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UniProtKB/Swiss-Prot entry Q14012


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name KCC1A_HUMAN
Primary accession number Q14012
Secondary accession number Q3KPF6
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 94)
Name and origin of the protein
Protein name Calcium/calmodulin-dependent protein kinase type 1
Synonyms EC 2.7.11.17
CaM kinase I
CaM-KI
CaM kinase I alpha
CaMKI-alpha
Gene name
Name: CAMK1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT THR-177, MUTAGENESIS OF LYS-49 AND THR-177, AND ENZYME REGULATION.
PubMed=7641687 [NCBI, ExPASy, EBI, Israel, Japan]
Haribabu B., Hook S.S., Selbert M.A., Goldstein E.G., Tomhave E.D., Edelman A.M., Snyderman R., Means A.R.;
"Human calcium-calmodulin dependent protein kinase I: cDNA cloning, domain structure and activation by phosphorylation at threonine-177 by calcium-calmodulin dependent protein kinase I kinase.";
EMBO J. 14:3679-3686(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 1-9.
TISSUE=Platelet;
DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan]
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[4]
PHOSPHORYLATION BY CAMKK1.
DOI=10.1159/000025324; PubMed=9662074 [NCBI, ExPASy, EBI, Israel, Japan]
Hsu L.-S., Tsou A.-P., Chi C.-W., Lee C.-H., Chen J.-Y.;
"Cloning, expression and chromosomal localization of human Ca2+/calmodulin-dependent protein kinase kinase.";
J. Biomed. Sci. 5:141-149(1998).
[5]
PHOSPHORYLATION BY CAMKK2.
DOI=10.1074/jbc.M011720200; PubMed=11395482 [NCBI, ExPASy, EBI, Israel, Japan]
Hsu L.-S., Chen G.-D., Lee L.-S., Chi C.-W., Cheng J.-F., Chen J.-Y.;
"Human Ca2+/calmodulin-dependent protein kinase kinase beta gene encodes multiple isoforms that display distinct kinase activity.";
J. Biol. Chem. 276:31113-31123(2001).
[6]
FUNCTION IN PHOSPHORYLATION OF EIF4G3.
DOI=10.1074/jbc.M308781200; PubMed=14507913 [NCBI, ExPASy, EBI, Israel, Japan]
Qin H., Raught B., Sonenberg N., Goldstein E.G., Edelman A.M.;
"Phosphorylation screening identifies translational initiation factor 4GII as an intracellular target of Ca(2+)/calmodulin-dependent protein kinase I.";
J. Biol. Chem. 278:48570-48579(2003).
[7]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[8]
VARIANTS [LARGE SCALE ANALYSIS] SER-217 AND LYS-361.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L41816; AAA99458.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC106754; AAI06755.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC106755; AAI06756.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00028296; -.
PIR S57347; S57347.
RefSeq NP_003647.1; -.
UniGene Hs.434875
3D structure databases
HSSP Q63450; 1A06. [HSSP ENTRY / PDB]
SMR Q14012; 10-316.
ModBase Q14012.
PTM databases
PhosphoSite Q14012; -.
Enzyme and pathway databases
BRENDA 2.7.11.17; 247.
Organism-specific databases
GeneCards GC03M009774; -.
H-InvDB HIX0018244; -.
HGNC HGNC:1459; CAMK1.
GenAtlas CAMK1.
MIM 604998; gene. [NCBI / EBI]
PharmGKB PA26048; -.
Gene expression databases
ArrayExpress Q14012; -.
Bgee Q14012; -.
CleanEx HS_CAMK1; -.
GermOnline ENSG00000134072; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005516; Molecular function: calmodulin binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004683; Molecular function: calmodulin-dependent protein kinase activity (inferred from electronic annotation from EC).
GO:0030154; Biological process: cell differentiation (inferred from electronic annotation from UniProtKB-KW).
GO:0007399; Biological process: nervous system development (inferred from electronic annotation from UniProtKB-KW).
GO:0006468; Biological process: protein amino acid phosphorylation (traceable author statement from ProtInc).
GO:0007165; Biological process: signal transduction (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR015734; Ca/calmodulin-dep_kinase_1.
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 of domain structure.
PANTHER PTHR22982:SF34; CaMKI; 1.
Pfam PF00069; Pkinase; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas Q14012; -.
PRIDE Q14012; -.
Genome annotation databases
Ensembl ENSG00000134072; Homo sapiens. [Contig view]
GeneID 8536; -.
KEGG hsa:8536; -.
NMPDR fig|9606.3.peg.22087; -.
Phylogenomic databases
HOGENOM Q14012; -.
HOVERGEN Q14012; -.
OMA Q14012; EEDSKIM.
Other
NextBio 31972; -.
SOURCE CAMK1; Homo sapiens.
ProtoNet Q14012.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Allosteric enzyme; ATP-binding; Calmodulin-binding; Cytoplasm; Developmental protein; Differentiation; Direct protein sequencing; Kinase; Neurogenesis; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   370  370     Calcium/calmodulin-dependent protein kinase type 1. PRO_0000086076
DOMAIN   20   276  257     Protein kinase. 
NP_BIND   26    34  9     ATP (By similarity). 
REGION   276   316  41     Autoinhibitory domain (By similarity). 
REGION   296   317  22     Calmodulin-binding (By similarity). 
MOTIF   315   321  7     Nuclear export signal (By similarity). 
ACT_SITE   141   141        Proton acceptor (By similarity). 
BINDING   49    49        ATP. 
MOD_RES   177   177        Phosphothreonine; by CaMKK1 and CaMKK2. 
VARIANT   217   217  1     P -> S (in a metastatic melanoma sample; somatic mutation). VAR_040596 
VARIANT   361   361  1     E -> K. VAR_040597 
MUTAGEN   49    49        K->A: Loss of activity. 
MUTAGEN   177   177        T->A: Loss of activation by CaMKK1. 
MUTAGEN   177   177        T->D: Partial activation in absence of CAMKK1. 
Sequence information
Length: 370 AA [This is the length of the unprocessed precursor] Molecular weight: 41337 Da [This is the MW of the unprocessed precursor] CRC64: 57FA20ECE00FA76C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLGAVEGPRW KQAEDIRDIY DFRDVLGTGA FSEVILAEDK RTQKLVAIKC IAKEALEGKE 

        70         80         90        100        110        120 
GSMENEIAVL HKIKHPNIVA LDDIYESGGH LYLIMQLVSG GELFDRIVEK GFYTERDASR 

       130        140        150        160        170        180 
LIFQVLDAVK YLHDLGIVHR DLKPENLLYY SLDEDSKIMI SDFGLSKMED PGSVLSTACG 

       190        200        210        220        230        240 
TPGYVAPEVL AQKPYSKAVD CWSIGVIAYI LLCGYPPFYD ENDAKLFEQI LKAEYEFDSP 

       250        260        270        280        290        300 
YWDDISDSAK DFIRHLMEKD PEKRFTCEQA LQHPWIAGDT ALDKNIHQSV SEQIKKNFAK 

       310        320        330        340        350        360 
SKWKQAFNAT AVVRHMRKLQ LGTSQEGQGQ TASHGELLTP VAGGPAAGCC CRDCCVEPGT 

       370 
ELSPTLPHQL 

Q14012 in FASTA format

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