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Q14012

- KCC1A_HUMAN

UniProt

Q14012 - KCC1A_HUMAN

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Protein

Calcium/calmodulin-dependent protein kinase type 1

Gene

CAMK1

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

Functioni

Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK1 signaling cascade and, upon calcium influx, regulates transcription activators activity, cell cycle, hormone production, cell differentiation, actin filament organization and neurite outgrowth. Recognizes the substrate consensus sequence [MVLIF]-x-R-x(2)-[ST]-x(3)-[MVLIF]. Regulates axonal extension and growth cone motility in hippocampal and cerebellar nerve cells. Upon NMDA receptor-mediated Ca2+ elevation, promotes dendritic growth in hippocampal neurons and is essential in synapses for full long-term potentiation (LTP) and ERK2-dependent translational activation. Downstream of NMDA receptors, promotes the formation of spines and synapses in hippocampal neurons by phosphorylating ARHGEF7/BETAPIX on 'Ser-694', which results in the enhancement of ARHGEF7 activity and activation of RAC1. Promotes neuronal differentiation and neurite outgrowth by activation and phosphorylation of MARK2 on 'Ser-91', 'Ser-92', 'Ser-93' and 'Ser-294'. Promotes nuclear export of HDAC5 and binding to 14-3-3 by phosphorylation of 'Ser-259' and 'Ser-498' in the regulation of muscle cell differentiation. Regulates NUMB-mediated endocytosis by phosphorylation of NUMB on 'Ser-276' and 'Ser-295'. Involved in the regulation of basal and estrogen-stimulated migration of medulloblastoma cells through ARHGEF7/BETAPIX phosphorylation (By similarity). Is required for proper activation of cyclin-D1/CDK4 complex during G1 progression in diploid fibroblasts. Plays a role in K+ and ANG2-mediated regulation of the aldosterone synthase (CYP11B2) to produce aldosterone in the adrenal cortex. Phosphorylates EIF4G3/eIF4GII. In vitro phosphorylates CREB1, ATF1, CFTR, MYL9 and SYN1/synapsin I.By similarity8 Publications

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 phosphorylation of Thr-177 within the activation loop by CaMKK1 or CaMKK2. Phosphorylation of Thr-177 results in several fold increase in total activity. Unlike CaMK4, is unable to exhibit autonomous activity after Ca2+/calmodulin activation.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei49 – 491ATP
Active sitei141 – 1411Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 349ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calmodulin-dependent protein kinase activity Source: UniProtKB

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. nucleocytoplasmic transport Source: Ensembl
  3. positive regulation of dendritic spine development Source: UniProtKB
  4. positive regulation of muscle cell differentiation Source: BHF-UCL
  5. positive regulation of neuron projection development Source: UniProtKB
  6. positive regulation of protein export from nucleus Source: Ensembl
  7. positive regulation of protein serine/threonine kinase activity Source: UniProtKB
  8. positive regulation of synapse structural plasticity Source: UniProtKB
  9. protein phosphorylation Source: UniProtKB
  10. regulation of muscle cell differentiation Source: UniProtKB
  11. regulation of protein binding Source: UniProtKB
  12. regulation of protein localization Source: UniProtKB
  13. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Biological processi

Cell cycle, Differentiation, Neurogenesis

Keywords - Ligandi

ATP-binding, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.17. 2681.
SignaLinkiQ14012.

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium/calmodulin-dependent protein kinase type 1 (EC:2.7.11.17)
Alternative name(s):
CaM kinase I
Short name:
CaM-KI
CaM kinase I alpha
Short name:
CaMKI-alpha
Gene namesi
Name:CAMK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:1459. CAMK1.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity
Note: Predominantly cytoplasmic.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi49 – 491K → A: Catalytically inactive form; prevents CDK4 activation. 2 Publications
Mutagenesisi177 – 1771T → A: Loss of activation by CaMKK1. 1 Publication
Mutagenesisi177 – 1771T → D: Partial activation in absence of CaMKK1. 1 Publication

Organism-specific databases

PharmGKBiPA26048.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 370370Calcium/calmodulin-dependent protein kinase type 1PRO_0000086076Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki59 – 59Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei177 – 1771Phosphothreonine; by CaMKK1 and CaMKK21 Publication

Post-translational modificationi

Phosphorylated by CaMKK1 and CaMKK2 on Thr-177.3 Publications
Polybiquitinated by the E3 ubiquitin-protein ligase complex SCF(FBXL12), leading to proteasomal degradation.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ14012.
PaxDbiQ14012.
PeptideAtlasiQ14012.
PRIDEiQ14012.

PTM databases

PhosphoSiteiQ14012.

Expressioni

Tissue specificityi

Widely expressed. Expressed in cells of the zona glomerulosa of the adrenal cortex.2 Publications

Gene expression databases

BgeeiQ14012.
CleanExiHS_CAMK1.
ExpressionAtlasiQ14012. baseline and differential.
GenevestigatoriQ14012.

Organism-specific databases

HPAiCAB031904.
HPA051409.

Interactioni

Subunit structurei

Monomer. Interacts with XPO1 (By similarity). Interacts with MARK2, ARHGEF7/BETAPIX and GIT1.By similarity2 Publications

Protein-protein interaction databases

BioGridi114106. 19 interactions.
DIPiDIP-41906N.
IntActiQ14012. 2 interactions.
MINTiMINT-201810.
STRINGi9606.ENSP00000256460.

Structurei

Secondary structure

1
370
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 183Combined sources
Beta strandi20 – 2910Combined sources
Beta strandi32 – 398Combined sources
Turni40 – 423Combined sources
Beta strandi45 – 528Combined sources
Helixi66 – 705Combined sources
Beta strandi81 – 866Combined sources
Beta strandi88 – 958Combined sources
Beta strandi100 – 1023Combined sources
Helixi103 – 1097Combined sources
Helixi115 – 13420Combined sources
Helixi144 – 1463Combined sources
Beta strandi147 – 1526Combined sources
Beta strandi158 – 1603Combined sources
Helixi166 – 1683Combined sources
Helixi171 – 1799Combined sources
Turni182 – 1843Combined sources
Helixi187 – 1904Combined sources
Helixi198 – 21316Combined sources
Helixi223 – 23210Combined sources
Turni239 – 2446Combined sources
Helixi247 – 25610Combined sources
Turni261 – 2633Combined sources
Helixi267 – 2726Combined sources
Helixi274 – 2774Combined sources
Helixi287 – 29711Combined sources
Helixi301 – 31111Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FG7X-ray2.70A1-293[»]
4FG8X-ray2.20A/B1-315[»]
4FG9X-ray2.40A/B1-320[»]
4FGBX-ray2.60A1-320[»]
ProteinModelPortaliQ14012.
SMRiQ14012. Positions 10-299.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 276257Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni276 – 31641Autoinhibitory domainAdd
BLAST
Regioni296 – 31722Calmodulin-bindingBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi315 – 3217Nuclear export signalBy similarity

Domaini

The autoinhibitory domain overlaps with the calmodulin binding region and interacts in the inactive folded state with the catalytic domain as a pseudosubstrate.1 Publication

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118944.
HOGENOMiHOG000233016.
HOVERGENiHBG108055.
InParanoidiQ14012.
KOiK08794.
OMAiARMYLMA.
OrthoDBiEOG7WHH9K.
PhylomeDBiQ14012.
TreeFamiTF314166.

Family and domain databases

InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
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.
PfamiPF00069. 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]

Sequencei

Sequence statusi: Complete.

Q14012-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLGAVEGPRW KQAEDIRDIY DFRDVLGTGA FSEVILAEDK RTQKLVAIKC
60 70 80 90 100
IAKEALEGKE GSMENEIAVL HKIKHPNIVA LDDIYESGGH LYLIMQLVSG
110 120 130 140 150
GELFDRIVEK GFYTERDASR LIFQVLDAVK YLHDLGIVHR DLKPENLLYY
160 170 180 190 200
SLDEDSKIMI SDFGLSKMED PGSVLSTACG TPGYVAPEVL AQKPYSKAVD
210 220 230 240 250
CWSIGVIAYI LLCGYPPFYD ENDAKLFEQI LKAEYEFDSP YWDDISDSAK
260 270 280 290 300
DFIRHLMEKD PEKRFTCEQA LQHPWIAGDT ALDKNIHQSV SEQIKKNFAK
310 320 330 340 350
SKWKQAFNAT AVVRHMRKLQ LGTSQEGQGQ TASHGELLTP VAGGPAAGCC
360 370
CRDCCVEPGT ELSPTLPHQL
Length:370
Mass (Da):41,337
Last modified:November 1, 1996 - v1
Checksum:i57FA20ECE00FA76C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti217 – 2171P → S in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_040596
Natural varianti361 – 3611E → K.1 Publication
Corresponds to variant rs56033923 [ dbSNP | Ensembl ].
VAR_040597

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L41816 mRNA. Translation: AAA99458.1.
BC106754 mRNA. Translation: AAI06755.1.
BC106755 mRNA. Translation: AAI06756.1.
CCDSiCCDS2582.1.
PIRiS57347.
RefSeqiNP_003647.1. NM_003656.4.
UniGeneiHs.434875.

Genome annotation databases

EnsembliENST00000256460; ENSP00000256460; ENSG00000134072.
GeneIDi8536.
KEGGihsa:8536.
UCSCiuc003bst.3. human.

Polymorphism databases

DMDMi3122301.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L41816 mRNA. Translation: AAA99458.1 .
BC106754 mRNA. Translation: AAI06755.1 .
BC106755 mRNA. Translation: AAI06756.1 .
CCDSi CCDS2582.1.
PIRi S57347.
RefSeqi NP_003647.1. NM_003656.4.
UniGenei Hs.434875.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4FG7 X-ray 2.70 A 1-293 [» ]
4FG8 X-ray 2.20 A/B 1-315 [» ]
4FG9 X-ray 2.40 A/B 1-320 [» ]
4FGB X-ray 2.60 A 1-320 [» ]
ProteinModelPortali Q14012.
SMRi Q14012. Positions 10-299.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114106. 19 interactions.
DIPi DIP-41906N.
IntActi Q14012. 2 interactions.
MINTi MINT-201810.
STRINGi 9606.ENSP00000256460.

Chemistry

BindingDBi Q14012.
ChEMBLi CHEMBL2493.
GuidetoPHARMACOLOGYi 1952.

PTM databases

PhosphoSitei Q14012.

Polymorphism databases

DMDMi 3122301.

Proteomic databases

MaxQBi Q14012.
PaxDbi Q14012.
PeptideAtlasi Q14012.
PRIDEi Q14012.

Protocols and materials databases

DNASUi 8536.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000256460 ; ENSP00000256460 ; ENSG00000134072 .
GeneIDi 8536.
KEGGi hsa:8536.
UCSCi uc003bst.3. human.

Organism-specific databases

CTDi 8536.
GeneCardsi GC03M009774.
HGNCi HGNC:1459. CAMK1.
HPAi CAB031904.
HPA051409.
MIMi 604998. gene.
neXtProti NX_Q14012.
PharmGKBi PA26048.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118944.
HOGENOMi HOG000233016.
HOVERGENi HBG108055.
InParanoidi Q14012.
KOi K08794.
OMAi ARMYLMA.
OrthoDBi EOG7WHH9K.
PhylomeDBi Q14012.
TreeFami TF314166.

Enzyme and pathway databases

BRENDAi 2.7.11.17. 2681.
SignaLinki Q14012.

Miscellaneous databases

GeneWikii CAMK1.
GenomeRNAii 8536.
NextBioi 31972.
PROi Q14012.
SOURCEi Search...

Gene expression databases

Bgeei Q14012.
CleanExi HS_CAMK1.
ExpressionAtlasi Q14012. baseline and differential.
Genevestigatori Q14012.

Family and domain databases

InterProi IPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
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 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. "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."
    Haribabu B., Hook S.S., Selbert M.A., Goldstein E.G., Tomhave E.D., Edelman A.M., Snyderman R., Means A.R.
    EMBO J. 14:3679-3686(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT THR-177, MUTAGENESIS OF LYS-49 AND THR-177, ENZYME REGULATION.
  2. "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].
  3. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-9.
    Tissue: Platelet.
  4. "Cloning, expression and chromosomal localization of human Ca2+/calmodulin-dependent protein kinase kinase."
    Hsu L.-S., Tsou A.-P., Chi C.-W., Lee C.-H., Chen J.-Y.
    J. Biomed. Sci. 5:141-149(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CAMKK1.
  5. "Activation of the myocyte enhancer factor-2 transcription factor by calcium/calmodulin-dependent protein kinase-stimulated binding of 14-3-3 to histone deacetylase 5."
    McKinsey T.A., Zhang C.-L., Olson E.N.
    Proc. Natl. Acad. Sci. U.S.A. 97:14400-14405(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF HDAC5.
  6. "Human Ca2+/calmodulin-dependent protein kinase kinase beta gene encodes multiple isoforms that display distinct kinase activity."
    Hsu L.-S., Chen G.-D., Lee L.-S., Chi C.-W., Cheng J.-F., Chen J.-Y.
    J. Biol. Chem. 276:31113-31123(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CAMKK2.
  7. "Calmodulin-dependent kinase I regulates adrenal cell expression of aldosterone synthase."
    Condon J.C., Pezzi V., Drummond B.M., Yin S., Rainey W.E.
    Endocrinology 143:3651-3657(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  8. "Phosphorylation screening identifies translational initiation factor 4GII as an intracellular target of Ca(2+)/calmodulin-dependent protein kinase I."
    Qin H., Raught B., Sonenberg N., Goldstein E.G., Edelman A.M.
    J. Biol. Chem. 278:48570-48579(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF EIF4G3.
  9. "Regulation of cyclin D1/Cdk4 complexes by calcium/calmodulin-dependent protein kinase I."
    Kahl C.R., Means A.R.
    J. Biol. Chem. 279:15411-15419(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CYCLIN-D1/CDK4 COMPLEX, MUTAGENESIS OF LYS-49.
  10. "A calcium- and calmodulin-dependent kinase Ialpha/microtubule affinity regulating kinase 2 signaling cascade mediates calcium-dependent neurite outgrowth."
    Uboha N.V., Flajolet M., Nairn A.C., Picciotto M.R.
    J. Neurosci. 27:4413-4423(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MARK2.
  11. "Spatiotemporal expression of four isoforms of Ca2+/calmodulin-dependent protein kinase I in brain and its possible roles in hippocampal dendritic growth."
    Kamata A., Sakagami H., Tokumitsu H., Owada Y., Fukunaga K., Kondo H.
    Neurosci. Res. 57:86-97(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HIPPOCAMPAL DENDRITITE GROWTH, TISSUE SPECIFICITY.
  12. "Activity-dependent synaptogenesis: regulation by a CaM-kinase kinase/CaM-kinase I/betaPIX signaling complex."
    Saneyoshi T., Wayman G., Fortin D., Davare M., Hoshi N., Nozaki N., Natsume T., Soderling T.R.
    Neuron 57:94-107(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF ARHGEF7/BETAPIX, INTERACTION WITH ARHGEF7/BETAPIX AND GIT1.
  13. "CaMKK-CaMKI signaling pathways differentially control axon and dendrite elongation in cortical neurons."
    Neal A.P., Molina-Campos E., Marrero-Rosado B., Bradford A.B., Fox S.M., Kovalova N., Hannon H.E.
    J. Neurosci. 30:2807-2809(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN AXON ELONGATION.
  14. "Structure and regulation of calcium/calmodulin-dependent protein kinases."
    Soderling T.R., Stull J.T.
    Chem. Rev. 101:2341-2352(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  15. "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.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Controlling the cell cycle: the role of calcium/calmodulin-stimulated protein kinases I and II."
    Skelding K.A., Rostas J.A., Verrills N.M.
    Cell Cycle 10:631-639(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON INVOLVEMENT IN CELL CYCLE.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Fbxl12 triggers G1 arrest by mediating degradation of calmodulin kinase I."
    Mallampalli R.K., Kaercher L., Snavely C., Pulijala R., Chen B.B., Coon T., Zhao J., Agassandian M.
    Cell. Signal. 25:2047-2059(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-59.
  20. "Crystal structures of human CaMKIalpha reveal insights into the regulation mechanism of CaMKI."
    Zha M., Zhong C., Ou Y., Han L., Wang J., Ding J.
    PLoS ONE 7:E44828-E44828(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-315 IN COMPLEXES WITH ATP, DOMAIN, ENZYME REGULATION.
  21. "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] SER-217 AND LYS-361.

Entry informationi

Entry nameiKCC1A_HUMAN
AccessioniPrimary (citable) accession number: Q14012
Secondary accession number(s): Q3KPF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 153 of the entry and version 1 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, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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