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Protein

Calcium/calmodulin-dependent protein kinase type IV

Gene

Camk4

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Isoform 1: Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK4 signaling cascade and regulates, mainly by phosphorylation, the activity of several transcription activators, such as CREB1, MEF2D, JUN and RORA, which play pivotal roles in immune response, inflammation, and memory consolidation. In the thymus, regulates the CD4+/CD8+ double positive thymocytes selection threshold during T-cell ontogeny. In CD4 memory T-cells, is required to link T-cell antigen receptor (TCR) signaling to the production of IL2, IFNG and IL4 (through the regulation of CREB and MEF2). Regulates the differentiation and survival phases of osteoclasts and dendritic cells (DCs). Mediates DCs survival by linking TLR4 and the regulation of temporal expression of BCL2. Phosphorylates the transcription activator CREB1 on 'Ser-133' in hippocampal neuron nuclei and contribute to memory consolidation and long term potentiation (LTP) in the hippocampus. Can activate the MAP kinases MAPK1/ERK2, MAPK8/JNK1 and MAPK14/p38 and stimulate transcription through the phosphorylation of ELK1 and ATF2. Can also phosphorylate in vitro CREBBP, PRM2, MEF2A and STMN1/OP18 (By similarity).By similarity
Isoform 2: Heat-stable, acidic, calmodulin-binding protein.3 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-196 within the activation loop by CaMKK1 or CaMKK2. Phosphorylation of Thr-196 results in a 10-20-fold increase in total activity to generate Ca2+/calmodulin-independent activity. Autophosphorylation of the N-terminus Ser-11 and Ser-12 is required for full activation. Inactivated by protein phosphatase 2A (PPP2CA/PPP2CB) which dephosphorylates Thr-196, thereby terminating autonomous activity and helping to maintain the enzyme in its autoinhibited state (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei71 – 711ATPPROSITE-ProRule annotation
Active sitei160 – 1601Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi48 – 569ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calmodulin-dependent protein kinase activity Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Adaptive immunity, Immunity, Inflammatory response

Keywords - Ligandi

ATP-binding, Calcium, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.17. 5301.
ReactomeiR-RNO-111932. CaMK IV-mediated phosphorylation of CREB.
R-RNO-442717. CREB phosphorylation through the activation of CaMKK.
R-RNO-442745. Activation of CaMK IV.

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium/calmodulin-dependent protein kinase type IV (EC:2.7.11.17)
Short name:
CaMK IV
Alternative name(s):
CaM kinase-GR
Calspermin
Gene namesi
Name:Camk4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 18

Organism-specific databases

RGDi2264. Camk4.

Subcellular locationi

  • Cytoplasm
  • Nucleus

  • Note: Localized in hippocampal neuron nuclei. In spermatids, associated with chromatin and nuclear matrix.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi71 – 711K → M: Loss of kinase activity; confers cytoplasmic localization. 1 Publication
Mutagenesisi196 – 1961T → A: Loss of kinase activity; confers nuclear localization. 2 Publications
Mutagenesisi207 – 2071E → K: Loss of kinase activity; confers nuclear localization. 1 Publication
Mutagenesisi305 – 3084HMDT → DEDD: Increases Ca(2+)/calmodulin-independent activity. 1 Publication
Mutagenesisi316 – 3172FN → DD: Increases Ca(2+)/calmodulin-independent activity. 1 Publication
Mutagenesisi332 – 3321S → A: No decrease in Ca(2+)/calmodulin-dependent activity after activation by CaMKKs. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 474474Calcium/calmodulin-dependent protein kinase type IVPRO_0000086108Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei11 – 111Phosphoserine; by autocatalysisBy similarity
Modified residuei12 – 121Phosphoserine; by autocatalysisBy similarity
Glycosylationi53 – 531O-linked (GlcNAc)By similarity
Glycosylationi54 – 541O-linked (GlcNAc)By similarity
Glycosylationi133 – 1331O-linked (GlcNAc)By similarity
Glycosylationi185 – 1851O-linked (GlcNAc)By similarity
Modified residuei196 – 1961Phosphothreonine; by CaMKK1 and CaMKK2By similarity
Modified residuei332 – 3321Phosphoserine; by autocatalysis1 Publication
Modified residuei337 – 3371PhosphoserineCombined sources
Glycosylationi340 – 3401O-linked (GlcNAc)By similarity
Glycosylationi341 – 3411O-linked (GlcNAc)By similarity
Glycosylationi352 – 3521O-linked (GlcNAc)By similarity
Modified residuei437 – 4371PhosphoserineCombined sources
Modified residuei443 – 4431PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated by CaMKK1 and CaMKK2 on Thr-196. Dephosphorylated by protein phosphatase 2A. Autophosphorylated on Ser-11 and Ser-12 (By similarity).By similarity
Glycosylation at Ser-185 modulates the phosphorylation of CaMK4 at Thr-196 and negatively regulates its activity toward CREB1 in basal conditions and during early inomycin stimulation.By similarity
The N-terminus of calspermin is blocked.

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP13234.
PRIDEiP13234.

PTM databases

iPTMnetiP13234.
PhosphoSiteiP13234.

Expressioni

Tissue specificityi

Isoform 1 is expressed in brain and isoform 2 is testis specific.

Gene expression databases

GenevisibleiP13234. RN.

Interactioni

Subunit structurei

Monomer. Interacts with protein phosphatase 2A (PPP2CA/PPP2CB); the interaction is mutually exclusive with binding to Ca2+/calmodulin.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027771.

Structurei

3D structure databases

ProteinModelPortaliP13234.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 296255Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni297 – 33640Autoinhibitory domainAdd
BLAST
Regioni302 – 31918PP2A-bindingBy similarityAdd
BLAST
Regioni318 – 33720Calmodulin-bindingSequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi393 – 3997Poly-Glu
Compositional biasi403 – 41311Poly-GluAdd
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.
InParanoidiP13234.
KOiK05869.
OMAiWIDGSNK.
OrthoDBiEOG764732.
PhylomeDBiP13234.
TreeFamiTF351230.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
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 promoter usage and alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P13234-1) [UniParc]FASTAAdd to basket

Also known as: Calcium-calmodulin-dependent protein kinase type IV, Beta

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
MLKVTVPSCP SSPCSSVTSS TENLVPDYWI DGSKRDPLSD FFEVESELGR
60 70 80 90 100
GATSIVYRCK QKGTQKPYAL KVLKKTVDKK IVRTEIGVLL RLSHPNIIKL
110 120 130 140 150
KEIFETPTEI SLVLELVTGG ELFDRIVEKG YYSERDAADA VKQILEAVAY
160 170 180 190 200
LHENGIVHRD LKPENLLYAT PAPDAPLKIA DFGLSKIVEH QVLMKTVCGT
210 220 230 240 250
PGYCAPEILR GCAYGPEVDM WSVGIITYIL LCGFEPFYDE RGDQFMFRRI
260 270 280 290 300
LNCEYYFISP WWDEVSLNAK DLVKKLIVLD PKKRLTTFQA LQHPWVTGKA
310 320 330 340 350
ANFVHMDTAQ KKLQEFNARR KLKAAVKAVV ASSRLGSASS SHTNIQESNK
360 370 380 390 400
ASSEAQPAQD GKDKTDPLEN KMQAGDHEAA KAAADETMKL QSEEVEEEEG
410 420 430 440 450
VKEEEEEEEE EEETSRMVPQ EPEDRLETDD QEMKRNSEET LKSVEEEMDP
460 470
KAEEEAAAVG LGVPPQQDAI LPEY
Length:474
Mass (Da):53,151
Last modified:February 1, 2005 - v3
Checksum:iE7B20E942419EB89
GO
Isoform 2 (identifier: P13234-2) [UniParc]FASTAAdd to basket

Also known as: Calspermin, Testis-specific

The sequence of this isoform differs from the canonical sequence as follows:
     1-305: Missing.

Show »
Length:169
Mass (Da):18,732
Checksum:i4E4EBE821D179CA2
GO

Sequence cautioni

The sequence AAB28372.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti142 – 1432KQ → NE in AAA40845 (PubMed:1648230).Curated
Sequence conflicti372 – 3721M → I in AAA40845 (PubMed:1648230).Curated
Sequence conflicti372 – 3721M → I in AAA40865 (PubMed:1648230).Curated
Sequence conflicti372 – 3721M → I in AAA41867 (PubMed:2538431).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 305305Missing in isoform 2. 2 PublicationsVSP_004789Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63334 mRNA. Translation: AAA40865.1.
M74488 Genomic DNA. Translation: AAA40845.1.
M64757 mRNA. Translation: AAA40856.1.
M64757 mRNA. Translation: AAA40857.1.
S65840 mRNA. Translation: AAB28372.1. Different initiation.
BC128706 mRNA. Translation: AAI28707.1.
J04600 mRNA. Translation: AAA41867.1.
J04446 mRNA. Translation: AAA40990.1.
PIRiA41103. TVRTC4.
I52637.
RefSeqiNP_036859.2. NM_012727.3. [P13234-1]
UniGeneiRn.11046.

Genome annotation databases

EnsembliENSRNOT00000027771; ENSRNOP00000027771; ENSRNOG00000020478. [P13234-1]
ENSRNOT00000078822; ENSRNOP00000072926; ENSRNOG00000020478. [P13234-2]
GeneIDi25050.
KEGGirno:25050.
UCSCiRGD:2264. rat. [P13234-1]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63334 mRNA. Translation: AAA40865.1.
M74488 Genomic DNA. Translation: AAA40845.1.
M64757 mRNA. Translation: AAA40856.1.
M64757 mRNA. Translation: AAA40857.1.
S65840 mRNA. Translation: AAB28372.1. Different initiation.
BC128706 mRNA. Translation: AAI28707.1.
J04600 mRNA. Translation: AAA41867.1.
J04446 mRNA. Translation: AAA40990.1.
PIRiA41103. TVRTC4.
I52637.
RefSeqiNP_036859.2. NM_012727.3. [P13234-1]
UniGeneiRn.11046.

3D structure databases

ProteinModelPortaliP13234.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027771.

PTM databases

iPTMnetiP13234.
PhosphoSiteiP13234.

Proteomic databases

PaxDbiP13234.
PRIDEiP13234.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000027771; ENSRNOP00000027771; ENSRNOG00000020478. [P13234-1]
ENSRNOT00000078822; ENSRNOP00000072926; ENSRNOG00000020478. [P13234-2]
GeneIDi25050.
KEGGirno:25050.
UCSCiRGD:2264. rat. [P13234-1]

Organism-specific databases

CTDi814.
RGDi2264. Camk4.

Phylogenomic databases

eggNOGiKOG0032. Eukaryota.
ENOG410XRMJ. LUCA.
GeneTreeiENSGT00760000118944.
HOGENOMiHOG000233016.
HOVERGENiHBG108055.
InParanoidiP13234.
KOiK05869.
OMAiWIDGSNK.
OrthoDBiEOG764732.
PhylomeDBiP13234.
TreeFamiTF351230.

Enzyme and pathway databases

BRENDAi2.7.11.17. 5301.
ReactomeiR-RNO-111932. CaMK IV-mediated phosphorylation of CREB.
R-RNO-442717. CREB phosphorylation through the activation of CaMKK.
R-RNO-442745. Activation of CaMK IV.

Miscellaneous databases

PROiP13234.

Gene expression databases

GenevisibleiP13234. RN.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
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. "Relationship of genes encoding Ca2+/calmodulin-dependent protein kinase Gr and calspermin: a gene within a gene."
    Ohmstede C.-A., Bland M.M., Merrill B.M., Sahyoun N.
    Proc. Natl. Acad. Sci. U.S.A. 88:5784-5788(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 437-474, PARTIAL PROTEIN SEQUENCE, ALTERNATIVE SPLICING.
  2. "A novel Ca2+/calmodulin-dependent protein kinase and a male germ cell-specific calmodulin-binding protein are derived from the same gene."
    Means A.R., Cruzalegui F., Lemagueresse B., Needleman D.S., Slaughter G.R., Ono T.
    Mol. Cell. Biol. 11:3960-3971(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  3. "Cloning and sequencing of a gene encoding the beta polypeptide of Ca2+/calmodulin-dependent protein kinase IV and its expression confined to the mature cerebellar granule cells."
    Sakagami H., Kondo H.
    Brain Res. Mol. Brain Res. 19:215-218(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Organization and analysis of the complete rat calmodulin-dependent protein kinase IV gene."
    Sun Z., Means R.L., LeMagueresse B., Means A.R.
    J. Biol. Chem. 270:29507-29514(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [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).
    Tissue: Testis.
  6. "Ca2+/calmodulin-dependent protein kinase enriched in cerebellar granule cells. Identification of a novel neuronal calmodulin-dependent protein kinase."
    Ohmstede C.-A., Jenson K.F., Sahyoun N.
    J. Biol. Chem. 264:5866-5875(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 250-474 (ISOFORM 1).
    Strain: Sprague-Dawley.
    Tissue: Brain.
  7. "Molecular cloning sequence and distribution of rat calspermin, a high affinity calmodulin-binding protein."
    Ono T., Slaughter G.R., Cook R.G., Means A.R.
    J. Biol. Chem. 264:2081-2087(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 306-474 (ISOFORM 2), PROTEIN SEQUENCE OF 335-361.
    Strain: Sprague-Dawley.
  8. "CREB: a Ca(2+)-regulated transcription factor phosphorylated by calmodulin-dependent kinases."
    Sheng M., Thompson M.A., Greenberg M.E.
    Science 252:1427-1430(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CREB1.
  9. "Activation mechanisms for Ca2+/calmodulin-dependent protein kinase IV. Identification of a brain CaM-kinase IV kinase."
    Tokumitsu H., Brickey D.A., Glod J., Hidaka H., Sikela J., Soderling T.R.
    J. Biol. Chem. 269:28640-28647(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, SUBUNIT, MUTAGENESIS OF 305-HIS--THR-308 AND 316-PHE-ASN-317.
  10. "Calcium/calmodulin-dependent protein kinase types II and IV differentially regulate CREB-dependent gene expression."
    Matthews R.P., Guthrie C.R., Wailes L.M., Zhao X., Means A.R., McKnight G.S.
    Mol. Cell. Biol. 14:6107-6116(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CREB1, SUBCELLULAR LOCATION.
  11. "Full activation of brain calmodulin-dependent protein kinase IV requires phosphorylation of the amino-terminal serine-rich region by calmodulin-dependent protein kinase IV kinase."
    Okuno S., Kitani T., Fujisawa H.
    J. Biochem. 117:686-690(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, PHOSPHORYLATION.
  12. "Phosphorylation and activation of Ca(2+)-calmodulin-dependent protein kinase IV by Ca(2+)-calmodulin-dependent protein kinase Ia kinase. Phosphorylation of threonine 196 is essential for activation."
    Selbert M.A., Anderson K.A., Huang Q.H., Goldstein E.G., Means A.R., Edelman A.M.
    J. Biol. Chem. 270:17616-17621(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, PHOSPHORYLATION AT THR-196, MUTAGENESIS OF THR-196.
  13. "Regulation of activating transcription factor-1 and the cAMP response element-binding protein by Ca2+/calmodulin-dependent protein kinases type I, II, and IV."
    Sun P., Lou L., Maurer R.A.
    J. Biol. Chem. 271:3066-3073(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF ATF1 AND CREB1.
  14. "Inactivation of calmodulin-dependent protein kinase IV by autophosphorylation of serine 332 within the putative calmodulin-binding domain."
    Watanabe S., Okuno S., Kitani T., Fujisawa H.
    J. Biol. Chem. 271:6903-6910(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, PHOSPHORYLATION AT SER-332, MUTAGENESIS OF SER-332.
  15. "Multiple Ca(2+)-calmodulin-dependent protein kinase kinases from rat brain. Purification, regulation by Ca(2+)-calmodulin, and partial amino acid sequence."
    Edelman A.M., Mitchelhill K.I., Selbert M.A., Anderson K.A., Hook S.S., Stapleton D., Goldstein E.G., Means A.R., Kemp B.E.
    J. Biol. Chem. 271:10806-10810(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CAMKK1 AND CAMKK2.
  16. "Components of a calmodulin-dependent protein kinase cascade. Molecular cloning, functional characterization and cellular localization of Ca2+/calmodulin-dependent protein kinase kinase beta."
    Anderson K.A., Means R.L., Huang Q.-H., Kemp B.E., Goldstein E.G., Selbert M.A., Edelman A.M., Fremeau R.T., Means A.R.
    J. Biol. Chem. 273:31880-31889(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CAMKK2.
  17. "A signaling complex of Ca2+-calmodulin-dependent protein kinase IV and protein phosphatase 2A."
    Westphal R.S., Anderson K.A., Means A.R., Wadzinski B.E.
    Science 280:1258-1261(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SERINE/THREONINE PROTEIN PHOSPHATASE 2A, DEPHOSPHORYLATION.
  18. "Substrate recognition by Ca2+/Calmodulin-dependent protein kinase kinase. Role of the arg-pro-rich insert domain."
    Tokumitsu H., Takahashi N., Eto K., Yano S., Soderling T.R., Muramatsu M.-A.
    J. Biol. Chem. 274:15803-15810(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CAMKK1.
  19. "Catalytic activity is required for calcium/calmodulin-dependent protein kinase IV to enter the nucleus."
    Lemrow S.M., Anderson K.A., Joseph J.D., Ribar T.J., Noeldner P.K., Means A.R.
    J. Biol. Chem. 279:11664-11671(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-71; THR-196 AND GLU-207.
  20. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337; SER-437 AND SER-443, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKCC4_RAT
AccessioniPrimary (citable) accession number: P13234
Secondary accession number(s): A1A5L5, Q63892
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: February 1, 2005
Last modified: June 8, 2016
This is version 156 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.