Q5R740 (PP1B_PONAB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase PP1-beta catalytic subunit
Short name=PP-1B
EC=3.1.3.16
EC=3.1.3.53

Gene names

Name:

PPP1CB

Organism

Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Ponginae › Pongo

Protein attributes

Sequence length	327 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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 By similarity.
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate. [Myosin light-chain] phosphate + H2O = [myosin light-chain] + phosphate.
Cofactor	Binds 1 iron ion per subunit By similarity. Binds 1 manganese ion per subunit By similarity.
Enzyme regulation	Inhibited by the toxins okadaic acid, tautomycin and microcystin Leu-Arg. The phosphatase activity of the PPP1R15A-PP1 complex toward EIF2S1 is specifically inhibited by Salubrinal, a drug that protects cells from endoplasmic reticulum stress By similarity.
Subunit structure	PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, which is folded into its native form by inhibitor 2 and glycogen synthetase kinase 3, and then complexed to one or several targeting or regulatory subunits. The targeting or regulatory subunits determine the substrate specificity of PP1. PPP1R12A, PPP1R12B and PPP1R12C mediate binding to myosin. PPP1R3A (in skeletal muscle), PPP1R3B (in liver), PPP1R3C, PPP1R3D and PPP1R3D (in brain) mediate binding to glycogen. PPP1R15A and PPP1R15B mediate binding to EIF2S1. Part of a complex containing PPP1R15B, PP1 and NCK1/2. Component of the MLL5-L complex, at least composed of MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with PPP1R7 and PPP1R12C. Interacts with PPP1R16B. Component of the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1R8. Interacts with PPP1R12A and NUAK1; the interaction is direct. Interacts with TRIM28; the interaction dephosphorylates TRIM28 on 'Ser-824' By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Nucleus › nucleoplasm By similarity. Nucleus › nucleolus By similarity. Note: 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 By similarity.
Sequence similarities	Belongs to the PPP phosphatase family. PP-1 subfamily.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cell cycle Cell division Glycogen metabolism
Cellular component	Cytoplasm Nucleus
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW glycogen metabolic process Inferred from electronic annotation. Source: UniProtKB-KW protein dephosphorylation Inferred from electronic annotation. Source: Compara regulation of cell adhesion Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	MLL5-L complex Inferred from electronic annotation. Source: Compara PTW/PP1 phosphatase complex Inferred from sequence or structural similarity. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW myosin phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB myosin-light-chain-phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 327	326	Serine/threonine-protein phosphatase PP1-beta catalytic subunit		PRO_0000293479
Sites
	Active site	124	1	Proton donor By similarity
	Metal binding	63	1	Iron By similarity
	Metal binding	65	1	Iron By similarity
	Metal binding	91	1	Iron By similarity
	Metal binding	91	1	Manganese By similarity
	Metal binding	123	1	Manganese By similarity
	Metal binding	172	1	Manganese By similarity
	Metal binding	247	1	Manganese By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	316	1	Phosphothreonine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5R740 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: E8356022E9B94ECD	FASTA	327	37,187
	10 20 30 40 50 60 MADGELNVDS LITRLLEVRG CRPGKIVQMT EAEVRGLCIK SREIFLSQPI LLELEAPLKI 70 80 90 100 110 120 CGDIHGQYTD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL ETICLLLAYK IKYPENFFLL 130 140 150 160 170 180 RGNHECASIN RIYGFYDECK RRFNIKLWKT FTDCFNCLPI AAIVDEKIFC CHGGLSPDLQ 190 200 210 220 230 240 SMEQIRRIMR PTDVPDTGLL CDLLWSDPDK DVQGWGENDR GVSFTFGADV VSKFLNRHDL 250 260 270 280 290 300 DLICRAHQVV EDGYEFFAKR QLVTLFSAPN YCGEFDNAGG MMSVDETLMC SFQILKPSEK 310 320 KAKYQYGGLN SGRPVTPPRT ANPPKKR

References

[1]	The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain cortex.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR860278 mRNA. Translation: CAH92420.1.
RefSeq	NP_001126427.1. NM_001132955.1.
UniGene	Pab.468.
3D structure databases
HSSP	HSSP built from PDB template 1S70 based on UniProtKB P62140.
ProteinModelPortal	Q5R740.
ModBase	Search...
Proteomic databases
PRIDE	Q5R740.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSPPYT00000014561; ENSPPYP00000013994; ENSPPYG00000012529.
GeneID	100173410.
KEGG	pon:100173410.
Organism-specific databases
CTD	5500.
Phylogenomic databases
GeneTree	ENSGT00530000062911.
HOVERGEN	HBG000216.
InParanoid	Q5R740.
KO	K06269.
OMA	PDLQGME.
Family and domain databases
InterPro	IPR004843. Metallo_PEstase_dom. IPR006186. Ser/Thr-sp_prot-phosphatase. [Graphical view]
Pfam	PF00149. Metallophos. 1 hit. [Graphical view]
PRINTS	PR00114. STPHPHTASE.
SMART	SM00156. PP2Ac. 1 hit. [Graphical view]
PROSITE	PS00125. SER_THR_PHOSPHATASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q5R740.

Entry information

Entry name

PP1B_PONAB

Accession

Primary (citable) accession number: Q5R740

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	December 21, 2004
Last modified:	May 1, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program