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Q13188

- STK3_HUMAN

UniProt

Q13188 - STK3_HUMAN

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Protein

Serine/threonine-protein kinase 3

Gene

STK3

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

Functioni

Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation. Phosphorylates NKX2-1 (By similarity). Phosphorylates NEK2 and plays a role in centrosome disjunction by regulating the localization of NEK2 to centrosome, and its ability to phosphorylate CROCC and CEP250. In conjunction with SAV1, activates the transcriptional activity of ESR1 through the modulation of its phosphorylation. Positively regulates RAF1 activation via suppression of the inhibitory phosphorylation of RAF1 on 'Ser-259'. Phosphorylates MOBKL1A and RASSF2. Phosphorylates MOBKL1B on 'Thr-74'. Acts cooperatively with MOBKL1B to activate STK38.By similarity10 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Enzyme regulationi

Inhibited by the C-terminal non-catalytic region. Activated by caspase-cleavage. Full activation also requires homodimerization and autophosphorylation of Thr-180, which are inhibited by the proto-oncogene product RAF1. Activated by RASSF1 which acts by preventing its dephosphorylation.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei56 – 561ATP
Active sitei146 – 1461Proton acceptorPROSITE-ProRule annotation
Sitei322 – 3232Cleavage; by caspase-3

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi33 – 419ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. magnesium ion binding Source: UniProtKB
  3. protein dimerization activity Source: UniProtKB
  4. protein kinase activity Source: ProtInc
  5. protein serine/threonine kinase activator activity Source: BHF-UCL
  6. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB
  2. cell differentiation involved in embryonic placenta development Source: Ensembl
  3. central nervous system development Source: Ensembl
  4. endocardium development Source: Ensembl
  5. hepatocyte apoptotic process Source: Ensembl
  6. hippo signaling Source: UniProtKB
  7. intracellular signal transduction Source: UniProtKB
  8. negative regulation of canonical Wnt signaling pathway Source: BHF-UCL
  9. negative regulation of cell proliferation Source: Ensembl
  10. negative regulation of organ growth Source: Ensembl
  11. neural tube formation Source: Ensembl
  12. positive regulation of apoptotic process Source: UniProtKB
  13. positive regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
  14. positive regulation of JNK cascade Source: Ensembl
  15. positive regulation of protein kinase B signaling Source: Ensembl
  16. positive regulation of protein serine/threonine kinase activity Source: GOC
  17. primitive hemopoiesis Source: Ensembl
  18. protein phosphorylation Source: UniProtKB
  19. 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

BRENDAi2.7.11.1. 2681.
ReactomeiREACT_118607. Signaling by Hippo.
SignaLinkiQ13188.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase 3 (EC:2.7.11.1)
Alternative name(s):
Mammalian STE20-like protein kinase 2
Short name:
MST-2
STE20-like kinase MST2
Serine/threonine-protein kinase Krs-1
Cleaved into the following 2 chains:
Gene namesi
Name:STK3
Synonyms:KRS1, MST2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:11406. STK3.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity
Note: The caspase-cleaved form cycles between nucleus and cytoplasm (By similarity). Phosphorylation at Thr-117 leads to inhibition of nuclear translocation.By similarity1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi56 – 561K → R: Loss of activity. 1 Publication
Mutagenesisi322 – 3221D → N: Resistant to proteolytic cleavage. 1 Publication

Organism-specific databases

PharmGKBiPA36213.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 491491Serine/threonine-protein kinase 3PRO_0000086689Add
BLAST
Chaini1 – 322322Serine/threonine-protein kinase 3 36kDa subunitPRO_0000413713Add
BLAST
Chaini323 – 491169Serine/threonine-protein kinase 3 20kDa subunitPRO_0000413714Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei15 – 151Phosphoserine1 Publication
Modified residuei117 – 1171Phosphothreonine; by PKB/AKT12 Publications
Modified residuei180 – 1801Phosphothreonine; by autocatalysisCurated
Modified residuei316 – 3161Phosphoserine5 Publications
Modified residuei336 – 3361Phosphothreonine1 Publication
Modified residuei384 – 3841Phosphothreonine; by PKB/AKT11 Publication
Modified residuei444 – 4441Phosphoserine2 Publications

Post-translational modificationi

Phosphorylation at Thr-117 and Thr-384 by PKB/AKT1, leads to inhibition of its: cleavage, kinase activity, autophosphorylation at Thr-180, binding to RASSF1 and nuclear translocation, and increase in its binding to RAF1.8 Publications
Proteolytically cleaved by caspase-3 during apoptosis. Proteolytic cleavage results in kinase activation and nuclear translocation of the truncated form (MST1/N).1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ13188.
PaxDbiQ13188.
PRIDEiQ13188.

2D gel databases

OGPiQ13188.

PTM databases

PhosphoSiteiQ13188.

Miscellaneous databases

PMAP-CutDBQ13188.

Expressioni

Tissue specificityi

Expressed at high levels in adult kidney, skeletal and placenta tissues and at very low levels in adult heart, lung and brain tissues.1 Publication

Inductioni

Activity increases during mitosis.1 Publication

Gene expression databases

BgeeiQ13188.
CleanExiHS_STK3.
ExpressionAtlasiQ13188. baseline and differential.
GenevestigatoriQ13188.

Organism-specific databases

HPAiCAB025316.
HPA007120.

Interactioni

Subunit structurei

Homodimer; mediated via the coiled-coil region. Interacts with NORE1, which inhibits autoactivation (By similarity). Interacts with and stabilizes SAV1. Interacts with RAF1, which prevents dimerization and phosphorylation. Interacts with RASSF1. Interacts (via SARAH domain) with isoform 1 of NEK2. Interacts with ESR1 only in the presence of SAV1. Interacts with PKB/AKT1. Forms a tripartite complex with MOBKL1B and STK38. Interacts with RASSF2 (via SARAH domain).By similarity11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GABARAPO951662EBI-992580,EBI-712001
GABARAPL1Q9H0R82EBI-992580,EBI-746969
GABARAPL2P605202EBI-992580,EBI-720116
MAP1LC3BQ9GZQ85EBI-992580,EBI-373144
MAP1LC3CQ9BXW42EBI-992580,EBI-2603996
RASSF1Q9NS23-23EBI-992580,EBI-438698
RASSF2P5074910EBI-992580,EBI-960081
RASSF3Q86WH26EBI-992580,EBI-2845202
RASSF4Q9H2L55EBI-992580,EBI-2933362
RASSF5Q8WWW07EBI-992580,EBI-367390
SAV1Q9H4B615EBI-992580,EBI-1017775
SLMAPQ14BN43EBI-992580,EBI-1043216
STK4Q1304315EBI-992580,EBI-367376

Protein-protein interaction databases

BioGridi112664. 69 interactions.
DIPiDIP-36128N.
IntActiQ13188. 61 interactions.
MINTiMINT-3027356.
STRINGi9606.ENSP00000377867.

Structurei

Secondary structure

1
491
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi17 – 204Combined sources
Helixi23 – 264Combined sources
Beta strandi27 – 348Combined sources
Beta strandi40 – 467Combined sources
Turni47 – 493Combined sources
Beta strandi52 – 587Combined sources
Helixi64 – 7613Combined sources
Beta strandi85 – 917Combined sources
Beta strandi94 – 1007Combined sources
Helixi107 – 1148Combined sources
Helixi120 – 13920Combined sources
Helixi149 – 1513Combined sources
Beta strandi152 – 1543Combined sources
Beta strandi160 – 1623Combined sources
Helixi170 – 1723Combined sources
Helixi175 – 1828Combined sources
Helixi190 – 1956Combined sources
Helixi201 – 21616Combined sources
Turni220 – 2234Combined sources
Helixi226 – 23510Combined sources
Helixi244 – 2463Combined sources
Helixi249 – 25810Combined sources
Helixi263 – 2653Combined sources
Helixi269 – 2724Combined sources
Helixi276 – 2794Combined sources
Helixi284 – 2874Combined sources
Helixi288 – 30619Combined sources
Helixi436 – 4405Combined sources
Helixi445 – 48339Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4HKDX-ray1.50A/B/C/D436-484[»]
4L0NX-ray1.40A/B/C/D/E/F/G/H/I/J436-484[»]
4LG4X-ray2.42A/B/C/D/E/F16-313[»]
4LGDX-ray3.05A/B/C/D9-491[»]
4OH9X-ray1.70A/B436-484[»]
ProteinModelPortaliQ13188.
SMRiQ13188. Positions 10-302, 386-489.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 278252Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini437 – 48448SARAHPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili287 – 32842Sequence AnalysisAdd
BLAST
Coiled coili442 – 47534Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi308 – 3147Poly-Glu
Compositional biasi370 – 3756Poly-Glu

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SARAH domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00640000091192.
HOGENOMiHOG000234203.
HOVERGENiHBG108518.
InParanoidiQ13188.
KOiK04412.
OMAiXDEDELD.
OrthoDBiEOG7TF79T.
PhylomeDBiQ13188.
TreeFamiTF354217.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR024205. Mst1_SARAH_domain.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR011524. SARAH_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
[Graphical view]
PfamiPF11629. Mst1_SARAH. 1 hit.
PF00069. 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.
PS50951. SARAH. 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 1 (identifier: Q13188-1) [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
MEQPPAPKSK LKKLSEDSLT KQPEEVFDVL EKLGEGSYGS VFKAIHKESG
60 70 80 90 100
QVVAIKQVPV ESDLQEIIKE ISIMQQCDSP YVVKYYGSYF KNTDLWIVME
110 120 130 140 150
YCGAGSVSDI IRLRNKTLIE DEIATILKST LKGLEYLHFM RKIHRDIKAG
160 170 180 190 200
NILLNTEGHA KLADFGVAGQ LTDTMAKRNT VIGTPFWMAP EVIQEIGYNC
210 220 230 240 250
VADIWSLGIT SIEMAEGKPP YADIHPMRAI FMIPTNPPPT FRKPELWSDD
260 270 280 290 300
FTDFVKKCLV KNPEQRATAT QLLQHPFIKN AKPVSILRDL ITEAMEIKAK
310 320 330 340 350
RHEEQQRELE EEEENSDEDE LDSHTMVKTS VESVGTMRAT STMSEGAQTM
360 370 380 390 400
IEHNSTMLES DLGTMVINSE DEEEEDGTMK RNATSPQVQR PSFMDYFDKQ
410 420 430 440 450
DFKNKSHENC NQNMHEPFPM SKNVFPDNWK VPQDGDFDFL KNLSLEELQM
460 470 480 490
RLKALDPMME REIEELRQRY TAKRQPILDA MDAKKRRQQN F
Length:491
Mass (Da):56,301
Last modified:April 26, 2004 - v2
Checksum:i84F598ED3617292C
GO
Isoform 2 (identifier: Q13188-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: MEQPPAPK → MLQLMDSGITICLRNGAASVFKKKEWSTQGEENKQD

Note: No experimental confirmation available.

Show »
Length:519
Mass (Da):59,462
Checksum:i84CB5FEAA629AE68
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 983WIV → YLY in CAA80909. (PubMed:8274451)Curated
Sequence conflicti121 – 1211D → Y in CAA80909. (PubMed:8274451)Curated
Sequence conflicti203 – 2031D → G in CAA80909. (PubMed:8274451)Curated
Sequence conflicti303 – 3031E → D in AAC50386. (PubMed:8566796)Curated
Sequence conflicti332 – 3343ESV → GEC in AAC50386. (PubMed:8566796)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti60 – 601V → L in an ovarian clear cell carcinoma sample; somatic mutation. 1 Publication
VAR_041122
Natural varianti418 – 4181F → C.
Corresponds to variant rs36047674 [ dbSNP | Ensembl ].
VAR_051670

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 88MEQPPAPK → MLQLMDSGITICLRNGAASV FKKKEWSTQGEENKQD in isoform 2. 1 PublicationVSP_054167

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U26424 mRNA. Translation: AAC50386.1.
U60206 mRNA. Translation: AAB17261.1.
AK131363 mRNA. Translation: BAG54769.1.
AK291837 mRNA. Translation: BAF84526.1.
AC016877 Genomic DNA. No translation available.
AP002087 Genomic DNA. No translation available.
AP003355 Genomic DNA. No translation available.
AP003467 Genomic DNA. No translation available.
AP003551 Genomic DNA. No translation available.
CH471060 Genomic DNA. Translation: EAW91781.1.
BC010640 mRNA. Translation: AAH10640.1.
Z25422 mRNA. Translation: CAA80909.1.
CCDSiCCDS47900.1. [Q13188-1]
CCDS59108.1. [Q13188-2]
PIRiI38212.
RefSeqiNP_001243241.1. NM_001256312.1. [Q13188-2]
NP_006272.2. NM_006281.3. [Q13188-1]
UniGeneiHs.492333.

Genome annotation databases

EnsembliENST00000419617; ENSP00000390500; ENSG00000104375. [Q13188-1]
ENST00000523601; ENSP00000429744; ENSG00000104375. [Q13188-2]
GeneIDi6788.
KEGGihsa:6788.
UCSCiuc003yip.4. human. [Q13188-1]

Polymorphism databases

DMDMi46577700.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U26424 mRNA. Translation: AAC50386.1 .
U60206 mRNA. Translation: AAB17261.1 .
AK131363 mRNA. Translation: BAG54769.1 .
AK291837 mRNA. Translation: BAF84526.1 .
AC016877 Genomic DNA. No translation available.
AP002087 Genomic DNA. No translation available.
AP003355 Genomic DNA. No translation available.
AP003467 Genomic DNA. No translation available.
AP003551 Genomic DNA. No translation available.
CH471060 Genomic DNA. Translation: EAW91781.1 .
BC010640 mRNA. Translation: AAH10640.1 .
Z25422 mRNA. Translation: CAA80909.1 .
CCDSi CCDS47900.1. [Q13188-1 ]
CCDS59108.1. [Q13188-2 ]
PIRi I38212.
RefSeqi NP_001243241.1. NM_001256312.1. [Q13188-2 ]
NP_006272.2. NM_006281.3. [Q13188-1 ]
UniGenei Hs.492333.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4HKD X-ray 1.50 A/B/C/D 436-484 [» ]
4L0N X-ray 1.40 A/B/C/D/E/F/G/H/I/J 436-484 [» ]
4LG4 X-ray 2.42 A/B/C/D/E/F 16-313 [» ]
4LGD X-ray 3.05 A/B/C/D 9-491 [» ]
4OH9 X-ray 1.70 A/B 436-484 [» ]
ProteinModelPortali Q13188.
SMRi Q13188. Positions 10-302, 386-489.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112664. 69 interactions.
DIPi DIP-36128N.
IntActi Q13188. 61 interactions.
MINTi MINT-3027356.
STRINGi 9606.ENSP00000377867.

Chemistry

BindingDBi Q13188.
ChEMBLi CHEMBL4708.
GuidetoPHARMACOLOGYi 2219.

PTM databases

PhosphoSitei Q13188.

Polymorphism databases

DMDMi 46577700.

2D gel databases

OGPi Q13188.

Proteomic databases

MaxQBi Q13188.
PaxDbi Q13188.
PRIDEi Q13188.

Protocols and materials databases

DNASUi 6788.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000419617 ; ENSP00000390500 ; ENSG00000104375 . [Q13188-1 ]
ENST00000523601 ; ENSP00000429744 ; ENSG00000104375 . [Q13188-2 ]
GeneIDi 6788.
KEGGi hsa:6788.
UCSCi uc003yip.4. human. [Q13188-1 ]

Organism-specific databases

CTDi 6788.
GeneCardsi GC08M099413.
HGNCi HGNC:11406. STK3.
HPAi CAB025316.
HPA007120.
MIMi 605030. gene.
neXtProti NX_Q13188.
PharmGKBi PA36213.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00640000091192.
HOGENOMi HOG000234203.
HOVERGENi HBG108518.
InParanoidi Q13188.
KOi K04412.
OMAi XDEDELD.
OrthoDBi EOG7TF79T.
PhylomeDBi Q13188.
TreeFami TF354217.

Enzyme and pathway databases

BRENDAi 2.7.11.1. 2681.
Reactomei REACT_118607. Signaling by Hippo.
SignaLinki Q13188.

Miscellaneous databases

ChiTaRSi STK3. human.
GeneWikii STK3.
GenomeRNAii 6788.
NextBioi 26504.
PMAP-CutDB Q13188.
PROi Q13188.
SOURCEi Search...

Gene expression databases

Bgeei Q13188.
CleanExi HS_STK3.
ExpressionAtlasi Q13188. baseline and differential.
Genevestigatori Q13188.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR024205. Mst1_SARAH_domain.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR011524. SARAH_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
[Graphical view ]
Pfami PF11629. Mst1_SARAH. 1 hit.
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.
PS50951. SARAH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a member of the MST subfamily of Ste20-like kinases."
    Creasy C.L., Chernoff J.
    Gene 167:303-306(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY.
  2. "Newly identified stress-responsive protein kinases, Krs-1 and Krs-2."
    Taylor L.K., Wang H.C., Erikson R.L.
    Proc. Natl. Acad. Sci. U.S.A. 93:10099-10104(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Uterus.
  4. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 1).
    Tissue: Eye.
  7. Bienvenut W.V., Matallanas D., Cooper W.N., Kolch W.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-8; 13-43; 57-69; 85-91; 115-128; 133-141; 149-178; 229-256; 267-298; 329-338; 382-403; 423-451; 462-467 AND 474-485, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Mammary carcinoma.
  8. "Identification of 21 novel human protein kinases, including 3 members of a family related to the cell cycle regulator nimA of Aspergillus nidulans."
    Schultz S.J., Nigg E.A.
    Cell Growth Differ. 4:821-830(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 96-203.
  9. "MST, a physiological caspase substrate, highly sensitizes apoptosis both upstream and downstream of caspase activation."
    Lee K.-K., Ohyama T., Yajima N., Tsubuki S., Yonehara S.
    J. Biol. Chem. 276:19276-19285(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING, MUTAGENESIS OF ASP-322.
  10. "Role of the kinase MST2 in suppression of apoptosis by the proto-oncogene product Raf-1."
    O'Neill E., Rushworth L., Baccarini M., Kolch W.
    Science 306:2267-2270(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAF1, ENZYME REGULATION.
  11. "The Ste20-like kinase Mst2 activates the human large tumor suppressor kinase Lats1."
    Chan E.H.Y., Nousiainen M., Chalamalasetty R.B., Schaefer A., Nigg E.A., Sillje H.H.W.
    Oncogene 24:2076-2086(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SAV1, FUNCTION.
  12. Cited for: INTERACTION WITH RASSF1.
  13. "Association of mammalian sterile twenty kinases, Mst1 and Mst2, with hSalvador via C-terminal coiled-coil domains, leads to its stabilization and phosphorylation."
    Callus B.A., Verhagen A.M., Vaux D.L.
    FEBS J. 273:4264-4276(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SAV1, MUTAGENESIS OF LYS-56.
  14. "MOBKL1A/MOBKL1B phosphorylation by MST1 and MST2 inhibits cell proliferation."
    Praskova M., Xia F., Avruch J.
    Curr. Biol. 18:311-321(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  15. "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-316 AND SER-444, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "Threonine 74 of MOB1 is a putative key phosphorylation site by MST2 to form the scaffold to activate nuclear Dbf2-related kinase 1."
    Hirabayashi S., Nakagawa K., Sumita K., Hidaka S., Kawai T., Ikeda M., Kawata A., Ohno K., Hata Y.
    Oncogene 27:4281-4292(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH STK38 AND MOBKL1B.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Mammalian NDR/LATS protein kinases in hippo tumor suppressor signaling."
    Hergovich A., Hemmings B.A.
    BioFactors 35:338-345(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-316; THR-336 AND SER-444, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "RASSF2 associates with and stabilizes the proapoptotic kinase MST2."
    Cooper W.N., Hesson L.B., Matallanas D., Dallol A., von Kriegsheim A., Ward R., Kolch W., Latif F.
    Oncogene 28:2988-2998(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RASSF2, SUBCELLULAR LOCATION.
  22. "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-316, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  23. "Proapoptotic kinase MST2 coordinates signaling crosstalk between RASSF1A, Raf-1, and Akt."
    Romano D., Matallanas D., Weitsman G., Preisinger C., Ng T., Kolch W.
    Cancer Res. 70:1195-1203(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-117 AND THR-384, INTERACTION WITH PKB/AKT1.
  24. "Mammalian Ste20-like kinase (Mst2) indirectly supports Raf-1/ERK pathway activity via maintenance of protein phosphatase-2A catalytic subunit levels and consequent suppression of inhibitory Raf-1 phosphorylation."
    Kilili G.K., Kyriakis J.M.
    J. Biol. Chem. 285:15076-15087(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  25. "Components of the Hippo pathway cooperate with Nek2 kinase to regulate centrosome disjunction."
    Mardin B.R., Lange C., Baxter J.E., Hardy T., Scholz S.R., Fry A.M., Schiebel E.
    Nat. Cell Biol. 12:1166-1176(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NEK2.
  26. "Regulation of proapoptotic mammalian ste20-like kinase MST2 by the IGF1-Akt pathway."
    Kim D., Shu S., Coppola M.D., Kaneko S., Yuan Z.Q., Cheng J.Q.
    PLoS ONE 5:E9616-E9616(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-117, INTERACTION WITH PKB/AKT1.
  27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "The tumor suppressor RASSF1A prevents dephosphorylation of the mammalian STE20-like kinases MST1 and MST2."
    Guo C., Zhang X., Pfeifer G.P.
    J. Biol. Chem. 286:6253-6261(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RASSF1, ENZYME REGULATION.
  29. "Mammalian MST2 kinase and human Salvador activate and reduce estrogen receptor alpha in the absence of ligand."
    Park Y., Park J., Lee Y., Lim W., Oh B.C., Shin C., Kim W., Lee Y.
    J. Mol. Med. 89:181-191(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ESR1.
  30. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "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: VARIANT [LARGE SCALE ANALYSIS] LEU-60.

Entry informationi

Entry nameiSTK3_HUMAN
AccessioniPrimary (citable) accession number: Q13188
Secondary accession number(s): A8K722
, B3KYA7, Q15445, Q15801, Q96FM6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: April 26, 2004
Last modified: November 26, 2014
This is version 152 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: 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