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Q9Y6E0

- STK24_HUMAN

UniProt

Q9Y6E0 - STK24_HUMAN

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Protein

Serine/threonine-protein kinase 24

Gene

STK24

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.5 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+1 Publication, Mn2+1 Publication, Co2+1 Publication, Zn2+1 Publication

Kineticsi

  1. KM=12.8 µM for manganese ions1 Publication
  2. KM=34.9 µM for cobalt ions1 Publication
  3. KM=22.7 µM for magnesium ions1 Publication
  4. KM=4.1 µM for zinc ions1 Publication

Vmax=2623.1 pmol/min/mg enzyme for manganese ions1 Publication

Vmax=1746.1 pmol/min/mg enzyme for cobalt ions1 Publication

Vmax=129.1 pmol/min/mg enzyme for magnesium ions1 Publication

Vmax=22.3 pmol/min/mg enzyme for zinc ions1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei65 – 651ATP
Active sitei156 – 1561Proton acceptorPROSITE-ProRule annotation
Metal bindingi161 – 1611Magnesium
Metal bindingi174 – 1741Magnesium
Sitei325 – 3262Cleavage; by caspase-3, caspase-7 and caspase-8

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi42 – 509ATP
Nucleotide bindingi112 – 1143ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. protein kinase activity Source: ProtInc
  4. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: Reactome
  2. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  3. execution phase of apoptosis Source: UniProtKB
  4. intrinsic apoptotic signaling pathway in response to oxidative stress Source: UniProtKB
  5. negative regulation of cell migration Source: UniProtKB
  6. protein autophosphorylation Source: UniProtKB
  7. protein phosphorylation Source: UniProtKB
  8. regulation of axon regeneration Source: UniProtKB
  9. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_107. Apoptotic cleavage of cellular proteins.
REACT_995. Apoptotic execution phase.
SignaLinkiQ9Y6E0.

Names & Taxonomyi

Protein namesi
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:
Alternative name(s):
Mammalian STE20-like protein kinase 3 N-terminal
Short name:
MST3/N
Alternative name(s):
Mammalian STE20-like protein kinase 3 C-terminal
Short name:
MST3/C
Gene namesi
Name:STK24
Synonyms:MST3, STK3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:11403. STK24.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
  4. membrane Source: UniProtKB-KW
  5. nucleolus Source: HPA
  6. nucleoplasm Source: Reactome
  7. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi18 – 181T → A: Loss of phosphorylation by PKA. 1 Publication
Mutagenesisi65 – 651K → A: Loss of activity and autophosphorylation. 1 Publication
Mutagenesisi190 – 1901T → A: Loss of activity and autophosphorylation. 1 Publication
Mutagenesisi321 – 3211D → N: Loss of proteolytic cleavage by caspases. 1 Publication

Organism-specific databases

PharmGKBiPA36210.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 443443Serine/threonine-protein kinase 24PRO_0000086711Add
BLAST
Chaini1 – 325325Serine/threonine-protein kinase 24 36 kDa subunitPRO_0000413618Add
BLAST
Chaini326 – 443118Serine/threonine-protein kinase 24 12 kDa subunitPRO_0000413619Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei18 – 181Phosphothreonine; by PKA1 Publication
Modified residuei190 – 1901Phosphothreonine; by autocatalysis3 Publications
Modified residuei320 – 3201Phosphoserine1 Publication

Post-translational modificationi

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.1 Publication
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.5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Y6E0.
PaxDbiQ9Y6E0.
PRIDEiQ9Y6E0.

PTM databases

PhosphoSiteiQ9Y6E0.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9Y6E0.
CleanExiHS_STK24.
HS_STK3.
ExpressionAtlasiQ9Y6E0. baseline and differential.
GenevestigatoriQ9Y6E0.

Organism-specific databases

HPAiHPA026435.
HPA026502.

Interactioni

Subunit structurei

Monomer. Interacts with CTTNBP2NL.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CTTNBP2NLQ9P2B44EBI-740175,EBI-1774273
PDCD10Q9BUL87EBI-740175,EBI-740195
STRNO438153EBI-740175,EBI-1046642
TRAF3IP3Q9Y2282EBI-740175,EBI-765817

Protein-protein interaction databases

BioGridi114011. 68 interactions.
DIPiDIP-40608N.
IntActiQ9Y6E0. 33 interactions.
MINTiMINT-3088034.
STRINGi9606.ENSP00000365730.

Structurei

Secondary structure

1
443
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi32 – 343Combined sources
Beta strandi36 – 449Combined sources
Beta strandi46 – 5510Combined sources
Turni56 – 583Combined sources
Beta strandi61 – 688Combined sources
Turni69 – 713Combined sources
Helixi76 – 8813Combined sources
Beta strandi97 – 1037Combined sources
Beta strandi106 – 1127Combined sources
Beta strandi116 – 1183Combined sources
Helixi119 – 1235Combined sources
Beta strandi124 – 1263Combined sources
Helixi130 – 14920Combined sources
Helixi159 – 1613Combined sources
Beta strandi162 – 1643Combined sources
Beta strandi166 – 1683Combined sources
Beta strandi170 – 1723Combined sources
Helixi180 – 1834Combined sources
Beta strandi186 – 1883Combined sources
Helixi195 – 1973Combined sources
Helixi200 – 2034Combined sources
Helixi211 – 22616Combined sources
Turni230 – 2334Combined sources
Helixi236 – 24510Combined sources
Helixi257 – 26610Combined sources
Helixi271 – 2733Combined sources
Helixi277 – 2804Combined sources
Helixi284 – 2896Combined sources
Helixi293 – 2964Combined sources
Helixi297 – 30913Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ9Y6E0.
SMRiQ9Y6E0. Positions 27-350, 372-434.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y6E0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 286251Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni335 – 38652Nuclear export signal (NES)Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi278 – 29215Bipartite nuclear localization signalAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00640000091192.
HOGENOMiHOG000234203.
HOVERGENiHBG108518.
InParanoidiQ9Y6E0.
KOiK08838.
OMAiGSDDWIF.
PhylomeDBiQ9Y6E0.
TreeFamiTF354217.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
[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.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform B (identifier: Q9Y6E0-1) [UniParc]FASTAAdd to Basket

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

        10         20         30         40         50
MDSRAQLWGL ALNKRRATLP HPGGSTNLKA DPEELFTKLE KIGKGSFGEV
60 70 80 90 100
FKGIDNRTQK VVAIKIIDLE EAEDEIEDIQ QEITVLSQCD SPYVTKYYGS
110 120 130 140 150
YLKDTKLWII MEYLGGGSAL DLLEPGPLDE TQIATILREI LKGLDYLHSE
160 170 180 190 200
KKIHRDIKAA NVLLSEHGEV KLADFGVAGQ LTDTQIKRNT FVGTPFWMAP
210 220 230 240 250
EVIKQSAYDS KADIWSLGIT AIELARGEPP HSELHPMKVL FLIPKNNPPT
260 270 280 290 300
LEGNYSKPLK EFVEACLNKE PSFRPTAKEL LKHKFILRNA KKTSYLTELI
310 320 330 340 350
DRYKRWKAEQ SHDDSSSEDS DAETDGQASG GSDSGDWIFT IREKDPKNLE
360 370 380 390 400
NGALQPSDLD RNKMKDIPKR PFSQCLSTII SPLFAELKEK SQACGGNLGS
410 420 430 440
IEELRGAIYL AEEACPGISD TMVAQLVQRL QRYSLSGGGT SSH
Length:443
Mass (Da):49,308
Last modified:November 1, 1999 - v1
Checksum:i4A9FF1F6B6A88A97
GO
Isoform A (identifier: Q9Y6E0-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:431
Mass (Da):47,913
Checksum:i26D863FDFEDF90AD
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti414 – 4141A → V.2 Publications
Corresponds to variant rs55953606 [ dbSNP | Ensembl ].
VAR_041148
Natural varianti426 – 4261L → I.1 Publication
Corresponds to variant rs55897869 [ dbSNP | Ensembl ].
VAR_041149

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2626MDSRA…PGGST → MAHSPVQSGLPGMQ in isoform A. 2 PublicationsVSP_004874Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS32001.1. [Q9Y6E0-2]
CCDS9488.1. [Q9Y6E0-1]
RefSeqiNP_001027467.2. NM_001032296.3. [Q9Y6E0-2]
NP_003567.2. NM_003576.4. [Q9Y6E0-1]
UniGeneiHs.508514.

Genome annotation databases

EnsembliENST00000376547; ENSP00000365730; ENSG00000102572. [Q9Y6E0-1]
ENST00000539966; ENSP00000442539; ENSG00000102572. [Q9Y6E0-2]
GeneIDi8428.
KEGGihsa:8428.
UCSCiuc001vnm.1. human. [Q9Y6E0-1]

Polymorphism databases

DMDMi13626607.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS32001.1. [Q9Y6E0-2 ]
CCDS9488.1. [Q9Y6E0-1 ]
RefSeqi NP_001027467.2. NM_001032296.3. [Q9Y6E0-2 ]
NP_003567.2. NM_003576.4. [Q9Y6E0-1 ]
UniGenei Hs.508514.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali Q9Y6E0.
SMRi Q9Y6E0. Positions 27-350, 372-434.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114011. 68 interactions.
DIPi DIP-40608N.
IntActi Q9Y6E0. 33 interactions.
MINTi MINT-3088034.
STRINGi 9606.ENSP00000365730.

Chemistry

BindingDBi Q9Y6E0.
ChEMBLi CHEMBL5082.
GuidetoPHARMACOLOGYi 2217.

PTM databases

PhosphoSitei Q9Y6E0.

Polymorphism databases

DMDMi 13626607.

Proteomic databases

MaxQBi Q9Y6E0.
PaxDbi Q9Y6E0.
PRIDEi Q9Y6E0.

Protocols and materials databases

DNASUi 8428.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000376547 ; ENSP00000365730 ; ENSG00000102572 . [Q9Y6E0-1 ]
ENST00000539966 ; ENSP00000442539 ; ENSG00000102572 . [Q9Y6E0-2 ]
GeneIDi 8428.
KEGGi hsa:8428.
UCSCi uc001vnm.1. human. [Q9Y6E0-1 ]

Organism-specific databases

CTDi 8428.
GeneCardsi GC13M099103.
HGNCi HGNC:11403. STK24.
HPAi HPA026435.
HPA026502.
MIMi 604984. gene.
neXtProti NX_Q9Y6E0.
PharmGKBi PA36210.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00640000091192.
HOGENOMi HOG000234203.
HOVERGENi HBG108518.
InParanoidi Q9Y6E0.
KOi K08838.
OMAi GSDDWIF.
PhylomeDBi Q9Y6E0.
TreeFami TF354217.

Enzyme and pathway databases

Reactomei REACT_107. Apoptotic cleavage of cellular proteins.
REACT_995. Apoptotic execution phase.
SignaLinki Q9Y6E0.

Miscellaneous databases

ChiTaRSi STK24. human.
EvolutionaryTracei Q9Y6E0.
GeneWikii STK24.
GenomeRNAii 8428.
NextBioi 31540.
PROi Q9Y6E0.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y6E0.
CleanExi HS_STK24.
HS_STK3.
ExpressionAtlasi Q9Y6E0. baseline and differential.
Genevestigatori Q9Y6E0.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
[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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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.
    , 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.

Entry informationi

Entry nameiSTK24_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6E0
Secondary accession number(s): O14840, Q5JV92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1999
Last modified: November 26, 2014
This is version 146 of the entry and version 1 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 13
    Human chromosome 13: 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