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P49760

- CLK2_HUMAN

UniProt

P49760 - CLK2_HUMAN

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Protein
Dual specificity protein kinase CLK2
Gene
CLK2
Organism
Homo sapiens (Human)
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. 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. Acts as a suppressor of hepatic gluconeogenesis and glucose output by repressing PPARGC1A transcriptional activity on gluconeogenic genes via its phosphorylation. Phosphorylates PPP2R5B thereby stimulating the assembly of PP2A phosphatase with the PPP2R5B-AKT1 complex leading to dephosphorylation of AKT1. Phosphorylates: PTPN1, SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells.4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

5,6-dichloro-1-b-D-ribofuranosylbenzimidazole (DRB) inhibits autophosphorylation. TG003 inhibits its kinase activity and affects the regulation of alternative splicing mediated by phosphorylation of SR proteins By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei193 – 1931ATP By similarity
Active sitei290 – 2901Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi169 – 1779ATP By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. negative regulation of gluconeogenesis Source: UniProtKB
  2. protein autophosphorylation Source: UniProtKB
  3. protein phosphorylation Source: UniProtKB
  4. regulation of RNA splicing Source: UniProtKB
  5. response to ionizing radiation Source: UniProtKB
  6. response to retinoic acid 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. 2681.
SignaLinkiP49760.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity protein kinase CLK2 (EC:2.7.12.1)
Alternative name(s):
CDC-like kinase 2
Gene namesi
Name:CLK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:2069. CLK2.

Subcellular locationi

Isoform 1 : Nucleus. Nucleus speckle
Note: Inhibition of phosphorylation at Ser-142 results in accumulation in the nuclear speckle By similarity.1 Publication
Isoform 2 : Nucleus speckle
Note: Co-localizes with serine- and arginine-rich (SR) proteins in the nuclear speckles.1 Publication

GO - Cellular componenti

  1. nuclear speck Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26595.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 499499Dual specificity protein kinase CLK2
PRO_0000085868Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei34 – 341Phosphoserine; by PKB/AKT11 Publication
Modified residuei98 – 981Phosphoserine; by autocatalysis By similarity
Modified residuei99 – 991Phosphotyrosine; by autocatalysis By similarity
Modified residuei127 – 1271Phosphothreonine; by PKB/AKT11 Publication
Modified residuei142 – 1421Phosphoserine; by autocatalysis3 Publications
Modified residuei153 – 1531Phosphotyrosine1 Publication
Modified residuei344 – 3441Phosphothreonine; by PKB/AKT2 By similarity

Post-translational modificationi

Autophosphorylates on all three types of residues. Phosphorylation on Ser-34 and Thr-127 by AKT1 is induced by ionizing radiation or insulin. Phosphorylation plays a critical role in cell proliferation following low dose radiation and prevents cell death following high dose radiation. Phosphorylation at Thr-344 by PKB/AKT2 induces its kinase activity which is required for its stability. The phosphorylation status at Ser-142 influences its subnuclear localization; inhibition of phosphorylation at Ser-142 results in accumulation in the nuclear speckle.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP49760.
PaxDbiP49760.
PRIDEiP49760.

PTM databases

PhosphoSiteiP49760.

Expressioni

Tissue specificityi

Endothelial cells.1 Publication

Gene expression databases

ArrayExpressiP49760.
BgeeiP49760.
CleanExiHS_CLK2.
GenevestigatoriP49760.

Organism-specific databases

HPAiHPA055366.

Interactioni

Subunit structurei

Interacts with RBMX. Interacts with AKT1 and UBL5.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CLK3P497613EBI-750020,EBI-745579
SNRNP70P086212EBI-750020,EBI-1049228

Protein-protein interaction databases

BioGridi107607. 40 interactions.
IntActiP49760. 30 interactions.
MINTiMINT-1683264.
STRINGi9606.ENSP00000354856.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni146 – 1494
Turni160 – 1623
Beta strandi163 – 17210
Beta strandi175 – 1828
Turni183 – 1875
Beta strandi189 – 1957
Helixi199 – 21820
Beta strandi229 – 2357
Beta strandi238 – 2447
Helixi250 – 2567
Turni257 – 2593
Helixi264 – 28320
Helixi293 – 2953
Beta strandi296 – 2994
Beta strandi317 – 3193
Beta strandi323 – 3253
Beta strandi332 – 3365
Helixi345 – 3473
Helixi350 – 3534
Helixi361 – 37616
Helixi386 – 39712
Helixi402 – 4076
Helixi411 – 4133
Helixi426 – 4349
Helixi438 – 4414
Helixi447 – 45913
Turni464 – 4663
Helixi470 – 4756
Helixi477 – 4793
Helixi480 – 4834

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NR9X-ray2.89A/B/C135-496[»]
ProteinModelPortaliP49760.
SMRiP49760. Positions 136-482.

Miscellaneous databases

EvolutionaryTraceiP49760.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini163 – 479317Protein kinase
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000203417.
HOVERGENiHBG107720.
InParanoidiP49760.
KOiK08823.
OMAiGHLIYRV.
PhylomeDBiP49760.
TreeFamiTF101041.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P49760-1) [UniParc]FASTAAdd to Basket

Also known as: Long

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

MPHPRRYHSS ERGSRGSYRE HYRSRKHKRR RSRSWSSSSD RTRRRRREDS    50
YHVRSRSSYD DRSSDRRVYD RRYCGSYRRN DYSRDRGDAY YDTDYRHSYE 100
YQRENSSYRS QRSSRRKHRR RRRRSRTFSR SSSQHSSRRA KSVEDDAEGH 150
LIYHVGDWLQ ERYEIVSTLG EGTFGRVVQC VDHRRGGARV ALKIIKNVEK 200
YKEAARLEIN VLEKINEKDP DNKNLCVQMF DWFDYHGHMC ISFELLGLST 250
FDFLKDNNYL PYPIHQVRHM AFQLCQAVKF LHDNKLTHTD LKPENILFVN 300
SDYELTYNLE KKRDERSVKS TAVRVVDFGS ATFDHEHHST IVSTRHYRAP 350
EVILELGWSQ PCDVWSIGCI IFEYYVGFTL FQTHDNREHL AMMERILGPI 400
PSRMIRKTRK QKYFYRGRLD WDENTSAGRY VRENCKPLRR YLTSEAEEHH 450
QLFDLIESML EYEPAKRLTL GEALQHPFFA RLRAEPPNKL WDSSRDISR 499
Length:499
Mass (Da):60,090
Last modified:October 1, 1996 - v1
Checksum:iE43BBF3BAD6EF991
GO
Isoform 2 (identifier: P49760-2) [UniParc]FASTAAdd to Basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     134-139: QHSSRR → MKSLAP
     140-499: Missing.

Note: Lacks the kinase domain. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Show »
Length:139
Mass (Da):17,569
Checksum:iCC9C9C63B3B07667
GO
Isoform 3 (identifier: P49760-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     134-134: Missing.

Show »
Length:498
Mass (Da):59,962
Checksum:i0A21FC66FD22DBC6
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei134 – 1396QHSSRR → MKSLAP in isoform 2.
VSP_004856
Alternative sequencei134 – 1341Missing in isoform 3.
VSP_038744
Alternative sequencei140 – 499360Missing in isoform 2.
VSP_004857Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L29218 mRNA. Translation: AAA61482.1.
L29216 mRNA. Translation: AAA61481.1.
AF023268 Genomic DNA. Translation: AAC51817.1.
AL713999 Genomic DNA. Translation: CAI95098.1.
BC014067 mRNA. Translation: AAH14067.1.
BC053603 mRNA. Translation: AAH53603.1.
CCDSiCCDS1107.1. [P49760-3]
PIRiS53637.
S53638.
RefSeqiNP_003984.2. NM_003993.2. [P49760-3]
XP_005244933.1. XM_005244876.1. [P49760-1]
XP_005276799.1. XM_005276742.1. [P49760-1]
UniGeneiHs.73986.

Genome annotation databases

EnsembliENST00000361168; ENSP00000354856; ENSG00000176444. [P49760-3]
ENST00000368361; ENSP00000357345; ENSG00000176444. [P49760-1]
ENST00000536801; ENSP00000441023; ENSG00000176444. [P49760-1]
ENST00000572269; ENSP00000459461; ENSG00000261893. [P49760-3]
ENST00000574445; ENSP00000460443; ENSG00000261893. [P49760-1]
GeneIDi1196.
KEGGihsa:1196.
UCSCiuc001fjw.3. human. [P49760-3]
uc001fjx.3. human. [P49760-1]

Polymorphism databases

DMDMi1705919.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L29218 mRNA. Translation: AAA61482.1 .
L29216 mRNA. Translation: AAA61481.1 .
AF023268 Genomic DNA. Translation: AAC51817.1 .
AL713999 Genomic DNA. Translation: CAI95098.1 .
BC014067 mRNA. Translation: AAH14067.1 .
BC053603 mRNA. Translation: AAH53603.1 .
CCDSi CCDS1107.1. [P49760-3 ]
PIRi S53637.
S53638.
RefSeqi NP_003984.2. NM_003993.2. [P49760-3 ]
XP_005244933.1. XM_005244876.1. [P49760-1 ]
XP_005276799.1. XM_005276742.1. [P49760-1 ]
UniGenei Hs.73986.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3NR9 X-ray 2.89 A/B/C 135-496 [» ]
ProteinModelPortali P49760.
SMRi P49760. Positions 136-482.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107607. 40 interactions.
IntActi P49760. 30 interactions.
MINTi MINT-1683264.
STRINGi 9606.ENSP00000354856.

Chemistry

BindingDBi P49760.
ChEMBLi CHEMBL4225.
GuidetoPHARMACOLOGYi 1991.

PTM databases

PhosphoSitei P49760.

Polymorphism databases

DMDMi 1705919.

Proteomic databases

MaxQBi P49760.
PaxDbi P49760.
PRIDEi P49760.

Protocols and materials databases

DNASUi 1196.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000361168 ; ENSP00000354856 ; ENSG00000176444 . [P49760-3 ]
ENST00000368361 ; ENSP00000357345 ; ENSG00000176444 . [P49760-1 ]
ENST00000536801 ; ENSP00000441023 ; ENSG00000176444 . [P49760-1 ]
ENST00000572269 ; ENSP00000459461 ; ENSG00000261893 . [P49760-3 ]
ENST00000574445 ; ENSP00000460443 ; ENSG00000261893 . [P49760-1 ]
GeneIDi 1196.
KEGGi hsa:1196.
UCSCi uc001fjw.3. human. [P49760-3 ]
uc001fjx.3. human. [P49760-1 ]

Organism-specific databases

CTDi 1196.
GeneCardsi GC01M155232.
H-InvDB HIX0001112.
HGNCi HGNC:2069. CLK2.
HPAi HPA055366.
MIMi 602989. gene.
neXtProti NX_P49760.
PharmGKBi PA26595.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000203417.
HOVERGENi HBG107720.
InParanoidi P49760.
KOi K08823.
OMAi GHLIYRV.
PhylomeDBi P49760.
TreeFami TF101041.

Enzyme and pathway databases

BRENDAi 2.7.12.1. 2681.
SignaLinki P49760.

Miscellaneous databases

ChiTaRSi CLK2. human.
EvolutionaryTracei P49760.
GeneWikii CLK2.
GenomeRNAii 1196.
NextBioi 4940.
PROi P49760.
SOURCEi Search...

Gene expression databases

ArrayExpressi P49760.
Bgeei P49760.
CleanExi HS_CLK2.
Genevestigatori P49760.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
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. "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] (ISOFORMS 1 AND 2).
  2. "Identification of three additional genes contiguous to the glucocerebrosidase locus on chromosome 1q21: implications for Gaucher disease."
    Winfield S.L., Tayebi N., Martin B.M., Ginns E.I., Sidransky E.
    Genome Res. 7:1020-1026(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORMS 1 AND 3).
    Tissue: Lung and Ovary.
  5. "Activity and autophosphorylation of LAMMER protein kinases."
    Lee K., Du C., Horn M., Rabinow L.
    J. Biol. Chem. 271:27299-27303(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "The Clk2 and Clk3 dual-specificity protein kinases regulate the intranuclear distribution of SR proteins and influence pre-mRNA splicing."
    Duncan P.I., Stojdl D.F., Marius R.M., Scheit K.H., Bell J.C.
    Exp. Cell Res. 241:300-308(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
  7. "The CLK family kinases, CLK1 and CLK2, phosphorylate and activate the tyrosine phosphatase, PTP-1B."
    Moeslein F.M., Myers M.P., Landreth G.E.
    J. Biol. Chem. 274:26697-26704(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. Cited for: INTERACTION WITH UBL5.
  9. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
  10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Cdc2-like kinases and DNA topoisomerase I regulate alternative splicing of tissue factor in human endothelial cells."
    Eisenreich A., Bogdanov V.Y., Zakrzewicz A., Pries A., Antoniak S., Poller W., Schultheiss H.P., Rauch U.
    Circ. Res. 104:589-599(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
  13. "Heterogeneous nuclear ribonucleoprotein G regulates splice site selection by binding to CC(A/C)-rich regions in pre-mRNA."
    Heinrich B., Zhang Z., Raitskin O., Hiller M., Benderska N., Hartmann A.M., Bracco L., Elliott D., Ben-Ari S., Soreq H., Sperling J., Sperling R., Stamm S.
    J. Biol. Chem. 284:14303-14315(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RBMX.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142 AND TYR-153, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Phosphorylation of CLK2 at serine 34 and threonine 127 by AKT controls cell survival after ionizing radiation."
    Nam S.Y., Seo H.H., Park H.S., An S., Kim J.Y., Yang K.H., Kim C.S., Jeong M., Jin Y.W.
    J. Biol. Chem. 285:31157-31163(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-34 AND THR-127, INTERACTION WITH AKT1.
  16. "Structure of human cdc2-like kinase 2 (clk2)."
    Structural genomics consortium (SGC)
    Submitted (AUG-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) OF 135-496.

Entry informationi

Entry nameiCLK2_HUMAN
AccessioniPrimary (citable) accession number: P49760
Secondary accession number(s): B1AVS9, B5MBX6, Q96CQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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