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Q9UW86 (PP1_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 95. 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
Alternative name(s):
Phosphoprotein phosphatase 1
Gene names
Name:pph-3
Synonyms:ppp-1
ORF Names:NCU00043
OrganismNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) [Reference proteome]
Taxonomic identifier367110 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora

Protein attributes

Sequence length308 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 2 manganese ions per subunit By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

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

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandManganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage checkpoint

Inferred from electronic annotation. Source: EnsemblFungi

DNA replication checkpoint

Inferred from electronic annotation. Source: EnsemblFungi

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 electronic annotation. Source: EnsemblFungi

glycogen metabolic process

Inferred from electronic annotation. Source: EnsemblFungi

histone dephosphorylation

Inferred from electronic annotation. Source: EnsemblFungi

meiotic nuclear division

Inferred from electronic annotation. Source: EnsemblFungi

mitotic spindle assembly checkpoint

Inferred from electronic annotation. Source: EnsemblFungi

protein localization to kinetochore

Inferred from electronic annotation. Source: EnsemblFungi

rRNA processing

Inferred from electronic annotation. Source: EnsemblFungi

regulation of carbohydrate metabolic process

Inferred from electronic annotation. Source: EnsemblFungi

regulation of cell shape during vegetative growth phase

Inferred from electronic annotation. Source: EnsemblFungi

replication fork processing

Inferred from electronic annotation. Source: EnsemblFungi

response to heat

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_componentcellular bud neck

Inferred from electronic annotation. Source: EnsemblFungi

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 electronic annotation. Source: EnsemblFungi

protein phosphatase type 1 complex

Inferred from electronic annotation. Source: EnsemblFungi

spindle pole body

Inferred from electronic annotation. Source: EnsemblFungi

   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 – 308308Serine/threonine-protein phosphatase PP1
PRO_0000058817

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 conflict1541D → E in AAC05275. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9UW86 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 333A728F20860AB1

FASTA30835,568
        10         20         30         40         50         60 
MADHTEVDLD SIIDRLLEVR GSRPGKQVQL LEAEIRYLCT KAREIFISQP ILLELEAPIK 

        70         80         90        100        110        120 
ICGDIHGQYY DLLRLFEYGG FPPEANYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFI 

       130        140        150        160        170        180 
LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIIDEKIF TMHGGLSPDL 

       190        200        210        220        230        240 
NSMEQIRRVM RPTDIPDCGL LCDLLWSDPD KDITGWSEND RGVSFTFGPD VVSRFLQKHD 

       250        260        270        280        290        300 
MDLICRAHQV VEDGYEFFSK RQLVTLFSAP NYCGEFDNAG AMMSVDESLL CSFQILKPAE 


KKQKFGRR 

« Hide

References

« Hide 'large scale' references
[1]"Searching for the role of protein phosphatases in eukaryotic microorganisms."
da-Silva A.M., Zapella P.D.A., Andrioli L.P.M., Campanha R.B., Fiorini L.C., Etchebehere L.C., da-Costa-Maia J.C., Terenzi H.F.
Braz. J. Med. Biol. Res. 32:835-839(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[2]"Expression of protein phosphatase 1 during the asexual development of Neurospora crassa."
Zeke T., Kokai E., Szoor B., Yatzkan E., Yarden O., Szirak K., Feher Z., Bagossi P., Gergely P., Dombradi V.
Comp. Biochem. Physiol. 134B:161-170(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 74-OR23-1VA / FGSC 2489.
[3]"The genome sequence of the filamentous fungus Neurospora crassa."
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. expand/collapse author list , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF049853 mRNA. Translation: AAC05275.1.
AF124149 Genomic DNA. Translation: AAD47567.1.
CM002238 Genomic DNA. Translation: EAA26918.2.
RefSeqXP_956154.2. XM_951061.2.
UniGeneNcr.4075.

3D structure databases

ProteinModelPortalQ9UW86.
SMRQ9UW86. Positions 1-305.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5141.NCU00043.1.

Proteomic databases

PRIDEQ9UW86.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEFNCRT00000000314; EFNCRP00000000314; EFNCRG00000000314.
GeneID3872306.
KEGGncr:NCU00043.

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000172697.
KOK06269.
OrthoDBEOG79KPQ9.

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 namePP1_NEUCR
AccessionPrimary (citable) accession number: Q9UW86
Secondary accession number(s): O59927, Q7RV51
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 95 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