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The following sections contain reference sequences that belong to a
specific genome build. Explain
This section includes genomic Reference
Sequences (RefSeqs) from all assemblies on which this gene is annotated, such as
RefSeqs for chromosomes and scaffolds (contigs) from both reference and alternate
assemblies. Model RNAs and proteins are also reported here.
Reference assembly
Genomic
-
NT_033779.5 Reference assembly
- Range
-
7801668..7810703 complement
- Download
- GenBank, FASTA, Sequence Viewer (Graphics)
mRNA and Protein(s)
-
NM_001298792.1 → NP_001285721.1 cell division cycle 14, isoform D [Drosophila melanogaster]
See identical proteins and their annotated locations for NP_001285721.1
Status: REVIEWED
- UniProtKB/TrEMBL
-
Q9VLW7
- Conserved Domains (3) summary
-
- COG2453
Location:229 → 330
- CDC14; Protein-tyrosine phosphatase [Signal transduction mechanisms]
- pfam14671
Location:19 → 156
- DSPn; Dual specificity protein phosphatase, N-terminal half
- cl21483
Location:217 → 331
- PTPc; Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr ...
-
NM_001169433.2 → NP_001162904.1 cell division cycle 14, isoform B [Drosophila melanogaster]
See identical proteins and their annotated locations for NP_001162904.1
Status: REVIEWED
- UniProtKB/TrEMBL
-
Q5U0V6
- Conserved Domains (3) summary
-
- COG2453
Location:229 → 330
- CDC14; Protein-tyrosine phosphatase [Signal transduction mechanisms]
- pfam14671
Location:19 → 156
- DSPn; Dual specificity protein phosphatase, N-terminal half
- cl21483
Location:217 → 331
- PTPc; Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr ...
-
NM_001169434.2 → NP_001162905.1 cell division cycle 14, isoform C [Drosophila melanogaster]
See identical proteins and their annotated locations for NP_001162905.1
Status: REVIEWED
- UniProtKB/TrEMBL
-
E1JHB2
- Conserved Domains (3) summary
-
- COG2453
Location:229 → 330
- CDC14; Protein-tyrosine phosphatase [Signal transduction mechanisms]
- pfam14671
Location:19 → 156
- DSPn; Dual specificity protein phosphatase, N-terminal half
- cl21483
Location:217 → 331
- PTPc; Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr ...
-
NM_135309.3 → NP_609153.1 cell division cycle 14, isoform A [Drosophila melanogaster]
See identical proteins and their annotated locations for NP_609153.1
Status: REVIEWED
- UniProtKB/TrEMBL
-
Q9VLW7
- Related
-
FBpp0079115
- Conserved Domains (3) summary
-
- COG2453
Location:229 → 330
- CDC14; Protein-tyrosine phosphatase [Signal transduction mechanisms]
- pfam14671
Location:19 → 156
- DSPn; Dual specificity protein phosphatase, N-terminal half
- cl21483
Location:217 → 331
- PTPc; Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr ...
-
NM_001298793.1 → NP_001285722.1 cell division cycle 14, isoform E [Drosophila melanogaster]
See identical proteins and their annotated locations for NP_001285722.1
Status: REVIEWED
- UniProtKB/TrEMBL
-
X2J9T8
- Conserved Domains (3) summary
-
- COG2453
Location:229 → 330
- CDC14; Protein-tyrosine phosphatase [Signal transduction mechanisms]
- pfam14671
Location:19 → 156
- DSPn; Dual specificity protein phosphatase, N-terminal half
- cl21483
Location:217 → 331
- PTPc; Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr ...