STK16_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: STK16_HUMAN
• UniProt AC: O75716
• Protein Name: Serine/threonine-protein kinase 16
• Gene Name: STK16
• Organism: Homo sapiens (Human).
• Sequence Length: 305
• Subcellular Localization: Cytoplasm, perinuclear region. Membrane; Lipid-anchor. Associates with Golgi and Golgi-derived vesicles..
• Protein Description: Membrane-associated protein kinase that phosphorylates on serine and threonine residues. In vitro substrates include DRG1, ENO1 and EIF4EBP1. Also autophosphorylates. May be involved in secretory vesicle trafficking or intracellular signaling. May have a role in regulating stromal-epithelial interactions that occur during ductal morphogenesis in the mammary gland. May be involved in TGF-beta signaling. Able to autophosphorylate on Tyr residue; it is however unclear whether it has tyrosine-protein kinase toward other proteins..
• Protein Sequence: MGHALCVCSRGTVIIDNKRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRERGAKHEAWLLLPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGSRQALTLQDWAAQRCTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEALQPPAPGQHTTQI

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
2	N-myristoyl glycine	------MGHALCVCS ------CCCEEEEEC	18.12	-
2	Myristoylation	------MGHALCVCS ------CCCEEEEEC	18.12	10364453
6	S-palmitoylation	--MGHALCVCSRGTV --CCCEEEEECCCEE	2.77	10364453
8	S-palmitoylation	MGHALCVCSRGTVII CCCEEEEECCCEEEE	1.93	10364453
53	S-nitrosylation	YALKRILCHEQQDRE HHHHHHHHCHHHCHH	2.86	24105792
102	Ubiquitination	WLLLPFFKRGTLWNE HHHHHHHHCCCHHHH	50.74	21890473
185	Phosphorylation	EGSRQALTLQDWAAQ ECCCCEEEHHHHHHH	25.95	18184589
197	Phosphorylation	AAQRCTISYRAPELF HHHHCCEEEECCCCE	7.16	18184589
198	Phosphorylation	AQRCTISYRAPELFS HHHCCEEEECCCCEE	13.62	18184589
244	Phosphorylation	MVFQKGDSVALAVQN EEEECCCHHEEEECC	20.25	25247763
258	Phosphorylation	NQLSIPQSPRHSSAL CCCCCCCCHHCHHHH	20.67	-

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
185	T	Phosphorylation	Kinase	STK16	O75716	GPS
197	S	Phosphorylation	Kinase	STK16	O75716	GPS
198	Y	Phosphorylation	Kinase	STK16	O75716	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
6	C	Palmitoylation	It is uncertain whether palmitoylation is on Cys-6 and/or Cys-8.	10364453
8	C	Palmitoylation	It is uncertain whether palmitoylation is on Cys-6 and/or Cys-8.	10364453

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of STK16_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NAGK_HUMAN	NAGK	physical	11741987
RPIA_HUMAN	RPIA	physical	16189514
KCD17_HUMAN	KCTD17	physical	16189514
ATL4_HUMAN	ADAMTSL4	physical	16189514
MKKS_HUMAN	MKKS	physical	17353931
EBLN2_HUMAN	EBLN2	physical	17353931
ELK1_HUMAN	ELK1	physical	10947953
STK16_HUMAN	STK16	physical	10947953
ATL4_HUMAN	ADAMTSL4	physical	19060904
DNJA3_HUMAN	DNAJA3	physical	25416956
CACO2_HUMAN	CALCOCO2	physical	25416956
SPY2_HUMAN	SPRY2	physical	25416956
CIKS_HUMAN	TRAF3IP2	physical	25416956
IKZF3_HUMAN	IKZF3	physical	25416956
RPIA_HUMAN	RPIA	physical	25416956
MTUS2_HUMAN	MTUS2	physical	25416956
FBLN4_HUMAN	EFEMP2	physical	25416956
PLS3_HUMAN	PLSCR3	physical	25416956
NIF3L_HUMAN	NIF3L1	physical	25416956
MIIP_HUMAN	MIIP	physical	25416956
KCD14_HUMAN	KCTD14	physical	25416956
KCD17_HUMAN	KCTD17	physical	25416956
CCD33_HUMAN	CCDC33	physical	25416956
EFHC2_HUMAN	EFHC2	physical	25416956
AL2SB_HUMAN	ALS2CR12	physical	25416956
KR131_HUMAN	KRTAP13-1	physical	25416956
MGT5B_HUMAN	MGAT5B	physical	25416956
SAXO1_HUMAN	FAM154A	physical	25416956
RFX6_HUMAN	RFX6	physical	25416956
TRI42_HUMAN	TRIM42	physical	25416956
KR107_HUMAN	KRTAP10-7	physical	25416956
KR109_HUMAN	KRTAP10-9	physical	25416956
KR108_HUMAN	KRTAP10-8	physical	25416956
KR103_HUMAN	KRTAP10-3	physical	25416956
INCA1_HUMAN	INCA1	physical	25416956
NT2NL_HUMAN	NOTCH2NL	physical	25416956
KR261_HUMAN	KRTAP26-1	physical	25416956
CE030_HUMAN	C5orf30	physical	28514442
ATG4B_HUMAN	ATG4B	physical	28514442
URFB1_HUMAN	UHRF1BP1	physical	28514442
TBB3_HUMAN	TUBB3	physical	28514442
TBB8_HUMAN	TUBB8	physical	28514442
POF1B_HUMAN	POF1B	physical	28514442
DCA10_HUMAN	DCAF10	physical	28514442
FILA_HUMAN	FLG	physical	28514442
FBX50_HUMAN	NCCRP1	physical	28514442

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.

Related Literatures of Post-Translational Modification

Myristoylation

"Identification and characterization of a myristylated andpalmitylated serine/threonine protein kinase.";
Berson A.E., Young C., Morrison S.L., Fujii G.H., Sheung J., Wu B.,Bolen J.B., Burkhardt A.L.;
Biochem. Biophys. Res. Commun. 259:533-538(1999).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION,AUTOPHOSPHORYLATION, MYRISTOYLATION AT GLY-2, PALMITOYLATION AT CYS-6AND CYS-8, AND MUTAGENESIS OF GLY-2; CYS-6 AND CYS-8.
PubMed: 10364453

Phosphorylation

"Structure of the human protein kinase MPSK1 reveals an atypicalactivation loop architecture.";
Eswaran J., Bernad A., Ligos J.M., Guinea B., Debreczeni J.E.,Sobott F., Parker S.A., Najmanovich R., Turk B.E., Knapp S.;
Structure 16:115-124(2008).
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 13-304 OF WILD TYPE AND INCOMPLEX WITH STAUROSPORINE, SUBUNIT, INTERACTION WITH DRG1,AUTOPHOSPHORYLATION AT THR-185; SER-197 AND TYR-198, AND MASSSPECTROMETRY.
PubMed: 18184589