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csp-1 Caspase A subunit p16 [ Caenorhabditis elegans ]

Gene ID: 175007, updated on 9-Dec-2024

Summary

Official Symbol
csp-1
Official Full Name
Caspase A subunit p16
Primary source
WormBase:WBGene00000819
Locus tag
CELE_Y48E1B.13
See related
AllianceGenome:WB:WBGene00000819
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 cysteine-type endopeptidase activity. Involved in several processes, including negative regulation of cellular response to manganese ion; positive regulation of apoptotic process; and protein processing. Located in germ cell nucleus. Is expressed in germ line. Human ortholog(s) of this gene implicated in autosomal recessive congenital ichthyosis; breast cancer; carcinoma (multiple); gastrointestinal system cancer (multiple); and neurodegenerative disease (multiple). Orthologous to several human genes including CASP14 (caspase 14); CASP3 (caspase 3); and CASP6 (caspase 6). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

See csp-1 in Genome Data Viewer
Location:
chromosome: II
Exon count:
10
Sequence:
Chromosome: II; NC_003280.10 (13601204..13605057)

Chromosome II - NC_003280.10Genomic Context describing neighboring genes Neighboring gene FTH domain-containing protein Neighboring gene Chromosome segregation and cytokinesis defective protein 1 Neighboring gene Glutathione S-transferase Neighboring gene Glutathione S-transferase

Pathways from PubChem

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Markers

Gene Ontology Provided by WormBase

Function Evidence Code Pubs
enables cysteine-type endopeptidase activity IEA
Inferred from Electronic Annotation
more info
 
enables cysteine-type endopeptidase activity IMP
Inferred from Mutant Phenotype
more info
PubMed 
enables cysteine-type peptidase activity IEA
Inferred from Electronic Annotation
more info
 
Component Evidence Code Pubs
located_in germ cell nucleus IDA
Inferred from Direct Assay
more info
PubMed 

General protein information

Preferred Names
Caspase A subunit p16
NP_001022452.1
  • Confirmed by transcript evidence
NP_001022453.1
  • Confirmed by transcript evidence
NP_001022454.1
  • Partially 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_003280.10 Reference assembly

    Range
    13601204..13605057
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001027281.1NP_001022452.1  Caspase A subunit p16 [Caenorhabditis elegans]

    See identical proteins and their annotated locations for NP_001022452.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    G5EBM1, G5EBN4, G5EG94
    Conserved Domains (2) summary
    smart00115
    Location:285533
    CASc; Caspase, interleukin-1 beta converting enzyme (ICE) homologues
    smart00583
    Location:76188
    SPK; domain in SET and PHD domain containing proteins and protein kinases
  2. NM_001027282.1NP_001022453.1  Caspase A subunit p16 [Caenorhabditis elegans]

    See identical proteins and their annotated locations for NP_001022453.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    G5EBM1
    Conserved Domains (1) summary
    smart00115
    Location:17265
    CASc; Caspase, interleukin-1 beta converting enzyme (ICE) homologues
  3. NM_001027283.1NP_001022454.1  Caspase A subunit p16 [Caenorhabditis elegans]

    See identical proteins and their annotated locations for NP_001022454.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    G5EBM1
    Conserved Domains (1) summary
    cl00042
    Location:17146
    CASc; Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine-dependent aspartate-directed proteases that mediate programmed cell death (apoptosis). Caspases are synthesized as inactive zymogens and activated by proteolysis of the peptide ...