dbPTM

STK39_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	STK39_MOUSE
UniProt AC	Q9Z1W9
Protein Name	STE20/SPS1-related proline-alanine-rich protein kinase
Gene Name	Stk39
Organism	Mus musculus (Mouse).
Sequence Length	556
Subcellular Localization	Cytoplasm . Nucleus . Nucleus when caspase-cleaved.
Protein Description	May act as a mediator of stress-activated signals. Mediates the inhibition of SLC4A4, SLC26A6 as well as CFTR activities by the WNK scaffolds, probably through phosphorylation. [PubMed: 21317537]
Protein Sequence	MAEPSGSPVHVQLSQQAAPVTAAAATAPAAATSAPAPAPAPAPAASAAPAPAPAAAPAPAPAAQAVGWPICRDAYELQEVIGSGATAVVQAALCKPRQERVAIKRINLEKCQTSMDELLKEIQAMSQCSHPNVVTYYTSFVVKDELWLVMKLLSGGSMLDIIKYIVNRGEHKNGVLEEAIIATILKEVLEGLDYLHRNGQIHRDLKAGNILLGEDGSVQIADFGVSAFLATGGDVTRNKVRKTFVGTPCWMAPEVMEQVRGYDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLETGVEDKEMMKKYGKSFRKLLSLCLQKDPSKRPTAAELLKCKFFQKAKNREYLIEKLLTRTPDIAQRAKKVRRVPGSSGHLHKTEDGDWEWSDDEMDEKSEEGKAAASQEKSRRVKEENSEISVNAGGIPEQIQSLSVHDSQAQPNANEDYREGPCAVNLVLRLRNSRKELNDIRFEFTPGRDTADGVSQELFSAGLVDGHDVVIVAANLQKIVDDPKALKTLTFKLASGCDGSEIPDEVKLIGFAQLSVS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
217	Phosphorylation	ILLGEDGSVQIADFG EEECCCCCEEEEECC	24.14	-
226	Phosphorylation	QIADFGVSAFLATGG EEEECCCCEEEEECC	17.43	-
236	Phosphorylation	LATGGDVTRNKVRKT EEECCCCCCCCCCCC	33.01	-
243	Phosphorylation	TRNKVRKTFVGTPCW CCCCCCCCCCCCCCC	17.00	22322096
247	Phosphorylation	VRKTFVGTPCWMAPE CCCCCCCCCCCCCHH	15.24	22322096
249	S-nitrosylation	KTFVGTPCWMAPEVM CCCCCCCCCCCHHHH	3.78	21278135
249	S-nitrosocysteine	KTFVGTPCWMAPEVM CCCCCCCCCCCHHHH	3.78	-
321	Phosphorylation	MMKKYGKSFRKLLSL HHHHHHHHHHHHHHH	26.39	-
324	Acetylation	KYGKSFRKLLSLCLQ HHHHHHHHHHHHHHC	52.34	19866035
361	Ubiquitination	NREYLIEKLLTRTPD CHHHHHHHHHHCCHH	41.63	-
361	Acetylation	NREYLIEKLLTRTPD CHHHHHHHHHHCCHH	41.63	-
364	Phosphorylation	YLIEKLLTRTPDIAQ HHHHHHHHCCHHHHH	42.82	26239621
366	Phosphorylation	IEKLLTRTPDIAQRA HHHHHHCCHHHHHHH	21.78	25521595
382	Phosphorylation	KVRRVPGSSGHLHKT HHHCCCCCCCCCEEC	27.38	26824392
383	Phosphorylation	VRRVPGSSGHLHKTE HHCCCCCCCCCEECC	35.83	21930439
389	Phosphorylation	SSGHLHKTEDGDWEW CCCCCEECCCCCCCC	28.67	29119230
397	Phosphorylation	EDGDWEWSDDEMDEK CCCCCCCCCHHHHHH	24.54	25521595
405	Phosphorylation	DDEMDEKSEEGKAAA CHHHHHHCHHHHHHH	38.54	25521595
536	S-nitrosylation	TFKLASGCDGSEIPD HHHCCCCCCCCCCCC	5.05	21278135
536	S-nitrosocysteine	TFKLASGCDGSEIPD HHHCCCCCCCCCCCC	5.05	-

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
243	T	Phosphorylation	Kinase	STK39	Q9Z1W9	PhosphoELM
243	T	Phosphorylation	Kinase	WNK4	Q80UE6	PSP
247	T	Phosphorylation	Kinase	STK39	Q9Z1W9	PhosphoELM
321	S	Phosphorylation	Kinase	PRKCQ	Q02111	Uniprot
382	S	Phosphorylation	Kinase	WNK4	Q96J92	PSP
383	S	Phosphorylation	Kinase	WNK4	Q80UE6	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
243	T	Phosphorylation	16530727
Autophosphorylation at Thr-243 positively regulates its activity.
321	S	Phosphorylation	21733846
Phosphorylated at Ser-321 by PRKCQ.

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 STK39_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of STK39_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of STK39_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"WNK2 is a novel regulator of essential neuronal cation-chloridecotransporters."; Rinehart J., Vazquez N., Kahle K.T., Hodson C.A., Ring A.M.,Gulcicek E.E., Louvi A., Bobadilla N.A., Gamba G., Lifton R.P.; J. Biol. Chem. 286:30171-30180(2011). Cited for: PHOSPHORYLATION AT THR-366 AND SER-383, AND INTERACTION WITH WNK2.	21733846 [Abstract]
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, AND MASSSPECTROMETRY.	17203969 [Abstract]