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P36874 (PP1GA_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length323 AA.
Sequence statusComplete.
Protein existenceEvidence 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 protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate. Ref.1

Cofactor

Binds 2 manganese ions 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. Nucleusnucleolus By similarity. Cleavage furrow By similarity. Nucleusnucleoplasm By similarity. Chromosomecentromerekinetochore 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 processCarbohydrate metabolism
Cell cycle
Cell division
Glycogen metabolism
Mitosis
   Cellular componentCentromere
Chromosome
Cytoplasm
Kinetochore
Membrane
Mitochondrion
Nucleus
   LigandManganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
Gene Ontology (GO)
   Biological_processglycogen metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic nuclear division

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_componentcleavage 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_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 19730412PubMed 20691903. Source: IntAct

protein serine/threonine phosphatase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 323323Serine/threonine-protein phosphatase PP1-gamma catalytic subunit A
PRO_0000058790

Sites

Active site1251Proton donor By similarity
Metal binding641Manganese 1 By similarity
Metal binding661Manganese 1 By similarity
Metal binding921Manganese 1 By similarity
Metal binding921Manganese 2 By similarity
Metal binding1241Manganese 2 By similarity
Metal binding1731Manganese 2 By similarity
Metal binding2481Manganese 2 By similarity

Experimental info

Sequence conflict2131V → I in AAA49934. Ref.2
Sequence conflict2201D → Y in AAA49934. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P36874 [UniParc].

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

FASTA32336,956
        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' 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.
RefSeqNP_001081308.1. NM_001087839.1.
UniGeneXl.6679.

3D structure databases

ProteinModelPortalP36874.
SMRP36874. Positions 6-300.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP36874. 2 interactions.
MINTMINT-7978751.

Proteomic databases

PRIDEP36874.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397767.
KEGGxla:397767.

Organism-specific databases

XenbaseXB-GENE-967940. ppp1cc.

Phylogenomic databases

HOVERGENHBG000216.
KOK06269.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMSSF56300. SSF56300. 1 hit.
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePP1GA_XENLA
AccessionPrimary (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: June 11, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families