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P49759

- CLK1_HUMAN

UniProt

P49759 - CLK1_HUMAN

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Protein
Dual specificity protein kinase CLK1
Gene
CLK1, CLK
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 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 By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei191 – 1911ATP By similarity
Active sitei288 – 2881Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi167 – 1759ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. non-membrane spanning protein tyrosine kinase activity Source: ProtInc
  3. protein serine/threonine kinase activity Source: UniProtKB
  4. protein serine/threonine/tyrosine kinase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. cell proliferation Source: ProtInc
  2. peptidyl-serine phosphorylation Source: Ensembl
  3. peptidyl-threonine phosphorylation Source: Ensembl
  4. protein autophosphorylation Source: Ensembl
  5. 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.
SignaLinkiP49759.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity protein kinase CLK1 (EC:2.7.12.1)
Alternative name(s):
CDC-like kinase 1
Gene namesi
Name:CLK1
Synonyms:CLK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:2068. CLK1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26594.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 484484Dual specificity protein kinase CLK1
PRO_0000085866Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei61 – 611Phosphoserine1 Publication
Modified residuei138 – 1381Phosphothreonine1 Publication
Modified residuei140 – 1401Phosphoserine4 Publications

Post-translational modificationi

Autophosphorylates on all three types of residues By similarity.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP49759.
PaxDbiP49759.
PRIDEiP49759.

PTM databases

PhosphoSiteiP49759.

Expressioni

Tissue specificityi

Endothelial cells.1 Publication

Gene expression databases

ArrayExpressiP49759.
BgeeiP49759.
CleanExiHS_CLK1.
GenevestigatoriP49759.

Organism-specific databases

HPAiCAB033141.

Interactioni

Subunit structurei

Interacts with PPIG and UBL5.1 Publication

Protein-protein interaction databases

BioGridi107606. 17 interactions.
IntActiP49759. 9 interactions.
MINTiMINT-8417657.
STRINGi9606.ENSP00000326830.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi148 – 1503
Turni158 – 1603
Beta strandi161 – 17010
Beta strandi173 – 1808
Turni181 – 1855
Beta strandi187 – 1937
Helixi197 – 21620
Beta strandi227 – 2337
Beta strandi236 – 2427
Helixi248 – 2547
Turni255 – 2573
Helixi262 – 28120
Helixi291 – 2933
Beta strandi294 – 2974
Beta strandi301 – 3055
Beta strandi312 – 3176
Beta strandi321 – 3233
Helixi343 – 3453
Helixi348 – 3514
Helixi359 – 37416
Helixi384 – 39512
Helixi400 – 4056
Helixi409 – 4113
Helixi424 – 4329
Helixi436 – 4394
Helixi445 – 45713
Turni462 – 4643
Helixi468 – 4714
Helixi475 – 4817

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z57X-ray1.70A148-484[»]
2VAGX-ray1.80A148-484[»]
ProteinModelPortaliP49759.
SMRiP49759. Positions 97-482.

Miscellaneous databases

EvolutionaryTraceiP49759.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini161 – 477317Protein kinase
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000203417.
HOVERGENiHBG107720.
InParanoidiP49759.
KOiK08823.
OMAiMLSQDVE.
OrthoDBiEOG7TBC1V.
PhylomeDBiP49759.
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: P49759-1) [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

MRHSKRTYCP DWDDKDWDYG KWRSSSSHKR RKRSHSSAQE NKRCKYNHSK    50
MCDSHYLESR SINEKDYHSR RYIDEYRNDY TQGCEPGHRQ RDHESRYQNH 100
SSKSSGRSGR SSYKSKHRIH HSTSHRRSHG KSHRRKRTRS VEDDEEGHLI 150
CQSGDVLSAR YEIVDTLGEG AFGKVVECID HKAGGRHVAV KIVKNVDRYC 200
EAARSEIQVL EHLNTTDPNS TFRCVQMLEW FEHHGHICIV FELLGLSTYD 250
FIKENGFLPF RLDHIRKMAY QICKSVNFLH SNKLTHTDLK PENILFVQSD 300
YTEAYNPKIK RDERTLINPD IKVVDFGSAT YDDEHHSTLV STRHYRAPEV 350
ILALGWSQPC DVWSIGCILI EYYLGFTVFP THDSKEHLAM MERILGPLPK 400
HMIQKTRKRK YFHHDRLDWD EHSSAGRYVS RRCKPLKEFM LSQDVEHERL 450
FDLIQKMLEY DPAKRITLRE ALKHPFFDLL KKSI 484
Length:484
Mass (Da):57,291
Last modified:September 23, 2008 - v2
Checksum:iF34B5B44988BD118
GO
Isoform 2 (identifier: P49759-2) [UniParc]FASTAAdd to Basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     131-136: KSHRRK → MKLLIL
     137-484: 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:136
Mass (Da):16,570
Checksum:i3A1B92FD19E2A521
GO
Isoform 3 (identifier: P49759-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAAGRRPASALWPERRGSPLRGDLLGFQNVREPSSCGETLSGM

Note: No experimental confirmation available.

Show »
Length:526
Mass (Da):61,757
Checksum:i8514814549CC0655
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti61 – 611S → F.1 Publication
Corresponds to variant rs55989135 [ dbSNP | Ensembl ].
VAR_040409
Natural varianti99 – 991N → D.
Corresponds to variant rs6735666 [ dbSNP | Ensembl ].
VAR_046551
Natural varianti118 – 1181R → G.1 Publication
Corresponds to variant rs56135616 [ dbSNP | Ensembl ].
VAR_040410
Natural varianti307 – 3071P → S.1 Publication
Corresponds to variant rs35412475 [ dbSNP | Ensembl ].
VAR_040411
Natural varianti440 – 4401M → T.1 Publication
Corresponds to variant rs35393352 [ dbSNP | Ensembl ].
VAR_040412
Natural varianti459 – 4591E → G.
Corresponds to variant rs12709 [ dbSNP | Ensembl ].
VAR_051620

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MAAGRRPASALWPERRGSPL RGDLLGFQNVREPSSCGETL SGM in isoform 3.
VSP_043578
Alternative sequencei131 – 1366KSHRRK → MKLLIL in isoform 2.
VSP_004852
Alternative sequencei137 – 484348Missing in isoform 2.
VSP_004853Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti432 – 4321R → A in AAA61480. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L29219 mRNA. Translation: AAA61480.1.
L29222 mRNA. Translation: AAB59459.1.
AK289365 mRNA. Translation: BAF82054.1.
AK294295 mRNA. Translation: BAG57578.1.
AC005037 Genomic DNA. Translation: AAY14722.1.
CH471063 Genomic DNA. Translation: EAW70217.1.
BC028149 mRNA. Translation: AAH28149.1.
BC031549 mRNA. Translation: AAH31549.1.
CCDSiCCDS2331.1. [P49759-1]
CCDS54427.1. [P49759-3]
PIRiS53641.
RefSeqiNP_001155879.1. NM_001162407.1. [P49759-3]
NP_004062.2. NM_004071.3. [P49759-1]
UniGeneiHs.433732.

Genome annotation databases

EnsembliENST00000321356; ENSP00000326830; ENSG00000013441. [P49759-1]
ENST00000432425; ENSP00000400487; ENSG00000013441. [P49759-2]
ENST00000434813; ENSP00000394734; ENSG00000013441. [P49759-3]
GeneIDi1195.
KEGGihsa:1195.
UCSCiuc002uwe.2. human. [P49759-1]
uc010zhi.1. human. [P49759-3]

Polymorphism databases

DMDMi206729857.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L29219 mRNA. Translation: AAA61480.1 .
L29222 mRNA. Translation: AAB59459.1 .
AK289365 mRNA. Translation: BAF82054.1 .
AK294295 mRNA. Translation: BAG57578.1 .
AC005037 Genomic DNA. Translation: AAY14722.1 .
CH471063 Genomic DNA. Translation: EAW70217.1 .
BC028149 mRNA. Translation: AAH28149.1 .
BC031549 mRNA. Translation: AAH31549.1 .
CCDSi CCDS2331.1. [P49759-1 ]
CCDS54427.1. [P49759-3 ]
PIRi S53641.
RefSeqi NP_001155879.1. NM_001162407.1. [P49759-3 ]
NP_004062.2. NM_004071.3. [P49759-1 ]
UniGenei Hs.433732.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Z57 X-ray 1.70 A 148-484 [» ]
2VAG X-ray 1.80 A 148-484 [» ]
ProteinModelPortali P49759.
SMRi P49759. Positions 97-482.
ModBasei Search...

Protein-protein interaction databases

BioGridi 107606. 17 interactions.
IntActi P49759. 9 interactions.
MINTi MINT-8417657.
STRINGi 9606.ENSP00000326830.

Chemistry

BindingDBi P49759.
ChEMBLi CHEMBL4224.
GuidetoPHARMACOLOGYi 1990.

PTM databases

PhosphoSitei P49759.

Polymorphism databases

DMDMi 206729857.

Proteomic databases

MaxQBi P49759.
PaxDbi P49759.
PRIDEi P49759.

Protocols and materials databases

DNASUi 1195.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000321356 ; ENSP00000326830 ; ENSG00000013441 . [P49759-1 ]
ENST00000432425 ; ENSP00000400487 ; ENSG00000013441 . [P49759-2 ]
ENST00000434813 ; ENSP00000394734 ; ENSG00000013441 . [P49759-3 ]
GeneIDi 1195.
KEGGi hsa:1195.
UCSCi uc002uwe.2. human. [P49759-1 ]
uc010zhi.1. human. [P49759-3 ]

Organism-specific databases

CTDi 1195.
GeneCardsi GC02M201717.
HGNCi HGNC:2068. CLK1.
HPAi CAB033141.
MIMi 601951. gene.
neXtProti NX_P49759.
PharmGKBi PA26594.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000203417.
HOVERGENi HBG107720.
InParanoidi P49759.
KOi K08823.
OMAi MLSQDVE.
OrthoDBi EOG7TBC1V.
PhylomeDBi P49759.
TreeFami TF101041.

Enzyme and pathway databases

BRENDAi 2.7.12.1. 2681.
SignaLinki P49759.

Miscellaneous databases

ChiTaRSi CLK1. human.
EvolutionaryTracei P49759.
GeneWikii CLK1.
GenomeRNAii 1195.
NextBioi 4936.
PROi P49759.
SOURCEi Search...

Gene expression databases

ArrayExpressi P49759.
Bgeei P49759.
CleanExi HS_CLK1.
Genevestigatori P49759.

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. "Molecular cloning of a novel human cdc2/CDC28-like protein kinase."
    Johnson K.W., Smith K.A.
    J. Biol. Chem. 266:3402-3407(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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 2).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Tissue: Amygdala.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 2).
    Tissue: Blood and Bone.
  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. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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-61 AND SER-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-138 AND SER-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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] PHE-61; GLY-118; SER-307 AND THR-440.

Entry informationi

Entry nameiCLK1_HUMAN
AccessioniPrimary (citable) accession number: P49759
Secondary accession number(s): B4DFW7, Q0P694, Q8N5V8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 23, 2008
Last modified: July 9, 2014
This is version 142 of the entry and version 2 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 2
    Human chromosome 2: 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

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