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Reviewed, UniProtKB/Swiss-Prot O35491 (CLK2_MOUSE)

Last modified October 13, 2009. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Dual specificity protein kinase CLK2
    EC=2.7.12.1
Alternative name(s):
    CDC-like kinase 2
Gene names
Name: Clk2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length499 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

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. Phosphorylates serines, threonines and tyrosines.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subcellular location

Nucleus By similarity.

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 499499Dual specificity protein kinase CLK2
PRO_0000085869

Regions

Domain163 – 479317Protein kinase
Nucleotide binding168 – 1769ATP By similarity

Sites

Active site2891Proton acceptor By similarity
Binding site1921ATP By similarity

Amino acid modifications

Modified residue511Phosphotyrosine By similarity
Modified residue981Phosphoserine By similarity
Modified residue1411Phosphoserine By similarity
Modified residue4931Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
O35491-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 092946BA171C9ADD

FASTA49959,955
        10         20         30         40         50         60 
MPHPRRYHSS ERGSRGSYHE HYQSRKHKRR RSRSWSSSSD RTRRRRREDS YHVRSRSSYD 

        70         80         90        100        110        120 
DHSSDRRLYD RRYCGSYRRN DYSRDRGEAY YDTDFRQSYE YHRENSSYRS QRSSRRKHRR 

       130        140        150        160        170        180 
RRRRSRTFSR SSSHSSRRAK SVEDDAEGHL IYHVGDWLQE RYEIVSTLGE GTSGRVVQCV 

       190        200        210        220        230        240 
DHRRGGTRVA LKIIKNVEKY KEAARLEINV LEKINEKDPD NKNLCVQMFD WFDYHGHMCI 

       250        260        270        280        290        300 
SFELLGLSTF DFLKDNNYLP YPIHQVRHMA FQLCQAVKFL HDNKLTHTDL KPENILFVNS 

       310        320        330        340        350        360 
DYELTYNLEK KRDERSVKST AVRVVDFGSA TFDHEHHSTI VSTRHYRAPE VILELGWSQP 

       370        380        390        400        410        420 
CDVWSIGCII FEYYVGFTLF QTHDNREHLA MMERILGPVP SRMIRKTRKQ KYFYRGRLDW 

       430        440        450        460        470        480 
DENTSAGRYV RENCKPLRRY LTSEAEDHHQ LFDLIENMLE YEPAKRLTLG EALQHPFFAC 

       490 
LRTEPPNTKL WDSSRDISR 

« Hide

References

[1]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

AF033564 mRNA. Translation: AAB87508.1.
IPIIPI00130951.
UniGeneMm.288098

3D structure databases

HSSPHSSP built from PDB template 1HOW based on UniProtKB Q03656.
SMRO35491. Positions 142-484.
ModBaseSearch...

Protein-protein interaction databases

STRINGO35491.

PTM databases

PhosphoSiteO35491.

Proteomic databases

PRIDEO35491.

Genome annotation databases

EnsemblENSMUST00000090927; ENSMUSP00000088445; ENSMUSG00000068917; Mus musculus. [Genome view]
ENSMUST00000121931; ENSMUSP00000113861; ENSMUSG00000068917; Mus musculus. [Genome view]
KEGGmmu:12748.
UCSCuc008pxt.1. mouse.

Organism-specific databases

CTD12748.
MGIMGI:1098669. Clk2.

Phylogenomic databases

HOGENOMO35491.
HOVERGENO35491.

Enzyme and pathway databases

BRENDA2.7.12.1. 244.

Gene expression databases

ArrayExpressO35491.
BgeeO35491.
GenevestigatorO35491.
GermOnlineENSMUSG00000068917. Mus musculus.

Family and domain databases

InterProIPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio282076.
SOURCESearch...

Entry information

Entry nameCLK2_MOUSE
AccessionPrimary (citable) accession number: O35491
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: October 13, 2009
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents