Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

Q9P7H1 · FLP1_SCHPO

Function

function

Protein phosphatase which antagonizes mitotic cyclin-dependent kinase cdc2, the inactivation of which is essential for exit from mitosis. To access its substrates, is released from nucleolar sequestration during mitosis. Plays an essential in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint. Involved in chromosome segregation, where it is required for meiosis I spindle dissambly as well as for establishing two consecutive chromosome segregation phases. Allows damaged actomyosin rings to be maintained to facilitate completion of cell division in response to minor perturbation of the cell division machinery. Dephosphorylates the mitotic inducer cdc25 for its rapid degradation. Down-regulation of cdc25 activity ensures a prompt inactivation of mitotic cdc2 complexes to trigger cell division. Dephosphorylates also cdc2-phosphorylated nsk1, allowing nsk1-binding to kinetochores and spindle. Dephosphorylates ase1, which is essential for spindle midzone assembly and for continuous extension of the anaphase spindle. Tethered to the contractile ring by mid1, where it dephosphorylates cdc15.

Catalytic activity

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site286Phosphocysteine intermediate

GO annotations

AspectTerm
Cellular Componentcell division site
Cellular Componentcytoplasm
Cellular Componentkinetochore
Cellular Componentmitotic actomyosin contractile ring
Cellular Componentmitotic actomyosin contractile ring, intermediate layer
Cellular Componentmitotic spindle
Cellular Componentmitotic spindle midzone
Cellular Componentmitotic spindle pole body
Cellular Componentnucleolar peripheral inclusion body
Cellular Componentnucleolus
Cellular Componentnucleoplasm
Cellular Componentnucleus
Cellular Componentspindle pole
Cellular Componentspindle pole body
Molecular Functionphosphoprotein phosphatase activity
Molecular Functionprotein serine/threonine phosphatase activity
Molecular Functionprotein tyrosine phosphatase activity
Biological Processdivision septum assembly
Biological ProcessDNA damage response
Biological Processmeiotic cell cycle
Biological Processmicrotubule cytoskeleton organization
Biological Processmitotic cytokinesis checkpoint signaling
Biological Processnegative regulation of G2/M transition of mitotic cell cycle
Biological Processpositive regulation of cytokinesis
Biological Processpositive regulation of exit from mitosis
Biological Processpositive regulation of mitotic actomyosin contractile ring assembly
Biological Processpositive regulation of mitotic cytokinesis
Biological Processpositive regulation of mitotic sister chromatid biorientation
Biological Processpositive regulation of mitotic spindle elongation
Biological Processpositive regulation of septation initiation signaling
Biological Processprotein dephosphorylation
Biological Processprotein localization to mitotic spindle pole body
Biological Processregulation of exit from mitosis
Biological Processregulation of mitotic cytokinesis
Biological Processresponse to mitotic cell cycle spindle assembly checkpoint signaling

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Tyrosine-protein phosphatase CDC14 homolog
  • EC number
  • Alternative names
    • CDC fourteen-like phosphatase 1

Gene names

    • Name
      clp1
    • Synonyms
      flp1
    • ORF names
      SPAC1782.09c

Organism names

Accessions

  • Primary accession
    Q9P7H1

Proteomes

Organism-specific databases

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis286Inactivates phosphatase activity.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 4 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00000948741-537Tyrosine-protein phosphatase CDC14 homolog
Modified residue453Phosphothreonine
Modified residue468Phosphoserine
Modified residue470Phosphoserine
Modified residue513Phosphoserine

Post-translational modification

Phosphorylated by cds1, chk1, pmk1, and cdc2 upon Hydroxylurea and H2O2 stress treatment. Phosphorylation regulates the nucleolar-to-nucleoplasmic transition. Is able to autodephosphorylate.

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Interacts with ark1 at the kinetochores. Interacts with bir1, cdc25, mid1, nbl1, pic1, and rad24.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntAct
BINARY Q9P7H1rad24 P426563EBI-704737, EBI-704791

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain182-345Tyrosine-protein phosphatase
Region359-537Disordered
Compositional bias368-384Polar residues
Compositional bias403-439Polar residues
Compositional bias447-527Polar residues

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    537
  • Mass (Da)
    60,253
  • Last updated
    2000-10-01 v1
  • MD5 Checksum
    372D34C281543350D38C561BD668D335
MDYQDDGLGEMIEFLEDKLYYTSLSQPPKAELYPHMHFFTIDDELIYNPFYHDFGPLNVSHLIRFAVIVHGIMGKHRQAKKSKAIVLYSSTDTRLRANAACLLACYMVLVQNWPPHLALAPLAQAEPPFLGFRDAGYAVSDYYITIQDCVYGLWRARESSILNIRNIDVHDYETYERVENGDFNWISPKFIAFASPIQAGWNHASTRPKKLPQPFAIVLDYFVANKVKLIVRLNGPLYDKKTFENVGIRHKEMYFEDGTVPELSLVKEFIDLTEEVEEDGVIAVHCKAGLGRTGCLIGAYLIYKHCFTANEVIAYMRIMRPGMVVGPQQHWLHINQVHFRAYFYEKAMGRAIQQATAAEPLATPPRHPLNATNGTSQSNISTPLPEPTPGQPRKVSGHNPPSARRLPSASSVKFNEKLKNASKQSIQNENKASYSSYEDSEIQNDDETRTVGTPTETISVVRLRRSSSQSNIEPNGVRSPTSSPTGSPIRRTSGNRWSSGSSHSKKSAQRSVSMSSLNNTSNGRVAKPKPSKSRLIS

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias368-384Polar residues
Compositional bias403-439Polar residues
Compositional bias447-527Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CU329670
EMBL· GenBank· DDBJ
CAB76271.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help