404. [Q13554-2]
ENST00000457475; ENSP00000390292; ENSG00000058404. [Q13554-5]
GeneIDi816.
KEGGihsa:816.
UCSCiuc003tkp.2. human. [Q13554-2]
uc003tkq.2. human. [Q13554-1]
uc003tkr.2. human. [Q13554-5]
uc003tks.2. human. [Q13554-8]
uc003tkt.2. human. [Q13554-6]
uc003tku.2. human. [Q13554-3]
uc003tkv.2. human. [Q13554-4]
uc003tkw.2. human. [Q13554-7]

Polymorphism databases

DMDMi334302890.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF078803 mRNA. Translation: AAD42035.1 .
AF081572 mRNA. Translation: AAD42036.1 .
AF081924 mRNA. Translation: AAD42037.1 .
AF083419 mRNA. Translation: AAD42038.1 .
AF140350 mRNA. Translation: AAD42070.1 .
U23460 mRNA. Translation: AAC99802.1 . Frameshift.
AF112472 mRNA. Translation: AAD03744.1 .
AF112471 mRNA. Translation: AAD03743.1 .
AJ252236 mRNA. Translation: CAB65120.1 .
AJ252237 mRNA. Translation: CAB65121.1 .
AJ252238 mRNA. Translation: CAB65122.1 .
AK290148 mRNA. Translation: BAF82837.1 .
AK315663 mRNA. Translation: BAG38029.1 .
CH236960 Genomic DNA. Translation: EAL23756.1 .
CH236960 Genomic DNA. Translation: EAL23757.1 .
CH236960 Genomic DNA. Translation: EAL23758.1 .
CH236960 Genomic DNA. Translation: EAL23759.1 .
CH236960 Genomic DNA. Translation: EAL23760.1 .
CH236960 Genomic DNA. Translation: EAL23761.1 .
CH236960 Genomic DNA. Translation: EAL23762.1 .
BC019070 mRNA. Translation: AAH19070.1 .
U50358 mRNA. Translation: AAB16863.1 .
CCDSi CCDS43573.1. [Q13554-8 ]
CCDS5483.1. [Q13554-1 ]
CCDS5484.1. [Q13554-2 ]
CCDS5485.1. [Q13554-5 ]
CCDS5486.1. [Q13554-3 ]
CCDS5487.1. [Q13554-6 ]
CCDS5488.1. [Q13554-4 ]
CCDS5489.1. [Q13554-7 ]
RefSeqi NP_001211.3. NM_001220.4. [Q13554-1 ]
NP_001280099.1. NM_001293170.1. [Q13554-2 ]
NP_742075.1. NM_172078.2. [Q13554-2 ]
NP_742076.1. NM_172079.2. [Q13554-5 ]
NP_742077.1. NM_172080.2. [Q13554-8 ]
NP_742078.1. NM_172081.2. [Q13554-3 ]
NP_742079.1. NM_172082.2. [Q13554-6 ]
NP_742080.1. NM_172083.2. [Q13554-4 ]
NP_742081.1. NM_172084.2. [Q13554-7 ]
XP_006715839.1. XM_006715776.1. [Q13554-1 ]
UniGenei Hs.351887.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3BHH X-ray 2.40 A/B/C/D 11-303 [» ]
ProteinModelPortali Q13554.
SMRi Q13554. Positions 10-396, 534-660.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107266. 20 interactions.
DIPi DIP-39770N.
IntActi Q13554. 4 interactions.

Chemistry

BindingDBi Q13554.
ChEMBLi CHEMBL4121.
GuidetoPHARMACOLOGYi 1556.

PTM databases

PhosphoSitei Q13554.

Polymorphism databases

DMDMi 334302890.

Proteomic databases

MaxQBi Q13554.
PaxDbi Q13554.
PRIDEi Q13554.

Protocols and materials databases

DNASUi 816.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000258682 ; ENSP00000258682 ; ENSG00000058404 . [Q13554-8 ]
ENST00000346990 ; ENSP00000326518 ; ENSG00000058404 . [Q13554-7 ]
ENST00000347193 ; ENSP00000326544 ; ENSG00000058404 . [Q13554-6 ]
ENST00000350811 ; ENSP00000326375 ; ENSG00000058404 . [Q13554-2 ]
ENST00000353625 ; ENSP00000326427 ; ENSG00000058404 . [Q13554-4 ]
ENST00000358707 ; ENSP00000351542 ; ENSG00000058404 . [Q13554-3 ]
ENST00000395747 ; ENSP00000379096 ; ENSG00000058404 . [Q13554-5 ]
ENST00000395749 ; ENSP00000379098 ; ENSG00000058404 . [Q13554-1 ]
ENST00000440254 ; ENSP00000397937 ; ENSG00000058404 . [Q13554-2 ]
ENST00000457475 ; ENSP00000390292 ; ENSG00000058404 . [Q13554-5 ]
GeneIDi 816.
KEGGi hsa:816.
UCSCi uc003tkp.2. human. [Q13554-2 ]
uc003tkq.2. human. [Q13554-1 ]
uc003tkr.2. human. [Q13554-5 ]
uc003tks.2. human. [Q13554-8 ]
uc003tkt.2. human. [Q13554-6 ]
uc003tku.2. human. [Q13554-3 ]
uc003tkv.2. human. [Q13554-4 ]
uc003tkw.2. human. [Q13554-7 ]

Organism-specific databases

CTDi 816.
GeneCardsi GC07M044225.
HGNCi HGNC:1461. CAMK2B.
HPAi CAB006849.
HPA026307.
HPA051783.
HPA051785.
HPA053973.
MIMi 607707. gene.
neXtProti NX_Q13554.
PharmGKBi PA91.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118944.
HOVERGENi HBG108055.
InParanoidi Q13554.
KOi K04515.
OMAi QGPPPCL.
OrthoDBi EOG7ZD1VM.
PhylomeDBi Q13554.
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 Q13554.

Miscellaneous databases

EvolutionaryTracei Q13554.
GeneWikii CAMK2B.
GenomeRNAii 816.
NextBioi 3310.
PROi Q13554.
SOURCEi Search...

Gene expression databases

Bgeei Q13554.
ExpressionAtlasi Q13554. baseline and differential.
Genevestigatori Q13554.

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.
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 of alternative splicing variants of the beta subunit of human Ca(2+)/calmodulin-dependent protein kinase II with different activities."
    Wang P., Wu Y., Zhou T.H., Sun Y., Pei G.
    FEBS Lett. 475:107-110(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 5; 6 AND 7).
    Tissue: Brain.
  2. Leddy J.J., Salih M., Tuana B.S.
    Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
    Tissue: Skeletal muscle.
  3. "Molecular cloning and sequencing of human calcium/calmodulin dependent protein kinase II beta subunit."
    Li G.Y., Cooper N.G.F.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 5).
    Tissue: Brain.
  4. "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] (ISOFORMS 2; 3 AND 5).
    Tissue: Insulinoma.
  5. "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] (ISOFORMS 1 AND 2).
    Tissue: Testis and Thalamus.
  6. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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 2).
    Tissue: Lung.
  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 302-605 (ISOFORM 2).
  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. "SynGAP-MUPP1-CaMKII synaptic complexes regulate p38 MAP kinase activity and NMDA receptor-dependent synaptic AMPA receptor potentiation."
    Krapivinsky G., Medina I., Krapivinsky L., Gapon S., Clapham D.E.
    Neuron 43:563-574(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MPDZ.
  11. "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.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: SUBCELLULAR LOCATION.
  14. "The role of calcium and calcium/calmodulin-dependent kinases in skeletal muscle plasticity and mitochondrial biogenesis."
    Chin E.R.
    Proc. Nutrit. Soc. 63:279-286(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION IN SKELETAL MUSCLE.
  15. "The Ca2+-calmodulin dependent protein kinase II system of skeletal muscle sarcoplasmic reticulum."
    Sacchetto R., Bovo E., Damiani E.
    Basic Appl. Myol. 15:5-17(2005)
    Cited for: REVIEW ON FUNCTION IN SKELETAL MUSCLE.
  16. "Calmodulin-kinases: modulators of neuronal development and plasticity."
    Wayman G.A., Lee Y.S., Tokumitsu H., Silva A.J., Silva A., Soderling T.R.
    Neuron 59:914-931(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION IN NEURONAL PLASTICITY.
  17. "The roles of CaMKII and F-actin in the structural plasticity of dendritic spines: a potential molecular identity of a synaptic tag?"
    Okamoto K., Bosch M., Hayashi Y.
    Physiology (Bethesda) 24:357-366(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION IN NEURONAL PLASTICITY.
  18. "Crystal structure of human calcium/calmodulin-dependent protein kinase IIb isoform 1 (CAMK2B)."
    Structural genomics consortium (SGC)
    Submitted (DEC-2007) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 11-303 IN COMPLEX WITH INHIBITOR.
  19. "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] LEU-489 AND LYS-510.

Entry informationi

Entry nameiKCC2B_HUMAN
AccessioniPrimary (citable) accession number: Q13554
Secondary accession number(s): A4D2K0
, A4D2K1, A4D2K2, A4D2K3, A4D2K4, A4D2K5, A4D2K6, O95437, O95438, O95599, Q9UGH7, Q9UGH8, Q9UGH9, Q9UNX0, Q9UNX7, Q9UP00, Q9Y5N4, Q9Y6F4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 31, 2011
Last modified: October 29, 2014
This is version 153 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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