PP1B_RABIT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PP1B_RABIT
• UniProt AC: P62143
• Protein Name: Serine/threonine-protein phosphatase PP1-beta catalytic subunit
• Gene Name: PPP1CB
• Organism: Oryctolagus cuniculus (Rabbit).
• Sequence Length: 327
• Subcellular Localization: Cytoplasm . Nucleus . Nucleus, nucleoplasm . Nucleus, nucleolus . Highly mobile in cells and can be relocalized through interaction with targeting subunits. In the presence of PPP1R8 relocalizes from the nucleus to nuclear speckles.
• Protein Description: Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase (PP1) is essential for cell division, it participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E (By similarity)..
• Protein Sequence: MADGELNVDSLITRLLEVRGCRPGKIVQMTEAEVRGLCIKSREIFLSQPILLELEAPLKICGDIHGQYTDLLRLFEYGGFPPEANYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRFNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVSKFLNRHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGGMMSVDETLMCSFQILKPSEKKAKYQYGGLNSGRPVTPPRTANPPKKR

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	------MADGELNVD ------CCCCCCCHH	33.25	-
126	S-nitrosocysteine	LLRGNHECASINRIY EECCCCHHHHHHHHE	2.53	-
126	S-nitrosylation	LLRGNHECASINRIY EECCCCHHHHHHHHE	2.53	21278135
201	S-nitrosocysteine	VPDTGLLCDLLWSDP CCCCCCHHHHHCCCC	4.10	-
201	S-nitrosylation	VPDTGLLCDLLWSDP CCCCCCHHHHHCCCC	4.10	21278135
244	S-nitrosocysteine	RHDLDLICRAHQVVE HHCHHHHHHHHHHHH	4.01	-
244	S-nitrosylation	RHDLDLICRAHQVVE HHCHHHHHHHHHHHH	4.01	21278135
316	Phosphorylation	LNSGRPVTPPRTANP CCCCCCCCCCCCCCC	30.20	-

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

Oops, there are no upstream regulatory protein records of PP1B_RABIT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PP1B_RABIT !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of PP1B_RABIT !!

Protein-Protein Interaction

Oops, there are no PPI records of PP1B_RABIT !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.