PPR1B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PPR1B_HUMAN
• UniProt AC: Q9UD71
• Protein Name: Protein phosphatase 1 regulatory subunit 1B
• Gene Name: PPP1R1B
• Organism: Homo sapiens (Human).
• Sequence Length: 204
• Subcellular Localization: Cytoplasm.
• Protein Description: Inhibitor of protein-phosphatase 1..
• Protein Sequence: MDPKDRKKIQFSVPAPPSQLDPRQVEMIRRRRPTPAMLFRLSEHSSPEEEASPHQRASGEGHHLKSKRPNPCAYTPPSLKAVQRIAESHLQSISNLNENQASEEEDELGELRELGYPREEDEEEEEDDEEEEEEEDSQAEVLKVIRQSAGQKTTCGQGLEGPWERPPPLDESERDGGSEDQVEDPALSEPGEEPQRPSPSEPGT

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
1	Acetylation	-------MDPKDRKK -------CCHHHHHC	21.02	-
9 (in isoform 2)	Phosphorylation	-	5.84	2557337
12	Phosphorylation	DRKKIQFSVPAPPSQ HHHCCCEECCCCHHH	15.71	27251275
18	Phosphorylation	FSVPAPPSQLDPRQV EECCCCHHHCCHHHH	42.17	30243723
34	Phosphorylation	MIRRRRPTPAMLFRL HHHHHCCCHHHHHHH	23.13	19651774
42	Phosphorylation	PAMLFRLSEHSSPEE HHHHHHHHCCCCHHH	29.07	23312004
45	Phosphorylation	LFRLSEHSSPEEEAS HHHHHCCCCHHHHCC	43.46	26657352
46	Phosphorylation	FRLSEHSSPEEEASP HHHHCCCCHHHHCCH	37.93	28188228
52	Phosphorylation	SSPEEEASPHQRASG CCHHHHCCHHHHCCC	26.62	23312004
58	Phosphorylation	ASPHQRASGEGHHLK CCHHHHCCCCCCCCC	39.30	24719451
66	Phosphorylation	GEGHHLKSKRPNPCA CCCCCCCCCCCCCCC	40.01	2557337
74	Phosphorylation	KRPNPCAYTPPSLKA CCCCCCCCCCHHHHH	26.88	23312004
75	Phosphorylation	RPNPCAYTPPSLKAV CCCCCCCCCHHHHHH	15.36	22617229
78	Phosphorylation	PCAYTPPSLKAVQRI CCCCCCHHHHHHHHH	43.64	22617229
92	Phosphorylation	IAESHLQSISNLNEN HHHHHHHHHHHCCCC	34.05	29802988
94	Phosphorylation	ESHLQSISNLNENQA HHHHHHHHHCCCCCC	40.28	26503514
102	Phosphorylation	NLNENQASEEEDELG HCCCCCCCHHHHHHH	35.46	28355574
116	Phosphorylation	GELRELGYPREEDEE HHHHHHCCCCCCCCC	16.25	-
137	Phosphorylation	EEEEEEDSQAEVLKV HHHHHHHHHHHHHHH	34.27	26657352
148	Phosphorylation	VLKVIRQSAGQKTTC HHHHHHHHCCCCCCC	25.23	24719451
153	Phosphorylation	RQSAGQKTTCGQGLE HHHCCCCCCCCCCCC	21.30	23312004
154	Phosphorylation	QSAGQKTTCGQGLEG HHCCCCCCCCCCCCC	22.98	23312004
172	Phosphorylation	RPPPLDESERDGGSE CCCCCCHHHCCCCCC	37.28	23312004
178	Phosphorylation	ESERDGGSEDQVEDP HHHCCCCCCCCCCCC	43.46	28348404
188	Phosphorylation	QVEDPALSEPGEEPQ CCCCCCCCCCCCCCC	43.80	28188228
198	Phosphorylation	GEEPQRPSPSEPGT- CCCCCCCCCCCCCC-	43.16	26657352
200	Phosphorylation	EPQRPSPSEPGT--- CCCCCCCCCCCC---	61.84	28348404

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
34	T	Phosphorylation	Kinase	PRKACA	P17612	GPS
34	T	Phosphorylation	Kinase	PKA	-	Uniprot
75	T	Phosphorylation	Kinase	CDK5	Q00535	Uniprot
75	T	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
75	T	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
34	T	Phosphorylation	Phosphorylation of Thr-34 is required for activity.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of PPR1B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DLGP4_HUMAN	DLGAP4	physical	16169070
KLHL6_HUMAN	KLHL6	physical	25416956
ACTBL_HUMAN	ACTBL2	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

Phosphorylation

"Phosphorylation of DARPP-32 by Cdk5 modulates dopamine signalling inneurons.";
Bibb J.A., Snyder G.L., Nishi A., Yan Z., Meijer L., Fienberg A.A.,Tsai L.-H., Kwon Y.T., Girault J.-A., Czernik A.J., Huganir R.L.,Hemmings H.C. Jr., Nairn A.C., Greengard P.;
Nature 402:669-671(1999).
Cited for: PHOSPHORYLATION AT THR-75 BY CDK5.
PubMed: 10604473