dbPTM

PP14B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PP14B_HUMAN
UniProt AC	Q96C90
Protein Name	Protein phosphatase 1 regulatory subunit 14B
Gene Name	PPP1R14B
Organism	Homo sapiens (Human).
Sequence Length	147
Subcellular Localization	Cytoplasm .
Protein Description	Inhibitor of PPP1CA. Has over 50-fold higher inhibitory activity when phosphorylated (By similarity)..
Protein Sequence	MADSGTAGGAALAAPAPGPGSGGPGPRVYFQSPPGAAGEGPGGADDEGPVRRQGKVTVKYDRKELRKRLNLEEWILEQLTRLYDCQEEEIPELEIDVDELLDMESDDARAARVKELLVDCYKPTEAFISGLLDKIRGMQKLSTPQKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADSGTAGG ------CCCCCCCCC	21.48	22223895
4	Phosphorylation	----MADSGTAGGAA ----CCCCCCCCCCE	28.62	25159151
6	Phosphorylation	--MADSGTAGGAALA --CCCCCCCCCCEEC	26.53	25627689
21	Phosphorylation	APAPGPGSGGPGPRV CCCCCCCCCCCCCCE	43.65	29255136
27	Methylation	GSGGPGPRVYFQSPP CCCCCCCCEEEECCC	41.50	115488487
29	Phosphorylation	GGPGPRVYFQSPPGA CCCCCCEEEECCCCC	9.36	23927012
32	Phosphorylation	GPRVYFQSPPGAAGE CCCEEEECCCCCCCC	24.14	20201521
57	Phosphorylation	VRRQGKVTVKYDRKE CCCCCEEEEEECHHH	18.11	16397254
59	Methylation	RQGKVTVKYDRKELR CCCEEEEEECHHHHH	31.87	30591467
59	Acetylation	RQGKVTVKYDRKELR CCCEEEEEECHHHHH	31.87	30591467
114	Ubiquitination	DARAARVKELLVDCY HHHHHHHHHHHHHHC	36.77	22053931
121	Phosphorylation	KELLVDCYKPTEAFI HHHHHHHCCCHHHHH	18.62	22817900
122	Ubiquitination	ELLVDCYKPTEAFIS HHHHHHCCCHHHHHH	52.36	-
122	Acetylation	ELLVDCYKPTEAFIS HHHHHHCCCHHHHHH	52.36	26051181
142	Phosphorylation	IRGMQKLSTPQKK-- HHCHHHCCCCCCC--	45.11	30266825
143	Phosphorylation	RGMQKLSTPQKK--- HCHHHCCCCCCC---	39.93	30266825
146	Acetylation	QKLSTPQKK------ HHCCCCCCC------	62.75	25953088
147	Ubiquitination	KLSTPQKK------- HCCCCCCC-------	61.39	24816145

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
57	T	Phosphorylation	Kinase	ILK	Q13418	PSP
57	T	Phosphorylation	Kinase	PRKCA	P17252	GPS
57	T	Phosphorylation	Kinase	PRKCD	Q05655	GPS
57	T	Phosphorylation	Kinase	ROCK2	O75116	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
57	T	Phosphorylation		-
Phosphorylated primarily on Thr-57 by PKC (in vitro).

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 PP14B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
SEP10_HUMAN	SEPT10	physical	26344197

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 PP14B_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-4, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-4, AND MASS SPECTROMETRY.	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-32, AND MASSSPECTROMETRY.	18669648 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND MASSSPECTROMETRY.	16964243 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29, AND MASSSPECTROMETRY.	19534553 [Abstract]

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