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Q9Y6E0 (STK24_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. 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:
Serine/threonine-protein kinase 24

EC=2.7.11.1
Alternative name(s):
Mammalian STE20-like protein kinase 3
Short name=MST-3
STE20-like kinase MST3

Cleaved into the following 2 chains:

  1. Serine/threonine-protein kinase 24 36 kDa subunit
    Alternative name(s):
    Mammalian STE20-like protein kinase 3 N-terminal
    Short name=MST3/N
  2. Serine/threonine-protein kinase 24 12 kDa subunit
    Alternative name(s):
    Mammalian STE20-like protein kinase 3 C-terminal
    Short name=MST3/C
Gene names
Name:STK24
Synonyms:MST3, STK3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length443 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine-protein kinase that acts on both serine and threonine residues and promotes apoptosis in response to stress stimuli and caspase activation. Mediates oxidative-stress-induced cell death by modulating phosphorylation of JNK1-JNK2 (MAPK8 and MAPK9), p38 (MAPK11, MAPK12, MAPK13 and MAPK14) during oxidative stress. Plays a role in a staurosporine-induced caspase-independent apoptotic pathway by regulating the nuclear translocation of AIFM1 and ENDOG and the DNase activity associated with ENDOG. Phosphorylates STK38L on 'Thr-442' and stimulates its kinase activity. Regulates cellular migration with alteration of PTPN12 activity and PXN phosphorylation: phosphorylates PTPN12 and inhibits its activity and may regulate PXN phosphorylation through PTPN12. May act as a key regulator of axon regeneration in the optic nerve and radial nerve. Ref.9 Ref.11 Ref.13 Ref.16 Ref.17

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Mg2+ or Mn2+ or Co2+ or Zn2+. Ref.8

Subunit structure

Monomer. Interacts with CTTNBP2NL. Ref.14 Ref.21

Subcellular location

Cytoplasm. Nucleus. Membrane. Note: The truncated form (MST3/N) translocates to the nucleus. Colocalizes with STK38L in the membrane. Ref.6 Ref.7 Ref.9

Tissue specificity

Isoform A is ubiquitous. Isoform B is expressed in brain with high expression in hippocampus and cerebral cortex.

Post-translational modification

Proteolytically processed by caspases during apoptosis. Proteolytic cleavage results in kinase activation, nuclear translocation of the truncated form (MST3/N) and the induction of apoptosis.

Isoform B is activated by phosphorylation by PKA. Oxidative stress induces phosphorylation. Activated by autophosphorylation at Thr-190 and phosphorylation at this site is essential for its function. Manganese, magnesium and cobalt-dependent autophosphorylation is mainly on threonine residues while zinc-dependent autophosphorylation is on both serine and threonine residues.

Sequence similarities

Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.

Contains 1 protein kinase domain.

Biophysicochemical properties

Kinetic parameters:

KM=12.8 µM for manganese ions Ref.8

KM=34.9 µM for cobalt ions

KM=22.7 µM for magnesium ions

KM=4.1 µM for zinc ions

Vmax=2623.1 pmol/min/mg enzyme for manganese ions

Vmax=1746.1 pmol/min/mg enzyme for cobalt ions

Vmax=129.1 pmol/min/mg enzyme for magnesium ions

Vmax=22.3 pmol/min/mg enzyme for zinc ions

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Traceable author statement. Source: Reactome

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

execution phase of apoptosis

Inferred from mutant phenotype Ref.6. Source: UniProtKB

intrinsic apoptotic signaling pathway in response to oxidative stress

Inferred from mutant phenotype Ref.13. Source: UniProtKB

negative regulation of cell migration

Inferred from mutant phenotype Ref.11. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay Ref.11. Source: UniProtKB

protein phosphorylation

Inferred from direct assay Ref.13. Source: UniProtKB

regulation of axon regeneration

Inferred from mutant phenotype Ref.16. Source: UniProtKB

signal transduction

Traceable author statement Ref.1. Source: ProtInc

signal transduction by phosphorylation

Inferred from Biological aspect of Ancestor. Source: GOC

   Cellular_componentcytoplasm

Inferred from direct assay Ref.6. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 16189514PubMed 17657516Ref.14PubMed 21516116PubMed 23455922. Source: IntAct

protein kinase activity

Traceable author statement Ref.1. Source: ProtInc

protein serine/threonine kinase activity

Inferred from direct assay Ref.9Ref.11. Source: UniProtKB

receptor signaling protein serine/threonine kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform B (identifier: Q9Y6E0-1)

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 A (identifier: Q9Y6E0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MDSRAQLWGLALNKRRATLPHPGGST → MAHSPVQSGLPGMQ
Note: Initiator Met-1 is removed. Contains a phosphoserine at position 4. Contains a N-acetylalanine at position 2.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 443443Serine/threonine-protein kinase 24
PRO_0000086711
Chain1 – 325325Serine/threonine-protein kinase 24 36 kDa subunit
PRO_0000413618
Chain326 – 443118Serine/threonine-protein kinase 24 12 kDa subunit
PRO_0000413619

Regions

Domain36 – 286251Protein kinase
Nucleotide binding42 – 509ATP
Nucleotide binding112 – 1143ATP
Region335 – 38652Nuclear export signal (NES)
Motif278 – 29215Bipartite nuclear localization signal

Sites

Active site1561Proton acceptor By similarity
Metal binding1611Magnesium
Metal binding1741Magnesium
Binding site651ATP
Site325 – 3262Cleavage; by caspase-3, caspase-7 and caspase-8

Amino acid modifications

Modified residue181Phosphothreonine; by PKA Ref.2
Modified residue1901Phosphothreonine; by autocatalysis Ref.11 Ref.13 Ref.21
Modified residue3201Phosphoserine Ref.10

Natural variations

Alternative sequence1 – 2626MDSRA…PGGST → MAHSPVQSGLPGMQ in isoform A.
VSP_004874
Natural variant4141A → V. Ref.2 Ref.22
Corresponds to variant rs55953606 [ dbSNP | Ensembl ].
VAR_041148
Natural variant4261L → I. Ref.22
Corresponds to variant rs55897869 [ dbSNP | Ensembl ].
VAR_041149

Experimental info

Mutagenesis181T → A: Loss of phosphorylation by PKA. Ref.2
Mutagenesis651K → A: Loss of activity and autophosphorylation. Ref.6
Mutagenesis1901T → A: Loss of activity and autophosphorylation. Ref.11
Mutagenesis3211D → N: Loss of proteolytic cleavage by caspases. Ref.6

Secondary structure

....................................................... 443
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1999. Version 1.
Checksum: 4A9FF1F6B6A88A97

FASTA44349,308
        10         20         30         40         50         60 
MDSRAQLWGL ALNKRRATLP HPGGSTNLKA DPEELFTKLE KIGKGSFGEV FKGIDNRTQK 

        70         80         90        100        110        120 
VVAIKIIDLE EAEDEIEDIQ QEITVLSQCD SPYVTKYYGS YLKDTKLWII MEYLGGGSAL 

       130        140        150        160        170        180 
DLLEPGPLDE TQIATILREI LKGLDYLHSE KKIHRDIKAA NVLLSEHGEV KLADFGVAGQ 

       190        200        210        220        230        240 
LTDTQIKRNT FVGTPFWMAP EVIKQSAYDS KADIWSLGIT AIELARGEPP HSELHPMKVL 

       250        260        270        280        290        300 
FLIPKNNPPT LEGNYSKPLK EFVEACLNKE PSFRPTAKEL LKHKFILRNA KKTSYLTELI 

       310        320        330        340        350        360 
DRYKRWKAEQ SHDDSSSEDS DAETDGQASG GSDSGDWIFT IREKDPKNLE NGALQPSDLD 

       370        380        390        400        410        420 
RNKMKDIPKR PFSQCLSTII SPLFAELKEK SQACGGNLGS IEELRGAIYL AEEACPGISD 

       430        440 
TMVAQLVQRL QRYSLSGGGT SSH 

« Hide

Isoform A [UniParc].

Checksum: 26D863FDFEDF90AD
Show »

FASTA43147,913

References

« Hide 'large scale' references
[1]"Cloning and characterization of a human STE20-like protein kinase with unusual cofactor requirements."
Schinkmann K., Blenis J.
J. Biol. Chem. 272:28695-28703(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[2]"Identification of a human brain-specific isoform of mammalian STE20-like kinase 3 that is regulated by cAMP-dependent protein kinase."
Zhou T.-H., Ling K., Guo J., Zhou H., Wu Y.-L., Jing Q., Ma L., Pei G.
J. Biol. Chem. 275:2513-2519(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), PHOSPHORYLATION AT THR-18, MUTAGENESIS OF THR-18, VARIANT VAL-414.
Tissue: Brain.
[3]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [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 (JUL-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 A).
Tissue: Skin.
[6]"Caspase activation of mammalian sterile 20-like kinase 3 (Mst3)."
Huang C.Y., Wu Y.M., Hsu C.Y., Lee W.S., Lai M.D., Lu T.J., Huang C.L., Leu T.H., Shih H.M., Fang H.I., Robinson D.R., Kung H.J., Yuan C.J.
J. Biol. Chem. 277:34367-34374(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-65 AND ASP-321.
[7]"Identification and characterization of the nuclear import and export signals of the mammalian Ste20-like protein kinase 3."
Lee W.S., Hsu C.Y., Wang P.L., Huang C.Y., Chang C.H., Yuan C.J.
FEBS Lett. 572:41-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, NUCLEAR EXPORT SIGNAL.
[8]"Zinc ion acts as a cofactor for serine/threonine kinase MST3 and has a distinct role in autophosphorylation of MST3."
Lu T.J., Huang C.Y., Yuan C.J., Lee Y.C., Leu T.H., Chang W.C., Lu T.L., Jeng W.Y., Lai M.D.
J. Inorg. Biochem. 99:1306-1313(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
[9]"Regulation of NDR protein kinase by hydrophobic motif phosphorylation mediated by the mammalian Ste20-like kinase MST3."
Stegert M.R., Hergovich A., Tamaskovic R., Bichsel S.J., Hemmings B.A.
Mol. Cell. Biol. 25:11019-11029(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[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-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Inhibition of cell migration by autophosphorylated mammalian sterile 20-like kinase 3 (MST3) involves paxillin and protein-tyrosine phosphatase-PEST."
Lu T.J., Lai W.Y., Huang C.Y., Hsieh W.J., Yu J.S., Hsieh Y.J., Chang W.T., Leu T.H., Chang W.C., Chuang W.J., Tang M.J., Chen T.Y., Lu T.L., Lai M.D.
J. Biol. Chem. 281:38405-38417(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT THR-190, MUTAGENESIS OF THR-190.
[12]"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-4 (ISOFORM A), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Mammalian sterile 20-like kinase 3 (MST3) mediates oxidative-stress-induced cell death by modulating JNK activation."
Chen C.B., Ng J.K., Choo P.H., Wu W., Porter A.G.
Biosci. Rep. 29:405-415(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT THR-190.
[14]"A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein."
Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G., Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I., Aebersold R., Raught B., Gingras A.C.
Mol. Cell. Proteomics 8:157-171(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CTTNBP2NL.
[15]"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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM A), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 (ISOFORM A), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[16]"Mst3b, an Ste20-like kinase, regulates axon regeneration in mature CNS and PNS pathways."
Lorber B., Howe M.L., Benowitz L.I., Irwin N.
Nat. Neurosci. 12:1407-1414(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"Mammalian Ste20-like protein kinase 3 induces a caspase-independent apoptotic pathway."
Lin C.Y., Wu H.Y., Wang P.L., Yuan C.J.
Int. J. Biochem. Cell Biol. 42:98-105(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM A), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 (ISOFORM A), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM A), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 (ISOFORM A), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Structures of human MST3 kinase in complex with adenine, ADP and Mn2+."
Ko T.P., Jeng W.Y., Liu C.I., Lai M.D., Wu C.L., Chang W.J., Shr H.L., Lu T.J., Wang A.H.
Acta Crystallogr. D 66:145-154(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 27-315 IN COMPLEX WITH ADENINE; ADP AND MANGANESE IONS, SUBUNIT, PHOSPHORYLATION AT THR-190.
[22]"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] VAL-414 AND ILE-426.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF024636 mRNA. Translation: AAB82560.1.
AF083420 mRNA. Translation: AAD42039.1.
AL356423, AL137249 Genomic DNA. Translation: CAI13114.1.
AL137249, AL356423 Genomic DNA. Translation: CAI39453.1.
CH471085 Genomic DNA. Translation: EAX08986.1.
BC035578 mRNA. Translation: AAH35578.1.
CCDSCCDS32001.1. [Q9Y6E0-2]
CCDS9488.1. [Q9Y6E0-1]
RefSeqNP_001027467.2. NM_001032296.3. [Q9Y6E0-2]
NP_003567.2. NM_003576.4. [Q9Y6E0-1]
UniGeneHs.508514.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3A7FX-ray1.55A27-315[»]
3A7GX-ray2.00A/B27-315[»]
3A7HX-ray1.96A/B27-315[»]
3A7IX-ray1.45A27-315[»]
3A7JX-ray1.50A27-315[»]
3CKWX-ray1.96A31-323[»]
3CKXX-ray2.70A31-323[»]
3ZHPX-ray2.90C/D31-301[»]
ProteinModelPortalQ9Y6E0.
SMRQ9Y6E0. Positions 27-350, 372-434.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114011. 188 interactions.
DIPDIP-40608N.
IntActQ9Y6E0. 33 interactions.
MINTMINT-3088034.
STRING9606.ENSP00000365730.

Chemistry

BindingDBQ9Y6E0.
ChEMBLCHEMBL5082.
GuidetoPHARMACOLOGY2217.

PTM databases

PhosphoSiteQ9Y6E0.

Polymorphism databases

DMDM13626607.

Proteomic databases

MaxQBQ9Y6E0.
PaxDbQ9Y6E0.
PRIDEQ9Y6E0.

Protocols and materials databases

DNASU8428.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000376547; ENSP00000365730; ENSG00000102572. [Q9Y6E0-1]
ENST00000397517; ENSP00000380651; ENSG00000102572. [Q9Y6E0-2]
GeneID8428.
KEGGhsa:8428.
UCSCuc001vnm.1. human. [Q9Y6E0-1]

Organism-specific databases

CTD8428.
GeneCardsGC13M099103.
HGNCHGNC:11403. STK24.
HPAHPA026435.
HPA026502.
MIM604984. gene.
neXtProtNX_Q9Y6E0.
PharmGKBPA36210.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000234203.
HOVERGENHBG108518.
KOK08838.
OMAGSDDWIF.
PhylomeDBQ9Y6E0.
TreeFamTF354217.

Enzyme and pathway databases

ReactomeREACT_578. Apoptosis.
SignaLinkQ9Y6E0.

Gene expression databases

ArrayExpressQ9Y6E0.
BgeeQ9Y6E0.
CleanExHS_STK24.
HS_STK3.
GenevestigatorQ9Y6E0.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
[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.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSTK24. human.
EvolutionaryTraceQ9Y6E0.
GeneWikiSTK24.
GenomeRNAi8428.
NextBio31540.
PROQ9Y6E0.
SOURCESearch...

Entry information

Entry nameSTK24_HUMAN
AccessionPrimary (citable) accession number: Q9Y6E0
Secondary accession number(s): O14840, Q5JV92
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 142 of the entry and version 1 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 13

Human chromosome 13: entries, gene names and cross-references to MIM