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Protein

Calcium/calmodulin-dependent protein kinase type 1G

Gene

CAMK1G

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

Functioni

Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade. In vitro phosphorylates transcription factor CREB1 (By similarity).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by Ca2+/calmodulin. Binding of calmodulin is thought to result in a conformational change and leads to activation through phosphorylation by CAMKK1 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei52 – 521ATPPROSITE-ProRule annotation
Active sitei143 – 1431Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi29 – 379ATPPROSITE-ProRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.17. 2681.
SignaLinkiQ96NX5.
SIGNORiQ96NX5.

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium/calmodulin-dependent protein kinase type 1G (EC:2.7.11.17)
Alternative name(s):
CaM kinase I gamma
Short name:
CaM kinase IG
Short name:
CaM-KI gamma
Short name:
CaMKI gamma
Short name:
CaMKIG
CaMK-like CREB kinase III
Short name:
CLICK III
Gene namesi
Name:CAMK1G
Synonyms:CLICK3, VWS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:14585. CAMK1G.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26049.

Chemistry

ChEMBLiCHEMBL5258.
GuidetoPHARMACOLOGYi1954.

Polymorphism and mutation databases

BioMutaiCAMK1G.
DMDMi73620970.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 476476Calcium/calmodulin-dependent protein kinase type 1GPRO_0000086084Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei121 – 1211PhosphoserineBy similarity
Modified residuei178 – 1781PhosphothreonineBy similarity

Post-translational modificationi

May be prenylated on Cys-473.By similarity

Keywords - PTMi

Lipoprotein, Phosphoprotein, Prenylation

Proteomic databases

PaxDbiQ96NX5.
PRIDEiQ96NX5.

PTM databases

iPTMnetiQ96NX5.
PhosphoSiteiQ96NX5.

Expressioni

Tissue specificityi

Mainly expressed in brain with small amounts in skeletal muscles, kidney, spleen and liver. Strongly expressed in forebrain neocortex, striatum and limbic system.1 Publication

Gene expression databases

BgeeiQ96NX5.
CleanExiHS_CAMK1G.
ExpressionAtlasiQ96NX5. baseline and differential.
GenevisibleiQ96NX5. HS.

Organism-specific databases

HPAiHPA023809.

Interactioni

Protein-protein interaction databases

BioGridi121424. 6 interactions.
IntActiQ96NX5. 2 interactions.
STRINGi9606.ENSP00000009105.

Chemistry

BindingDBiQ96NX5.

Structurei

Secondary structure

1
476
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi19 – 224Combined sources
Beta strandi23 – 319Combined sources
Beta strandi33 – 4210Combined sources
Turni43 – 453Combined sources
Beta strandi48 – 558Combined sources
Helixi64 – 7411Combined sources
Beta strandi83 – 886Combined sources
Beta strandi90 – 978Combined sources
Helixi105 – 1128Combined sources
Helixi117 – 13620Combined sources
Helixi146 – 1483Combined sources
Beta strandi150 – 1556Combined sources
Beta strandi160 – 1623Combined sources
Helixi177 – 1804Combined sources
Turni188 – 1903Combined sources
Beta strandi191 – 1933Combined sources
Helixi198 – 21417Combined sources
Turni218 – 2214Combined sources
Helixi224 – 23310Combined sources
Turni240 – 2456Combined sources
Helixi248 – 25811Combined sources
Turni262 – 2643Combined sources
Helixi268 – 2725Combined sources
Helixi275 – 2784Combined sources
Helixi288 – 29811Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JAMX-ray1.70A/B18-316[»]
ProteinModelPortaliQ96NX5.
SMRiQ96NX5. Positions 16-301.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96NX5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 277255Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni277 – 31741Autoinhibitory domainBy similarityAdd
BLAST
Regioni297 – 31822Calmodulin-bindingBy similarityAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0032. Eukaryota.
ENOG410XRMJ. LUCA.
GeneTreeiENSGT00760000118944.
HOGENOMiHOG000233016.
HOVERGENiHBG108055.
InParanoidiQ96NX5.
KOiK08794.
OMAiMVPVKTS.
OrthoDBiEOG7WHH9K.
PhylomeDBiQ96NX5.
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.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96NX5-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGRKEEDDCS SWKKQTTNIR KTFIFMEVLG SGAFSEVFLV KQRLTGKLFA
60 70 80 90 100
LKCIKKSPAF RDSSLENEIA VLKKIKHENI VTLEDIYEST THYYLVMQLV
110 120 130 140 150
SGGELFDRIL ERGVYTEKDA SLVIQQVLSA VKYLHENGIV HRDLKPENLL
160 170 180 190 200
YLTPEENSKI MITDFGLSKM EQNGIMSTAC GTPGYVAPEV LAQKPYSKAV
210 220 230 240 250
DCWSIGVITY ILLCGYPPFY EETESKLFEK IKEGYYEFES PFWDDISESA
260 270 280 290 300
KDFICHLLEK DPNERYTCEK ALSHPWIDGN TALHRDIYPS VSLQIQKNFA
310 320 330 340 350
KSKWRQAFNA AAVVHHMRKL HMNLHSPGVR PEVENRPPET QASETSRPSS
360 370 380 390 400
PEITITEAPV LDHSVALPAL TQLPCQHGRR PTAPGGRSLN CLVNGSLHIS
410 420 430 440 450
SSLVPMHQGS LAAGPCGCCS SCLNIGSKGK SSYCSEPTLL KKANKKQNFK
460 470
SEVMVPVKAS GSSHCRAGQT GVCLIM
Length:476
Mass (Da):53,087
Last modified:August 16, 2005 - v3
Checksum:iDD009D9CF2FE3CBE
GO
Isoform 2 (identifier: Q96NX5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     448-476: NFKSEVMVPVKASGSSHCRAGQTGVCLIM → YVFLAKDGAPAWV

Show »
Length:460
Mass (Da):51,486
Checksum:iA16971DC50344496
GO

Sequence cautioni

The sequence CAB41259.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti427 – 4271S → N in AAL28100 (PubMed:10645953).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti259 – 2591E → Q.1 Publication
Corresponds to variant rs35561962 [ dbSNP | Ensembl ].
VAR_040600
Natural varianti329 – 3291V → I.2 Publications
Corresponds to variant rs11119315 [ dbSNP | Ensembl ].
VAR_020530
Natural varianti443 – 4431A → T in a breast infiltrating ductal carcinoma sample; somatic mutation. 1 Publication
VAR_040601

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei448 – 47629NFKSE…VCLIM → YVFLAKDGAPAWV in isoform 2. 1 PublicationVSP_012138Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF428261 mRNA. Translation: AAL28100.1.
AY212935 mRNA. Translation: AAP29964.1.
AL049688 mRNA. Translation: CAB41259.1. Different initiation.
AL023754 Genomic DNA. Translation: CAI19991.1.
BC032787 mRNA. Translation: AAH32787.1.
CCDSiCCDS1486.1. [Q96NX5-1]
RefSeqiNP_065172.1. NM_020439.2. [Q96NX5-1]
UniGeneiHs.199068.

Genome annotation databases

EnsembliENST00000009105; ENSP00000009105; ENSG00000008118. [Q96NX5-1]
ENST00000361322; ENSP00000354861; ENSG00000008118. [Q96NX5-1]
GeneIDi57172.
KEGGihsa:57172.
UCSCiuc001hhd.4. human. [Q96NX5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF428261 mRNA. Translation: AAL28100.1.
AY212935 mRNA. Translation: AAP29964.1.
AL049688 mRNA. Translation: CAB41259.1. Different initiation.
AL023754 Genomic DNA. Translation: CAI19991.1.
BC032787 mRNA. Translation: AAH32787.1.
CCDSiCCDS1486.1. [Q96NX5-1]
RefSeqiNP_065172.1. NM_020439.2. [Q96NX5-1]
UniGeneiHs.199068.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JAMX-ray1.70A/B18-316[»]
ProteinModelPortaliQ96NX5.
SMRiQ96NX5. Positions 16-301.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121424. 6 interactions.
IntActiQ96NX5. 2 interactions.
STRINGi9606.ENSP00000009105.

Chemistry

BindingDBiQ96NX5.
ChEMBLiCHEMBL5258.
GuidetoPHARMACOLOGYi1954.

PTM databases

iPTMnetiQ96NX5.
PhosphoSiteiQ96NX5.

Polymorphism and mutation databases

BioMutaiCAMK1G.
DMDMi73620970.

Proteomic databases

PaxDbiQ96NX5.
PRIDEiQ96NX5.

Protocols and materials databases

DNASUi57172.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000009105; ENSP00000009105; ENSG00000008118. [Q96NX5-1]
ENST00000361322; ENSP00000354861; ENSG00000008118. [Q96NX5-1]
GeneIDi57172.
KEGGihsa:57172.
UCSCiuc001hhd.4. human. [Q96NX5-1]

Organism-specific databases

CTDi57172.
GeneCardsiCAMK1G.
HGNCiHGNC:14585. CAMK1G.
HPAiHPA023809.
MIMi614994. gene.
neXtProtiNX_Q96NX5.
PharmGKBiPA26049.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0032. Eukaryota.
ENOG410XRMJ. LUCA.
GeneTreeiENSGT00760000118944.
HOGENOMiHOG000233016.
HOVERGENiHBG108055.
InParanoidiQ96NX5.
KOiK08794.
OMAiMVPVKTS.
OrthoDBiEOG7WHH9K.
PhylomeDBiQ96NX5.
TreeFamiTF314166.

Enzyme and pathway databases

BRENDAi2.7.11.17. 2681.
SignaLinkiQ96NX5.
SIGNORiQ96NX5.

Miscellaneous databases

EvolutionaryTraceiQ96NX5.
GenomeRNAii57172.
PROiQ96NX5.
SOURCEiSearch...

Gene expression databases

BgeeiQ96NX5.
CleanExiHS_CAMK1G.
ExpressionAtlasiQ96NX5. baseline and differential.
GenevisibleiQ96NX5. HS.

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.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A preliminary gene map for the Van der Woude syndrome critical region derived from 900 kb of genomic sequence at 1q32-q41."
    Schutte B.C., Bjork B.C., Coppage K.B., Malik M.I., Gregory S.G., Scott D.J., Brentzell L.M., Watanabe Y., Dixon M.J., Murray J.C.
    Genome Res. 10:81-94(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ILE-329.
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
  3. Rhodes S.
    Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1).
  6. "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] GLN-259; ILE-329 AND THR-443.

Entry informationi

Entry nameiKCC1G_HUMAN
AccessioniPrimary (citable) accession number: Q96NX5
Secondary accession number(s): Q86UH5, Q9Y3J7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: August 16, 2005
Last modified: June 8, 2016
This is version 139 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.