(data stored in ACNUC26462 zone)

HOGENOM: HS3_PE196

ID   HS3_PE196                            STANDARD;      PRT;   370 AA.
AC   HS3_PE196; Q14012; Q3KPF6;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Calcium/calmodulin-dependent protein kinase type 1;
DE   EC=2.7.11 17;AltName: Full=CaM kinase I; Short=CaM-KI;AltName: Full=CaM
DE   kinase I alpha; Short=CaMKI-alpha; (HS3.PE196).
GN   Name=CAMK1;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS3.PE196.
CC       Homo sapiens chromosome 3 GRCh37  sequence 1..197962430 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:KCC1A_HUMAN
CC   -!- FUNCTION: Calcium/calmodulin-dependent protein kinase that
CC       operates in the calcium-triggered CaMKK-CaMK1 signaling cascade
CC       and, upon calcium influx, regulates transcription activators
CC       activity, cell cycle, hormone production, cell differentiation,
CC       actin filament organization and neurite outgrowth. Recognizes the
CC       substrate consensus sequence [MVLIF]-x-R-x(2)-[ST]-x(3)-[MVLIF].
CC       Regulates axonal extension and growth cone motility in hippocampal
CC       and cerebellar nerve cells. Upon NMDA receptor-mediated Ca(2+)
CC       elevation, promotes dendritic growth in hippocampal neurons and is
CC       essential in synapses for full long-term potentiation (LTP) and
CC       ERK2-dependent translational activation. Downstream of NMDA
CC       receptors, promotes the formation of spines and synapses in
CC       hippocampal neurons by phopshorylating ARHGEF7/BETAPIX on 'Ser-
CC       694', which results in the enhancement of ARHGEF7 activity and
CC       activation of RAC1. Promotes neuronal differentiation and neurite
CC       outgrowth by activation and phosphorylation of MARK2 on 'Ser-91',
CC       'Ser-92', 'Ser-93' and 'Ser-294'. Promotes nuclear export of HDAC5
CC       and binding to 14-3-3 by phosphorylation of 'Ser-259' and 'Ser-
CC       498' in the regulation of muscle cell differentiation. Regulates
CC       NUMB-mediated endocytosis by phosphorylation of NUMB on 'Ser-276'
CC       and 'Ser-295'. Involved in the regulation of basal and estrogen-
CC       stimulated migration of medulloblastoma cells through
CC       ARHGEF7/BETAPIX phosphorylation (By similarity). Is required for
CC       proper activation of cyclin-D1/CDK4 complex during G1 progression
CC       in diploid fibroblasts. Plays a role in K(+) and ANG2-mediated
CC       regulation of the aldosterone synthase (CYP11B2) to produce
CC       aldosterone in the adrenal cortex. Phosphorylates EIF4G3/eIF4GII.
CC       In vitro phosphorylates CREB1, ATF1, CFTR, MYL9, SYN1/synapsin I
CC       and SYNII/synapsin II.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Activated by Ca(2+)/calmodulin. Binding of
CC       calmodulin results in conformational change that relieves
CC       intrasteric autoinhibition and allows phosphorylation of Thr-177
CC       within the activation loop by CaMKK1 or CaMKK2. Phosphorylation of
CC       Thr-177 results in several fold increase in total activity. Unlike
CC       CaMK4, is unable to exhibit autonomous activity after
CC       Ca(2+)/calmodulin activation.
CC   -!- SUBUNIT: Monomer. Interacts with XPO1 (By similarity). Interacts
CC       with MARK2, ARHGEF7/BETAPIX and GIT1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Predominantly cytoplasmic (By similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed in cells of the
CC       zona glomerulosa of the adrenal cortex.
CC   -!- DOMAIN: The autoinhibitory domain overlaps with the calmodulin
CC       binding region and interacts in the inactive folded state with the
CC       catalytic domain as a pseudosubstrate (By similarity).
CC   -!- PTM: Phosphorylated by CaMKK1 and CaMKK2 on Thr-177.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. CaMK subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- GENE_FAMILY: HOG000233016 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000134072;ENST00000256460;ENSP00000256460.
DR   EMBL; AB451277; - ;
DR   EMBL; AB451407; - ;
DR   EMBL; AK314917; - ;
DR   EMBL; BC106754; - ;
DR   EMBL; BC106755; - ;
DR   EMBL; CH471055; - ;
DR   EMBL; EF444963; - ;
DR   EMBL; L41816; - ;
DR   UniProtKB/Swiss-Prot; Q14012; Q3KPF6; -.
DR   EMBL; L41816; AAA99458.1; -; mRNA.
DR   EMBL; BC106754; AAI06755.1; -; mRNA.
DR   EMBL; BC106755; AAI06756.1; -; mRNA.
DR   IPI; IPI00028296; -.
DR   PIR; S57347; S57347.
DR   RefSeq; NP_003647.1; NM_003656.4.
DR   UniGene; Hs.434875; -.
DR   ProteinModelPortal; Q14012; -.
DR   SMR; Q14012; 10-316.
DR   STRING; Q14012; -.
DR   PhosphoSite; Q14012; -.
DR   PeptideAtlas; Q14012; -.
DR   PRIDE; Q14012; -.
DR   Ensembl; ENST00000256460; ENSP00000256460; ENSG00000134072.
DR   GeneID; 8536; -.
DR   KEGG; hsa:8536; -.
DR   NMPDR; fig|9606.3.peg.22087; -.
DR   UCSC; uc003bst.1; human.
DR   CTD; 8536; -.
DR   GeneCards; GC03M009774; -.
DR   H-InvDB; HIX0200512; -.
DR   HGNC; HGNC:1459; CAMK1.
DR   HPA; CAB031904; -.
DR   MIM; 604998; gene.
DR   neXtProt; NX_Q14012; -.
DR   eggNOG; prNOG07976; -.
DR   GeneTree; ENSGT00600000084207; -.
DR   InParanoid; Q14012; -.
DR   OMA; RHNNIVQ; -.
DR   OrthoDB; EOG46Q6SS; -.
DR   PhylomeDB; Q14012; -.
DR   BRENDA; 2.7.11.17; 2681.
DR   NextBio; 31972; -.
DR   ArrayExpress; Q14012; -.
DR   Bgee; Q14012; -.
DR   CleanEx; HS_CAMK1; -.
DR   Genevestigator; Q14012; -.
DR   GermOnline; ENSG00000134072; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IEA:EC.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0051149; P:positive regulation of muscle cell differentiation; IMP:BHF-UCL.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   InterPro; IPR020636; Ca/CaM-dep_Ca-dep_prot_Kinase.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_kinase_dom.
DR   PANTHER; PTHR24347; PTHR24347; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   HOGENOMDNA; HS3.PE196; -.
KW   ENSG000001340721755old_1320000031; ENSP000002564607901old_1320000031;
KW   B0YIY3_HUMAN; B5BU41_HUMAN; AB451277; AB451407; AK314917; BC106754;
KW   CH471055; EF444963; L41816;
KW   Allosteric enzyme; ATP-binding; Calmodulin-binding; Cell cycle;
KW   Complete proteome; Cytoplasm; Developmental protein; Differentiation;
KW   Direct protein sequencing; Kinase; Neurogenesis; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
SQ   SEQUENCE   370 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLGAVEGPRW KQAEDIRDIY DFRDVLGTGA FSEVILAEDK RTQKLVAIKC IAKEALEGKE
     GSMENEIAVL HKIKHPNIVA LDDIYESGGH LYLIMQLVSG GELFDRIVEK GFYTERDASR
     LIFQVLDAVK YLHDLGIVHR DLKPENLLYY SLDEDSKIMI SDFGLSKMED PGSVLSTACG
     TPGYVAPEVL AQKPYSKAVD CWSIGVIAYI LLCGYPPFYD ENDAKLFEQI LKAEYEFDSP
     YWDDISDSAK DFIRHLMEKD PEKRFTCEQA LQHPWIAGDT ALDKNIHQSV SEQIKKNFAK
     SKWKQAFNAT AVVRHMRKLQ LGTSQEGQGQ TASHGELLTP VAGGPAAGCC CRDCCVEPGT
     ELSPTLPHQL
//

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