dbPTM

KLF16_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KLF16_HUMAN
UniProt AC	Q9BXK1
Protein Name	Krueppel-like factor 16
Gene Name	KLF16
Organism	Homo sapiens (Human).
Sequence Length	252
Subcellular Localization	Nucleus.
Protein Description	Transcription factor that binds GC and GT boxes and displaces Sp1 and Sp3 from these sequences. Modulates dopaminergic transmission in the brain (By similarity)..
Protein Sequence	MSAAVACVDYFAADVLMAISSGAVVHRGRPGPEGAGPAAGLDVRAARREAASPGTPGPPPPPPAASGPGPGAAAAPHLLAASILADLRGGPGAAPGGASPASSSSAASSPSSGRAPGAAPSAAAKSHRCPFPDCAKAYYKSSHLKSHLRTHTGERPFACDWQGCDKKFARSDELARHHRTHTGEKRFSCPLCSKRFTRSDHLAKHARRHPGFHPDLLRRPGARSTSPSDSLPCSLAGSPAPSPAPSPAPAGL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSAAVACVD ------CCHHHHHHH	25.57	24719451
10	Phosphorylation	AAVACVDYFAADVLM HHHHHHHHHHHHHHH	3.76	22203677
21	Phosphorylation	DVLMAISSGAVVHRG HHHHHHHCCCEEECC	25.34	24719451
52	Phosphorylation	AARREAASPGTPGPP HHHHHHCCCCCCCCC	30.80	29255136
55	Phosphorylation	REAASPGTPGPPPPP HHHCCCCCCCCCCCC	28.58	29255136
66	Phosphorylation	PPPPPAASGPGPGAA CCCCCCCCCCCCCCH	47.85	27174698
82	Phosphorylation	APHLLAASILADLRG HHHHHHHHHHHHHHC	16.72	23898821
99	Phosphorylation	GAAPGGASPASSSSA CCCCCCCCCCCCCCC	25.03	25159151
102	Phosphorylation	PGGASPASSSSAASS CCCCCCCCCCCCCCC	33.85	23401153
103	Phosphorylation	GGASPASSSSAASSP CCCCCCCCCCCCCCC	30.34	21955146
104	Phosphorylation	GASPASSSSAASSPS CCCCCCCCCCCCCCC	22.85	28176443
105	Phosphorylation	ASPASSSSAASSPSS CCCCCCCCCCCCCCC	29.78	28176443
108	Phosphorylation	ASSSSAASSPSSGRA CCCCCCCCCCCCCCC	42.36	23401153
109	Phosphorylation	SSSSAASSPSSGRAP CCCCCCCCCCCCCCC	24.87	23401153
111	Phosphorylation	SSAASSPSSGRAPGA CCCCCCCCCCCCCCC	47.58	28176443
112	Phosphorylation	SAASSPSSGRAPGAA CCCCCCCCCCCCCCC	35.36	28176443
121	Phosphorylation	RAPGAAPSAAAKSHR CCCCCCCCHHHHHCC	26.30	30576142
150	Phosphorylation	HLKSHLRTHTGERPF HHHHHHHHCCCCCCC	30.10	24719451
152	Phosphorylation	KSHLRTHTGERPFAC HHHHHHCCCCCCCCC	39.87	25159151
180	Phosphorylation	ELARHHRTHTGEKRF HHHHHHHCCCCCCCC	21.31	-
182	Phosphorylation	ARHHRTHTGEKRFSC HHHHHCCCCCCCCCC	46.56	-
188	Phosphorylation	HTGEKRFSCPLCSKR CCCCCCCCCCCCCCC	20.89	25159151
199	Phosphorylation	CSKRFTRSDHLAKHA CCCCCCCHHHHHHHH	26.73	28555341
224	Phosphorylation	LRRPGARSTSPSDSL HCCCCCCCCCCCCCC	32.47	30278072
225	Phosphorylation	RRPGARSTSPSDSLP CCCCCCCCCCCCCCC	38.82	30278072
226	Phosphorylation	RPGARSTSPSDSLPC CCCCCCCCCCCCCCC	24.53	30278072
228	Phosphorylation	GARSTSPSDSLPCSL CCCCCCCCCCCCCCC	39.33	30278072
230	Phosphorylation	RSTSPSDSLPCSLAG CCCCCCCCCCCCCCC	38.25	30278072
234	Phosphorylation	PSDSLPCSLAGSPAP CCCCCCCCCCCCCCC	21.22	30278072
238	Phosphorylation	LPCSLAGSPAPSPAP CCCCCCCCCCCCCCC	16.57	30278072
242	Phosphorylation	LAGSPAPSPAPSPAP CCCCCCCCCCCCCCC	35.48	22617229
246	Phosphorylation	PAPSPAPSPAPAGL- CCCCCCCCCCCCCC-	35.48	30278072

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
10	Y	Phosphorylation	Kinase	SRC	P12931	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KLF16_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 KLF16_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SIN3A_HUMAN	SIN3A	physical	11438660
SIN3A_HUMAN	SIN3A	physical	12036432
SIN3A_HUMAN	SIN3A	physical	22203677
SIN3B_HUMAN	SIN3B	physical	22203677
EP300_HUMAN	EP300	physical	22203677
WASF2_HUMAN	WASF2	physical	22939629

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 KLF16_HUMAN

Related Literatures of Post-Translational Modification

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-99, AND MASSSPECTROMETRY.	19690332 [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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND SER-109, AND MASSSPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-102; SER-109 ANDTHR-152, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND SER-109, AND MASSSPECTROMETRY.	18220336 [Abstract]