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P20654 (PP1_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase PP1

EC=3.1.3.16
Gene names
Name:bimG
ORF Names:AN0410
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length323 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Plays an important role in the control of mitosis by reversing the action of the nimA kinase.

Catalytic activity

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

Cofactor

Binds 1 iron ion per subunit By similarity.

Binds 1 manganese ion per subunit By similarity.

Sequence similarities

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

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   LigandIron
Manganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication checkpoint

Inferred from electronic annotation. Source: EnsemblFungi

anisotropic cell growth

Inferred from mutant phenotype Ref.1. Source: ASPGD

ascospore formation

Inferred from electronic annotation. Source: EnsemblFungi

cell budding

Inferred from electronic annotation. Source: EnsemblFungi

cellular ion homeostasis

Inferred from electronic annotation. Source: EnsemblFungi

chromosome segregation

Inferred from mutant phenotype Ref.1. Source: ASPGD

establishment of cell polarity

Inferred from mutant phenotype Ref.1. Source: ASPGD

histone dephosphorylation

Inferred from electronic annotation. Source: EnsemblFungi

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic spindle elongation

Inferred from mutant phenotype Ref.1. Source: ASPGD

protein localization to kinetochore

Inferred from electronic annotation. Source: EnsemblFungi

rRNA processing

Inferred from electronic annotation. Source: EnsemblFungi

regulation of cell cycle

Inferred from electronic annotation. Source: EnsemblFungi

replication fork processing

Inferred from electronic annotation. Source: EnsemblFungi

termination of RNA polymerase II transcription, exosome-dependent

Inferred from electronic annotation. Source: EnsemblFungi

termination of RNA polymerase II transcription, poly(A)-coupled

Inferred from electronic annotation. Source: EnsemblFungi

   Cellular_componentcell septum

Inferred from direct assay PubMed 12207691. Source: ASPGD

condensed nuclear chromosome kinetochore

Inferred from electronic annotation. Source: EnsemblFungi

mRNA cleavage and polyadenylation specificity factor complex

Inferred from electronic annotation. Source: EnsemblFungi

mating projection base

Inferred from electronic annotation. Source: EnsemblFungi

nucleolus

Inferred from direct assay PubMed 12207691. Source: ASPGD

spindle pole body

Inferred from direct assay PubMed 12207691. Source: ASPGD

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine phosphatase activity

Inferred from electronic annotation. Source: EnsemblFungi

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 323323Serine/threonine-protein phosphatase PP1
PRO_0000058816

Sites

Active site1241Proton donor By similarity
Metal binding631Iron By similarity
Metal binding651Iron By similarity
Metal binding911Iron By similarity
Metal binding911Manganese By similarity
Metal binding1231Manganese By similarity
Metal binding1721Manganese By similarity
Metal binding2471Manganese By similarity

Sequences

Sequence LengthMass (Da)Tools
P20654 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 9CED43E15C5AA5BA

FASTA32337,176
        10         20         30         40         50         60 
MADQDVDLDS IIDRLLEVRG SRPGKQVQLL ESEIRYLCTK AREIFISQPI LLELEAPIKI 

        70         80         90        100        110        120 
CGDIHGQYYD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL ETICLLLAYK IKYPENFFVL 

       130        140        150        160        170        180 
RGNHECASIN RIYGFYDECK RRYNIKLWKT FTDCFNCLPI AAIIDEKIFT MHGGLSPDLN 

       190        200        210        220        230        240 
SMEQIRRVMR PTDIPDCGLL CDLLWSDPDK DITGWSENDR GVSFTFGPDV VSRFLQKHDM 

       250        260        270        280        290        300 
DLICRAHQVV EDGYEFFSKR QLVTLFSAPN YCGEFDNAGA MMSVDESLLC SFQILKPAEK 

       310        320 
KQKYVYGAMS SGRPITPPRK QKK 

« Hide

References

« Hide 'large scale' references
[1]"The bimG gene of Aspergillus nidulans, required for completion of anaphase, encodes a homolog of mammalian phosphoprotein phosphatase 1."
Doonan J.H., Morris N.R.
Cell 57:987-996(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[3]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M27067 mRNA. Translation: AAA33299.1.
AACD01000007 Genomic DNA. Translation: EAA66509.1.
BN001308 Genomic DNA. Translation: CBF89542.1.
PIRA32549.
RefSeqXP_658014.1. XM_652922.1.

3D structure databases

ProteinModelPortalP20654.
SMRP20654. Positions 1-308.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING162425.CADANIAP00002289.

Proteomic databases

PRIDEP20654.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00002289; CADANIAP00002289; CADANIAG00002289.
GeneID2876189.
KEGGani:AN0410.2.

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000172697.
KOK06269.
OMALEHEIRY.
OrthoDBEOG79KPQ9.

Family and domain databases

InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePP1_EMENI
AccessionPrimary (citable) accession number: P20654
Secondary accession number(s): C8VTH6, Q5BGC0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: April 16, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families