O35492 (CLK3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dual specificity protein kinase CLK3
EC=2.7.12.1

Alternative name(s):
CDC-like kinase 3

Gene names

Name:

Clk3

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	638 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.3
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.4
Enzyme regulation	Leucettine L41 inhibits its kinase activity and affects the regulation of alternative splicing mediated by phosphorylation of SR proteins. Ref.6
Subcellular location	Nucleus. Cytoplasm. Cytoplasmic vesicle › secretory vesicle › acrosome Ref.3 Ref.4.
Tissue specificity	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). Ref.4
Post-translational modification	Autophosphorylates on all three types of residues.
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. Lammer subfamily. Contains 1 protein kinase domain.
Sequence caution	The sequence AAB87509.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAH85084.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAC41138.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAE21937.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAE32308.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAE39405.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAE39405.1 differs from that shown. Reason: Frameshift at position 15.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoplasmic vesicle Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	peptidyl-tyrosine phosphorylation Inferred from direct assay Ref.3. Source: MGI protein autophosphorylation Inferred from direct assay Ref.3. Source: MGI
Cellular component	acrosomal vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.3. Source: MGI
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from direct assay Ref.3. Source: UniProtKB protein serine/threonine/tyrosine kinase activity Inferred from electronic annotation. Source: EC protein tyrosine kinase activity Inferred from direct assay Ref.3. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 638	638	Dual specificity protein kinase CLK3		PRO_0000085871
Regions
	Domain	304 – 620	317	Protein kinase
	Nucleotide binding	310 – 318	9	ATP By similarity
	Compositional bias	7 – 264	258	Arg-rich
Sites
	Active site	431	1	Proton acceptor By similarity
	Binding site	334	1	ATP By similarity
Amino acid modifications
	Modified residue	155	1	Phosphotyrosine Ref.5
	Modified residue	157	1	Phosphoserine By similarity
	Modified residue	197	1	Phosphoserine By similarity
	Modified residue	199	1	Phosphoserine By similarity
	Modified residue	215	1	Phosphoserine By similarity
	Modified residue	224	1	Phosphoserine By similarity
	Modified residue	226	1	Phosphoserine By similarity
	Modified residue	283	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	68	1	P → T in BAE39405. Ref.1
	Sequence conflict	165	1	S → T in AAB87509. Ref.3
	Sequence conflict	314	1	T → L in BAE43216. Ref.1
	Sequence conflict	428	1	T → A in BAC41138. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O35492 [UniParc]. Last modified June 12, 2007. Version 2. Checksum: 3CE7BFD35FB09A3C	FASTA	638	73,798
	10 20 30 40 50 60 MPVLSARRKR LASTAGPRRG SGPSLAVRWV PPLGPEPSSD RGRAPMRPRG PTCSTTRRGA 70 80 90 100 110 120 GRGPRLLPGP PGRDLHRCRP DPGGAGQSPR VCEFGARAVR PLGRVEPGPP TAASREGAVL 130 140 150 160 170 180 PRAEARAGSG RGARSGEWGL AAAGAWETMH HCKRYRSPEP DPYLSYRWKR RRSYSREHEG 190 200 210 220 230 240 RLRYPSRREP PPRRSRSRSH DRIPYQRRYR EHRDSDTYRC EERSPSFGED CYGSSRSRHR 250 260 270 280 290 300 RRSRERAPYR TRKHAHHCHK RRTRSCSSAS SRSQQSSKRS SRSVEDDKEG HLVCRIGDWL 310 320 330 340 350 360 QERYEIVGNL GEGTFGKVVE CLDHARGKSQ VALKIIRNVG KYREAARLEI NVLKKIKEKD 370 380 390 400 410 420 KENKFLCVLM SDWFNFHGHM CIAFELLGKN TFEFLKENNF QPYPLPHVRH MAYQLCHALR 430 440 450 460 470 480 FLHENQLTHT DLKPENILFV NSEFETLYNE HKSCEEKSVK NTSIRVADFG SATFDHEHHT 490 500 510 520 530 540 TIVATRHYRP PEVILELGWA QPCDVWSIGC ILFEYYRGFT LFQTHENREH LVMMEKILGP 550 560 570 580 590 600 IPSHMIHRTR KQKYFYKGGL VWDENSSDGR YVKENCKPLK SYMLQDSLEH VQLFDLMRRM 610 620 630 LEFDPAQRIT LAEALLHPFF AGLTPEERSF HSSRNPSR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 16141072] [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: 15489334] [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: 9307018] [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: 10585269] [Abstract] Cited for: TISSUE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
[5]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-155, MASS SPECTROMETRY. Tissue: Liver.
[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: 21615147] [Abstract] Cited for: ENZYME REGULATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00314963.
RefSeq	NP_031739.3. NM_007713.4.
UniGene	Mm.25720.
3D structure databases
ProteinModelPortal	O35492.
SMR	O35492. Positions 282-631.
ModBase	Search...
Protein-protein interaction databases
STRING	O35492.
PTM databases
PhosphoSite	O35492.
Proteomic databases
PRIDE	O35492.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000065330; ENSMUSP00000067341; ENSMUSG00000032316.
GeneID	102414.
KEGG	mmu:102414.
UCSC	uc009pvr.1. mouse.
Organism-specific databases
CTD	1198.
MGI	MGI:1098670. Clk3.
Phylogenomic databases
eggNOG	roNOG09009.
HOGENOM	HBG755340.
HOVERGEN	HBG107720.
InParanoid	O35492.
OMA	CRKRRTR.
OrthoDB	EOG49ZXP2.
PhylomeDB	O35492.
Enzyme and pathway databases
BRENDA	2.7.12.1. 3474.
Gene expression databases
ArrayExpress	O35492.
Bgee	O35492.
CleanEx	MM_CLK3.
Genevestigator	O35492.
GermOnline	ENSMUSG00000032316. Mus musculus.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. [Graphical view]
KO	K08823.
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
NextBio	355462.
SOURCE	Search...

Entry information

Entry name

CLK3_MOUSE

Accession

Primary (citable) accession number: O35492
Secondary accession number(s): Q3TJU0 , Q3UIF5, Q3V463, Q5U4I1, Q8C1V1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	June 12, 2007
Last modified:	November 16, 2011
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program