Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q13188 (STK3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 145. 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 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:

  1. Serine/threonine-protein kinase 3 36kDa subunit
    Short name=MST2/N
  2. Serine/threonine-protein kinase 3 20kDa subunit
    Short name=MST2/C
Gene names
Name:STK3
Synonyms:KRS1, MST2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length491 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.11 Ref.13 Ref.14 Ref.16 Ref.21 Ref.24 Ref.25 Ref.29

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium.

Enzyme regulation

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. Ref.10 Ref.28

Subunit structure

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). Ref.10 Ref.11 Ref.12 Ref.13 Ref.16 Ref.21 Ref.23 Ref.25 Ref.26 Ref.28 Ref.29

Subcellular location

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. Ref.21

Tissue specificity

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

Induction

Activity increases during mitosis. Ref.10 Ref.14 Ref.28

Post-translational modification

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.

Proteolytically cleaved by caspase-3 during apoptosis. Proteolytic cleavage results in kinase activation and nuclear translocation of the truncated form (MST1/N). Ref.9

Sequence similarities

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

Contains 1 protein kinase domain.

Contains 1 SARAH domain.

Ontologies

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

Traceable author statement Ref.9. Source: UniProtKB

hippo signaling

Traceable author statement Ref.19. Source: UniProtKB

intracellular signal transduction

Inferred from direct assay Ref.1. Source: UniProtKB

negative regulation of canonical Wnt signaling pathway

Inferred from mutant phenotype PubMed 20412773. Source: BHF-UCL

positive regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein serine/threonine kinase activity

Traceable author statement PubMed 20412773. Source: GOC

protein phosphorylation

Inferred from direct assay Ref.23Ref.26Ref.1. Source: UniProtKB

signal transduction

Traceable author statement Ref.2. Source: ProtInc

signal transduction by phosphorylation

Inferred from Biological aspect of Ancestor. Source: GOC

   Cellular_componentcytoplasm

Inferred from direct assay Ref.21. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from direct assay Ref.1. Source: UniProtKB

magnesium ion binding

Inferred from direct assay Ref.1. Source: UniProtKB

protein dimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase activity

Traceable author statement PubMed 10840030Ref.2. Source: ProtInc

protein serine/threonine kinase activator activity

Traceable author statement PubMed 20412773. Source: BHF-UCL

protein serine/threonine kinase activity

Inferred from direct assay Ref.14Ref.16Ref.21Ref.1. Source: UniProtKB

receptor signaling protein serine/threonine kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13188-1)

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 2 (identifier: Q13188-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: MEQPPAPK → MLQLMDSGITICLRNGAASVFKKKEWSTQGEENKQD
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 491491Serine/threonine-protein kinase 3
PRO_0000086689
Chain1 – 322322Serine/threonine-protein kinase 3 36kDa subunit
PRO_0000413713
Chain323 – 491169Serine/threonine-protein kinase 3 20kDa subunit
PRO_0000413714

Regions

Domain27 – 278252Protein kinase
Domain437 – 48448SARAH
Nucleotide binding33 – 419ATP By similarity
Coiled coil287 – 32842 Potential
Coiled coil442 – 47534 Potential
Compositional bias308 – 3147Poly-Glu
Compositional bias370 – 3756Poly-Glu

Sites

Active site1461Proton acceptor By similarity
Binding site561ATP
Site322 – 3232Cleavage; by caspase-3

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7 Ref.18
Modified residue151Phosphoserine Ref.20
Modified residue1171Phosphothreonine; by PKB/AKT1 Ref.23 Ref.26
Modified residue1801Phosphothreonine; by autocatalysis Probable
Modified residue3161Phosphoserine Ref.15 Ref.17 Ref.20 Ref.22 Ref.30
Modified residue3361Phosphothreonine Ref.20
Modified residue3841Phosphothreonine; by PKB/AKT1 Ref.23
Modified residue4441Phosphoserine Ref.15 Ref.20

Natural variations

Alternative sequence1 – 88MEQPPAPK → MLQLMDSGITICLRNGAASV FKKKEWSTQGEENKQD in isoform 2.
VSP_054167
Natural variant601V → L in an ovarian clear cell carcinoma sample; somatic mutation. Ref.31
VAR_041122
Natural variant4181F → C.
Corresponds to variant rs36047674 [ dbSNP | Ensembl ].
VAR_051670

Experimental info

Mutagenesis561K → R: Loss of activity. Ref.13
Mutagenesis3221D → N: Resistant to proteolytic cleavage. Ref.9
Sequence conflict96 – 983WIV → YLY in CAA80909. Ref.8
Sequence conflict1211D → Y in CAA80909. Ref.8
Sequence conflict2031D → G in CAA80909. Ref.8
Sequence conflict3031E → D in AAC50386. Ref.1
Sequence conflict332 – 3343ESV → GEC in AAC50386. Ref.1

Secondary structure

....................................................... 491
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 26, 2004. Version 2.
Checksum: 84F598ED3617292C

FASTA49156,301
        10         20         30         40         50         60 
MEQPPAPKSK LKKLSEDSLT KQPEEVFDVL EKLGEGSYGS VFKAIHKESG QVVAIKQVPV 

        70         80         90        100        110        120 
ESDLQEIIKE ISIMQQCDSP YVVKYYGSYF KNTDLWIVME YCGAGSVSDI IRLRNKTLIE 

       130        140        150        160        170        180 
DEIATILKST LKGLEYLHFM RKIHRDIKAG NILLNTEGHA KLADFGVAGQ LTDTMAKRNT 

       190        200        210        220        230        240 
VIGTPFWMAP EVIQEIGYNC VADIWSLGIT SIEMAEGKPP YADIHPMRAI FMIPTNPPPT 

       250        260        270        280        290        300 
FRKPELWSDD FTDFVKKCLV KNPEQRATAT QLLQHPFIKN AKPVSILRDL ITEAMEIKAK 

       310        320        330        340        350        360 
RHEEQQRELE EEEENSDEDE LDSHTMVKTS VESVGTMRAT STMSEGAQTM IEHNSTMLES 

       370        380        390        400        410        420 
DLGTMVINSE DEEEEDGTMK RNATSPQVQR PSFMDYFDKQ DFKNKSHENC NQNMHEPFPM 

       430        440        450        460        470        480 
SKNVFPDNWK VPQDGDFDFL KNLSLEELQM RLKALDPMME REIEELRQRY TAKRQPILDA 

       490 
MDAKKRRQQN F 

« Hide

Isoform 2 [UniParc].

Checksum: 84CB5FEAA629AE68
Show »

FASTA51959,462

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]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].
[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]"Role of the tumor suppressor RASSF1A in Mst1-mediated apoptosis."
Oh H.J., Lee K.-K., Song S.J., Jin M.S., Song M.S., Lee J.H., Im C.R., Lee J.-O., Yonehara S., Lim D.-S.
Cancer Res. 66:2562-2569(2006) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT 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]"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: 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]"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].
[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. 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: VARIANT [LARGE SCALE ANALYSIS] LEU-60.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRI38212.
RefSeqNP_006272.2. NM_006281.3.
UniGeneHs.492333.

3D structure databases

PDBe
RCSB PDB
PDBj
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/D10-491[»]
ProteinModelPortalQ13188.
SMRQ13188. Positions 10-302, 386-489.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112664. 133 interactions.
DIPDIP-36128N.
IntActQ13188. 59 interactions.
MINTMINT-3027356.
STRING9606.ENSP00000377867.

Chemistry

BindingDBQ13188.
ChEMBLCHEMBL4708.
GuidetoPHARMACOLOGY2219.

PTM databases

PhosphoSiteQ13188.

Polymorphism databases

DMDM46577700.

2D gel databases

OGPQ13188.

Proteomic databases

PaxDbQ13188.
PRIDEQ13188.

Protocols and materials databases

DNASU6788.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000419617; ENSP00000390500; ENSG00000104375.
ENST00000523601; ENSP00000429744; ENSG00000104375.
GeneID6788.
KEGGhsa:6788.
UCSCuc003yip.4. human.

Organism-specific databases

CTD6788.
GeneCardsGC08M099413.
HGNCHGNC:11406. STK3.
HPACAB025316.
HPA007120.
MIM605030. gene.
neXtProtNX_Q13188.
PharmGKBPA36213.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000234203.
HOVERGENHBG108518.
InParanoidQ13188.
KOK04412.
OMAXDEDELD.
OrthoDBEOG7TF79T.
PhylomeDBQ13188.
TreeFamTF354217.

Enzyme and pathway databases

BRENDA2.7.11.1. 2681.
ReactomeREACT_111102. Signal Transduction.
SignaLinkQ13188.

Gene expression databases

ArrayExpressQ13188.
BgeeQ13188.
CleanExHS_STK3.
GenevestigatorQ13188.

Family and domain databases

InterProIPR011009. 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_dom.
[Graphical view]
PfamPF11629. Mst1_SARAH. 1 hit.
PF00069. 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.
PS50951. SARAH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSTK3. human.
GeneWikiSTK3.
GenomeRNAi6788.
NextBio26504.
PMAP-CutDBQ13188.
PROQ13188.
SOURCESearch...

Entry information

Entry nameSTK3_HUMAN
AccessionPrimary (citable) accession number: Q13188
Secondary accession number(s): A8K722 expand/collapse secondary AC list , B3KYA7, Q15445, Q15801, Q96FM6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: April 26, 2004
Last modified: April 16, 2014
This is version 145 of the entry and version 2 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 8

Human chromosome 8: entries, gene names and cross-references to MIM