dbPTM

STK24_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	STK24_MOUSE
UniProt AC	Q99KH8
Protein Name	Serine/threonine-protein kinase 24
Gene Name	Stk24
Organism	Mus musculus (Mouse).
Sequence Length	431
Subcellular Localization	Cytoplasm. Nucleus. Membrane. The truncated form (MST3/N) translocates to the nucleus. Colocalizes with STK38L in the membrane (By similarity)..
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. 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. Acts as a key regulator of axon regeneration in the optic nerve and radial nerve (By similarity)..
Protein Sequence	MAHSPVQSGLPGMQNLKADPEELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGSALDLLEPGPLDEIQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRNTFVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELAKGEPPHSELHPMKVLFLIPKNNPPTLEGNYSKPLKEFVEACLNKEPSFRPTAKELLKHKFIIRNAKKTSYLTELIDRYKRWKAEQSHEDSSSEDSDVETDGQASGGSDSGDWIFTIREKDPKNLENGTLQLSDLERNKMKDIPKRPFSQCLSTIISPLFAELKEKSQACGGNLGSIEELRGAIYLAEEACPGISDTMVAQLVQRLQRYSLSGGGASAH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAHSPVQSG ------CCCCCCCCC	16.32	19131326
4	Phosphorylation	----MAHSPVQSGLP ----CCCCCCCCCCC	19.75	23527152
8	Phosphorylation	MAHSPVQSGLPGMQN CCCCCCCCCCCCHHC	42.40	25619855
25	Phosphorylation	ADPEELFTKLEKIGK CCHHHHHHHHHHHCC	47.55	25367039
34	Phosphorylation	LEKIGKGSFGEVFKG HHHHCCCCHHHHCCC	33.30	-
79	Phosphorylation	TVLSQCDSPYVTKYY HHHHCCCCCCHHCCC	26.25	-
81	Phosphorylation	LSQCDSPYVTKYYGS HHCCCCCCHHCCCCC	25.38	-
130	Acetylation	TILREILKGLDYLHS HHHHHHHHHHHHHHC	64.19	66691615
170	Phosphorylation	FGVAGQLTDTQIKRN EEECCCCCCCCHHHC	29.16	22322096
172	Phosphorylation	VAGQLTDTQIKRNTF ECCCCCCCCHHHCCC	27.27	25521595
178	Phosphorylation	DTQIKRNTFVGTPFW CCCHHHCCCCCCCCC	24.59	25521595
182	Phosphorylation	KRNTFVGTPFWMAPE HHCCCCCCCCCCCHH	15.26	22322096
226	Ubiquitination	HSELHPMKVLFLIPK CCCCCCCEEEEEECC	39.99	-
233	Ubiquitination	KVLFLIPKNNPPTLE EEEEEECCCCCCCCC	63.46	-
280	Ubiquitination	FIIRNAKKTSYLTEL HHHCCCCCHHHHHHH	40.05	-
281	Phosphorylation	IIRNAKKTSYLTELI HHCCCCCHHHHHHHH	23.15	25293948
282	Phosphorylation	IRNAKKTSYLTELID HCCCCCHHHHHHHHH	27.33	21183079
283	Phosphorylation	RNAKKTSYLTELIDR CCCCCHHHHHHHHHH	23.91	25293948
285	Phosphorylation	AKKTSYLTELIDRYK CCCHHHHHHHHHHHH	22.10	25293948
299	Phosphorylation	KRWKAEQSHEDSSSE HHHHHHHCCCCCCCC	21.98	22817900
303	Phosphorylation	AEQSHEDSSSEDSDV HHHCCCCCCCCCCCC	32.55	19060867
304	Phosphorylation	EQSHEDSSSEDSDVE HHCCCCCCCCCCCCC	50.50	19060867
305	Phosphorylation	QSHEDSSSEDSDVET HCCCCCCCCCCCCCC	49.74	26525534
308	Phosphorylation	EDSSSEDSDVETDGQ CCCCCCCCCCCCCCC	39.23	19854140
341	Phosphorylation	PKNLENGTLQLSDLE CCCCCCCCEEHHHHH	23.94	25521595
345	Phosphorylation	ENGTLQLSDLERNKM CCCCEEHHHHHHHCC	27.47	25266776
369	Phosphorylation	QCLSTIISPLFAELK HHHHHHHHHHHHHHH	16.23	23984901

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
79	S	Phosphorylation	Kinase	CDK5	Q00535	PSP
79	S	Phosphorylation	Kinase	CDK5	P49615	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
178	T	Phosphorylation		-
Activated by autophosphorylation at Thr-178 and phosphorylation at this site is essential for its function.

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of STK24_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of STK24_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND MASSSPECTROMETRY.	19131326 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND MASSSPECTROMETRY.	17242355 [Abstract]
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line."; Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.; Mol. Cell. Proteomics 3:279-286(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-341, AND MASSSPECTROMETRY.	14729942 [Abstract]

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