Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P49761

- CLK3_HUMAN

UniProt

P49761 - CLK3_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Dual specificity protein kinase CLK3

Gene

CLK3

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. Phosphorylates SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Leucettine L41 inhibits its kinase activity and affects the regulation of alternative splicing mediated by phosphorylation of SR proteins.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei334 – 3341ATPPROSITE-ProRule annotation
Active sitei431 – 4311Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi310 – 3189ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. protein autophosphorylation Source: Ensembl
  2. protein phosphorylation Source: UniProtKB
  3. regulation of RNA splicing Source: UniProtKB
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.
SignaLinkiP49761.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity protein kinase CLK3 (EC:2.7.12.1)
Alternative name(s):
CDC-like kinase 3
Gene namesi
Name:CLK3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:2071. CLK3.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasmic vesicle Source: UniProtKB-KW
  2. intermediate filament cytoskeleton Source: HPA
  3. membrane Source: UniProtKB
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26597.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 638638Dual specificity protein kinase CLK3PRO_0000085870Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei155 – 1551Phosphotyrosine1 Publication
Modified residuei157 – 1571Phosphoserine2 Publications
Modified residuei215 – 2151Phosphoserine1 Publication
Modified residuei224 – 2241Phosphoserine2 Publications
Modified residuei226 – 2261Phosphoserine2 Publications
Modified residuei283 – 2831Phosphoserine1 Publication

Post-translational modificationi

Autophosphorylates on all three types of residues.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP49761.
PaxDbiP49761.
PRIDEiP49761.

PTM databases

PhosphoSiteiP49761.

Expressioni

Tissue specificityi

Endothelial cells.1 Publication

Gene expression databases

BgeeiP49761.
CleanExiHS_CLK3.
ExpressionAtlasiP49761. baseline and differential.
GenevestigatoriP49761.

Organism-specific databases

HPAiHPA046817.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CLK2P497603EBI-745579,EBI-750020
SUV39H1O434632EBI-745579,EBI-349968

Protein-protein interaction databases

BioGridi107609. 50 interactions.
IntActiP49761. 33 interactions.
MINTiMINT-1448658.
STRINGi9606.ENSP00000391518.

Structurei

Secondary structure

1
638
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni301 – 3033Combined sources
Beta strandi304 – 31310Combined sources
Beta strandi316 – 3238Combined sources
Turni324 – 3285Combined sources
Beta strandi330 – 3367Combined sources
Helixi340 – 35920Combined sources
Beta strandi370 – 3767Combined sources
Beta strandi379 – 3857Combined sources
Helixi391 – 3977Combined sources
Turni398 – 4003Combined sources
Helixi405 – 42319Combined sources
Turni424 – 4263Combined sources
Helixi434 – 4363Combined sources
Beta strandi437 – 4404Combined sources
Beta strandi444 – 4485Combined sources
Turni450 – 4534Combined sources
Beta strandi456 – 4605Combined sources
Beta strandi464 – 4663Combined sources
Helixi469 – 4713Combined sources
Helixi486 – 4883Combined sources
Helixi491 – 4944Combined sources
Helixi502 – 51716Combined sources
Helixi527 – 53812Combined sources
Helixi543 – 5486Combined sources
Helixi552 – 5543Combined sources
Helixi567 – 5759Combined sources
Helixi579 – 5824Combined sources
Helixi588 – 60013Combined sources
Turni605 – 6073Combined sources
Helixi611 – 6144Combined sources
Helixi618 – 6225Combined sources
Helixi625 – 6284Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EU9X-ray1.53A284-638[»]
2EXEX-ray2.35A275-631[»]
2WU6X-ray1.92A275-632[»]
2WU7X-ray2.25A275-632[»]
3RAWX-ray2.09A/B275-632[»]
ProteinModelPortaliP49761.
SMRiP49761. Positions 284-629.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49761.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini304 – 620317Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi167 – 26498Arg-richAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00580000081366.
HOGENOMiHOG000203417.
HOVERGENiHBG107720.
InParanoidiP49761.
KOiK08823.
OMAiNENKSCE.
OrthoDBiEOG7TBC1V.
PhylomeDBiP49761.
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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 4 (identifier: P49761-4) [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
MPVLSARRRE LADHAGSGRR SGPSPTARSG PHLSALRAQP ARAAHLSGRG
60 70 80 90 100
TYVRRDTAGG GPGQARPLGP PGTSLLGRGA RRSGEGWCPG AFESGARAAR
110 120 130 140 150
PPSRVEPRLA TAASREGAGL PRAEVAAGSG RGARSGEWGL AAAGAWETMH
160 170 180 190 200
HCKRYRSPEP DPYLSYRWKR RRSYSREHEG RLRYPSRREP PPRRSRSRSH
210 220 230 240 250
DRLPYQRRYR ERRDSDTYRC EERSPSFGED YYGPSRSRHR RRSRERGPYR
260 270 280 290 300
TRKHAHHCHK RRTRSCSSAS SRSQQSSKRS SRSVEDDKEG HLVCRIGDWL
310 320 330 340 350
QERYEIVGNL GEGTFGKVVE CLDHARGKSQ VALKIIRNVG KYREAARLEI
360 370 380 390 400
NVLKKIKEKD KENKFLCVLM SDWFNFHGHM CIAFELLGKN TFEFLKENNF
410 420 430 440 450
QPYPLPHVRH MAYQLCHALR FLHENQLTHT DLKPENILFV NSEFETLYNE
460 470 480 490 500
HKSCEEKSVK NTSIRVADFG SATFDHEHHT TIVATRHYRP PEVILELGWA
510 520 530 540 550
QPCDVWSIGC ILFEYYRGFT LFQTHENREH LVMMEKILGP IPSHMIHRTR
560 570 580 590 600
KQKYFYKGGL VWDENSSDGR YVKENCKPLK SYMLQDSLEH VQLFDLMRRM
610 620 630
LEFDPAQRIT LAEALLHPFF AGLTPEERSF HTSRNPSR
Length:638
Mass (Da):73,515
Last modified:June 12, 2007 - v3
Checksum:iD3B60A9DB4ECEC94
GO
Isoform 1 (identifier: P49761-1) [UniParc]FASTAAdd to Basket

Also known as: Long

The sequence of this isoform differs from the canonical sequence as follows:
     1-148: Missing.

Show »
Length:490
Mass (Da):58,588
Checksum:i86A342ABB8AB24CA
GO
Isoform 2 (identifier: P49761-2) [UniParc]FASTAAdd to Basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     1-148: Missing.
     272-300: RSQQSSKRSSRSVEDDKEGHLVCRIGDWL → MRLWGTWVKAPLARWWSAWTMPEGSLRLP
     301-638: 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:152
Mass (Da):18,971
Checksum:i5BABA6574A0E9801
GO
Isoform 3 (identifier: P49761-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-148: Missing.
     306-328: Missing.

Show »
Length:467
Mass (Da):56,207
Checksum:i2890E88AE23AE7BC
GO

Sequence cautioni

The sequence AAH02555.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAH19881.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti280 – 2812SS → TG in AAA61484. (PubMed:7990150)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti486 – 4861R → C.1 Publication
VAR_040413
Natural varianti607 – 6071Q → R.1 Publication
VAR_045579
Natural varianti628 – 6281R → W.1 Publication
VAR_045580

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 148148Missing in isoform 1, isoform 2 and isoform 3. 3 PublicationsVSP_026138Add
BLAST
Alternative sequencei272 – 30029RSQQS…IGDWL → MRLWGTWVKAPLARWWSAWT MPEGSLRLP in isoform 2. 1 PublicationVSP_004858Add
BLAST
Alternative sequencei301 – 638338Missing in isoform 2. 1 PublicationVSP_004859Add
BLAST
Alternative sequencei306 – 32823Missing in isoform 3. 1 PublicationVSP_004860Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L29220 mRNA. Translation: AAA61483.1.
L29217 mRNA. Translation: AAA61484.1.
BT006993 mRNA. Translation: AAP35639.1.
AC100835 Genomic DNA. No translation available.
CH471136 Genomic DNA. Translation: EAW99321.1.
CH471136 Genomic DNA. Translation: EAW99322.1.
BC002555 mRNA. Translation: AAH02555.1. Different initiation.
BC006103 mRNA. Translation: AAH06103.1.
BC019881 mRNA. Translation: AAH19881.1. Different initiation.
CCDSiCCDS10265.1. [P49761-1]
CCDS45304.1. [P49761-4]
PIRiS53639.
S53640.
RefSeqiNP_001123500.1. NM_001130028.1. [P49761-4]
NP_003983.2. NM_003992.4. [P49761-1]
XP_005254210.1. XM_005254153.2. [P49761-1]
UniGeneiHs.584748.

Genome annotation databases

EnsembliENST00000345005; ENSP00000344112; ENSG00000179335. [P49761-1]
ENST00000395066; ENSP00000378505; ENSG00000179335. [P49761-4]
ENST00000483723; ENSP00000431825; ENSG00000179335. [P49761-2]
GeneIDi1198.
KEGGihsa:1198.
UCSCiuc002ayg.4. human. [P49761-4]

Polymorphism databases

DMDMi148887358.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L29220 mRNA. Translation: AAA61483.1 .
L29217 mRNA. Translation: AAA61484.1 .
BT006993 mRNA. Translation: AAP35639.1 .
AC100835 Genomic DNA. No translation available.
CH471136 Genomic DNA. Translation: EAW99321.1 .
CH471136 Genomic DNA. Translation: EAW99322.1 .
BC002555 mRNA. Translation: AAH02555.1 . Different initiation.
BC006103 mRNA. Translation: AAH06103.1 .
BC019881 mRNA. Translation: AAH19881.1 . Different initiation.
CCDSi CCDS10265.1. [P49761-1 ]
CCDS45304.1. [P49761-4 ]
PIRi S53639.
S53640.
RefSeqi NP_001123500.1. NM_001130028.1. [P49761-4 ]
NP_003983.2. NM_003992.4. [P49761-1 ]
XP_005254210.1. XM_005254153.2. [P49761-1 ]
UniGenei Hs.584748.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2EU9 X-ray 1.53 A 284-638 [» ]
2EXE X-ray 2.35 A 275-631 [» ]
2WU6 X-ray 1.92 A 275-632 [» ]
2WU7 X-ray 2.25 A 275-632 [» ]
3RAW X-ray 2.09 A/B 275-632 [» ]
ProteinModelPortali P49761.
SMRi P49761. Positions 284-629.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107609. 50 interactions.
IntActi P49761. 33 interactions.
MINTi MINT-1448658.
STRINGi 9606.ENSP00000391518.

Chemistry

BindingDBi P49761.
ChEMBLi CHEMBL4226.
GuidetoPHARMACOLOGYi 1992.

PTM databases

PhosphoSitei P49761.

Polymorphism databases

DMDMi 148887358.

Proteomic databases

MaxQBi P49761.
PaxDbi P49761.
PRIDEi P49761.

Protocols and materials databases

DNASUi 1198.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000345005 ; ENSP00000344112 ; ENSG00000179335 . [P49761-1 ]
ENST00000395066 ; ENSP00000378505 ; ENSG00000179335 . [P49761-4 ]
ENST00000483723 ; ENSP00000431825 ; ENSG00000179335 . [P49761-2 ]
GeneIDi 1198.
KEGGi hsa:1198.
UCSCi uc002ayg.4. human. [P49761-4 ]

Organism-specific databases

CTDi 1198.
GeneCardsi GC15P074900.
HGNCi HGNC:2071. CLK3.
HPAi HPA046817.
MIMi 602990. gene.
neXtProti NX_P49761.
PharmGKBi PA26597.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00580000081366.
HOGENOMi HOG000203417.
HOVERGENi HBG107720.
InParanoidi P49761.
KOi K08823.
OMAi NENKSCE.
OrthoDBi EOG7TBC1V.
PhylomeDBi P49761.
TreeFami TF101041.

Enzyme and pathway databases

BRENDAi 2.7.12.1. 2681.
SignaLinki P49761.

Miscellaneous databases

EvolutionaryTracei P49761.
GeneWikii CLK3_(gene).
GenomeRNAii 1198.
NextBioi 4949.
PROi P49761.
SOURCEi Search...

Gene expression databases

Bgeei P49761.
CleanExi HS_CLK3.
ExpressionAtlasi P49761. baseline and differential.
Genevestigatori P49761.

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. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 137-638 (ISOFORM 4).
    Tissue: Cervix and Placenta.
  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. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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-283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-155; SER-157; SER-224 AND SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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.
  12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; SER-224 AND SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 284-638.
  15. "Crystal structure of the phosphorylated clk3."
    Structural genomics consortium (SGC)
    Submitted (APR-2007) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 275-627.
  16. "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: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 275-632 IN COMPLEX WITH LEUCETTINE L41.
  17. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-486; ARG-607 AND TRP-628.

Entry informationi

Entry nameiCLK3_HUMAN
AccessioniPrimary (citable) accession number: P49761
Secondary accession number(s): D3DW59
, Q53Y48, Q9BRS3, Q9BUJ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: June 12, 2007
Last modified: October 29, 2014
This is version 154 of the entry and version 3 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 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3