Calcium/calmodulin-dependent protein kinase kinase 2

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Reviewed, UniProtKB/Swiss-Prot O88831 (KKCC2_RAT)

Last modified October 13, 2009. Version 75. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Calcium/calmodulin-dependent protein kinase kinase 2
    EC=2.7.11.17
Alternative name(s):
    Calcium/calmodulin-dependent protein kinase kinase beta
      Short name=CaM-kinase kinase beta
      Short name=CaM-KK beta
      Short name=CaMKK beta

Gene names

Name:

Camkk2

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length	587 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Phosphorylates CAMK1 and CAMK4. Phosphorylates CAMK1D By similarity. Seems to be involved in hippocampal activation of CREB1 By similarity.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Activated by Ca²⁺/calmodulin. Binding of calmodulin may releave intrasteric autoinhibition. Autophosphorylation does not alter activity or regulation by Ca²⁺/calmodulin. In part, activity is independent on Ca²⁺/calmodulin.
Subunit structure	Interacts with calmodulin. Ref.3
Subcellular location	Cytoplasm. Ref.4 Ref.5
Tissue specificity	Mainly expressed in brain, but detected in all tissues tested (at protein level). In situ hybridization in brain shows a differential expression with CAMKK1 and a pattern similar to the one of CAMK4.
Domain	The autoinhibitory domain overlaps with the calmodulin binding region and may be involved in intrasteric autoinhibition. The RP domain (arginine/proline-rich) is involved in the recognition of CAMKI and CAMK4 as substrates By similarity.
Post-translational modification	Autophosphorylated. Ref.3 Ref.2
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 1 protein kinase domain.

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Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Calmodulin-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	activation of protein kinase activity Inferred from direct assay. Source: RGD protein amino acid autophosphorylation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell soluble fraction Inferred from direct assay. Source: RGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium ion binding Inferred from sequence or structural similarity. Source: UniProtKB calmodulin binding Inferred from electronic annotation. Source: UniProtKB-KW calmodulin-dependent protein kinase activity Ref.1 Inferred from direct assay. Source: RGD protein kinase activator activity Ref.1 Traceable author statement. Source: RGD
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 587

587

Calcium/calmodulin-dependent protein kinase kinase 2

PRO_0000086146

Regions

Domain

164 – 445

282

Protein kinase

Nucleotide binding

170 – 178

ATP By similarity

Region

203 – 225

RP domain

Region

471 – 476

Autoinhibitory domain By similarity

Region

474 – 499

Calmodulin-binding By similarity

Compositional bias

110 – 113

Poly-Ser

Compositional bias

548 – 551

Poly-Gly

Sites

Active site

311

Proton acceptor By similarity

Binding site

193

ATP By similarity

Amino acid modifications

Modified residue

128

Phosphoserine By similarity

Modified residue

132

Phosphoserine By similarity

Modified residue

494

Phosphoserine By similarity

Modified residue

510

Phosphoserine By similarity

Experimental info

Sequence conflict

180

L → S AA sequence Ref.2

Sequence conflict

245

P → V AA sequence Ref.2

Sequence conflict

300

Missing AA sequence Ref.2

Sequence conflict

465

V → S AA sequence Ref.2

Sequence conflict

468

E → T AA sequence Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

O88831-1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: C9E49B72578F3971
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FASTA

587

64,446

        10         20         30         40         50         60 
MSSCVSSQPT SDRAAPQDEL GSGGVSRESQ KPCEALRGLS SLSIHLGMES FIVVTECEPG 

        70         80         90        100        110        120 
RGVDLSLARD QPLEADGQEL PLDASEPESR SLLSGGKMSL QERSQGGPAS SSSLDMNGRC 

       130        140        150        160        170        180 
ICPSLSYSPA SSPQSSPRMP RRPTVESHHV SITGLQDCVQ LNQYTLKDEI GKGSYGVVKL 

       190        200        210        220        230        240 
AYNENDNTYY AMKVLSKKKL IRQAGFPRRP PPRGTRPAPG GCIQPRGPIE QVYQEIAILK 

       250        260        270        280        290        300 
KLDHPNVVKL VEVLDDPNED HLYMVFELVN QGPVMEVPTL KPLSEDQARF YFQDLIKGIE 

       310        320        330        340        350        360 
YLHYQKIIHR DIKPSNLLVG EDGHIKIADF GVSNEFKGSD ALLSNTVGTP AFMAPESLSE 

       370        380        390        400        410        420 
TRKIFSGKAL DVWAMGVTLY CFVFGQCPFM DERIMCLHSK IKSQALEFPD QPDIAEDLKD 

       430        440        450        460        470        480 
LITRMLDKNP ESRIVVPEIK LHPWVTRHGA EPLPSEDENC TLVEVTEEEV ENSVKHIPSL 

       490        500        510        520        530        540 
ATVILVKTMI RKRSFGNPFE GSRREERSLS APGNLLTKKP TREWEPLSEP KEARQRRQPP 

       550        560        570        580 
GPRASPCGGG GSALVKGGPC VESCGAPAPG SPPRTPPQQP EEAMEPE

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References

[1]	"Molecular cloning of Ca2+/calmodulin-dependent protein kinase kinase beta." Kitani T., Okuno S., Fujisawa H. J. Biochem. 122:243-250(1997) [PubMed: 9276695] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Cerebellum.
[2]	"Multiple Ca(2+)-calmodulin-dependent protein kinase kinases from rat brain. Purification, regulation by Ca(2+)-calmodulin, and partial amino acid sequence." Edelman A.M., Mitchelhill K.I., Selbert M.A., Anderson K.A., Hook S.S., Stapleton D., Goldstein E.G., Means A.R., Kemp B.E. J. Biol. Chem. 271:10806-10810(1996) [PubMed: 8631893] [Abstract] Cited for: PROTEIN SEQUENCE OF 180-184; 227-280; 290-294; 298-306; 327-335; 338-355; 403-418; 425-429; 434-445; 448-469 AND 494-503, FUNCTION IN PHOSPHORYLATION OF CAMK1 AND CAMK4.
[3]	"Components of a calmodulin-dependent protein kinase cascade. Molecular cloning, functional characterization and cellular localization of Ca2+/calmodulin-dependent protein kinase kinase beta." Anderson K.A., Means R.L., Huang Q.-H., Kemp B.E., Goldstein E.G., Selbert M.A., Edelman A.M., Fremeau R.T., Means A.R. J. Biol. Chem. 273:31880-31889(1998) [PubMed: 9822657] [Abstract] Cited for: CHARACTERIZATION, INTERACTION WITH CALMODULIN, FUNCTION IN PHOSPHORYLATION OF CAMK1 AND CAMK4, AUTOPHOSPHORYLATION.
[4]	"Distinct immunohistochemical localization of two isoforms of Ca2+/calmodulin-dependent protein kinase kinases in the adult rat brain." Sakagami H., Umemiya M., Saito S., Kondo H. Eur. J. Neurosci. 12:89-99(2000) [PubMed: 10651863] [Abstract] Cited for: SUBCELLULAR LOCATION.
[5]	"Ca(2+)/CaM-dependent kinases: from activation to function." Hook S.S., Means A.R. Annu. Rev. Pharmacol. Toxicol. 41:471-505(2001) [PubMed: 11264466] [Abstract] Cited for: SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	AB018081 mRNA. Translation: BAA33524.1.
IPI	IPI00213319.
PIR	JC5669.
RefSeq	NP_112628.1.
UniGene	Rn.88589
3D structure databases
HSSP	HSSP built from PDB template 1OL6 based on UniProtKB O14965.
ModBase	Search...
Protein-protein interaction databases
STRING	O88831.
PTM databases
PhosphoSite	O88831.
Proteomic databases
PRIDE	O88831.
Genome annotation databases
Ensembl	ENSRNOT00000001774; ENSRNOP00000001774; ENSRNOG00000001309; Rattus norvegicus. [Genome view] ENSRNOT00000001778; ENSRNOP00000001778; ENSRNOG00000001309; Rattus norvegicus. [Genome view]
GeneID	83506.
KEGG	rno:83506.
UCSC	NM_031338. rat.
Organism-specific databases
CTD	83506.
RGD	620092. Camkk2.
Phylogenomic databases
HOVERGEN	O88831.
Enzyme and pathway databases
BRENDA	2.7.11.17. 248.
Gene expression databases
ArrayExpress	O88831.
Genevestigator	O88831.
GermOnline	ENSRNOG00000001309. Rattus norvegicus.
Family and domain databases
InterPro	IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	615936.

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Entry information

Entry name

KKCC2_RAT

Accession

Primary (citable) accession number: O88831

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 7, 2004
Last sequence update:	November 1, 1998
Last modified:	October 13, 2009
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents