Reviewed, UniProtKB/Swiss-Prot P49760 (CLK2_HUMAN)

Names and origin

Protein names

Recommended name:
    Dual specificity protein kinase CLK2
    EC=2.7.12.1
Alternative name(s):
    CDC-like kinase 2

Gene names

Name:

CLK2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	499 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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 By similarity. Ref.5
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.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Ref.1 Traceable author statement. Source: ProtInc protein tyrosine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: P49760-1)

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.

Isoform Short (identifier: P49760-2)

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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 499	499	Dual specificity protein kinase CLK2		PRO_0000085868
Regions
	Domain	163 – 479	317	Protein kinase
	Nucleotide binding	169 – 177	9	ATP By similarity
Sites
	Active site	290	1	Proton acceptor By similarity
	Binding site	193	1	ATP By similarity
Amino acid modifications
	Modified residue	7	1	Phosphotyrosine
	Modified residue	50	1	Phosphoserine
	Modified residue	51	1	Phosphotyrosine Ref.7
	Modified residue	83	1	Phosphoserine
	Modified residue	98	1	Phosphoserine Ref.7
	Modified residue	106	1	Phosphoserine
	Modified residue	142	1	Phosphoserine Ref.7 Ref.8
	Modified residue	153	1	Phosphotyrosine
	Modified residue	167	1	Phosphoserine
	Modified residue	493	1	Phosphoserine Ref.7
Natural variations
	Alternative sequence	134 – 139	6	QHSSRR → MKSLAP in isoform Short.		VSP_004856
	Alternative sequence	140 – 499	360	Missing in isoform Short.		VSP_004857
Experimental info
	Sequence conflict	134	1	Missing in AAH14067. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified October 1, 1996. Version 1. Checksum: E43BBF3BAD6EF991	FASTA	499	60,090
	10 20 30 40 50 60 MPHPRRYHSS ERGSRGSYRE HYRSRKHKRR RSRSWSSSSD RTRRRRREDS YHVRSRSSYD 70 80 90 100 110 120 DRSSDRRVYD RRYCGSYRRN DYSRDRGDAY YDTDYRHSYE YQRENSSYRS QRSSRRKHRR 130 140 150 160 170 180 RRRRSRTFSR SSSQHSSRRA KSVEDDAEGH LIYHVGDWLQ ERYEIVSTLG EGTFGRVVQC 190 200 210 220 230 240 VDHRRGGARV ALKIIKNVEK YKEAARLEIN VLEKINEKDP DNKNLCVQMF DWFDYHGHMC 250 260 270 280 290 300 ISFELLGLST FDFLKDNNYL PYPIHQVRHM AFQLCQAVKF LHDNKLTHTD LKPENILFVN 310 320 330 340 350 360 SDYELTYNLE KKRDERSVKS TAVRVVDFGS ATFDHEHHST IVSTRHYRAP EVILELGWSQ 370 380 390 400 410 420 PCDVWSIGCI IFEYYVGFTL FQTHDNREHL AMMERILGPI PSRMIRKTRK QKYFYRGRLD 430 440 450 460 470 480 WDENTSAGRY VRENCKPLRR YLTSEAEEHH QLFDLIESML EYEPAKRLTL GEALQHPFFA 490 RLRAEPPNKL WDSSRDISR
	Isoform Short. Checksum: CC9C9C63B3B07667	FASTA	139	17,569
	10 20 30 40 50 60 MPHPRRYHSS ERGSRGSYRE HYRSRKHKRR RSRSWSSSSD RTRRRRREDS YHVRSRSSYD 70 80 90 100 110 120 DRSSDRRVYD RRYCGSYRRN DYSRDRGDAY YDTDYRHSYE YQRENSSYRS QRSSRRKHRR 130 RRRRSRTFSR SSSMKSLAP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7990150] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
[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: 9331372] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG).
[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: 16710414] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG). 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: 8910305] [Abstract] Cited for: FUNCTION.
[6]	"An unappreciated role for RNA surveillance." Hillman R.T., Green R.E., Brenner S.E. Genome Biol. 5:R8.1-R8.16(2004) [PubMed: 14759258] [Abstract] Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[7]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-51; SER-98; SER-142 AND SER-493, MASS SPECTROMETRY.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, MASS SPECTROMETRY.
[9]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-7; SER-50; SER-83; SER-106; SER-142; TYR-153; SER-167 AND SER-493, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L29218 mRNA. Translation: AAA61482.1. L29216 mRNA. Translation: AAA61481.1. AF023268 Genomic DNA. Translation: AAC51817.1. AL713999 Genomic DNA. No translation available. BC014067 mRNA. Translation: AAH14067.1. BC053603 mRNA. Translation: AAH53603.1.
IPI	IPI00028071. IPI00937288.
PIR	S53637. S53638.
RefSeq	NP_003984.2.
UniGene	Hs.73986
3D structure databases
SMR	P49760. Positions 143-485.
ModBase	Search...
Protein-protein interaction databases
IntAct	P49760. 2 interactions.
STRING	P49760.
PTM databases
PhosphoSite	P49760.
Proteomic databases
PRIDE	P49760.
Genome annotation databases
Ensembl	ENST00000368361; ENSP00000357345; ENSG00000176444; Homo sapiens. [Genome view]
GeneID	1196.
KEGG	hsa:1196.
UCSC	uc001fjy.1. human.
Organism-specific databases
CTD	1196.
GeneCards	GC01M153499.
H-InvDB	HIX0001112.
HGNC	HGNC:2069. CLK2.
MIM	602989. gene.
PharmGKB	PA26595.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG11725.
HOGENOM	HBG755340.
HOVERGEN	P49760.
InParanoid	P49760.
OMA	SEAEDHH.
OrthoDB	EOG9X3KM2.
PhylomeDB	P49760.
Enzyme and pathway databases
BRENDA	2.7.12.1. 247.
Gene expression databases
ArrayExpress	P49760.
Bgee	P49760.
CleanEx	HS_CLK2.
Genevestigator	P49760.
GermOnline	ENSG00000176444. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_prot_kinase-like_dom. IPR008271. Ser/Thr_prot_kinase_AS. IPR002290. Ser/Thr_prot_kinase_dom. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	4940.
SOURCE	Search...

Entry information

Entry name

CLK2_HUMAN

Accession

Primary (citable) accession number: P49760
Secondary accession number(s): B5MBX6, Q96CQ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	February 9, 2010
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.