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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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei193 – 1931ATPPROSITE-ProRule annotation
Active sitei290 – 2901Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi169 – 1779ATPPROSITE-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: UniProtKB
  4. 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, UP000005640: Unplaced

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
Isoform 2 : Nucleus speckle
Note: Co-localizes with serine- and arginine-rich (SR) proteins in the nuclear speckles.

GO - Cellular componenti

  1. 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 CLK2PRO_0000085868Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei34 – 341Phosphoserine; by PKB/AKT11 Publication
Modified residuei98 – 981Phosphoserine; by autocatalysisBy similarity
Modified residuei99 – 991Phosphotyrosine; by autocatalysisBy similarity
Modified residuei127 – 1271Phosphothreonine; by PKB/AKT11 Publication
Modified residuei142 – 1421Phosphoserine; by autocatalysis3 Publications
Modified residuei153 – 1531Phosphotyrosine1 Publication
Modified residuei344 – 3441Phosphothreonine; by PKB/AKT2By 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.5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP49760.
PaxDbiP49760.
PRIDEiP49760.

PTM databases

PhosphoSiteiP49760.

Expressioni

Tissue specificityi

Endothelial cells.1 Publication

Gene expression databases

BgeeiP49760.
CleanExiHS_CLK2.
ExpressionAtlasiP49760. baseline and differential.
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. 43 interactions.
IntActiP49760. 30 interactions.
MINTiMINT-1683264.
STRINGi9606.ENSP00000354856.

Structurei

Secondary structure

1
499
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni146 – 1494Combined sources
Turni160 – 1623Combined sources
Beta strandi163 – 17210Combined sources
Beta strandi175 – 1828Combined sources
Turni183 – 1875Combined sources
Beta strandi189 – 1957Combined sources
Helixi199 – 21820Combined sources
Beta strandi229 – 2357Combined sources
Beta strandi238 – 2447Combined sources
Helixi250 – 2567Combined sources
Turni257 – 2593Combined sources
Helixi264 – 28320Combined sources
Helixi293 – 2953Combined sources
Beta strandi296 – 2994Combined sources
Beta strandi317 – 3193Combined sources
Beta strandi323 – 3253Combined sources
Beta strandi332 – 3365Combined sources
Helixi345 – 3473Combined sources
Helixi350 – 3534Combined sources
Helixi361 – 37616Combined sources
Helixi386 – 39712Combined sources
Helixi402 – 4076Combined sources
Helixi411 – 4133Combined sources
Helixi426 – 4349Combined sources
Helixi438 – 4414Combined sources
Helixi447 – 45913Combined sources
Turni464 – 4663Combined sources
Helixi470 – 4756Combined sources
Helixi477 – 4793Combined sources
Helixi480 – 4834Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP49760.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini163 – 479317Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00580000081366.
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.
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

        10         20         30         40         50
MPHPRRYHSS ERGSRGSYRE HYRSRKHKRR RSRSWSSSSD RTRRRRREDS
60 70 80 90 100
YHVRSRSSYD DRSSDRRVYD RRYCGSYRRN DYSRDRGDAY YDTDYRHSYE
110 120 130 140 150
YQRENSSYRS QRSSRRKHRR RRRRSRTFSR SSSQHSSRRA KSVEDDAEGH
160 170 180 190 200
LIYHVGDWLQ ERYEIVSTLG EGTFGRVVQC VDHRRGGARV ALKIIKNVEK
210 220 230 240 250
YKEAARLEIN VLEKINEKDP DNKNLCVQMF DWFDYHGHMC ISFELLGLST
260 270 280 290 300
FDFLKDNNYL PYPIHQVRHM AFQLCQAVKF LHDNKLTHTD LKPENILFVN
310 320 330 340 350
SDYELTYNLE KKRDERSVKS TAVRVVDFGS ATFDHEHHST IVSTRHYRAP
360 370 380 390 400
EVILELGWSQ PCDVWSIGCI IFEYYVGFTL FQTHDNREHL AMMERILGPI
410 420 430 440 450
PSRMIRKTRK QKYFYRGRLD WDENTSAGRY VRENCKPLRR YLTSEAEEHH
460 470 480 490
QLFDLIESML EYEPAKRLTL GEALQHPFFA RLRAEPPNKL WDSSRDISR
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. 1 PublicationVSP_004856
Alternative sequencei134 – 1341Missing in isoform 3. 1 PublicationVSP_038744
Alternative sequencei140 – 499360Missing in isoform 2. 1 PublicationVSP_004857Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS72939.1. [P49760-1]
PIRiS53637.
S53638.
RefSeqiNP_001281267.1. NM_001294338.1. [P49760-1]
NP_001281268.1. NM_001294339.1.
NP_003984.2. NM_003993.3. [P49760-3]
UniGeneiHs.73986.

Genome annotation databases

EnsembliENST00000361168; ENSP00000354856; ENSG00000176444. [P49760-3]
ENST00000368361; ENSP00000357345; 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:
EMBLi
GenBanki
DDBJi
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 ]
CCDS72939.1. [P49760-1 ]
PIRi S53637.
S53638.
RefSeqi NP_001281267.1. NM_001294338.1. [P49760-1 ]
NP_001281268.1. NM_001294339.1.
NP_003984.2. NM_003993.3. [P49760-3 ]
UniGenei Hs.73986.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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. 43 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 ]
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.
GeneTreei ENSGT00580000081366.
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

Bgeei P49760.
CleanExi HS_CLK2.
ExpressionAtlasi P49760. baseline and differential.
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.
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: October 29, 2014
This is version 151 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