Q96NX5 (KCC1G_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	CAMK1G
Synonyms:	CLICK3, VWS1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	476 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade. In vitro phosphorylates transcription factor CREB1 By similarity.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	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.
Subcellular location	Cytoplasm By similarity. Golgi apparatus membrane; Peripheral membrane protein By similarity. Cell membrane; Peripheral membrane protein By similarity.
Tissue specificity	Mainly expressed in brain with small amounts in skeletal muscles, kidney, spleen and liver. Strongly expressed in forebrain neocortex, striatum and limbic system. Ref.2
Domain	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.
Post-translational modification	May be prenylated on Cys-473 By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily. Contains 1 protein kinase domain.
Sequence caution	The sequence CAB41259.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Calmodulin-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Lipoprotein Prenylation
Technical term	3D-structure Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell calcium- and calmodulin-dependent protein kinase complex Inferred from electronic annotation. Source: Compara neuron projection Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calmodulin-dependent protein kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q96NX5-1)

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.

Isoform 2 (identifier: Q96NX5-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 476

476

Calcium/calmodulin-dependent protein kinase type 1G

PRO_0000086084

Regions

Domain

23 – 277

255

Protein kinase

Nucleotide binding

29 – 37

9

ATP By similarity

Region

277 – 317

41

Autoinhibitory domain By similarity

Region

297 – 318

22

Calmodulin-binding By similarity

Sites

Active site

143

1

Proton acceptor By similarity

Binding site

52

1

ATP By similarity

Natural variations

Alternative sequence

448 – 476

29

NFKSE…VCLIM → YVFLAKDGAPAWV in isoform 2.

VSP_012138

Natural variant

259

1

E → Q. Ref.6
Corresponds to variant rs35561962 [ dbSNP | Ensembl ].

VAR_040600

Natural variant

329

1

V → I. Ref.1 Ref.6
Corresponds to variant rs11119315 [ dbSNP | Ensembl ].

VAR_020530

Natural variant

443

1

A → T in a breast infiltrating ductal carcinoma sample; somatic mutation. Ref.6

VAR_040601

Experimental info

Sequence conflict

427

1

S → N in AAL28100. Ref.1

Secondary structure

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476

Helix Strand Turn

Details...

Helix

19 – 22

4

Beta strand

23 – 31

9

Beta strand

33 – 42

10

Turn

43 – 45

3

Beta strand

48 – 55

8

Helix

64 – 74

11

Beta strand

83 – 88

6

Beta strand

90 – 97

8

Helix

105 – 112

8

Helix

117 – 136

20

Helix

146 – 148

3

Beta strand

150 – 155

6

Beta strand

160 – 162

3

Helix

177 – 180

4

Turn

188 – 190

3

Beta strand

191 – 193

3

Helix

198 – 214

17

Turn

218 – 221

4

Helix

224 – 233

10

Turn

240 – 245

6

Helix

248 – 258

11

Turn

262 – 264

3

Helix

268 – 272

5

Helix

275 – 278

4

Helix

288 – 298

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 16, 2005. Version 3. Checksum: DD009D9CF2FE3CBE	FASTA	476	53,087
	10 20 30 40 50 60 MGRKEEDDCS SWKKQTTNIR KTFIFMEVLG SGAFSEVFLV KQRLTGKLFA LKCIKKSPAF 70 80 90 100 110 120 RDSSLENEIA VLKKIKHENI VTLEDIYEST THYYLVMQLV SGGELFDRIL ERGVYTEKDA 130 140 150 160 170 180 SLVIQQVLSA VKYLHENGIV HRDLKPENLL YLTPEENSKI MITDFGLSKM EQNGIMSTAC 190 200 210 220 230 240 GTPGYVAPEV LAQKPYSKAV DCWSIGVITY ILLCGYPPFY EETESKLFEK IKEGYYEFES 250 260 270 280 290 300 PFWDDISESA KDFICHLLEK DPNERYTCEK ALSHPWIDGN TALHRDIYPS VSLQIQKNFA 310 320 330 340 350 360 KSKWRQAFNA AAVVHHMRKL HMNLHSPGVR PEVENRPPET QASETSRPSS PEITITEAPV 370 380 390 400 410 420 LDHSVALPAL TQLPCQHGRR PTAPGGRSLN CLVNGSLHIS SSLVPMHQGS LAAGPCGCCS 430 440 450 460 470 SCLNIGSKGK SSYCSEPTLL KKANKKQNFK SEVMVPVKAS GSSHCRAGQT GVCLIM
	Isoform 2 [UniParc]. Checksum: A16971DC50344496	FASTA	460	51,486
	10 20 30 40 50 60 MGRKEEDDCS SWKKQTTNIR KTFIFMEVLG SGAFSEVFLV KQRLTGKLFA LKCIKKSPAF 70 80 90 100 110 120 RDSSLENEIA VLKKIKHENI VTLEDIYEST THYYLVMQLV SGGELFDRIL ERGVYTEKDA 130 140 150 160 170 180 SLVIQQVLSA VKYLHENGIV HRDLKPENLL YLTPEENSKI MITDFGLSKM EQNGIMSTAC 190 200 210 220 230 240 GTPGYVAPEV LAQKPYSKAV DCWSIGVITY ILLCGYPPFY EETESKLFEK IKEGYYEFES 250 260 270 280 290 300 PFWDDISESA KDFICHLLEK DPNERYTCEK ALSHPWIDGN TALHRDIYPS VSLQIQKNFA 310 320 330 340 350 360 KSKWRQAFNA AAVVHHMRKL HMNLHSPGVR PEVENRPPET QASETSRPSS PEITITEAPV 370 380 390 400 410 420 LDHSVALPAL TQLPCQHGRR PTAPGGRSLN CLVNGSLHIS SSLVPMHQGS LAAGPCGCCS 430 440 450 460 SCLNIGSKGK SSYCSEPTLL KKANKKQYVF LAKDGAPAWV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00000026.
IPI00479272.

RefSeq

NP_065172.1. NM_020439.2.

UniGene

Hs.199068.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JAM	X-ray	1.70	A/B	18-316	[»]

ProteinModelPortal

Q96NX5.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q96NX5. 2 interactions.

STRING

9606.ENSP00000009105.

PTM databases

PhosphoSite

Q96NX5.

Polymorphism databases

DMDM

73620970.

Proteomic databases

PaxDb

Q96NX5.

PRIDE

Q96NX5.

Protocols and materials databases

DNASU

57172.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000009105; ENSP00000009105; ENSG00000008118.
ENST00000361322; ENSP00000354861; ENSG00000008118.

GeneID

57172.

KEGG

hsa:57172.

UCSC

uc001hhd.3. human.
uc001hhf.4. human.

Organism-specific databases

CTD

57172.

GeneCards

GC01P209757.

HGNC

HGNC:14585. CAMK1G.

HPA

HPA023809.

MIM

614994. gene.

neXtProt

NX_Q96NX5.

PharmGKB

PA26049.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233016.

HOVERGEN

HBG108055.

InParanoid

Q96NX5.

KO

K08794.

OMA

LPCQHSP.

OrthoDB

EOG4Q58P6.

PhylomeDB

Q96NX5.

Enzyme and pathway databases

BRENDA

2.7.11.17. 2681.

Gene expression databases

ArrayExpress

Q96NX5.

Bgee

Q96NX5.

CleanEx

HS_CAMK1G.

Genevestigator

Q96NX5.

GermOnline

ENSG00000008118. Homo sapiens.

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.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

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

BindingDB

Q96NX5.

ChEMBL

CHEMBL5258.

EvolutionaryTrace

Q96NX5.

GenomeRNAi

57172.

NextBio

63193.

SOURCE

Search...

Entry information

Entry name

KCC1G_HUMAN

Accession

Primary (citable) accession number: Q96NX5
Secondary accession number(s): Q86UH5, Q9Y3J7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 7, 2004
Last sequence update:	August 16, 2005
Last modified:	May 1, 2013
This is version 110 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.