Serine/threonine-protein phosphatase PP1-gamma catalytic subunit A

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P36874 (PP1GA_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 28, 2012. Version 85. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit A
Short name=PP-1G-A
Short name=xPP1-gamma1
EC=3.1.3.16

Gene names

Name:	ppp1cc-a
Synonyms:	ppp1cc

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	323 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis By similarity. Promotes nuclear envelope reassembly by targeting nuclear membrane vesicles to chromatin at the end of mitosis. Acts by dephosphorylating membrane proteins such as lamin B receptor (lbr) to regulate the binding of membrane proteins to chromatin. Ref.1
Catalytic activity	A phosphoprotein + H₂O = a protein + phosphate. Ref.1
Cofactor	Binds 1 iron ion per subunit By similarity. Binds 1 manganese ion per subunit By similarity.
Subunit structure	PP1 comprises a catalytic subunit, ppp1c1, ppp1cb or ppp1cc, which is folded into its native form by inhibitor 2 and glycogen synthetase kinase 3, and then is complexed to one or several targeting or regulatory subunits By similarity.
Subcellular location	Cytoplasm. Nucleus By similarity. Nucleus › nucleolus By similarity. Cleavage furrow By similarity. Nucleus › nucleoplasm By similarity. Chromosome › centromere › kinetochore By similarity. Nucleus speckle By similarity. Midbody By similarity. Mitochondrion By similarity. Membrane Ref.1.
Sequence similarities	Belongs to the PPP phosphatase family. PP-1 subfamily.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cell cycle Cell division Glycogen metabolism Mitosis
Cellular component	Centromere Chromosome Cytoplasm Kinetochore Membrane Mitochondrion Nucleus
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW glycogen metabolic process Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW mitotic nuclear envelope reassembly Inferred from mutant phenotype Ref.1. Source: UniProtKB protein dephosphorylation Inferred from direct assay Ref.1. Source: UniProtKB
Cellular_component	cleavage furrow Inferred from electronic annotation. Source: UniProtKB-SubCell condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from direct assay Ref.1. Source: UniProtKB midbody Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from sequence or structural similarity. Source: UniProtKB nuclear speck 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 protein serine/threonine phosphatase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
cenpe	O42263	2	EBI-2908704,EBI-2607221

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 323

323

Serine/threonine-protein phosphatase PP1-gamma catalytic subunit A

PRO_0000058790

Sites

Active site

125

Proton donor By similarity

Metal binding

Iron By similarity

Metal binding

Iron By similarity

Metal binding

Iron By similarity

Metal binding

Manganese By similarity

Metal binding

124

Manganese By similarity

Metal binding

173

Manganese By similarity

Metal binding

248

Manganese By similarity

Experimental info

Sequence conflict

213

V → I in AAA49934. Ref.2

Sequence conflict

220

D → Y in AAA49934. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P36874 [UniParc].

Last modified March 3, 2009. Version 2.
Checksum: 8CD4C5DE036A8C2B
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FASTA

323

36,956

        10         20         30         40         50         60 
MADVDKLNID SIIQRLLEVR GSKPGKNVQL QENEIRGLCL KSREIFLSQP ILLELEAPLK 

        70         80         90        100        110        120 
ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFL 

       130        140        150        160        170        180 
LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL 

       190        200        210        220        230        240 
QSMEQIRRIM RPTDVPDQGL LCDLLWSDPD KDVLGWGEND RGVSFTFGAE VVAKFLHKHD 

       250        260        270        280        290        300 
LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAE 

       310        320 
KKKPNASRPV TPPRGMITKQ AKK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nuclear envelope precursor vesicle targeting to chromatin is stimulated by protein phosphatase 1 in Xenopus egg extracts." Ito H., Koyama Y., Takano M., Ishii K., Maeno M., Furukawa K., Horigome T. Exp. Cell Res. 313:1897-1910(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION. Tissue: Oocyte.
[2]	"The C-terminus of Xenopus protein phosphatase 1-gamma1 determines its cell cycle-dependent regulation and phosphorylation." Walker D.H., Rempel R., Maller J.L. Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	NIH - Xenopus Gene Collection (XGC) project Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Egg.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB106881 mRNA. Translation: BAF51554.1. L17039 mRNA. Translation: AAA49934.1. BC090213 mRNA. Translation: AAH90213.1.
RefSeq	NP_001081308.1. NM_001087839.1.
UniGene	Xl.6679.
3D structure databases
ProteinModelPortal	P36874.
SMR	P36874. Positions 6-300.
ModBase	Search...
Protein-protein interaction databases
IntAct	P36874. 1 interaction.
Proteomic databases
PRIDE	P36874.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	397767.
KEGG	xla:397767.
Organism-specific databases
Xenbase	XB-GENE-967940. ppp1cc.
Phylogenomic databases
HOVERGEN	HBG000216.
KO	K06269.
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...

Entry information

Entry name

PP1GA_XENLA

Accession

Primary (citable) accession number: P36874
Secondary accession number(s): Q5EAX1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	March 3, 2009
Last modified:	November 28, 2012
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents