Serine/threonine-protein phosphatase PP1-beta

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P48727 (GLC7B_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 98. History...

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

Documents (2) |

Third-party data

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

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase PP1-beta
EC=3.1.3.16

Alternative name(s):
CeGLC-7-beta
Glc seven-like phosphatase 2

Gene names

Name:	gsp-2
ORF Names:	F56C9.1

Organism

Caenorhabditis elegans [Reference proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	333 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Serine/threonine-protein phosphatase essential for chromosomal dynamics during meiosis and mitosis. Antagonizes the function of air-2 in the regulation of chromosome cohesion. Dephosphorylates histone H3 at 'Ser-10'. Also involved in the activation of chloride channel clh-3 during cell swelling and meiotic maturation. Essential for embryogenesis. Ref.2 Ref.3 Ref.4 Ref.5 Ref.6
Catalytic activity	A phosphoprotein + H₂O = a protein + phosphate.
Cofactor	Binds 1 iron ion per subunit By similarity. Binds 1 manganese ion per subunit By similarity.
Enzyme regulation	Inhibited by okadaic acid. Ref.5
Subcellular location	Cytoplasm. Nucleus Ref.5.
Tissue specificity	Expressed in gonads, nervous system, intestine and muscles. Ref.5
Developmental stage	Expressed at early embryonic stages. Ref.5
Sequence similarities	Belongs to the PPP phosphatase family. PP-1 subfamily.

Ontologies

Keywords
Biological process	Cell cycle Cell division Meiosis Mitosis
Cellular component	Cytoplasm Nucleus
Ligand	Iron Manganese Metal-binding
Molecular function	Chromatin regulator Developmental protein Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW meiosis Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-serine dephosphorylation Inferred from direct assay Ref.5. Source: WormBase
Cellular_component	chromosome Inferred from direct assay Ref.5. Source: WormBase cytoplasm Inferred from direct assay Ref.5. Source: WormBase nuclear membrane Inferred from direct assay Ref.5. Source: WormBase
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine phosphatase activity Inferred from direct assay Ref.5. Source: WormBase
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 333

333

Serine/threonine-protein phosphatase PP1-beta

PRO_0000058913

Sites

Active site

124

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

123

Manganese By similarity

Metal binding

172

Manganese By similarity

Metal binding

247

Manganese By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P48727 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: A73CE460AC78054E
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FASTA

333

37,792

        10         20         30         40         50         60 
MDVEKLNLDN IISRLLEVRG SKPGKNVQLT ESEIKGLCQK SREIFLSQPI LLELEAPLKI 

        70         80         90        100        110        120 
CGDVHGQYYD LLRLFEYGGF PPESNYLFLG DYVDRGKQSL ETICLLLAYK IKYPENFFLL 

       130        140        150        160        170        180 
RGNHECASIN RIYGFYDECK RRYNIKLWKT FTDCFNCLPV AAIIDEKIFC CHGGLSPDLQ 

       190        200        210        220        230        240 
SMEQIRRIMR PTDVPDQGLL CDLLWSDPDK DVTGWGENDR GVSFTFGPEV VAKFLHKHDL 

       250        260        270        280        290        300 
DLICRAHQVV EDGYEFFAKR QLVTLFSAPN YCGEFDNAGS MMTVDETLMC SFQILKPADK 

       310        320        330 
KKYPYGAGGV GSNRPVTPPR NAPAAQPKKG AKK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[2]	"Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes." Hsu J.-Y., Sun Z.-W., Li X., Reuben M., Tatchell K., Bishop D.K., Grushcow J.M., Brame C.J., Caldwell J.A., Hunt D.F., Lin R., Smith M.M., Allis C.D. Cell 102:279-291(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[3]	"The aurora kinase AIR-2 functions in the release of chromosome cohesion in Caenorhabditis elegans meiosis." Rogers E., Bishop J.D., Waddle J.A., Schumacher J.M., Lin R. J. Cell Biol. 157:219-229(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[4]	"Cell cycle- and swelling-induced activation of a Caenorhabditis elegans ClC channel is mediated by CeGLC-7alpha/beta phosphatases." Rutledge E., Denton J., Strange K. J. Cell Biol. 158:435-444(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[5]	"Role of Caenorhabditis elegans protein phosphatase type 1, CeGLC-7 beta, in metaphase to anaphase transition during embryonic development." Sassa T., Ueda-Ohba H., Kitamura K., Harada S., Hosono R. Exp. Cell Res. 287:350-360(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION.
[6]	"Caenorhabditis elegans RBX1 is essential for meiosis, mitotic chromosomal condensation and segregation, and cytokinesis." Sasagawa Y., Urano T., Kohara Y., Takahashi H., Higashitani A. Genes Cells 8:857-872(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	FO080186 Genomic DNA. Translation: CCD61828.1.
PIR	T16476.
RefSeq	NP_001022616.1. NM_001027445.4.
3D structure databases
ProteinModelPortal	P48727.
SMR	P48727. Positions 6-298.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-25119N.
IntAct	P48727. 2 interactions.
STRING	6239.F56C9.1.
Proteomic databases
PaxDb	P48727.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	F56C9.1.1; F56C9.1.1; F56C9.1. F56C9.1.2; F56C9.1.2; F56C9.1.
GeneID	3564807.
KEGG	cel:CELE_F56C9.1.
UCSC	F56C9.1. c. elegans.
Organism-specific databases
CTD	3564807.
WormBase	F56C9.1; CE01319; WBGene00001748; gsp-2.
Phylogenomic databases
eggNOG	COG0639.
GeneTree	ENSGT00530000062911.
HOGENOM	HOG000172697.
InParanoid	P48727.
KO	K06269.
OMA	VMGWGEN.
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
NextBio	954057.

Entry information

Entry name

GLC7B_CAEEL

Accession

Primary (citable) accession number: P48727

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

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

Other

Entry information

Relevant documents