dbPTM

STK39_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	STK39_HUMAN
UniProt AC	Q9UEW8
Protein Name	STE20/SPS1-related proline-alanine-rich protein kinase
Gene Name	STK39
Organism	Homo sapiens (Human).
Sequence Length	545
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..
Protein Sequence	MAEPSGSPVHVQLPQQAAPVTAAAAAAPAAATAAPAPAAPAAPAPAPAPAAQAVGWPICRDAYELQEVIGSGATAVVQAALCKPRQERVAIKRINLEKCQTSMDELLKEIQAMSQCSHPNVVTYYTSFVVKDELWLVMKLLSGGSMLDIIKYIVNRGEHKNGVLEEAIIATILKEVLEGLDYLHRNGQIHRDLKAGNILLGEDGSVQIADFGVSAFLATGGDVTRNKVRKTFVGTPCWMAPEVMEQVRGYDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLETGVEDKEMMKKYGKSFRKLLSLCLQKDPSKRPTAAELLKCKFFQKAKNREYLIEKLLTRTPDIAQRAKKVRRVPGSSGHLHKTEDGDWEWSDDEMDEKSEEGKAAFSQEKSRRVKEENPEIAVSASTIPEQIQSLSVHDSQGPPNANEDYREASSCAVNLVLRLRNSRKELNDIRFEFTPGRDTADGVSQELFSAGLVDGHDVVIVAANLQKIVDDPKALKTLTFKLASGCDGSEIPDEVKLIGFAQLSVS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAEPSGSPV ------CCCCCCCCC	37.09	-
5	Phosphorylation	---MAEPSGSPVHVQ ---CCCCCCCCCEEE	43.33	28348404
7	Phosphorylation	-MAEPSGSPVHVQLP -CCCCCCCCCEEECC	28.25	28464451
32	Phosphorylation	AAAPAAATAAPAPAA HHCHHHHHCCCCCCC	20.73	27251275
63	Phosphorylation	WPICRDAYELQEVIG CCCCCCHHHHHHHHC	22.82	-
83	Ubiquitination	VVQAALCKPRQERVA HHHHHHCCCHHHHHH	44.05	-
98	Ubiquitination	IKRINLEKCQTSMDE HEECCHHHHCCCHHH	34.51	30230243
101	Phosphorylation	INLEKCQTSMDELLK CCHHHHCCCHHHHHH	35.17	23917254
102	Phosphorylation	NLEKCQTSMDELLKE CHHHHCCCHHHHHHH	9.81	23917254
114	Phosphorylation	LKEIQAMSQCSHPNV HHHHHHHHCCCCCCC	30.93	30576142
124	Phosphorylation	SHPNVVTYYTSFVVK CCCCCHHEEEEEEEC	7.98	28985074
125	Phosphorylation	HPNVVTYYTSFVVKD CCCCHHEEEEEEECH	6.12	30576142
127	Phosphorylation	NVVTYYTSFVVKDEL CCHHEEEEEEECHHH	10.42	30576142
142	Phosphorylation	WLVMKLLSGGSMLDI HHHHHHHCCCCHHHH	52.09	21406692
145	Phosphorylation	MKLLSGGSMLDIIKY HHHHCCCCHHHHHHH	21.50	21406692
160	Ubiquitination	IVNRGEHKNGVLEEA HHHCCCCCCCHHHHH	51.61	29967540
175	Ubiquitination	IIATILKEVLEGLDY HHHHHHHHHHHHHHH	49.22	27667366
182	Phosphorylation	EVLEGLDYLHRNGQI HHHHHHHHHHHCCCC	14.95	28152594
185	Ubiquitination	EGLDYLHRNGQIHRD HHHHHHHHCCCCCCC	46.51	21890473
219	Phosphorylation	GVSAFLATGGDVTRN CCCEEEEECCCCCCC	43.79	-
224	Phosphorylation	LATGGDVTRNKVRKT EEECCCCCCCCCCCC	33.01	-
230	Ubiquitination	VTRNKVRKTFVGTPC CCCCCCCCCCCCCCC	49.67	30230243
231	Phosphorylation	TRNKVRKTFVGTPCW CCCCCCCCCCCCCCC	17.00	22322096
233	Phosphorylation	NKVRKTFVGTPCWMA CCCCCCCCCCCCCCC	11.47	16083423
235	Phosphorylation	VRKTFVGTPCWMAPE CCCCCCCCCCCCCHH	15.24	23403867
237	Ubiquitination	KTFVGTPCWMAPEVM CCCCCCCCCCCHHHH	3.78	27667366
240	Ubiquitination	VGTPCWMAPEVMEQV CCCCCCCCHHHHHHH	3.44	27667366
247	Ubiquitination	APEVMEQVRGYDFKA CHHHHHHHCCCCCCH	3.06	21890473
273	Phosphorylation	LATGAAPYHKYPPMK HHHCCCCCCCCCCCE	13.25	20044836
276	Phosphorylation	GAAPYHKYPPMKVLM CCCCCCCCCCCEEEE	10.15	20044836
299	Ubiquitination	TLETGVEDKEMMKKY CCCCCCCCHHHHHHH	50.21	24816145
302	Ubiquitination	TGVEDKEMMKKYGKS CCCCCHHHHHHHHHH	6.17	27667366
306	Phosphorylation	DKEMMKKYGKSFRKL CHHHHHHHHHHHHHH	25.03	-
309	Phosphorylation	MMKKYGKSFRKLLSL HHHHHHHHHHHHHHH	26.39	14988727
311	Phosphorylation	KKYGKSFRKLLSLCL HHHHHHHHHHHHHHH	35.48	14988727
312	Malonylation	KYGKSFRKLLSLCLQ HHHHHHHHHHHHHHC	52.34	32601280
312	Methylation	KYGKSFRKLLSLCLQ HHHHHHHHHHHHHHC	52.34	19866039
312	Acetylation	KYGKSFRKLLSLCLQ HHHHHHHHHHHHHHC	52.34	25953088
312	Ubiquitination	KYGKSFRKLLSLCLQ HHHHHHHHHHHHHHC	52.34	29967540
315	Phosphorylation	KSFRKLLSLCLQKDP HHHHHHHHHHHCCCC	27.72	28857561
320	Ubiquitination	LLSLCLQKDPSKRPT HHHHHHCCCCCCCCC	59.67	29967540
320	Methylation	LLSLCLQKDPSKRPT HHHHHHCCCCCCCCC	59.67	115980409
323	Phosphorylation	LCLQKDPSKRPTAAE HHHCCCCCCCCCHHH	51.97	20873877
324	Acetylation	CLQKDPSKRPTAAEL HHCCCCCCCCCHHHH	68.72	25953088
324	Ubiquitination	CLQKDPSKRPTAAEL HHCCCCCCCCCHHHH	68.72	29967540
325	Phosphorylation	LQKDPSKRPTAAELL HCCCCCCCCCHHHHH	37.83	14988727
333	Ubiquitination	PTAAELLKCKFFQKA CCHHHHHHCHHHHHH	48.26	32015554
339	Ubiquitination	LKCKFFQKAKNREYL HHCHHHHHHCCHHHH	57.05	27667366
341	Ubiquitination	CKFFQKAKNREYLIE CHHHHHHCCHHHHHH	64.67	29967540
345	Phosphorylation	QKAKNREYLIEKLLT HHHCCHHHHHHHHHH	15.11	28152594
349	Ubiquitination	NREYLIEKLLTRTPD CHHHHHHHHHHCCHH	41.63	19608861
349	Acetylation	NREYLIEKLLTRTPD CHHHHHHHHHHCCHH	41.63	19608861
351	Ubiquitination	EYLIEKLLTRTPDIA HHHHHHHHHCCHHHH	4.51	21890473
351	Ubiquitination	EYLIEKLLTRTPDIA HHHHHHHHHCCHHHH	4.51	21890473
351	Ubiquitination	EYLIEKLLTRTPDIA HHHHHHHHHCCHHHH	4.51	21890473
351	Ubiquitination	EYLIEKLLTRTPDIA HHHHHHHHHCCHHHH	4.51	21890473
352	Phosphorylation	YLIEKLLTRTPDIAQ HHHHHHHHCCHHHHH	42.82	23401153
354	Phosphorylation	IEKLLTRTPDIAQRA HHHHHHCCHHHHHHH	21.78	29255136
356	Phosphorylation	KLLTRTPDIAQRAKK HHHHCCHHHHHHHHH	48.52	16964243
361	Ubiquitination	TPDIAQRAKKVRRVP CHHHHHHHHHHHCCC	12.16	24816145
370	Phosphorylation	KVRRVPGSSGHLHKT HHHCCCCCCCCCEEC	27.38	23401153
371	Phosphorylation	VRRVPGSSGHLHKTE HHCCCCCCCCCEECC	35.83	29255136
372	Phosphorylation	RRVPGSSGHLHKTED HCCCCCCCCCEECCC	29.13	18088087
373	Phosphorylation	RVPGSSGHLHKTEDG CCCCCCCCCEECCCC	27.06	18088087
377	Phosphorylation	SSGHLHKTEDGDWEW CCCCCEECCCCCCCC	28.67	23403867
385	Phosphorylation	EDGDWEWSDDEMDEK CCCCCCCCCHHHHHH	24.54	22167270
387	Phosphorylation	GDWEWSDDEMDEKSE CCCCCCCHHHHHHCH	47.83	18088087
393	Phosphorylation	DDEMDEKSEEGKAAF CHHHHHHCHHHHHHH	38.54	23403867
401	Phosphorylation	EEGKAAFSQEKSRRV HHHHHHHHHHHHHHH	32.47	29396449
404	Ubiquitination	KAAFSQEKSRRVKEE HHHHHHHHHHHHHHH	41.44	27667366
430	Phosphorylation	PEQIQSLSVHDSQGP CHHHHHCCCCCCCCC	23.74	-
442	Ubiquitination	QGPPNANEDYREASS CCCCCCCCCHHHHHH	54.75	24816145
444	Phosphorylation	PPNANEDYREASSCA CCCCCCCHHHHHHHH	12.27	20736484
448	Phosphorylation	NEDYREASSCAVNLV CCCHHHHHHHHHHHH	22.61	-
463	Ubiquitination	LRLRNSRKELNDIRF HHHHHCCHHHCCCEE	67.39	24816145
469	Methylation	RKELNDIRFEFTPGR CHHHCCCEEEECCCC	28.10	-
512	Acetylation	QKIVDDPKALKTLTF HHHCCCHHHHHHHHH	73.65	23749302
512	Ubiquitination	QKIVDDPKALKTLTF HHHCCCHHHHHHHHH	73.65	29967540
515	Ubiquitination	VDDPKALKTLTFKLA CCCHHHHHHHHHHCC	46.47	29967540
515	Acetylation	VDDPKALKTLTFKLA CCCHHHHHHHHHHCC	46.47	25953088
520	Ubiquitination	ALKTLTFKLASGCDG HHHHHHHHCCCCCCC	37.60	32015554
520	Acetylation	ALKTLTFKLASGCDG HHHHHHHHCCCCCCC	37.60	25953088

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
231	T	Phosphorylation	Kinase	WNK1	Q9H4A3	PSP
233	T	Phosphorylation	Kinase	WNK1	Q9H4A3	PhosphoELM
309	S	Phosphorylation	Kinase	PKCT	Q04759	PSP
311	S	Phosphorylation	Kinase	KPCT	Q04759	PhosphoELM
323	S	Phosphorylation	Kinase	PRKCQ	Q04759	GPS
325	S	Phosphorylation	Kinase	KPCT	Q04759	PhosphoELM
354	T	Phosphorylation	Kinase	WNK2	Q9Y3S1	PSP
371	S	Phosphorylation	Kinase	WNK1	Q9H4A3	PSP
371	S	Phosphorylation	Kinase	WNK2	Q9Y3S1	PSP
373	S	Phosphorylation	Kinase	WNK1	Q9H4A3	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
231	T	Phosphorylation	14988727
Autophosphorylation at Thr-231 positively regulates its activity (By similarity).
309	S	Phosphorylation	14988727
Phosphorylated at Ser-309 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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
S12A2_HUMAN	SLC12A2	physical	14563843
LMTK1_HUMAN	AATK	physical	14563843
GELS_HUMAN	GSN	physical	14563843
OTOF_HUMAN	OTOF	physical	14563843
WNK4_HUMAN	WNK4	physical	14563843
HS105_HUMAN	HSPH1	physical	14563843
STK39_HUMAN	STK39	physical	10980603
MBP_HUMAN	MBP	physical	10980603
API5_HUMAN	API5	physical	22863883
NOL3_HUMAN	NOL3	physical	22863883
NUBP1_HUMAN	NUBP1	physical	22863883
PCNA_HUMAN	PCNA	physical	22863883
XPP1_HUMAN	XPNPEP1	physical	22863883

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 STK39_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-385, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-349, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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 SER-385, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-371 AND SER-385, ANDMASS SPECTROMETRY.	19369195 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-385, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370; SER-371 ANDSER-385, AND MASS SPECTROMETRY.	18088087 [Abstract]
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline."; Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; Electrophoresis 28:2027-2034(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, AND MASSSPECTROMETRY.	17487921 [Abstract]
"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-370, AND MASSSPECTROMETRY.	17081983 [Abstract]
"SPAK kinase is a substrate and target of PKCtheta in T-cell receptor-induced AP-1 activation pathway."; Li Y., Hu J., Vita R., Sun B., Tabata H., Altman A.; EMBO J. 23:1112-1122(2004). Cited for: PHOSPHORYLATION AT SER-309.	14988727 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-354, AND MASSSPECTROMETRY.	16964243 [Abstract]

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