Q9Y6E0 (STK24_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	443 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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+.
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. Co-localizes 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 process	Apoptosis
Cellular component	Cytoplasm Membrane Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular component disassembly involved in execution phase of apoptosis Traceable author statement. Source: Reactome induction 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 regulation of axon regeneration Inferred from mutant phenotype Ref.16. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from direct assay Ref.9Ref.11. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CTTNBP2NL	Q9P2B4	4	EBI-740175,EBI-1774273
PDCD10	Q9BUL8	5	EBI-740175,EBI-740195
STRN	O43815	3	EBI-740175,EBI-1046642
TRAF3IP3	Q9Y228	2	EBI-740175,EBI-765817

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: Contains a phosphoserine at position 4. Initiator Met-1 is removed. Contains a N-acetylalanine at position 2.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 443

443

Serine/threonine-protein kinase 24

PRO_0000086711

Chain

1 – 325

325

Serine/threonine-protein kinase 24 36 kDa subunit

PRO_0000413618

Chain

326 – 443

118

Serine/threonine-protein kinase 24 12 kDa subunit

PRO_0000413619

Regions

Domain

36 – 286

251

Protein kinase

Nucleotide binding

42 – 50

9

ATP

Nucleotide binding

112 – 114

3

ATP

Region

335 – 386

52

Nuclear export signal (NES)

Motif

278 – 292

15

Bipartite nuclear localization signal

Sites

Active site

156

1

Proton acceptor By similarity

Metal binding

161

1

Magnesium

Metal binding

174

1

Magnesium

Binding site

65

1

ATP

Site

325 – 326

2

Cleavage; by caspase-3, caspase-7 and caspase-8

Amino acid modifications

Modified residue

18

1

Phosphothreonine; by PKA Ref.2

Modified residue

190

1

Phosphothreonine; by autocatalysis Ref.11 Ref.13 Ref.21

Modified residue

320

1

Phosphoserine Ref.10

Natural variations

Alternative sequence

1 – 26

26

MDSRA…PGGST → MAHSPVQSGLPGMQ in isoform A.

VSP_004874

Natural variant

414

1

A → V. Ref.2 Ref.22
Corresponds to variant rs55953606 [ dbSNP | Ensembl ].

VAR_041148

Natural variant

426

1

L → I. Ref.22
Corresponds to variant rs55897869 [ dbSNP | Ensembl ].

VAR_041149

Experimental info

Mutagenesis

18

1

T → A: Loss of phosphorylation by PKA. Ref.2

Mutagenesis

65

1

K → A: Loss of activity and autophosphorylation. Ref.6

Mutagenesis

190

1

T → A: Loss of activity and autophosphorylation. Ref.11

Mutagenesis

321

1

D → N: Loss of proteolytic cleavage by caspases. Ref.6

Secondary structure

1

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443

Helix Strand Turn

Details...

Helix

32 – 34

3

Beta strand

36 – 44

9

Beta strand

46 – 55

10

Turn

56 – 58

3

Beta strand

61 – 68

8

Turn

69 – 71

3

Helix

76 – 88

13

Beta strand

97 – 103

7

Beta strand

106 – 112

7

Beta strand

116 – 118

3

Helix

119 – 123

5

Beta strand

124 – 126

3

Helix

130 – 149

20

Helix

159 – 161

3

Beta strand

162 – 164

3

Beta strand

166 – 168

3

Beta strand

170 – 172

3

Helix

180 – 183

4

Beta strand

186 – 188

3

Helix

195 – 197

3

Helix

200 – 203

4

Helix

211 – 226

16

Turn

230 – 233

4

Helix

236 – 245

10

Helix

257 – 266

10

Helix

271 – 273

3

Helix

277 – 280

4

Helix

284 – 289

6

Helix

293 – 296

4

Helix

297 – 309

13

Sequences

	Sequence		Length	Mass (Da)
	Isoform B [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 4A9FF1F6B6A88A97	FASTA	443	49,308
	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
	Isoform A [UniParc]. Checksum: 26D863FDFEDF90AD	FASTA	431	47,913
	10 20 30 40 50 60 MAHSPVQSGL PGMQNLKADP EELFTKLEKI GKGSFGEVFK GIDNRTQKVV AIKIIDLEEA 70 80 90 100 110 120 EDEIEDIQQE ITVLSQCDSP YVTKYYGSYL KDTKLWIIME YLGGGSALDL LEPGPLDETQ 130 140 150 160 170 180 IATILREILK GLDYLHSEKK IHRDIKAANV LLSEHGEVKL ADFGVAGQLT DTQIKRNTFV 190 200 210 220 230 240 GTPFWMAPEV IKQSAYDSKA DIWSLGITAI ELARGEPPHS ELHPMKVLFL IPKNNPPTLE 250 260 270 280 290 300 GNYSKPLKEF VEACLNKEPS FRPTAKELLK HKFILRNAKK TSYLTELIDR YKRWKAEQSH 310 320 330 340 350 360 DDSSSEDSDA ETDGQASGGS DSGDWIFTIR EKDPKNLENG ALQPSDLDRN KMKDIPKRPF 370 380 390 400 410 420 SQCLSTIISP LFAELKEKSQ ACGGNLGSIE ELRGAIYLAE EACPGISDTM VAQLVQRLQR 430 YSLSGGGTSS H

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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), MASS SPECTROMETRY. 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), MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE.
[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), MASS SPECTROMETRY. 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), MASS SPECTROMETRY.
[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. , 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.

IPI

IPI00002212.
IPI00981772.

RefSeq

NP_001027467.2. NM_001032296.2.
NP_003567.2. NM_003576.3.

UniGene

Hs.508514.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3A7F	X-ray	1.55	A	27-315	[»]
3A7G	X-ray	2.00	A/B	27-315	[»]
3A7H	X-ray	1.96	A/B	27-315	[»]
3A7I	X-ray	1.45	A	27-315	[»]
3A7J	X-ray	1.50	A	27-315	[»]
3CKW	X-ray	1.96	A	31-323	[»]
3CKX	X-ray	2.70	A	31-323	[»]
3ZHP	X-ray	2.90	C/D	31-301	[»]

ProteinModelPortal

Q9Y6E0.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9Y6E0. 32 interactions.

STRING

9606.ENSP00000365730.

PTM databases

PhosphoSite

Q9Y6E0.

Polymorphism databases

DMDM

13626607.

Proteomic databases

PaxDb

Q9Y6E0.

PRIDE

Q9Y6E0.

Protocols and materials databases

DNASU

8428.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000376547; ENSP00000365730; ENSG00000102572.
ENST00000397517; ENSP00000380651; ENSG00000102572.

GeneID

8428.

KEGG

hsa:8428.

UCSC

uc001vnm.1. human.

Organism-specific databases

CTD

8428.

GeneCards

GC13M099103.

HGNC

HGNC:11403. STK24.

HPA

HPA026435.
HPA026502.

MIM

604984. gene.

neXtProt

NX_Q9Y6E0.

PharmGKB

PA36210.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000234203.

HOVERGEN

HBG108518.

KO

K08838.

OMA

GSDDWIF.

PhylomeDB

Q9Y6E0.

Enzyme and pathway databases

Reactome

REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

Q9Y6E0.

Bgee

Q9Y6E0.

CleanEx

HS_STK24.
HS_STK3.

Genevestigator

Q9Y6E0.

GermOnline

ENSG00000102572. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. False negative.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9Y6E0.

ChEMBL

CHEMBL5082.

ChiTaRS

STK24. human.

EvolutionaryTrace

Q9Y6E0.

GenomeRNAi

8428.

NextBio

31540.

SOURCE

Search...

Entry information

Entry name

STK24_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 130 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.