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Protein

Dual specificity protein kinase CLK3

Gene

Clk3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Phosphorylates SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Enzyme regulationi

Leucettine L41 inhibits its kinase activity and affects the regulation of alternative splicing mediated by phosphorylation of SR proteins.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei334 – 3341ATPPROSITE-ProRule annotation
Active sitei431 – 4311Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi310 – 3189ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: MGI
  • protein serine/threonine/tyrosine kinase activity Source: UniProtKB-EC
  • protein serine/threonine kinase activity Source: UniProtKB
  • protein tyrosine kinase activity Source: MGI

GO - Biological processi

  • peptidyl-tyrosine phosphorylation Source: MGI
  • protein autophosphorylation Source: MGI
  • protein phosphorylation Source: UniProtKB
  • regulation of RNA splicing Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.12.1. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity protein kinase CLK3 (EC:2.7.12.1)
Alternative name(s):
CDC-like kinase 3
Gene namesi
Name:Clk3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1098670. Clk3.

Subcellular locationi

GO - Cellular componenti

  • acrosomal vesicle Source: UniProtKB-SubCell
  • intermediate filament cytoskeleton Source: MGI
  • membrane Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Nucleus

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1075282.
GuidetoPHARMACOLOGYi1992.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 638638Dual specificity protein kinase CLK3PRO_0000085871Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei155 – 1551PhosphotyrosineBy similarity
Modified residuei157 – 1571PhosphoserineCombined sources
Modified residuei197 – 1971PhosphoserineBy similarity
Modified residuei199 – 1991PhosphoserineBy similarity
Modified residuei215 – 2151PhosphoserineBy similarity
Modified residuei224 – 2241PhosphoserineCombined sources
Modified residuei226 – 2261PhosphoserineCombined sources
Modified residuei283 – 2831PhosphoserineBy similarity

Post-translational modificationi

Autophosphorylates on all three types of residues.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO35492.
MaxQBiO35492.
PaxDbiO35492.
PeptideAtlasiO35492.
PRIDEiO35492.

PTM databases

iPTMnetiO35492.
PhosphoSiteiO35492.

Expressioni

Tissue specificityi

Present at high levels in testis and ovary. In testis, expression is restricted to elongated, maturing spermatozoa. Also present in spleen, brain, lung and liver (at protein level).1 Publication

Gene expression databases

BgeeiO35492.
CleanExiMM_CLK3.
GenevisibleiO35492. MM.

Interactioni

Protein-protein interaction databases

BioGridi221868. 2 interactions.
IntActiO35492. 1 interaction.
MINTiMINT-8174106.
STRINGi10090.ENSMUSP00000067341.

Chemistry

BindingDBiO35492.

Structurei

3D structure databases

ProteinModelPortaliO35492.
SMRiO35492. Positions 282-631.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini304 – 620317Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi7 – 264258Arg-richAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0671. Eukaryota.
ENOG410XQF2. LUCA.
GeneTreeiENSGT00580000081366.
HOGENOMiHOG000203417.
HOVERGENiHBG107720.
InParanoidiO35492.
KOiK08823.
OMAiNENKSCE.
OrthoDBiEOG7TBC1V.
PhylomeDBiO35492.
TreeFamiTF101041.

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]

Sequencei

Sequence statusi: Complete.

O35492-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVLSARRKR LASTAGPRRG SGPSLAVRWV PPLGPEPSSD RGRAPMRPRG
60 70 80 90 100
PTCSTTRRGA GRGPRLLPGP PGRDLHRCRP DPGGAGQSPR VCEFGARAVR
110 120 130 140 150
PLGRVEPGPP TAASREGAVL PRAEARAGSG RGARSGEWGL AAAGAWETMH
160 170 180 190 200
HCKRYRSPEP DPYLSYRWKR RRSYSREHEG RLRYPSRREP PPRRSRSRSH
210 220 230 240 250
DRIPYQRRYR EHRDSDTYRC EERSPSFGED CYGSSRSRHR RRSRERAPYR
260 270 280 290 300
TRKHAHHCHK RRTRSCSSAS SRSQQSSKRS SRSVEDDKEG HLVCRIGDWL
310 320 330 340 350
QERYEIVGNL GEGTFGKVVE CLDHARGKSQ VALKIIRNVG KYREAARLEI
360 370 380 390 400
NVLKKIKEKD KENKFLCVLM SDWFNFHGHM CIAFELLGKN TFEFLKENNF
410 420 430 440 450
QPYPLPHVRH MAYQLCHALR FLHENQLTHT DLKPENILFV NSEFETLYNE
460 470 480 490 500
HKSCEEKSVK NTSIRVADFG SATFDHEHHT TIVATRHYRP PEVILELGWA
510 520 530 540 550
QPCDVWSIGC ILFEYYRGFT LFQTHENREH LVMMEKILGP IPSHMIHRTR
560 570 580 590 600
KQKYFYKGGL VWDENSSDGR YVKENCKPLK SYMLQDSLEH VQLFDLMRRM
610 620 630
LEFDPAQRIT LAEALLHPFF AGLTPEERSF HSSRNPSR
Length:638
Mass (Da):73,798
Last modified:June 12, 2007 - v2
Checksum:i3CE7BFD35FB09A3C
GO

Sequence cautioni

The sequence AAB87509.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH85084.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC41138.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAE21937.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAE32308.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAE39405.1 differs from that shown. Reason: Frameshift at position 15. Curated
The sequence BAE39405.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681P → T in BAE39405 (PubMed:16141072).Curated
Sequence conflicti165 – 1651S → T in AAB87509 (PubMed:9307018).Curated
Sequence conflicti314 – 3141T → L in BAE43216 (PubMed:16141072).Curated
Sequence conflicti428 – 4281T → A in BAC41138 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK090215 mRNA. Translation: BAC41138.1. Different initiation.
AK133936 mRNA. Translation: BAE21937.1. Different initiation.
AK146942 mRNA. Translation: BAE27551.1.
AK154003 mRNA. Translation: BAE32308.1. Different initiation.
AK167300 mRNA. Translation: BAE39405.1. Sequence problems.
AK009908 mRNA. Translation: BAE43216.1.
BC085084 mRNA. Translation: AAH85084.1. Different initiation.
AF033565 mRNA. Translation: AAB87509.1. Different initiation.
CCDSiCCDS23232.1.
RefSeqiNP_031739.3. NM_007713.4.
XP_006510802.1. XM_006510739.2.
UniGeneiMm.25720.

Genome annotation databases

EnsembliENSMUST00000065330; ENSMUSP00000067341; ENSMUSG00000032316.
GeneIDi102414.
KEGGimmu:102414.
UCSCiuc009pvr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK090215 mRNA. Translation: BAC41138.1. Different initiation.
AK133936 mRNA. Translation: BAE21937.1. Different initiation.
AK146942 mRNA. Translation: BAE27551.1.
AK154003 mRNA. Translation: BAE32308.1. Different initiation.
AK167300 mRNA. Translation: BAE39405.1. Sequence problems.
AK009908 mRNA. Translation: BAE43216.1.
BC085084 mRNA. Translation: AAH85084.1. Different initiation.
AF033565 mRNA. Translation: AAB87509.1. Different initiation.
CCDSiCCDS23232.1.
RefSeqiNP_031739.3. NM_007713.4.
XP_006510802.1. XM_006510739.2.
UniGeneiMm.25720.

3D structure databases

ProteinModelPortaliO35492.
SMRiO35492. Positions 282-631.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi221868. 2 interactions.
IntActiO35492. 1 interaction.
MINTiMINT-8174106.
STRINGi10090.ENSMUSP00000067341.

Chemistry

BindingDBiO35492.
ChEMBLiCHEMBL1075282.
GuidetoPHARMACOLOGYi1992.

PTM databases

iPTMnetiO35492.
PhosphoSiteiO35492.

Proteomic databases

EPDiO35492.
MaxQBiO35492.
PaxDbiO35492.
PeptideAtlasiO35492.
PRIDEiO35492.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000065330; ENSMUSP00000067341; ENSMUSG00000032316.
GeneIDi102414.
KEGGimmu:102414.
UCSCiuc009pvr.1. mouse.

Organism-specific databases

CTDi1198.
MGIiMGI:1098670. Clk3.

Phylogenomic databases

eggNOGiKOG0671. Eukaryota.
ENOG410XQF2. LUCA.
GeneTreeiENSGT00580000081366.
HOGENOMiHOG000203417.
HOVERGENiHBG107720.
InParanoidiO35492.
KOiK08823.
OMAiNENKSCE.
OrthoDBiEOG7TBC1V.
PhylomeDBiO35492.
TreeFamiTF101041.

Enzyme and pathway databases

BRENDAi2.7.12.1. 3474.

Miscellaneous databases

ChiTaRSiClk3. mouse.
PROiO35492.
SOURCEiSearch...

Gene expression databases

BgeeiO35492.
CleanExiMM_CLK3.
GenevisibleiO35492. MM.

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. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Brain, Kidney, Placenta, Thymus and Tongue.
  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] OF 139-638.
    Tissue: Olfactory epithelium.
  3. "Characterization and comparison of four serine- and arginine-rich (SR) protein kinases."
    Nayler O., Stamm S., Ullrich A.
    Biochem. J. 326:693-700(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 141-638, FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION.
  4. "The dual specificity protein kinase CLK3 is abundantly expressed in mature mouse spermatozoa."
    Menegay H., Moeslein F., Landreth G.
    Exp. Cell Res. 253:463-473(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-224 AND SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "Leucettines, a class of potent inhibitors of cdc2-like kinases and dual specificity, tyrosine phosphorylation regulated kinases derived from the marine sponge leucettamine B: modulation of alternative pre-RNA splicing."
    Debdab M., Carreaux F., Renault S., Soundararajan M., Fedorov O., Filippakopoulos P., Lozach O., Babault L., Tahtouh T., Baratte B., Ogawa Y., Hagiwara M., Eisenreich A., Rauch U., Knapp S., Meijer L., Bazureau J.P.
    J. Med. Chem. 54:4172-4186(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.

Entry informationi

Entry nameiCLK3_MOUSE
AccessioniPrimary (citable) accession number: O35492
Secondary accession number(s): Q3TJU0
, Q3UIF5, Q3V463, Q5U4I1, Q8C1V1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 12, 2007
Last modified: July 6, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. 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.