PP1RB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PP1RB_HUMAN
• UniProt AC: O60927
• Protein Name: E3 ubiquitin-protein ligase PPP1R11 {ECO:0000303|PubMed:27805901}
• Gene Name: PPP1R11
• Organism: Homo sapiens (Human).
• Sequence Length: 126
• Protein Description: Atypical E3 ubiquitin-protein ligase which ubiquitinates TLR2 at 'Lys-754' leading to its degradation by the proteasome. Plays a role in regulating inflammatory cytokine release and gram-positive bacterial clearance by functioning, in part, through the ubiquitination and degradation of TLR2. [PubMed: 27805901 Inhibitor of protein phosphatase 1]
• Protein Sequence: MAEAGAGLSETVTETTVTVTTEPENRSLTIKLRKRKPEKKVEWTSDTVDNEHMGRRSSKCCCIYEKPRAFGESSTESDEEEEEGCGHTHCVRGHRKGRRRATLGPTPTTPPQPPDPSQPPPGPMQH

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	Acetylation	------MAEAGAGLS ------CCCCCCCCC	18.49	22814378
9	Phosphorylation	AEAGAGLSETVTETT CCCCCCCCCCEEEEE	30.24	24043423
11	Phosphorylation	AGAGLSETVTETTVT CCCCCCCCEEEEEEE	29.38	20068231
13	Phosphorylation	AGLSETVTETTVTVT CCCCCCEEEEEEEEE	34.73	20068231
15	Phosphorylation	LSETVTETTVTVTTE CCCCEEEEEEEEECC	19.73	20068231
16	O-linked_Glycosylation	SETVTETTVTVTTEP CCCEEEEEEEEECCC	14.14	29351928
16	Phosphorylation	SETVTETTVTVTTEP CCCEEEEEEEEECCC	14.14	20068231
18	Phosphorylation	TVTETTVTVTTEPEN CEEEEEEEEECCCCC	15.28	20068231
20	Phosphorylation	TETTVTVTTEPENRS EEEEEEEECCCCCCE	18.97	20068231
21	Phosphorylation	ETTVTVTTEPENRSL EEEEEEECCCCCCEE	45.25	20068231
27	Phosphorylation	TTEPENRSLTIKLRK ECCCCCCEEEEEEEC	41.25	24719451
29	Phosphorylation	EPENRSLTIKLRKRK CCCCCEEEEEEECCC	19.81	-
31	Acetylation	ENRSLTIKLRKRKPE CCCEEEEEEECCCCC	36.68	25953088
44	Phosphorylation	PEKKVEWTSDTVDNE CCCCEECCCCCCCCC	11.83	28555341
45	Phosphorylation	EKKVEWTSDTVDNEH CCCEECCCCCCCCCC	32.15	25159151
47	Phosphorylation	KVEWTSDTVDNEHMG CEECCCCCCCCCCCC	29.53	27251275
53	Sulfoxidation	DTVDNEHMGRRSSKC CCCCCCCCCCCCCCE	3.49	30846556
57	Phosphorylation	NEHMGRRSSKCCCIY CCCCCCCCCCEEEEE	32.56	23927012
58	Phosphorylation	EHMGRRSSKCCCIYE CCCCCCCCCEEEEEE	28.09	29496963
59	Ubiquitination	HMGRRSSKCCCIYEK CCCCCCCCEEEEEEC	32.32	-
59	Acetylation	HMGRRSSKCCCIYEK CCCCCCCCEEEEEEC	32.32	25953088
64	Phosphorylation	SSKCCCIYEKPRAFG CCCEEEEEECCCCCC	12.18	21945579
66	Ubiquitination	KCCCIYEKPRAFGES CEEEEEECCCCCCCC	23.88	-
66	Acetylation	KCCCIYEKPRAFGES CEEEEEECCCCCCCC	23.88	23749302
73	Phosphorylation	KPRAFGESSTESDEE CCCCCCCCCCCCHHH	42.83	21955146
74	Phosphorylation	PRAFGESSTESDEEE CCCCCCCCCCCHHHH	31.71	21955146
75	Phosphorylation	RAFGESSTESDEEEE CCCCCCCCCCHHHHH	49.11	23401153
77	Phosphorylation	FGESSTESDEEEEEG CCCCCCCCHHHHHCC	50.87	22617229
88	Phosphorylation	EEEGCGHTHCVRGHR HHCCCCCCHHHCCCC	11.40	30576142
102	Phosphorylation	RKGRRRATLGPTPTT CCCCCCCCCCCCCCC	30.36	21955146
106	Phosphorylation	RRATLGPTPTTPPQP CCCCCCCCCCCCCCC	31.31	21955146
108	Phosphorylation	ATLGPTPTTPPQPPD CCCCCCCCCCCCCCC	55.18	25159151
109	Phosphorylation	TLGPTPTTPPQPPDP CCCCCCCCCCCCCCC	33.89	25159151
117	Phosphorylation	PPQPPDPSQPPPGPM CCCCCCCCCCCCCCC	63.80	30576142

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of PP1RB_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PP1RB_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of PP1RB_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DUT_HUMAN	DUT	physical	26344197
PP1B_HUMAN	PPP1CB	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.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-73; SER-74; THR-75;SER-77 AND THR-109, AND MASS SPECTROMETRY.
PubMed: 18669648

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-74; THR-75 ANDSER-77, AND MASS SPECTROMETRY.
PubMed: 17081983

"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 THR-109, AND MASSSPECTROMETRY.
PubMed: 19690332

"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-64, AND MASSSPECTROMETRY.
PubMed: 15592455