STK24_HUMAN - dbPTM
STK24_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STK24_HUMAN
UniProt AC Q9Y6E0
Protein Name Serine/threonine-protein kinase 24
Gene Name STK24
Organism Homo sapiens (Human).
Sequence Length 443
Subcellular Localization Cytoplasm. Nucleus. Membrane. The truncated form (MST3/N) translocates to the nucleus. Colocalizes with STK38L in the membrane.
Protein Description 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. In association with STK26 negatively regulates Golgi reorientation in polarized cell migration upon RHO activation. [PubMed: 27807006 Regulates also 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.]
Protein Sequence MDSRAQLWGLALNKRRATLPHPGGSTNLKADPEELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGSALDLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRNTFVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEGNYSKPLKEFVEACLNKEPSFRPTAKELLKHKFILRNAKKTSYLTELIDRYKRWKAEQSHDDSSSEDSDAETDGQASGGSDSGDWIFTIREKDPKNLENGALQPSDLDRNKMKDIPKRPFSQCLSTIISPLFAELKEKSQACGGNLGSIEELRGAIYLAEEACPGISDTMVAQLVQRLQRYSLSGGGTSSH
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2 (in isoform 2)Acetylation-46.9919369195
4 (in isoform 2)Phosphorylation-23.3025159151
8 (in isoform 2)Phosphorylation-6.4122617229
18PhosphorylationALNKRRATLPHPGGS
HHHCCCCCCCCCCCC		38.7210644707
25 (in isoform 2)Phosphorylation-21.7526270265
38UbiquitinationDPEELFTKLEKIGKG
CHHHHHHHHHHHCCC		47.52-
44UbiquitinationTKLEKIGKGSFGEVF
HHHHHHCCCCHHHHC		55.65-
46PhosphorylationLEKIGKGSFGEVFKG
HHHHCCCCHHHHCCC		33.3020873877
52UbiquitinationGSFGEVFKGIDNRTQ
CCHHHHCCCCCCCCC		61.2021890473
52 (in isoform 1)Ubiquitination-61.2021890473
52UbiquitinationGSFGEVFKGIDNRTQ
CCHHHHCCCCCCCCC		61.20-
59 (in isoform 2)Ubiquitination-33.0521890473
93PhosphorylationLSQCDSPYVTKYYGS
HHCCCCCCHHCCCCC		25.38-
113PhosphorylationKLWIIMEYLGGGSAL
EEEEEEEHHCCCCHH		8.02-
142UbiquitinationTILREILKGLDYLHS
HHHHHHHHHHHHHHC		64.19-
142MalonylationTILREILKGLDYLHS
HHHHHHHHHHHHHHC		64.1926320211
151UbiquitinationLDYLHSEKKIHRDIK
HHHHHCCCHHHHCHH		61.10-
152UbiquitinationDYLHSEKKIHRDIKA
HHHHCCCHHHHCHHH		39.43-
175 (in isoform 2)Ubiquitination-7.63-
182PhosphorylationFGVAGQLTDTQIKRN
EEECCCCCCCCHHHC		29.1630266825
184PhosphorylationVAGQLTDTQIKRNTF
ECCCCCCCCHHHCCC		27.2722322096
187UbiquitinationQLTDTQIKRNTFVGT
CCCCCCHHHCCCCCC		29.76-
190PhosphorylationDTQIKRNTFVGTPFW
CCCHHHCCCCCCCCC		24.5922322096
194PhosphorylationKRNTFVGTPFWMAPE
HHCCCCCCCCCCCHH		15.2630266825
237SulfoxidationPHSELHPMKVLFLIP
CCCCCCCCEEEEEEC		3.0630846556
238UbiquitinationHSELHPMKVLFLIPK
CCCCCCCEEEEEECC		39.9921890473
238 (in isoform 1)Ubiquitination-39.9921890473
238UbiquitinationHSELHPMKVLFLIPK
CCCCCCCEEEEEECC		39.9921890473
245 (in isoform 2)Ubiquitination-63.4621890473
245UbiquitinationKVLFLIPKNNPPTLE
EEEEEECCCCCCCCC		63.46-
256PhosphorylationPTLEGNYSKPLKEFV
CCCCCCCCHHHHHHH		31.6224719451
257UbiquitinationTLEGNYSKPLKEFVE
CCCCCCCHHHHHHHH		43.97-
278UbiquitinationPSFRPTAKELLKHKF
CCCCCCHHHHHHCHH		51.91-
280 (in isoform 2)Ubiquitination-8.33-
2922-HydroxyisobutyrylationFILRNAKKTSYLTEL
HHHHCCCCHHHHHHH		40.05-
292UbiquitinationFILRNAKKTSYLTEL
HHHHCCCCHHHHHHH		40.052189047
292 (in isoform 1)Ubiquitination-40.0521890473
292MalonylationFILRNAKKTSYLTEL
HHHHCCCCHHHHHHH		40.0526320211
292UbiquitinationFILRNAKKTSYLTEL
HHHHCCCCHHHHHHH		40.0521890473
293PhosphorylationILRNAKKTSYLTELI
HHHCCCCHHHHHHHH		23.1528152594
294PhosphorylationLRNAKKTSYLTELID
HHCCCCHHHHHHHHH		27.3328152594
295PhosphorylationRNAKKTSYLTELIDR
HCCCCHHHHHHHHHH		23.9128152594
297PhosphorylationAKKTSYLTELIDRYK
CCCHHHHHHHHHHHH		22.1028152594
299 (in isoform 2)Ubiquitination-4.0921890473
303PhosphorylationLTELIDRYKRWKAEQ
HHHHHHHHHHHHHHH		10.93-
311PhosphorylationKRWKAEQSHDDSSSE
HHHHHHHCCCCCCCC		22.0118691976
315PhosphorylationAEQSHDDSSSEDSDA
HHHCCCCCCCCCCCC		41.6517081983
316PhosphorylationEQSHDDSSSEDSDAE
HHCCCCCCCCCCCCC		44.7517081983
317PhosphorylationQSHDDSSSEDSDAET
HCCCCCCCCCCCCCC		49.7417081983
320PhosphorylationDDSSSEDSDAETDGQ
CCCCCCCCCCCCCCC		34.3712107159
324PhosphorylationSEDSDAETDGQASGG
CCCCCCCCCCCCCCC		47.3428857561
329PhosphorylationAETDGQASGGSDSGD
CCCCCCCCCCCCCCC		35.4825841592
340PhosphorylationDSGDWIFTIREKDPK
CCCCEEEEEEECCCC		15.2524719451
347UbiquitinationTIREKDPKNLENGAL
EEEECCCCCCCCCCC		81.79-
373PhosphorylationDIPKRPFSQCLSTII
CCCCCCHHHHHHHHH		23.7526074081
377PhosphorylationRPFSQCLSTIISPLF
CCHHHHHHHHHHHHH		25.7826074081
378PhosphorylationPFSQCLSTIISPLFA
CHHHHHHHHHHHHHH		14.9126074081
381PhosphorylationQCLSTIISPLFAELK
HHHHHHHHHHHHHHH		16.2328450419
390UbiquitinationLFAELKEKSQACGGN
HHHHHHHHHHHCCCC		46.40-
400PhosphorylationACGGNLGSIEELRGA
HCCCCCCCHHHHHHH		29.9626657352
433PhosphorylationLVQRLQRYSLSGGGT
HHHHHHHHCCCCCCC		10.87-
434PhosphorylationVQRLQRYSLSGGGTS
HHHHHHHCCCCCCCC		20.4628555341
436PhosphorylationRLQRYSLSGGGTSSH
HHHHHCCCCCCCCCC		29.4723090842
440PhosphorylationYSLSGGGTSSH----
HCCCCCCCCCC----		30.2626434776
441PhosphorylationSLSGGGTSSH-----
CCCCCCCCCC-----		29.6828985074
442PhosphorylationLSGGGTSSH------
CCCCCCCCC------		32.8122617229
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
18TPhosphorylationKinasePRKACAP17612
GPS
18TPhosphorylationKinasePKA-FAMILY-GPS
18TPhosphorylationKinasePKA-Uniprot
18TPhosphorylationKinasePKA_GROUP-PhosphoELM
190TPhosphorylationKinaseSTK24Q9Y6E0
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
190TPhosphorylation

17046825
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of STK24_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDC10_HUMANPDCD10physical
16189514
STRN_HUMANSTRNphysical
17353931
STRN3_HUMANSTRN3physical
17353931
2AAA_HUMANPPP2R1Aphysical
17353931
PDC10_HUMANPDCD10physical
17353931
STRN4_HUMANSTRN4physical
17353931
PHOCN_HUMANMOB4physical
17353931
STK25_HUMANSTK25physical
17353931
STRP1_HUMANSTRIP1physical
17353931
PP2AB_HUMANPPP2CBphysical
17353931
SLMAP_HUMANSLMAPphysical
17353931
APOD_HUMANAPODphysical
17353931
DDX5_HUMANDDX5physical
17353931
G3BP2_HUMANG3BP2physical
17353931
HNRH3_HUMANHNRNPH3physical
17353931
PDC6I_HUMANPDCD6IPphysical
17353931
ZBT24_HUMANZBTB24physical
17353931
JPH3_HUMANJPH3physical
17353931
HNRPQ_HUMANSYNCRIPphysical
17353931
ROA3_HUMANHNRNPA3physical
17353931
FABP5_HUMANFABP5physical
17353931
DESP_HUMANDSPphysical
17353931
2AAA_HUMANPPP2R1Aphysical
18782753
PP2AA_HUMANPPP2CAphysical
18782753
STRN_HUMANSTRNphysical
18782753
STRP1_HUMANSTRIP1physical
18782753
STRN3_HUMANSTRN3physical
18782753
2AAB_HUMANPPP2R1Bphysical
18782753
STRN4_HUMANSTRN4physical
18782753
PHOCN_HUMANMOB4physical
18782753
PDC10_HUMANPDCD10physical
18782753
CT2NL_HUMANCTTNBP2NLphysical
18782753
SIKE1_HUMANSIKE1physical
18782753
STRP2_HUMANSTRIP2physical
18782753
SLMAP_HUMANSLMAPphysical
18782753
TCPB_HUMANCCT2physical
18782753
TCPQ_HUMANCCT8physical
18782753
CTTB2_HUMANCTTNBP2physical
18782753
TCPG_HUMANCCT3physical
18782753
TCPA_HUMANTCP1physical
18782753
TCPE_HUMANCCT5physical
18782753
FGOP2_HUMANFGFR1OP2physical
18782753
TCPZ_HUMANCCT6Aphysical
18782753
TCPH_HUMANCCT7physical
18782753
TCPD_HUMANCCT4physical
18782753
AL7A1_HUMANALDH7A1physical
22863883
ASNS_HUMANASNSphysical
22863883
IF5_HUMANEIF5physical
22863883
ISOC1_HUMANISOC1physical
22863883
MAT2B_HUMANMAT2Bphysical
22863883
MOES_HUMANMSNphysical
22863883
PDC10_HUMANPDCD10physical
22863883
PDIA4_HUMANPDIA4physical
22863883
PP1A_HUMANPPP1CAphysical
22863883
RISC_HUMANSCPEP1physical
22863883
TBB5_HUMANTUBBphysical
22863883
XPO1_HUMANXPO1physical
22863883
STK25_HUMANSTK25physical
23455922
STRN_HUMANSTRNphysical
23455922
2AAA_HUMANPPP2R1Aphysical
23455922
2AAB_HUMANPPP2R1Bphysical
23455922
PP2AB_HUMANPPP2CBphysical
23455922
DYL1_HUMANDYNLL1physical
23455922
PP2AA_HUMANPPP2CAphysical
23455922
STRN3_HUMANSTRN3physical
23455922
SLMAP_HUMANSLMAPphysical
23455922
PRSR2_HUMANPROSER2physical
23455922
CTTB2_HUMANCTTNBP2physical
23455922
SIKE1_HUMANSIKE1physical
23455922
PDC10_HUMANPDCD10physical
23455922
STRN4_HUMANSTRN4physical
23455922
FGOP2_HUMANFGFR1OP2physical
23455922
STK26_HUMANSTK26physical
23455922
CT2NL_HUMANCTTNBP2NLphysical
23455922
STRP2_HUMANSTRIP2physical
23455922
PHOCN_HUMANMOB4physical
23455922
PDC10_HUMANPDCD10physical
25416956
STK24_HUMANSTK24physical
18082144
TLK2_HUMANTLK2physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STK24_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311; SER-315; SER-316;SER-317 AND SER-320, AND MASS SPECTROMETRY.
"Structures of human MST3 kinase in complex with adenine, ADP andMn2+.";
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).
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 27-315 IN COMPLEX WITHADENINE; ADP AND MANGANESE IONS, SUBUNIT, AND PHOSPHORYLATION ATTHR-190.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-190, AND MASSSPECTROMETRY.
"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).
Cited for: FUNCTION, AND PHOSPHORYLATION AT THR-190.
"Inhibition of cell migration by autophosphorylated mammalian sterile20-like kinase 3 (MST3) involves paxillin and protein-tyrosinephosphatase-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).
Cited for: FUNCTION, PHOSPHORYLATION AT THR-190, AND MUTAGENESIS OF THR-190.
"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).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), PHOSPHORYLATION AT THR-18,MUTAGENESIS OF THR-18, AND VARIANT VAL-414.

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