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par-2 RING-type domain-containing protein [ Caenorhabditis elegans ]

Gene ID: 175275, updated on 9-Dec-2024

Summary

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Official Symbol
par-2
Official Full Name
RING-type domain-containing protein
Primary source
WormBase:WBGene00003917
Locus tag
CELE_F58B6.3
See related
AllianceGenome:WB:WBGene00003917
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Caenorhabditis elegans (strain: Bristol N2)
Lineage
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis
Summary
Enables microtubule binding activity; phosphatidylinositol phosphate binding activity; and protein kinase binding activity. Involved in asymmetric cell division; asymmetric protein localization involved in cell fate determination; and establishment of mitotic spindle orientation. Located in P granule and posterior cell cortex. Part of protein-containing complex. Is expressed in several structures, including EMS; P0; Psub1; germ line; and oocyte. [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See par-2 in Genome Data Viewer
Location:
chromosome: III
Exon count:
11
Sequence:
Chromosome: III; NC_003281.10 (1081395..1095082)

Chromosome III - NC_003281.10Genomic Context describing neighboring genes Neighboring gene Ras-related protein Rab-18 Neighboring gene KNL (kinetochore null) Binding Protein Neighboring gene Uncharacterized protein Neighboring gene ncRNA Neighboring gene ncRNA

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_003281.10

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. A portable, low-cost device for precise control of specimen temperature under stereomicroscopes. Testa ND, et al. PLoS One, 2020. PMID 32160236, Free PMC Article
  2. Acute heat shock leads to cortical domain internalization and polarity loss in the C. elegans embryo. Singh D, et al. Genesis, 2016 Apr. PMID 26934337
  3. Coupling of rotational cortical flow, asymmetric midbody positioning, and spindle rotation mediates dorsoventral axis formation in C. elegans. Singh D, et al. Dev Cell, 2014 Feb 10. PMID 24525186
  4. The oogenic germline starvation response in C. elegans. Seidel HS, et al. PLoS One, 2011. PMID 22164230, Free PMC Article
  5. The PAR network: redundancy and robustness in a symmetry-breaking system. Motegi F, et al. Philos Trans R Soc Lond B Biol Sci, 2013. PMID 24062581, Free PMC Article

See all (194) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. PP1 phosphatases control PAR-2 localization and polarity establishment in C. elegans embryos.
    Title: PP1 phosphatases control PAR-2 localization and polarity establishment in C. elegans embryos.
  2. a Rho GEF, ECT-2, acts downstream of AIR-1 in regulating contractility and PAR-2 localisation, and AIR-1 depletion influences ECT-2 cortical localisation
    Title: Centrosome Aurora A regulates RhoGEF ECT-2 localisation and ensures a single PAR-2 polarity axis in C. elegans embryos.
  3. Cortical polarity of PAR-2 is maintained by exchange rate kinetics at the cortical-cytoplasmic boundary.
    Title: Cortical Polarity of the RING Protein PAR-2 Is Maintained by Exchange Rate Kinetics at the Cortical-Cytoplasmic Boundary.
  4. Data indicate that a positive correlation between SRC-1 and the on-rate of PAR-2 is the essential mechanism underlying polarity reversal.
    Title: Positioning of polarity formation by extracellular signaling during asymmetric cell division.
  5. LGL-1 and PAR-2 affect cortical myosin distribution.
    Title: PAR-2, LGL-1 and the CDC-42 GAP CHIN-1 act in distinct pathways to maintain polarity in the C. elegans embryo.
  6. evidence PAR polarity arises from coupling of advective transport by flowing cell cortex to a multistable PAR reaction-diffusion system; advection in active, flowing medium provides mechanism for mechanically templated pattern formation in development
    Title: Polarization of PAR proteins by advective triggering of a pattern-forming system.
  7. PAR-2 and PAR-6, which localize to opposing PAR domains, undergo exchange between well mixed cytoplasmic populations and laterally diffusing membrane-associated states
    Title: PAR proteins diffuse freely across the anterior-posterior boundary in polarized C. elegans embryos.
  8. Overexpression of LGL-1 is sufficient to rescue loss of PAR-2 function.
    Title: The C. elegans homolog of Drosophila Lethal giant larvae functions redundantly with PAR-2 to maintain polarity in the early embryo.
  9. PAR-2 localization during the asymmetric P2 and P3 divisions is controlled by extracellular signals via MES-1/SRC-1 signaling
    Title: Extracellular control of PAR protein localization during asymmetric cell division in the C. elegans embryo.
  10. Polarity in the C. elegans zygote is initiated by redundant ECT-2- and PAR-2-dependent mechanisms that lower PAR-3 levels locally, triggering a positive-feedback loop that polarizes the entire cortex.
    Title: Symmetry breaking and polarization of the C. elegans zygote by the polarity protein PAR-2.
Submit: New GeneRIF Correction See all GeneRIFs (11)

Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Markers

Homology

Gene Ontology Provided by WormBase

Function Evidence Code Pubs
enables ATP binding ISS
Inferred from Sequence or Structural Similarity
more info
 PubMed 
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables microtubule binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables phosphatidylinositol-3,4,5-trisphosphate binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables phosphatidylinositol-4,5-bisphosphate binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables protein kinase binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables ubiquitin protein ligase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables ubiquitin protein ligase activity IEA
Inferred from Electronic Annotation
more info
  
enables ubiquitin protein ligase activity ISS
Inferred from Sequence or Structural Similarity
more info
 PubMed 
enables zinc ion binding ISS
Inferred from Sequence or Structural Similarity
more info
 PubMed 
Process Evidence Code Pubs
involved_in asymmetric cell division IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in asymmetric protein localization involved in cell fate determination IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in establishment of cell polarity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in establishment of mitotic spindle orientation IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in proteasome-mediated ubiquitin-dependent protein catabolic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in protein polyubiquitination ISS
Inferred from Sequence or Structural Similarity
more info
 PubMed 
Component Evidence Code Pubs
located_in P granule IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cell cortex IDA
Inferred from Direct Assay
more info
 PubMed 
located_in posterior cell cortex IDA
Inferred from Direct Assay
more info
 PubMed 
part_of protein-containing complex IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

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Preferred Names
RING-type domain-containing protein
NP_001022630.2
  • Confirmed by transcript evidence
NP_001368104.1
  • Confirmed by transcript evidence
NP_001407525.1
  • Confirmed by transcript evidence
NP_001407526.1
  • Confirmed by transcript evidence
NP_001407527.1
  • Confirmed by transcript evidence

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_003281.10 Reference assembly

    Range
    1081395..1095082
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001420606.1 → NP_001407525.1  RING-type domain-containing protein [Caenorhabditis elegans]

    Status: REVIEWED

    UniProtKB/TrEMBL
    A0A8S4SQT8, Q21610

  2. NM_001027459.7 → NP_001022630.2  RING-type domain-containing protein [Caenorhabditis elegans]

    See identical proteins and their annotated locations for NP_001022630.2

    Status: REVIEWED

    UniProtKB/TrEMBL
    Q21610, Q965F9
    Conserved Domains (1) summary
    PRK07429
    Location:364 → 409
    PRK07429; phosphoribulokinase; Provisional

  3. NM_001420609.1 → NP_001407527.1  RING-type domain-containing protein [Caenorhabditis elegans]

    Status: REVIEWED

    UniProtKB/TrEMBL
    A0A8S4SL65

  4. NM_001420607.1 → NP_001407526.1  RING-type domain-containing protein [Caenorhabditis elegans]

    Status: REVIEWED

    UniProtKB/TrEMBL
    A0A8S4SK97, Q21610

  5. NM_001381725.1 → NP_001368104.1  RING-type domain-containing protein [Caenorhabditis elegans]

    Status: REVIEWED

    UniProtKB/TrEMBL
    H1ZUX3
Nucleotide Protein
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