G5ECH5 · PP4R1_CAEEL
- ProteinSerine/threonine-protein phosphatase 4 regulatory subunit 1
- Geneppfr-1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1562 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Probable regulatory subunit of serine/threonine-protein phosphatase PP4 which may play a role in meiosis and embryonic mitosis. Probably in association with catalytic subunit pph-4.1, regulates microtubule severing during oocyte meiosis II by dephosphorylating and likely activating mei-1, a component of the katanin microtubule severing complex.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | protein domain specific binding | |
Molecular Function | protein phosphatase activator activity | |
Molecular Function | protein phosphatase regulator activity | |
Biological Process | embryo development ending in birth or egg hatching | |
Biological Process | establishment of mitotic spindle orientation | |
Biological Process | negative regulation of meiotic spindle elongation | |
Biological Process | polar body extrusion after meiotic divisions | |
Biological Process | regulation of mitotic spindle elongation |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein phosphatase 4 regulatory subunit 1
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionG5ECH5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes to the cytoplasm during meiosis and mitosis.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Embryonic lethal in 10 percent of animals and slight increase in the number of males produced (PubMed:19087961).
In oocytes, slight increase in metaphase and anaphase meiotic spindle length, persistence of microtubules around chromatids during anaphase and delay in spindle assembly in meiosis II (PubMed:19087961, PubMed:23918937).
However, localization of spindle pole marker aspm-1 and the shape of the meiotic spindle are normal (PubMed:23918937).
The second polar body has a larger size and in 16 percent of animals its extrusion fails resulting in aneuploidy (PubMed:19087961).
The size of the polar body is further increased in a mei-1 (or646) mutant background (PubMed:23918937).
Increases mei-1 phosphorylation in a gain of function mei-1 (ct46) and tbb-2 (sb26) mutant background (PubMed:23918937).
In gain of function mei-1 (ct46) mutant background, RNAi-mediated knockdown partially rescues embryonic lethality and improves embryonic mitotic spindle morphology in terms of length and orientation (PubMed:19087961).
In oocytes, slight increase in metaphase and anaphase meiotic spindle length, persistence of microtubules around chromatids during anaphase and delay in spindle assembly in meiosis II (PubMed:19087961, PubMed:23918937).
However, localization of spindle pole marker aspm-1 and the shape of the meiotic spindle are normal (PubMed:23918937).
The second polar body has a larger size and in 16 percent of animals its extrusion fails resulting in aneuploidy (PubMed:19087961).
The size of the polar body is further increased in a mei-1 (or646) mutant background (PubMed:23918937).
Increases mei-1 phosphorylation in a gain of function mei-1 (ct46) and tbb-2 (sb26) mutant background (PubMed:23918937).
In gain of function mei-1 (ct46) mutant background, RNAi-mediated knockdown partially rescues embryonic lethality and improves embryonic mitotic spindle morphology in terms of length and orientation (PubMed:19087961).
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000443998 | 1-1562 | Serine/threonine-protein phosphatase 4 regulatory subunit 1 | |||
Sequence: MIKSQFATLIRVLIDFQKFWVFLSIFCTFLVVFKFDNLMFQKVRRVFQQNRKNSESIQPKLSTVSGSNSGEGMDKRNTGFSNLQQLGGAIFIDDAEDEPPRVKSSEDSRPAPHWLDSPRDSTTLPDIIASTYSDFIDEAEYATKQMLAILETLNPIEEYIELFESSFKAIEVRLPFDVILNDEKKPDWDAIRRKLIMGSLTVNTTSEKPGITTNQMTAIFDAIPFLFDAVACNPELYEYQNTLSMIVMIAMTGNSMIRRQSINAVQALMERNMLDQDFMRDGVVPGLFNIYQSGVGAFQSNDLRMECVQALCQVISYDAIHDRRWLFDNFLPRFSQMLKDPTMHVRKSALHIFGNLGNMFGQKFTEVFLVPHLITLSCDMTWAVRKVACEIFVKVAECASNQVRIDILSPNFVRLLNDPNKWVSFIAYQQLGPFISLFANPDITGLELRNGQVVVRDPVVLEPSVTEQEDPSNSTFSEDTSDDFRTLPKDTWLPEVDFNDDFEYQLGSIDNTQNQKELTTVTTALVKTPKRGERVMDSVLSGINKMFGSLERSSPKSKEVEKIAATFSSPSKRSPLSLHSAVSLIDKFSKRSNPNNPQRFPVFDSANSDSTLSSNSSNNNSSEQQNSTGIAAKCSSTDDLTKLGLEDDDSPDAAEDSDDFTSETRTTSPRGRRIATNAWSKLDIRQKIFLRRLGALPPSFPKKKATHSSSSSPRKSPTRSPLLSSRKKGLLFDFAAPIEIKSSSSDHSETIPVRTANQQQEKADDDKLNTDERQQYMENSGPKFNTDEDSTNDSDSDDEDNDFEKSFVADEDDGEQDDSPLSIEIKSSSSSDFESVSAATPTSQEPVSNEFSLTYWSSNYAISSIEDELKPFGSSSSFTNSPTSNSYLESRFDVMKVNLSPRARSVSFGTNGSPISTSPRRKANSTSEPSPPNTGNLKSDDSIVMLNTEEKEKLGILDFDEMNMSISSNSSIHGEAAMTEDSDISLTSIEQAALQHVPVDLVESYMRVMGPIGGSGSGGGGNGSSTTIATGDPSLCAETYRHCAHNFPAVCYTLGRAAWPRLKLVFRKLAMDEQARVRQSISHSIHEIANMLGQEITDEDLLPVFYDLRNDQNPDVRNGILIHLYDFVKFLSPEKRDEMILSLPQFFPIGAQPGNQAQNGDWRSRFELISQLSKLCSLYSIQDVNFHMSGIALTLADDRVAEVRREAVMLVSTIVGALVTAEWDNIKGVRDIENGHVDVKKKSNKTDFLSEQFVDDIVSSFAKTQKWTRRQTFCFICAQILRDKQCDGIQFRYFFATPLQQLAQDKVPNVRLASCEALSVWRKTLIAARAQERRGQSPISSPASEPSAIRRDINLVSDMMVKLSNDSDIDAAFIAKKCQGLTDDHQPVDVASRTTRMREREEQFFGDIILSYSPGCNARVSGKEIKQLIRHDQGAVQKAAPLQSMEDFGDEILAHAADSVNIQTPPEVVATVQRVSITNEQFEDNTEAVDMEIEEDEDENSTEKKENTEKTAEEESENVKNTEDELDIPMDPAPTLPPPVTSKNQSSSPITASSSDNNETSA |
Proteomic databases
Expression
Interaction
Subunit
Serine/threonine-protein phosphatase 4 (PP4) occurs in different assemblies of the catalytic and one or more regulatory subunits (By similarity).
The catalytic subunit is likely to be pph-4.1 (PubMed:19087961).
Interacts (via C-terminus) with mel-26 (probably via MATH domain); the interaction targets ppfr-1 for ubiquitin-mediated proteolysis (PubMed:23918937).
The catalytic subunit is likely to be pph-4.1 (PubMed:19087961).
Interacts (via C-terminus) with mel-26 (probably via MATH domain); the interaction targets ppfr-1 for ubiquitin-mediated proteolysis (PubMed:23918937).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | G5ECH5 | mel-26 Q94420 | 4 | EBI-6691815, EBI-320790 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, repeat, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 98-114 | Basic and acidic residues | ||||
Sequence: EPPRVKSSEDSRPAPHW | ||||||
Region | 98-120 | Disordered | ||||
Sequence: EPPRVKSSEDSRPAPHWLDSPRD | ||||||
Repeat | 330-366 | HEAT 1 | ||||
Sequence: FLPRFSQMLKDPTMHVRKSALHIFGNLGNMFGQKFTE | ||||||
Repeat | 369-406 | HEAT 2 | ||||
Sequence: LVPHLITLSCDMTWAVRKVACEIFVKVAECASNQVRID | ||||||
Repeat | 408-446 | HEAT 3 | ||||
Sequence: LSPNFVRLLNDPNKWVSFIAYQQLGPFISLFANPDITGL | ||||||
Compositional bias | 588-635 | Polar residues | ||||
Sequence: FSKRSNPNNPQRFPVFDSANSDSTLSSNSSNNNSSEQQNSTGIAAKCS | ||||||
Region | 588-672 | Disordered | ||||
Sequence: FSKRSNPNNPQRFPVFDSANSDSTLSSNSSNNNSSEQQNSTGIAAKCSSTDDLTKLGLEDDDSPDAAEDSDDFTSETRTTSPRGR | ||||||
Region | 695-726 | Disordered | ||||
Sequence: ALPPSFPKKKATHSSSSSPRKSPTRSPLLSSR | ||||||
Compositional bias | 703-723 | Polar residues | ||||
Sequence: KKATHSSSSSPRKSPTRSPLL | ||||||
Compositional bias | 741-758 | Polar residues | ||||
Sequence: KSSSSDHSETIPVRTANQ | ||||||
Region | 741-847 | Disordered | ||||
Sequence: KSSSSDHSETIPVRTANQQQEKADDDKLNTDERQQYMENSGPKFNTDEDSTNDSDSDDEDNDFEKSFVADEDDGEQDDSPLSIEIKSSSSSDFESVSAATPTSQEPV | ||||||
Compositional bias | 759-773 | Basic and acidic residues | ||||
Sequence: QQEKADDDKLNTDER | ||||||
Compositional bias | 791-818 | Acidic residues | ||||
Sequence: TNDSDSDDEDNDFEKSFVADEDDGEQDD | ||||||
Compositional bias | 821-847 | Polar residues | ||||
Sequence: LSIEIKSSSSSDFESVSAATPTSQEPV | ||||||
Region | 905-943 | Disordered | ||||
Sequence: SVSFGTNGSPISTSPRRKANSTSEPSPPNTGNLKSDDSI | ||||||
Repeat | 1062-1100 | HEAT 4 | ||||
Sequence: LKLVFRKLAMDEQARVRQSISHSIHEIANMLGQEITDED | ||||||
Repeat | 1101-1139 | HEAT 5 | ||||
Sequence: LLPVFYDLRNDQNPDVRNGILIHLYDFVKFLSPEKRDEM | ||||||
Repeat | 1295-1333 | HEAT 6 | ||||
Sequence: FATPLQQLAQDKVPNVRLASCEALSVWRKTLIAARAQER | ||||||
Coiled coil | 1479-1528 | |||||
Sequence: NEQFEDNTEAVDMEIEEDEDENSTEKKENTEKTAEEESENVKNTEDELDI | ||||||
Region | 1480-1562 | Disordered | ||||
Sequence: EQFEDNTEAVDMEIEEDEDENSTEKKENTEKTAEEESENVKNTEDELDIPMDPAPTLPPPVTSKNQSSSPITASSSDNNETSA | ||||||
Compositional bias | 1485-1502 | Acidic residues | ||||
Sequence: NTEAVDMEIEEDEDENST | ||||||
Compositional bias | 1503-1527 | Basic and acidic residues | ||||
Sequence: EKKENTEKTAEEESENVKNTEDELD | ||||||
Compositional bias | 1540-1562 | Polar residues | ||||
Sequence: VTSKNQSSSPITASSSDNNETSA |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
G5ECH5-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Named
- Length1,562
- Mass (Da)174,187
- Last updated2011-12-14 v1
- Checksum3346A9020A9D8B82
G5ECH5-2
- Namea
- Differences from canonical
- 1-72: Missing
G5ECH5-3
- Nameb
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
G5EFN0 | G5EFN0_CAEEL | ppfr-1 | 1046 |
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_059538 | 1-72 | in isoform a and isoform b | |||
Sequence: Missing | ||||||
Compositional bias | 98-114 | Basic and acidic residues | ||||
Sequence: EPPRVKSSEDSRPAPHW | ||||||
Compositional bias | 588-635 | Polar residues | ||||
Sequence: FSKRSNPNNPQRFPVFDSANSDSTLSSNSSNNNSSEQQNSTGIAAKCS | ||||||
Alternative sequence | VSP_059539 | 650-775 | in isoform b | |||
Sequence: Missing | ||||||
Compositional bias | 703-723 | Polar residues | ||||
Sequence: KKATHSSSSSPRKSPTRSPLL | ||||||
Compositional bias | 741-758 | Polar residues | ||||
Sequence: KSSSSDHSETIPVRTANQ | ||||||
Compositional bias | 759-773 | Basic and acidic residues | ||||
Sequence: QQEKADDDKLNTDER | ||||||
Compositional bias | 791-818 | Acidic residues | ||||
Sequence: TNDSDSDDEDNDFEKSFVADEDDGEQDD | ||||||
Compositional bias | 821-847 | Polar residues | ||||
Sequence: LSIEIKSSSSSDFESVSAATPTSQEPV | ||||||
Compositional bias | 1485-1502 | Acidic residues | ||||
Sequence: NTEAVDMEIEEDEDENST | ||||||
Compositional bias | 1503-1527 | Basic and acidic residues | ||||
Sequence: EKKENTEKTAEEESENVKNTEDELD | ||||||
Compositional bias | 1540-1562 | Polar residues | ||||
Sequence: VTSKNQSSSPITASSSDNNETSA |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BX284601 EMBL· GenBank· DDBJ | CAH10794.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BX284601 EMBL· GenBank· DDBJ | CAH10795.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BX284601 EMBL· GenBank· DDBJ | CAP72367.2 EMBL· GenBank· DDBJ | Genomic DNA |