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P22518

- CLK1_MOUSE

UniProt

P22518 - CLK1_MOUSE

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Protein

Dual specificity protein kinase CLK1

Gene

Clk1

Organism
Mus musculus (Mouse)
Status
Reviewed - 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 and may be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates: SRSF1, SRSF3 and PTPN1. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells and adenovirus E1A pre-mRNA.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Regulates splicing of its own pre-mRNA according to its kinase activity; increased expression of the catalytically active form influences splicing to generate the catalytically inactive splicing variant lacking the kinase domain. Leucettine L41 inhibits its kinase activity and affects the regulation of alternative splicing mediated by phosphorylation of SR proteins.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei190 – 1901ATPPROSITE-ProRule annotation
Active sitei287 – 2871Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi166 – 1749ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein serine/threonine/tyrosine kinase activity Source: UniProtKB-EC
  3. protein serine/threonine kinase activity Source: MGI
  4. protein tyrosine kinase activity Source: MGI

GO - Biological processi

  1. peptidyl-serine phosphorylation Source: MGI
  2. peptidyl-threonine phosphorylation Source: MGI
  3. peptidyl-tyrosine phosphorylation Source: MGI
  4. protein autophosphorylation Source: MGI
  5. regulation of RNA splicing Source: Ensembl
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 CLK1 (EC:2.7.12.1)
Alternative name(s):
CDC-like kinase 1
Protein kinase STY
Gene namesi
Name:Clk1
Synonyms:Clk, Sty
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:107403. Clk1.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi190 – 1901K → R: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 483483Dual specificity protein kinase CLK1PRO_0000085867Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei61 – 611PhosphoserineBy similarity
Modified residuei139 – 1391Phosphoserine1 Publication

Post-translational modificationi

Autophosphorylates on all three types of residues.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP22518.

PTM databases

PhosphoSiteiP22518.

Expressioni

Gene expression databases

BgeeiP22518.
CleanExiMM_CLK1.
ExpressionAtlasiP22518. baseline and differential.
GenevestigatoriP22518.

Interactioni

Subunit structurei

Interacts with PPIG and UBL5.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
lubXQ5ZRQ03EBI-6479117,EBI-6402540From a different organism.

Protein-protein interaction databases

IntActiP22518. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP22518.
SMRiP22518. Positions 147-481.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini160 – 476317Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi29 – 335Nuclear localization signalSequence Analysis

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00580000081366.
HOGENOMiHOG000203417.
HOVERGENiHBG107720.
InParanoidiP22518.
KOiK08823.
OMAiMLSQDVE.
OrthoDBiEOG7TBC1V.
TreeFamiTF101041.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
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 splicing. Align

Isoform Long (identifier: P22518-1) [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
MRHSKRTYCP DWDERDWDYG TWRSSSSHKR KKRSHSSARE QKRCRYDHSK
60 70 80 90 100
TTDSYYLESR SINEKAYHSR RYVDEYRNDY MGYEPGHPYG EPGSRYQMHS
110 120 130 140 150
SKSSGRSGRS SYKSKHRSRH HTSQHHSHGK SHRRKRSRSV EDDEEGHLIC
160 170 180 190 200
QSGDVLSARY EIVDTLGEGA FGKVVECIDH KVGGRRVAVK IVKNVDRYCE
210 220 230 240 250
AAQSEIQVLE HLNTTDPHST FRCVQMLEWF EHRGHICIVF ELLGLSTYDF
260 270 280 290 300
IKENSFLPFR MDHIRKMAYQ ICKSVNFLHS NKLTHTDLKP ENILFVKSDY
310 320 330 340 350
TEAYNPKMKR DERTIVNPDI KVVDFGSATY DDEHHSTLVS TRHYRAPEVI
360 370 380 390 400
LALGWSQPCD VWSIGCILIE YYLGFTVFPT HDSREHLAMM ERILGPLPKH
410 420 430 440 450
MIQKTRKRRY FHHDRLDWDE HSSAGRYVSR RCKPLKEFML SQDAEHELLF
460 470 480
DLIGKMLEYD PAKRITLKEA LKHPFFYPLK KHT
Length:483
Mass (Da):57,093
Last modified:July 27, 2011 - v2
Checksum:i96FEBC20EC90D8E8
GO
Isoform Short (identifier: P22518-2) [UniParc]FASTAAdd to Basket

Also known as: Clk1T

The sequence of this isoform differs from the canonical sequence as follows:
     130-135: KSHRRK → MKLLIL
     136-483: Missing.

Note: Lacks the kinase domain.

Show »
Length:135
Mass (Da):16,318
Checksum:i44BBA47A5D09705A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti379 – 3791P → S in AAA40151. (PubMed:1986248)Curated
Sequence conflicti448 – 4481L → F in CAA40473. (PubMed:1825055)Curated
Sequence conflicti453 – 4531I → V in CAA40473. (PubMed:1825055)Curated
Sequence conflicti456 – 4561M → I in CAA40473. (PubMed:1825055)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei130 – 1356KSHRRK → MKLLIL in isoform Short. 3 PublicationsVSP_004854
Alternative sequencei136 – 483348Missing in isoform Short. 3 PublicationsVSP_004855Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57186 mRNA. Translation: CAA40473.1.
M38381 mRNA. Translation: AAA40151.1.
U21209 mRNA. Translation: AAC52257.1.
L29221 mRNA. Translation: AAA61485.1.
AK135765 mRNA. Translation: BAE22647.1.
CH466548 Genomic DNA. Translation: EDL00074.1.
BC145905 mRNA. Translation: AAI45906.1.
BC145911 mRNA. Translation: AAI45912.1.
CCDSiCCDS35577.1. [P22518-1]
PIRiA39676.
I49275.
RefSeqiNP_001036099.1. NM_001042634.2. [P22518-1]
UniGeneiMm.1761.

Genome annotation databases

EnsembliENSMUST00000034868; ENSMUSP00000034868; ENSMUSG00000026034. [P22518-1]
ENSMUST00000148330; ENSMUSP00000137649; ENSMUSG00000026034. [P22518-2]
ENSMUST00000151338; ENSMUSP00000137815; ENSMUSG00000026034. [P22518-2]
GeneIDi12747.
KEGGimmu:12747.
UCSCiuc007bbs.2. mouse. [P22518-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57186 mRNA. Translation: CAA40473.1 .
M38381 mRNA. Translation: AAA40151.1 .
U21209 mRNA. Translation: AAC52257.1 .
L29221 mRNA. Translation: AAA61485.1 .
AK135765 mRNA. Translation: BAE22647.1 .
CH466548 Genomic DNA. Translation: EDL00074.1 .
BC145905 mRNA. Translation: AAI45906.1 .
BC145911 mRNA. Translation: AAI45912.1 .
CCDSi CCDS35577.1. [P22518-1 ]
PIRi A39676.
I49275.
RefSeqi NP_001036099.1. NM_001042634.2. [P22518-1 ]
UniGenei Mm.1761.

3D structure databases

ProteinModelPortali P22518.
SMRi P22518. Positions 147-481.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P22518. 1 interaction.

Chemistry

BindingDBi P22518.
ChEMBLi CHEMBL1075280.

PTM databases

PhosphoSitei P22518.

Proteomic databases

PRIDEi P22518.

Protocols and materials databases

DNASUi 12747.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034868 ; ENSMUSP00000034868 ; ENSMUSG00000026034 . [P22518-1 ]
ENSMUST00000148330 ; ENSMUSP00000137649 ; ENSMUSG00000026034 . [P22518-2 ]
ENSMUST00000151338 ; ENSMUSP00000137815 ; ENSMUSG00000026034 . [P22518-2 ]
GeneIDi 12747.
KEGGi mmu:12747.
UCSCi uc007bbs.2. mouse. [P22518-1 ]

Organism-specific databases

CTDi 1195.
MGIi MGI:107403. Clk1.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00580000081366.
HOGENOMi HOG000203417.
HOVERGENi HBG107720.
InParanoidi P22518.
KOi K08823.
OMAi MLSQDVE.
OrthoDBi EOG7TBC1V.
TreeFami TF101041.

Enzyme and pathway databases

BRENDAi 2.7.12.1. 3474.

Miscellaneous databases

ChiTaRSi Clk1. mouse.
NextBioi 282070.
PROi P22518.
SOURCEi Search...

Gene expression databases

Bgeei P22518.
CleanExi MM_CLK1.
ExpressionAtlasi P22518. baseline and differential.
Genevestigatori P22518.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A mammalian protein kinase with potential for serine/threonine and tyrosine phosphorylation is related to cell cycle regulators."
    Ben-David Y., Letwin K., Tannock L., Bernstein A., Pawson T.
    EMBO J. 10:317-325(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), MUTAGENESIS OF LYS-190.
  2. "STY, a tyrosine-phosphorylating enzyme with sequence homology to serine/threonine kinases."
    Howell B.W., Afar D.E., Lew J., Douville E.M., Icely P.L., Gray D.A., Bell J.C.
    Mol. Cell. Biol. 11:568-572(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Alternative splicing of STY, a nuclear dual specificity kinase."
    Duncan P.I., Howell B.W., Marius R.M., Drmanic S., Douville E.M., Bell J.C.
    J. Biol. Chem. 270:21524-21531(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
  4. "Characterization by cDNA cloning of two new human protein kinases. Evidence by sequence comparison of a new family of mammalian protein kinases."
    Hanes J.J., der Kammer H., Klaudiny J.J., Scheit K.H.
    J. Mol. Biol. 244:665-672(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
  5. "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] (ISOFORM LONG).
    Strain: C57BL/6J.
  6. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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 SHORT).
    Tissue: Brain.
  8. "The Clk/Sty protein kinase phosphorylates SR splicing factors and regulates their intranuclear distribution."
    Colwill K., Pawson T., Andrews B., Prasad J., Manley J.L., Bell J.C., Duncan P.I.
    EMBO J. 15:265-275(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  9. "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: FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION.
  10. "In vivo regulation of alternative pre-mRNA splicing by the Clk1 protein kinase."
    Duncan P.I., Stojdl D.F., Marius R.M., Bell J.C.
    Mol. Cell. Biol. 17:5996-6001(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "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 nameiCLK1_MOUSE
AccessioniPrimary (citable) accession number: P22518
Secondary accession number(s): A6H6K2, Q3UXB6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 129 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

External Data

Dasty 3