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Protein

Serine/threonine-protein phosphatase PP1-alpha

Gene

gsp-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Serine/threonine-protein phosphatase which 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.4 Publications

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi64 – 641Manganese 1By similarity
Metal bindingi66 – 661Manganese 1By similarity
Metal bindingi92 – 921Manganese 1By similarity
Metal bindingi92 – 921Manganese 2By similarity
Metal bindingi124 – 1241Manganese 2By similarity
Active sitei125 – 1251Proton donorBy similarity
Metal bindingi173 – 1731Manganese 2By similarity
Metal bindingi248 – 2481Manganese 2By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. phosphoprotein phosphatase activity Source: UniProtKB-KW

GO - Biological processi

  1. cell division Source: UniProtKB-KW
  2. chromatin modification Source: UniProtKB-KW
  3. meiotic cell cycle Source: UniProtKB-KW
  4. mitotic nuclear division Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle, Cell division, Meiosis, Mitosis

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_332332. Regulation of PLK1 Activity at G2/M Transition.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase PP1-alpha (EC:3.1.3.16)
Alternative name(s):
CeGLC-7-alpha
Glc seven-like phosphatase 1
Gene namesi
Name:gsp-1
ORF Names:F29F11.6
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940 Componenti: Chromosome V

Organism-specific databases

WormBaseiF29F11.6a; CE20735; WBGene00001747; gsp-1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 329329Serine/threonine-protein phosphatase PP1-alphaPRO_0000268637Add
BLAST

Proteomic databases

PaxDbiQ27497.
PRIDEiQ27497.

Expressioni

Gene expression databases

ExpressionAtlasiQ27497. baseline.

Interactioni

Protein-protein interaction databases

BioGridi44515. 2 interactions.
DIPiDIP-55373N.
IntActiQ27497. 3 interactions.
STRINGi6239.F29F11.6.

Structurei

3D structure databases

ProteinModelPortaliQ27497.
SMRiQ27497. Positions 4-309.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PPP phosphatase family. PP-1 subfamily.Curated

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00530000062911.
HOGENOMiHOG000172697.
InParanoidiQ27497.
KOiK06269.
OMAiRSCRTGK.
PhylomeDBiQ27497.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q27497-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNDGDLNID NLITRLLEVR GCRPGKPVTM SEAEIRALCH KSREIFLSQP
60 70 80 90 100
ILLELEAPLK ICGDIHGQYN DLLRLFEYGG FPPEANYLFL GDYVDRGKQS
110 120 130 140 150
LETICLLLAY KVKYPENFFL LRGNHECASI NRIYGFYDEC KRRFSIKLWK
160 170 180 190 200
TFTDCFNCLP IAALIDEKIF CCHGGLSPDL QNMEQIRRVM RPTDVPDTGL
210 220 230 240 250
LCDLLWSDPD KDVTGWGEND RGVSFTFGPD VVAKFLNRHD LDLICRAHQV
260 270 280 290 300
VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG GMMSVDETLM CSFQILKPSE
310 320
KKAKYQYQGM NSGRPAVGGG RPGTTAGKK
Length:329
Mass (Da):37,205
Last modified:December 31, 1998 - v2
Checksum:i500145324CA16D1B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z73974 Genomic DNA. Translation: CAA98273.1.
PIRiT21553.
RefSeqiNP_001256249.1. NM_001269320.1.
NP_001256250.1. NM_001269321.1.
UniGeneiCel.17676.

Genome annotation databases

EnsemblMetazoaiF29F11.6a; F29F11.6a; WBGene00001747.
F29F11.6b; F29F11.6b; WBGene00001747.
GeneIDi179486.
KEGGicel:CELE_F29F11.6.
UCSCiF29F11.6. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z73974 Genomic DNA. Translation: CAA98273.1.
PIRiT21553.
RefSeqiNP_001256249.1. NM_001269320.1.
NP_001256250.1. NM_001269321.1.
UniGeneiCel.17676.

3D structure databases

ProteinModelPortaliQ27497.
SMRiQ27497. Positions 4-309.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi44515. 2 interactions.
DIPiDIP-55373N.
IntActiQ27497. 3 interactions.
STRINGi6239.F29F11.6.

Proteomic databases

PaxDbiQ27497.
PRIDEiQ27497.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiF29F11.6a; F29F11.6a; WBGene00001747.
F29F11.6b; F29F11.6b; WBGene00001747.
GeneIDi179486.
KEGGicel:CELE_F29F11.6.
UCSCiF29F11.6. c. elegans.

Organism-specific databases

CTDi179486.
WormBaseiF29F11.6a; CE20735; WBGene00001747; gsp-1.

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00530000062911.
HOGENOMiHOG000172697.
InParanoidiQ27497.
KOiK06269.
OMAiRSCRTGK.
PhylomeDBiQ27497.

Enzyme and pathway databases

ReactomeiREACT_332332. Regulation of PLK1 Activity at G2/M Transition.

Miscellaneous databases

NextBioi905606.
PROiQ27497.

Gene expression databases

ExpressionAtlasiQ27497. baseline.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1997) [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(1999) [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(2001) [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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiGLC7A_CAEEL
AccessioniPrimary (citable) accession number: Q27497
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 11, 2006
Last sequence update: December 31, 1998
Last modified: March 31, 2015
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.