STK38_HUMAN - dbPTM
STK38_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STK38_HUMAN
UniProt AC Q15208
Protein Name Serine/threonine-protein kinase 38
Gene Name STK38 {ECO:0000312|EMBL:AAH12085.1}
Organism Homo sapiens (Human).
Sequence Length 465
Subcellular Localization Nucleus. Cytoplasm.
Protein Description Negative regulator of MAP3K1/2 signaling. Converts MAP3K2 from its phosphorylated form to its non-phosphorylated form and inhibits autophosphorylation of MAP3K2..
Protein Sequence MAMTGSTPCSSMSNHTKERVTMTKVTLENFYSNLIAQHEEREMRQKKLEKVMEEEGLKDEEKRLRRSAHARKETEFLRLKRTRLGLEDFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIMEFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTGLKKAHRTEFYRNLNHSLPSDFTFQNMNSKRKAETWKRNRRQLAFSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQETYKKVMNWKETLTFPPEVPISEKAKDLILRFCCEWEHRIGAPGVEEIKSNSFFEGVDWEHIRERPAAISIEIKSIDDTSNFDEFPESDILKPTVATSNHPETDYKNKDWVFINYTYKRFEGLTARGAIPSYMKAAK
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
2Acetylation------MAMTGSTPC
------CCCCCCCCC		12.30-
4Phosphorylation----MAMTGSTPCSS
----CCCCCCCCCHH		20.6024043423
6Phosphorylation--MAMTGSTPCSSMS
--CCCCCCCCCHHCC		21.7325159151
7Phosphorylation-MAMTGSTPCSSMSN
-CCCCCCCCCHHCCC		29.6525159151
10PhosphorylationMTGSTPCSSMSNHTK
CCCCCCCHHCCCCCC		30.2222142472
11PhosphorylationTGSTPCSSMSNHTKE
CCCCCCHHCCCCCCC		32.7122142472
13PhosphorylationSTPCSSMSNHTKERV
CCCCHHCCCCCCCCE		27.6624043423
16PhosphorylationCSSMSNHTKERVTMT
CHHCCCCCCCCEEEE		38.5624043423
17UbiquitinationSSMSNHTKERVTMTK
HHCCCCCCCCEEEEE		35.65-
21PhosphorylationNHTKERVTMTKVTLE
CCCCCCEEEEEHHHH		25.9124043423
23PhosphorylationTKERVTMTKVTLENF
CCCCEEEEEHHHHHH		17.0124043423
26PhosphorylationRVTMTKVTLENFYSN
CEEEEEHHHHHHHHH		29.8822817900
31PhosphorylationKVTLENFYSNLIAQH
EHHHHHHHHHHHHHH		14.2919836237
32PhosphorylationVTLENFYSNLIAQHE
HHHHHHHHHHHHHHH		22.4828796482
52SulfoxidationQKKLEKVMEEEGLKD
HHHHHHHHHHCCCCH		8.7521406390
58AcetylationVMEEEGLKDEEKRLR
HHHHCCCCHHHHHHH		74.1530590699
62UbiquitinationEGLKDEEKRLRRSAH
CCCCHHHHHHHHHHH		55.47-
72UbiquitinationRRSAHARKETEFLRL
HHHHHHHHHHHHHHH		70.53-
74PhosphorylationSAHARKETEFLRLKR
HHHHHHHHHHHHHHC		34.7612493777
91PhosphorylationLGLEDFESLKVIGRG
CCCCCHHHCEEEECC		33.22-
93UbiquitinationLEDFESLKVIGRGAF
CCCHHHCEEEECCCC		40.8821906983
109UbiquitinationEVRLVQKKDTGHVYA
EEEEEEECCCCCEEH		43.35-
115PhosphorylationKKDTGHVYAMKILRK
ECCCCCEEHHHHHHH		8.7029496907
118UbiquitinationTGHVYAMKILRKADM
CCCEEHHHHHHHHHC		30.34-
122UbiquitinationYAMKILRKADMLEKE
EHHHHHHHHHCCCHH		45.34-
128UbiquitinationRKADMLEKEQVGHIR
HHHHCCCHHHHCCCC		49.86-
183PhosphorylationTLLMKKDTLTEEETQ
HEEECCCCCCHHHHH		44.45-
214UbiquitinationGFIHRDIKPDNLLLD
CCCCCCCCCCCEEEC		51.0821906983
227UbiquitinationLDSKGHVKLSDFGLC
ECCCCCEEHHHCCCC		36.28-
234S-nitrosylationKLSDFGLCTGLKKAH
EHHHCCCCCCCCHHH		2.6522178444
235PhosphorylationLSDFGLCTGLKKAHR
HHHCCCCCCCCHHHH		51.0620068231
238UbiquitinationFGLCTGLKKAHRTEF
CCCCCCCCHHHHHHH		49.62-
238AcetylationFGLCTGLKKAHRTEF
CCCCCCCCHHHHHHH		49.6225953088
239UbiquitinationGLCTGLKKAHRTEFY
CCCCCCCHHHHHHHH		55.24-
252PhosphorylationFYRNLNHSLPSDFTF
HHHHCCCCCCCCCCC		40.6823403867
255PhosphorylationNLNHSLPSDFTFQNM
HCCCCCCCCCCCCCC		51.1223403867
258PhosphorylationHSLPSDFTFQNMNSK
CCCCCCCCCCCCCCH		29.3323403867
264PhosphorylationFTFQNMNSKRKAETW
CCCCCCCCHHHHHHH		24.0623401153
265UbiquitinationTFQNMNSKRKAETWK
CCCCCCCHHHHHHHH		53.57-
270PhosphorylationNSKRKAETWKRNRRQ
CCHHHHHHHHHHHHH		40.9424719451
281PhosphorylationNRRQLAFSTVGTPDY
HHHHHHHCCCCCCCC		19.3112493777
282PhosphorylationRRQLAFSTVGTPDYI
HHHHHHCCCCCCCCC		19.2521712546
285PhosphorylationLAFSTVGTPDYIAPE
HHHCCCCCCCCCCHH		14.5128102081
288PhosphorylationSTVGTPDYIAPEVFM
CCCCCCCCCCHHHHH		10.5321712546
297PhosphorylationAPEVFMQTGYNKLCD
CHHHHHHCCCHHHHH		29.8226074081
299PhosphorylationEVFMQTGYNKLCDWW
HHHHHCCCHHHHHHH		16.7126074081
338UbiquitinationYKKVMNWKETLTFPP
HHHHCCHHHHCCCCC		35.50-
354UbiquitinationVPISEKAKDLILRFC
CCCCHHHHHHHHHHH		65.22-
377UbiquitinationAPGVEEIKSNSFFEG
CCCCHHHHCCCCCCC		47.03-
407PhosphorylationEIKSIDDTSNFDEFP
EEEECCCCCCCCCCC		23.09-
420UbiquitinationFPESDILKPTVATSN
CCHHHCCCCEEECCC		38.69-
434UbiquitinationNHPETDYKNKDWVFI
CCCCCCCCCCCEEEE		61.40-
443PhosphorylationKDWVFINYTYKRFEG
CCEEEEEEEEEECCC		13.46-
444PhosphorylationDWVFINYTYKRFEGL
CEEEEEEEEEECCCC		20.3412493777
445PhosphorylationWVFINYTYKRFEGLT
EEEEEEEEEECCCCC		6.9822322096
452PhosphorylationYKRFEGLTARGAIPS
EEECCCCCCCCCCCH		25.7628060719
454MethylationRFEGLTARGAIPSYM
ECCCCCCCCCCCHHH		29.82115484657
460PhosphorylationARGAIPSYMKAAK--
CCCCCCHHHHHCC--		9.40-
462UbiquitinationGAIPSYMKAAK----
CCCCHHHHHCC----		36.64-
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
6SPhosphorylationKinaseGSK3BP49841
PSP
7TPhosphorylationKinaseGSK3BP49841
PSP
7TPhosphorylationKinasePLK1P53350
PSP
10SPhosphorylationKinasePRKACAP17612
GPS
11SPhosphorylationKinasePRKACAP17612
GPS
74TPhosphorylationKinaseMEKK2Q9Y2U5
PSP
91SPhosphorylationKinaseMEKK2Q9Y2U5
PSP
183TPhosphorylationKinasePLK1P53350
PSP
243TPhosphorylationKinaseMEKK2Q9Y2U5
PSP
270TPhosphorylationKinaseMEKK2Q9Y2U5
PSP
281SPhosphorylationKinaseSTK38Q15208
PhosphoELM
407TPhosphorylationKinasePLK1P53350
PSP
444TPhosphorylationKinaseSTK24Q9Y6E0
GPS
444TPhosphorylationKinaseSTK38Q15208
GPS
444TPhosphorylationKinaseSTK4Q13043
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STK38_HUMAN !!
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 STK38_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTDP1_HUMANCTDP1physical
15670829
M3K1_HUMANMAP3K1physical
17906693
M3K2_HUMANMAP3K2physical
17906693
MOB2_HUMANMOB2physical
20624913
MOB1A_HUMANMOB1Aphysical
20624913
STK38_HUMANSTK38physical
9774336
MOB1A_HUMANMOB1Aphysical
15197186
MOB2_HUMANMOB2physical
15067004
MOB1B_HUMANMOB1Bphysical
15067004
MOB2_HUMANMOB2physical
25852190
MOB1A_HUMANMOB1Aphysical
25852190
EM55_HUMANMPP1physical
26344197
H2A2C_HUMANHIST2H2ACphysical
26527279
H2B2E_HUMANHIST2H2BEphysical
26527279
SOCS2_HUMANSOCS2physical
28216640
HEY1_HUMANHEY1physical
27129302
TRAF3_HUMANTRAF3physical
28219902
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 STK38_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Mechanism of Ca2+-mediated regulation of NDR protein kinase throughautophosphorylation and phosphorylation by an upstream kinase.";
Tamaskovic R., Bichsel S.J., Rogniaux H., Stegert M.R., Hemmings B.A.;
J. Biol. Chem. 278:6710-6718(2003).
Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-74; SER-281 ANDTHR-444, AND MUTAGENESIS OF THR-74; LYS-118; SER-281 AND THR-444.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-26, AND MASSSPECTROMETRY.

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