dbPTM

ST38L_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ST38L_MOUSE
UniProt AC	Q7TSE6
Protein Name	Serine/threonine-protein kinase 38-like
Gene Name	Stk38l {ECO:0000312\|EMBL:AAP44998.1}
Organism	Mus musculus (Mouse).
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	MAMTAGATTTFPMSNHTRERVTVAKLTLENFYSNLILQHEERETRQKKLEVAMEEEGLADEEKKLRRSQHARKETEFLRLKRTRLGLDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRAERDILVEADGAWVVKMFYSFQDKRNLYLIMEFLPGGDMMTLLMKKDTLTEEETQFYISETVLAIDAIHQLGFIHRDVKPDNLLLDAKGHVKLSDFGLCTGLKKAHRTEFYRNLTHNPPSDFSFQNMNSKRKAETWKKNRRQLAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGFPPFCSETPQETYRKVMSWKETLAFPPEVPVSEKAKDLILRFCTDSENRIGNGGVEEIKGHPFFEGVDWGHIRERPAAIPIEIRSIDDTSNFDDFPESDILQPVPNTTEPDYKSKDWVFLNYTYKRFEGLTQRGSIPTYMKAGKL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAMTAGATT ------CCCCCCCEE	12.20	-
14	Phosphorylation	ATTTFPMSNHTRERV CEEEECCCCCCHHCE	26.20	-
17	Phosphorylation	TFPMSNHTRERVTVA EECCCCCCHHCEEEE	38.18	-
68	Phosphorylation	EEKKLRRSQHARKET HHHHHHHHHHHHHHH	21.63	-
75	Phosphorylation	SQHARKETEFLRLKR HHHHHHHHHHHHHHC	34.76	-
265	Phosphorylation	FSFQNMNSKRKAETW CCCCCCCCHHHHHHH	24.06	22817900
281	Phosphorylation	KNRRQLAYSTVGTPD HHHHHHHHCCCCCCC	17.29	26745281
282	Phosphorylation	NRRQLAYSTVGTPDY HHHHHHHCCCCCCCC	15.83	27087446
283	Phosphorylation	RRQLAYSTVGTPDYI HHHHHHCCCCCCCCC	15.41	26745281
286	Phosphorylation	LAYSTVGTPDYIAPE HHHCCCCCCCCCCHH	14.51	26745281
289	Phosphorylation	STVGTPDYIAPEVFM CCCCCCCCCCHHHHH	10.53	26745281
442	Phosphorylation	DWVFLNYTYKRFEGL CEEEEEEEEEECCCC	22.84	29899451
450	Phosphorylation	YKRFEGLTQRGSIPT EEECCCCCCCCCCCC	27.38	17525332
454	Phosphorylation	EGLTQRGSIPTYMKA CCCCCCCCCCCCCCC	27.81	29514104

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
442	T	Phosphorylation	Kinase	MST3	Q99KH8	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ST38L_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of ST38L_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of ST38L_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, AND MASSSPECTROMETRY.	17525332 [Abstract]