ST38L_HUMAN - dbPTM
ST38L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ST38L_HUMAN
UniProt AC Q9Y2H1
Protein Name Serine/threonine-protein kinase 38-like
Gene Name STK38L {ECO:0000312|EMBL:AAH28603.1}
Organism Homo sapiens (Human).
Sequence Length 464
Subcellular Localization Cytoplasm. Cytoplasm, cytoskeleton. Membrane. Associated with the actin cytoskeleton. Co-localizes with STK24/MST3 in the membrane.
Protein Description Involved in the regulation of structural processes in differentiating and mature neuronal cells..
Protein Sequence MAMTAGTTTTFPMSNHTRERVTVAKLTLENFYSNLILQHEERETRQKKLEVAMEEEGLADEEKKLRRSQHARKETEFLRLKRTRLGLDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKSDMLEKEQVAHIRAERDILVEADGAWVVKMFYSFQDKRNLYLIMEFLPGGDMMTLLMKKDTLTEEETQFYISETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTGLKKAHRTEFYRNLTHNPPSDFSFQNMNSKRKAETWKKNRRQLAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQETYRKVMNWKETLVFPPEVPISEKAKDLILRFCIDSENRIGNSGVEEIKGHPFFEGVDWEHIRERPAAIPIEIKSIDDTSNFDDFPESDILQPVPNTTEPDYKSKDWVFLNYTYKRFEGLTQRGSIPTYMKAGKL
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------MAMTAGTTT
------CCCCCCCEE		12.20-
4Phosphorylation----MAMTAGTTTTF
----CCCCCCCEEEE		16.6423401153
7Phosphorylation-MAMTAGTTTTFPMS
-CCCCCCCEEEECCC		20.6421406692
8PhosphorylationMAMTAGTTTTFPMSN
CCCCCCCEEEECCCC		23.9523401153
9PhosphorylationAMTAGTTTTFPMSNH
CCCCCCEEEECCCCC		26.6923401153
10PhosphorylationMTAGTTTTFPMSNHT
CCCCCEEEECCCCCC		24.5323401153
14PhosphorylationTTTTFPMSNHTRERV
CEEEECCCCCCHHCE		26.2023401153
17PhosphorylationTFPMSNHTRERVTVA
EECCCCCCHHCEEEE		38.1823401153
17UbiquitinationTFPMSNHTRERVTVA
EECCCCCCHHCEEEE		38.18-
21UbiquitinationSNHTRERVTVAKLTL
CCCCHHCEEEEEEHH		4.2924816145
26UbiquitinationERVTVAKLTLENFYS
HCEEEEEEHHHHHHH		4.82-
30UbiquitinationVAKLTLENFYSNLIL
EEEEHHHHHHHHHHH		44.2424816145
32PhosphorylationKLTLENFYSNLILQH
EEHHHHHHHHHHHHH		14.2927642862
42UbiquitinationLILQHEERETRQKKL
HHHHHHHHHHHHHHH		47.8322817900
71UbiquitinationKLRRSQHARKETEFL
HHHHHHHHHHHHHHH		19.3224816145
73UbiquitinationRRSQHARKETEFLRL
HHHHHHHHHHHHHHH		70.5324816145
75PhosphorylationSQHARKETEFLRLKR
HHHHHHHHHHHHHHC		34.7628857561
82UbiquitinationTEFLRLKRTRLGLDD
HHHHHHHCCCCCCCC		29.6624816145
94UbiquitinationLDDFESLKVIGRGAF
CCCHHHCEEEECCCC		40.8821906983
110UbiquitinationEVRLVQKKDTGHIYA
EEEEEEECCCCCEEE		43.35-
116PhosphorylationKKDTGHIYAMKILRK
ECCCCCEEEEEEHHH		8.5829496907
119UbiquitinationTGHIYAMKILRKSDM
CCCEEEEEEHHHHHC		30.34-
122UbiquitinationIYAMKILRKSDMLEK
EEEEEEHHHHHCCCH		39.65-
122UbiquitinationIYAMKILRKSDMLEK
EEEEEEHHHHHCCCH		39.6522817900
123UbiquitinationYAMKILRKSDMLEKE
EEEEEHHHHHCCCHH		47.5724816145
129UbiquitinationRKSDMLEKEQVAHIR
HHHHCCCHHHHHHHH		49.8629967540
131UbiquitinationSDMLEKEQVAHIRAE
HHCCCHHHHHHHHHH		49.0922817900
131UbiquitinationSDMLEKEQVAHIRAE
HHCCCHHHHHHHHHH		49.09-
135UbiquitinationEKEQVAHIRAERDIL
CHHHHHHHHHHCCEE		3.0022817900
135UbiquitinationEKEQVAHIRAERDIL
CHHHHHHHHHHCCEE		3.00-
146UbiquitinationRDILVEADGAWVVKM
CCEEEEECCCEEEEE		33.56-
147UbiquitinationDILVEADGAWVVKMF
CEEEEECCCEEEEEE		28.52-
163UbiquitinationSFQDKRNLYLIMEFL
EECCCCCEEEEEECC		4.2322817900
164PhosphorylationFQDKRNLYLIMEFLP
ECCCCCEEEEEECCC		9.5723532336
172UbiquitinationLIMEFLPGGDMMTLL
EEEECCCCCCHHHEE		47.0522817900
173UbiquitinationIMEFLPGGDMMTLLM
EEECCCCCCHHHEEE		20.08-
173UbiquitinationIMEFLPGGDMMTLLM
EEECCCCCCHHHEEE		20.0827667366
174UbiquitinationMEFLPGGDMMTLLMK
EECCCCCCHHHEEEC		29.6022817900
176UbiquitinationFLPGGDMMTLLMKKD
CCCCCCHHHEEECCC		2.5822817900
177PhosphorylationLPGGDMMTLLMKKDT
CCCCCHHHEEECCCC		15.3123532336
183UbiquitinationMTLLMKKDTLTEEET
HHEEECCCCCCHHHH		41.2422817900
184PhosphorylationTLLMKKDTLTEEETQ
HEEECCCCCCHHHHH		44.45-
187UbiquitinationMKKDTLTEEETQFYI
ECCCCCCHHHHHHHH		57.8822817900
214UbiquitinationLGFIHRDIKPDNLLL
HCCCCCCCCCCCEEE		7.6127667366
215UbiquitinationGFIHRDIKPDNLLLD
CCCCCCCCCCCEEEC		51.0821906983
224UbiquitinationDNLLLDAKGHVKLSD
CCEEECCCCCEEHHH		49.5721906983
225UbiquitinationNLLLDAKGHVKLSDF
CEEECCCCCEEHHHC		32.3227667366
228UbiquitinationLDAKGHVKLSDFGLC
ECCCCCEEHHHCCCC		36.2822817900
236PhosphorylationLSDFGLCTGLKKAHR
HHHCCCCCCCCHHHH		51.0620068231
239UbiquitinationFGLCTGLKKAHRTEF
CCCCCCCCHHHHCHH		49.62-
259PhosphorylationHNPPSDFSFQNMNSK
CCCCCCCCCCCCCCH		30.8028122231
265PhosphorylationFSFQNMNSKRKAETW
CCCCCCCCHHHHHHH		24.0628450419
266UbiquitinationSFQNMNSKRKAETWK
CCCCCCCHHHHHHHH		53.5727667366
281PhosphorylationKNRRQLAYSTVGTPD
HHHHHHHHCCCCCCC		17.2921712546
282PhosphorylationNRRQLAYSTVGTPDY
HHHHHHHCCCCCCCC		15.8323401153
283PhosphorylationRRQLAYSTVGTPDYI
HHHHHHCCCCCCCCC		15.4121712546
285UbiquitinationQLAYSTVGTPDYIAP
HHHHCCCCCCCCCCH		31.45-
286PhosphorylationLAYSTVGTPDYIAPE
HHHCCCCCCCCCCHH		14.5128102081
289PhosphorylationSTVGTPDYIAPEVFM
CCCCCCCCCCHHHHH		10.5323403867
298PhosphorylationAPEVFMQTGYNKLCD
CHHHHHHCCCHHHHH		29.8221406692
300PhosphorylationEVFMQTGYNKLCDWW
HHHHHCCCHHHHHHH		16.7121406692
355UbiquitinationVPISEKAKDLILRFC
CCCCHHHHHHHHHHH		65.22-
367UbiquitinationRFCIDSENRIGNSGV
HHHCCCCCCCCCCCC		44.83-
378UbiquitinationNSGVEEIKGHPFFEG
CCCCHHHCCCCCCCC		55.2229967540
403UbiquitinationAAIPIEIKSIDDTSN
CCCCEEEEECCCCCC		28.6829967540
441PhosphorylationKDWVFLNYTYKRFEG
CCEEEEEEEEEECCC		17.3729523821
442PhosphorylationDWVFLNYTYKRFEGL
CEEEEEEEEEECCCC		22.8422322096
443PhosphorylationWVFLNYTYKRFEGLT
EEEEEEEEEECCCCC		6.9822322096
450PhosphorylationYKRFEGLTQRGSIPT
EEECCCCCCCCCCCC		27.3823403867
452MethylationRFEGLTQRGSIPTYM
ECCCCCCCCCCCCCC		35.27115484663
454PhosphorylationEGLTQRGSIPTYMKA
CCCCCCCCCCCCCCC		27.8123403867
457PhosphorylationTQRGSIPTYMKAGKL
CCCCCCCCCCCCCCC		34.2823403867
458PhosphorylationQRGSIPTYMKAGKL-
CCCCCCCCCCCCCC-		7.4020068231
460UbiquitinationGSIPTYMKAGKL---
CCCCCCCCCCCC---		43.50-
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
282SPhosphorylationKinaseSTK38LQ9Y2H1
GPS
442TPhosphorylationKinaseSTK24Q9Y6E0
PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ST38L_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 ST38L_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
K1H1_HUMANKRT31physical
17353931
MOB1A_HUMANMOB1Aphysical
17353931
MOB2_HUMANMOB2physical
20624913
MOB2_HUMANMOB2physical
15067004
MOB1B_HUMANMOB1Bphysical
15067004
MOB2_HUMANMOB2physical
25852190
MOB1A_HUMANMOB1Aphysical
25852190
CDC37_HUMANCDC37physical
24366813
MOB1A_HUMANMOB1Aphysical
24366813
MOB1B_HUMANMOB1Bphysical
24366813
MOB2_HUMANMOB2physical
24366813
TRY1_HUMANPRSS1physical
24366813
MOB2_HUMANMOB2physical
28514442
MOB1A_HUMANMOB1Aphysical
28514442
PERI_HUMANPRPHphysical
28514442
HEY1_HUMANHEY1physical
27129302
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 ST38L_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Regulation of NDR2 protein kinase by multi-site phosphorylation andthe S100B calcium-binding protein.";
Stegert M.R., Tamaskovic R., Bichsel S.J., Hergovich A.,Hemmings B.A.;
J. Biol. Chem. 279:23806-23812(2004).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, ENZYMEREGULATION, INTERACTION WITH S100, PHOSPHORYLATION AT THR-75; SER-282AND THR-442, AND MUTAGENESIS OF THR-75; LYS-119; SER-282 AND THR-442.
"Regulation of NDR protein kinase by hydrophobic motif phosphorylationmediated by the mammalian Ste20-like kinase MST3.";
Stegert M.R., Hergovich A., Tamaskovic R., Bichsel S.J.,Hemmings B.A.;
Mol. Cell. Biol. 25:11019-11029(2005).
Cited for: PHOSPHORYLATION AT THR-442, ENZYME REGULATION, AND SUBCELLULARLOCATION.

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