CPLM-012564

Genbank Nucleotide ID

Protein phosphatase 1 regulatory subunit 7

Protein Synonyms/Alias

Protein phosphatase 1 regulatory subunit 22

Homo sapiens (Human)

Position	Peptide	Type	References
90	LNHYRIGKIEGFEVL	ubiquitination	[1, 2, 3]
98	IEGFEVLKKVKTLCL	ubiquitination	[3]
99	EGFEVLKKVKTLCLR	ubiquitination	[3]
101	FEVLKKVKTLCLRQN	ubiquitination	[3, 4, 5]
111	CLRQNLIKCIENLEE	ubiquitination	[3]
133	DLYDNQIKKIENLEA	ubiquitination	[1, 3]
162	RNIEGVDKLTRLKKL	ubiquitination	[1, 3]
167	VDKLTRLKKLFLVNN	ubiquitination	[3]
168	DKLTRLKKLFLVNNK	ubiquitination	[3, 4, 5]
175	KLFLVNNKISKIENL	ubiquitination	[3, 4, 5, 6]
178	LVNNKISKIENLSNL	ubiquitination	[3, 4, 5]
217	LESLFLGKNKITKLQ	ubiquitination	[1, 3, 4, 5, 6]
219	SLFLGKNKITKLQNL	ubiquitination	[3]
222	LGKNKITKLQNLDAL	ubiquitination	[1, 3, 4, 5]
244	MQSNRLTKIEGLQNL	ubiquitination	[1, 2, 3, 4, 5, 6]
335	LERNPLQKDPQYRRK	ubiquitination	[2]

[1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]

Functional Description

Regulatory subunit of protein phosphatase 1 (By similarity).

REPEAT 77 98 LRR 1.
REPEAT 99 120 LRR 2.
REPEAT 121 142 LRR 3.
REPEAT 143 164 LRR 4.
REPEAT 165 186 LRR 5.
REPEAT 187 208 LRR 6.
REPEAT 209 230 LRR 7.
REPEAT 231 252 LRR 8.
REPEAT 253 274 LRR 9.
REPEAT 275 296 LRR 10.
REPEAT 297 318 LRR 11.
DOMAIN 331 360 LRRCT.
MOD_RES 2 2 N-acetylalanine.
MOD_RES 12 12 Phosphoserine.
MOD_RES 24 24 Phosphoserine.
MOD_RES 27 27 Phosphoserine.
MOD_RES 44 44 Phosphoserine.
MOD_RES 47 47 Phosphoserine.

Acetylation; Alternative splicing; Complete proteome; Leucine-rich repeat; Nucleus; Phosphoprotein; Reference proteome; Repeat.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; TAS:ProtInc.
GO:0005634; C:nucleus; TAS:ProtInc.
GO:0008599; F:protein phosphatase type 1 regulator activity; TAS:ProtInc.

IPR001611; Leu-rich_rpt.
IPR025875; Leu-rich_rpt_4.
IPR003603; U2A'_phosphoprotein32A_C.