Calcium/calmodulin-dependent protein kinase kinase 1

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Q8VBY2 (KKCC1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 86. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Calcium/calmodulin-dependent protein kinase kinase 1
Short name=CaM-KK 1
Short name=CaM-kinase kinase 1
Short name=CaMKK 1
EC=2.7.11.17

Alternative name(s):
CaM-kinase IV kinase
Calcium/calmodulin-dependent protein kinase kinase alpha
Short name=CaM-KK alpha
Short name=CaM-kinase kinase alpha
Short name=CaMKK alpha

Gene names

Name:	Camkk1
Synonyms:	Camkk

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	505 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Calcium/calmodulin-dependent protein kinase that belongs to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Phosphorylates CAMK1, CAMK1D, CAMK1G and CAMK4. Involved in regulating cell apoptosis. Promotes cell survival by phosphorylating AKT1/PKB that inhibits pro-apoptotic BAD/Bcl2-antagonist of cell death. Ref.6
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Activated by Ca²⁺/calmodulin. Binding of calmodulin may relieve intrasteric autoinhibition. Partially inhibited upon phosphorylation by PRCAKA/PKA By similarity. May be regulated through phosphorylation by CAMK1 and CAMK4.
Subunit structure	Interacts with CAMK4 and calmodulin By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Tissue specificity	Widely expressed. Differentially expressed in various brain regions. Ref.5
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	Appears to be autophosphorylated in a Ca²⁺/calmodulin-dependent manner. Phosphorylated at multiple sites by PRCAKA/PKA. Phosphorylation of Ser-458 is blocked upon binding to Ca²⁺/calmodulin. In vitro, phosphorylated by CAMK1 and CAMK4 By similarity. Ref.6 Ref.7
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Calmodulin-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calmodulin binding Inferred from electronic annotation. Source: UniProtKB-KW calmodulin-dependent protein kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 505

505

Calcium/calmodulin-dependent protein kinase kinase 1

PRO_0000086142

Regions

Domain

128 – 409

282

Protein kinase

Nucleotide binding

134 – 142

ATP By similarity

Region

167 – 189

RP domain

Region

435 – 440

Autoinhibitory domain By similarity

Region

438 – 463

Calmodulin-binding By similarity

Sites

Active site

275

Proton acceptor By similarity

Binding site

157

ATP By similarity

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

108

Phosphothreonine By similarity

Modified residue

458

Phosphoserine Ref.7

Modified residue

475

Phosphoserine Ref.7

Modified residue

492

Phosphoserine By similarity

Modified residue

505

Phosphoserine By similarity

Experimental info

Sequence conflict

99 – 100

IS → MC in AAF08348. Ref.1

Sequence conflict

198 – 199

QE → HD in AAF08348. Ref.1

Sequence conflict

382

L → S in AAF08348. Ref.1

Sequence conflict

417

L → I in AAF08348. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q8VBY2 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 179915A25628F9C4
Show »

FASTA

505

55,838

        10         20         30         40         50         60 
MESGPAVCCQ DPRAELVDRV AAINVAHLEE ADEGPEPARN GVDPPPRARA ASVIPGSASR 

        70         80         90        100        110        120 
PTPVRPSLSA RKFSLQERPA GSCLGAQVGP YSTGPASHIS PRSWRRPTIE SHRVAISDTE 

       130        140        150        160        170        180 
DCVQLNQYKL QSEIGKGAYG VVRLAYNESE DRHYAMKVLS KKKLLKQYGF PRRPPPRGSQ 

       190        200        210        220        230        240 
ATQGGPAKQL LPLERVYQEI AILKKLDHVN VVKLIEVLDD PAEDNLYLVF DLLRKGPVME 

       250        260        270        280        290        300 
VPCDKPFPEE QARLYLRDII LGLEYLHCQK IVHRDIKPSN LLLGDDGHVK IADFGVSNQF 

       310        320        330        340        350        360 
EGNDAQLSST AGTPAFMAPE AISDSGQSFS GKALDVWATG VTLYCFVYGK CPFIDDYILT 

       370        380        390        400        410        420 
LHRKIKNEAV VFPEEPEVSE DLKDLILRML DKNPETRIGV SDIKLHPWVT KHGEEPLPSE 

       430        440        450        460        470        480 
EEHCSVVEVT EEEVKNSVRL IPSWTTVILV KSMLRKRSFG NPFEPQARRE ERSMSAPGSL 

       490        500 
LMKEGCGEGC KSPELPGVQE DEAAS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Modulation of a calcium/calmodulin-dependent protein kinase cascade by retinoic acid during neutrophil maturation." Lawson N.D., Zain M., Zibello T., Picciotto M.R., Nairn A.C., Berliner N. Exp. Hematol. 27:1682-1690(1999) [PubMed: 10560916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Long-term memory deficits in Pavlovian fear conditioning in Ca2+/calmodulin kinase kinase alpha-deficient mice." Blaeser F., Sanders M.J., Truong N., Ko S., Wu L.J., Wozniak D.F., Fanselow M.S., Zhuo M., Chatila T.A. Mol. Cell. Biol. 26:9105-9115(2006) [PubMed: 17015467] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/SvJ.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Salivary gland.
[4]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 114-129 AND 440-451, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
[5]	"Cloning of mouse Ca2+/calmodulin-dependent protein kinase kinase beta (CaMKKbeta) and characterization of CaMKKbeta and CaMKKalpha distribution in the adult mouse brain." Vinet J., Carra S., Blom J.M.C., Harvey M., Brunello N., Barden N., Tascedda F. Brain Res. Mol. Brain Res. 111:216-221(2003) [PubMed: 12654522] [Abstract] Cited for: TISSUE SPECIFICITY.
[6]	"Molecular cloning and characterization of CLICK-III/CaMKIgamma, a novel membrane-anchored neuronal Ca2+/calmodulin-dependent protein kinase (CaMK)." Takemoto-Kimura S., Terai H., Takamoto M., Ohmae S., Kikumura S., Segi E., Arakawa Y., Furuyashiki T., Narumiya S., Bito H. J. Biol. Chem. 278:18597-18605(2003) [PubMed: 12637513] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF CAMK1G.
[7]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458 AND SER-475, MASS SPECTROMETRY. Tissue: Brain cortex.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF117384 mRNA. Translation: AAF08348.1. AF461706 , AF461702, AF461703, AF461705, AF461704 Genomic DNA. Translation: AAL67849.1. BC017529 mRNA. Translation: AAH17529.1.
IPI	IPI00626535.
RefSeq	NP_061371.2. NM_018883.2.
UniGene	Mm.9998.
3D structure databases
ProteinModelPortal	Q8VBY2.
SMR	Q8VBY2. Positions 123-411, 438-463.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-102795.
STRING	Q8VBY2.
PTM databases
PhosphoSite	Q8VBY2.
Proteomic databases
PRIDE	Q8VBY2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000092937; ENSMUSP00000090613; ENSMUSG00000020785.
GeneID	55984.
KEGG	mmu:55984.
Organism-specific databases
CTD	84254.
MGI	MGI:1891766. Camkk1.
Phylogenomic databases
eggNOG	roNOG15074.
GeneTree	ENSGT00530000063214.
HOGENOM	HBG755340.
HOVERGEN	HBG052262.
InParanoid	Q8VBY2.
OMA	LHCQKIV.
OrthoDB	EOG4TF0JX.
PhylomeDB	Q8VBY2.
Gene expression databases
ArrayExpress	Q8VBY2.
Bgee	Q8VBY2.
Genevestigator	Q8VBY2.
GermOnline	ENSMUSG00000020785. Mus musculus.
Family and domain databases
InterPro	IPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase. 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]
KO	K07359.
PANTHER	PTHR24347. PTHR24347. 1 hit.
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	311694.
SOURCE	Search...

Entry information

Entry name

KKCC1_MOUSE

Accession

Primary (citable) accession number: Q8VBY2
Secondary accession number(s): Q9R054

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 7, 2004
Last sequence update:	March 1, 2002
Last modified:	November 16, 2011
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata 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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

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

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents