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P49761 (CLK3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dual specificity protein kinase CLK3

EC=2.7.12.1
Alternative name(s):
CDC-like kinase 3
Gene names
Name:CLK3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length638 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.11

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

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

Subcellular location

Isoform 1: Nucleus. Cytoplasm By similarity. Cytoplasmic vesiclesecretory vesicleacrosome By similarity Ref.6.

Isoform 2: Nucleus speckle. Note: Co-localizes with serine- and arginine-rich (SR) proteins in the nuclear speckles. Ref.6

Tissue specificity

Endothelial cells. Ref.11

Post-translational modification

Autophosphorylates on all three types of residues By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. Lammer subfamily.

Contains 1 protein kinase domain.

Sequence caution

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.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoplasmic vesicle
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
Tyrosine-protein kinase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from direct assay Ref.6. Source: UniProtKB

regulation of RNA splicing

Inferred from direct assay Ref.6. Source: UniProtKB

   Cellular_componentacrosomal vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

intermediate filament cytoskeleton

Inferred from direct assay. Source: HPA

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 16189514PubMed 21516116PubMed 23455924. Source: IntAct

protein serine/threonine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein serine/threonine/tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CLK2P497603EBI-745579,EBI-750020
SUV39H1O434632EBI-745579,EBI-349968

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 4 (identifier: P49761-4)

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 1 (identifier: P49761-1)

Also known as: Long;

The sequence of this isoform differs from the canonical sequence as follows:
     1-148: Missing.
Isoform 2 (identifier: P49761-2)

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.
Isoform 3 (identifier: P49761-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 638638Dual specificity protein kinase CLK3
PRO_0000085870

Regions

Domain304 – 620317Protein kinase
Nucleotide binding310 – 3189ATP By similarity
Compositional bias167 – 26498Arg-rich

Sites

Active site4311Proton acceptor By similarity
Binding site3341ATP By similarity

Amino acid modifications

Modified residue1551Phosphotyrosine Ref.10
Modified residue1571Phosphoserine Ref.10 Ref.12
Modified residue2151Phosphoserine Ref.13
Modified residue2241Phosphoserine Ref.10 Ref.13
Modified residue2261Phosphoserine Ref.10 Ref.13
Modified residue2831Phosphoserine Ref.9

Natural variations

Alternative sequence1 – 148148Missing in isoform 1, isoform 2 and isoform 3.
VSP_026138
Alternative sequence272 – 30029RSQQS…IGDWL → MRLWGTWVKAPLARWWSAWT MPEGSLRLP in isoform 2.
VSP_004858
Alternative sequence301 – 638338Missing in isoform 2.
VSP_004859
Alternative sequence306 – 32823Missing in isoform 3.
VSP_004860
Natural variant4861R → C. Ref.17
VAR_040413
Natural variant6071Q → R. Ref.17
VAR_045579
Natural variant6281R → W. Ref.17
VAR_045580

Experimental info

Sequence conflict280 – 2812SS → TG in AAA61484. Ref.1

Secondary structure

............................................................ 638
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 4 [UniParc].

Last modified June 12, 2007. Version 3.
Checksum: D3B60A9DB4ECEC94

FASTA63873,515
        10         20         30         40         50         60 
MPVLSARRRE LADHAGSGRR SGPSPTARSG PHLSALRAQP ARAAHLSGRG TYVRRDTAGG 

        70         80         90        100        110        120 
GPGQARPLGP PGTSLLGRGA RRSGEGWCPG AFESGARAAR PPSRVEPRLA TAASREGAGL 

       130        140        150        160        170        180 
PRAEVAAGSG RGARSGEWGL AAAGAWETMH HCKRYRSPEP DPYLSYRWKR RRSYSREHEG 

       190        200        210        220        230        240 
RLRYPSRREP PPRRSRSRSH DRLPYQRRYR ERRDSDTYRC EERSPSFGED YYGPSRSRHR 

       250        260        270        280        290        300 
RRSRERGPYR TRKHAHHCHK RRTRSCSSAS SRSQQSSKRS SRSVEDDKEG HLVCRIGDWL 

       310        320        330        340        350        360 
QERYEIVGNL GEGTFGKVVE CLDHARGKSQ VALKIIRNVG KYREAARLEI NVLKKIKEKD 

       370        380        390        400        410        420 
KENKFLCVLM SDWFNFHGHM CIAFELLGKN TFEFLKENNF QPYPLPHVRH MAYQLCHALR 

       430        440        450        460        470        480 
FLHENQLTHT DLKPENILFV NSEFETLYNE HKSCEEKSVK NTSIRVADFG SATFDHEHHT 

       490        500        510        520        530        540 
TIVATRHYRP PEVILELGWA QPCDVWSIGC ILFEYYRGFT LFQTHENREH LVMMEKILGP 

       550        560        570        580        590        600 
IPSHMIHRTR KQKYFYKGGL VWDENSSDGR YVKENCKPLK SYMLQDSLEH VQLFDLMRRM 

       610        620        630 
LEFDPAQRIT LAEALLHPFF AGLTPEERSF HTSRNPSR 

« Hide

Isoform 1 (Long) [UniParc].

Checksum: 86A342ABB8AB24CA
Show »

FASTA49058,588
Isoform 2 (Short) [UniParc].

Checksum: 5BABA6574A0E9801
Show »

FASTA15218,971
Isoform 3 [UniParc].

Checksum: 2890E88AE23AE7BC
Show »

FASTA46756,207

References

« Hide '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] [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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"An unappreciated role for RNA surveillance."
Hillman R.T., Green R.E., Brenner S.E.
Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract]
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]"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] [Europe PMC] [Abstract]
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]"Crystal structure of CLK3."
Papagrigoriou E., Rellos P., Das S., Ugochukwu E., Turnbull A., von Delft F., Bunkoczi G., Sobott F., Bullock A., Fedorov O., Gileadi C., Savitsky P., Edwards A., Aerrowsmith C., Weigel J., Sundstrom M., Knapp S.
Submitted (NOV-2005) to the PDB data bank
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS10265.1. [P49761-1]
CCDS45304.1. [P49761-4]
PIRS53639.
S53640.
RefSeqNP_001123500.1. NM_001130028.1. [P49761-4]
NP_003983.2. NM_003992.4. [P49761-1]
XP_005254210.1. XM_005254153.2. [P49761-1]
UniGeneHs.584748.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EU9X-ray1.53A284-638[»]
2EXEX-ray2.35A275-631[»]
2WU6X-ray1.92A275-632[»]
2WU7X-ray2.25A275-632[»]
3RAWX-ray2.09A/B275-632[»]
ProteinModelPortalP49761.
SMRP49761. Positions 284-629.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107609. 46 interactions.
IntActP49761. 33 interactions.
MINTMINT-1448658.
STRING9606.ENSP00000391518.

Chemistry

BindingDBP49761.
ChEMBLCHEMBL4226.
GuidetoPHARMACOLOGY1992.

PTM databases

PhosphoSiteP49761.

Polymorphism databases

DMDM148887358.

Proteomic databases

MaxQBP49761.
PaxDbP49761.
PRIDEP49761.

Protocols and materials databases

DNASU1198.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000345005; ENSP00000344112; ENSG00000179335. [P49761-1]
ENST00000348245; ENSP00000321136; ENSG00000179335. [P49761-2]
ENST00000395066; ENSP00000378505; ENSG00000179335. [P49761-4]
ENST00000483723; ENSP00000431825; ENSG00000179335. [P49761-2]
GeneID1198.
KEGGhsa:1198.
UCSCuc002ayg.4. human. [P49761-4]

Organism-specific databases

CTD1198.
GeneCardsGC15P074900.
HGNCHGNC:2071. CLK3.
HPAHPA046817.
MIM602990. gene.
neXtProtNX_P49761.
PharmGKBPA26597.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000203417.
HOVERGENHBG107720.
KOK08823.
OMANENKSCE.
OrthoDBEOG7TBC1V.
PhylomeDBP49761.
TreeFamTF101041.

Enzyme and pathway databases

BRENDA2.7.12.1. 2681.
SignaLinkP49761.

Gene expression databases

ArrayExpressP49761.
BgeeP49761.
CleanExHS_CLK3.
GenevestigatorP49761.

Family and domain databases

InterProIPR011009. 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]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP49761.
GeneWikiCLK3_(gene).
GenomeRNAi1198.
NextBio4949.
PROP49761.
SOURCESearch...

Entry information

Entry nameCLK3_HUMAN
AccessionPrimary (citable) accession number: P49761
Secondary accession number(s): D3DW59 expand/collapse secondary AC list , Q53Y48, Q9BRS3, Q9BUJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: June 12, 2007
Last modified: July 9, 2014
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM