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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 EquCab3.0 Primary Assembly
Genomic
-
NC_009162.3 Reference EquCab3.0 Primary Assembly
- Range
-
39475571..39517246
- Download
- GenBank, FASTA, Sequence Viewer (Graphics)
mRNA and Protein(s)
-
XM_005601933.3 → XP_005601990.1 poly [ADP-ribose] polymerase 9 isoform X1
- UniProtKB/TrEMBL
-
F6SSB5
- Related
- ENSECAP00000010175.4, ENSECAT00000012874.4
- Conserved Domains (4) summary
-
- COG2110
Location:82 → 262
- YmdB; O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ribosomal structure and biogenesis]
- cd01439
Location:672 → 791
- TCCD_inducible_PARP_like; Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component ...
- cd02903
Location:286 → 424
- Macro_BAL_like; Macro domain, BAL_like family. The macro domain is a high-affinity ADP-ribose binding module found in a variety of proteins as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). ...
- cd02907
Location:82 → 260
- Macro_Af1521_BAL_like; Macro domain, Af1521- and BAL-like family. The macro domain is a high-affinity ADP-ribose binding module found in a variety of proteins as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose ...
-
XM_005601934.3 → XP_005601991.1 poly [ADP-ribose] polymerase 9 isoform X2
- UniProtKB/TrEMBL
-
F6SSB5
- Conserved Domains (4) summary
-
- COG2110
Location:82 → 262
- YmdB; O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ribosomal structure and biogenesis]
- cd01439
Location:638 → 757
- TCCD_inducible_PARP_like; Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component ...
- cd02907
Location:82 → 260
- Macro_Af1521_BAL_like; Macro domain, Af1521- and BAL-like family. The macro domain is a high-affinity ADP-ribose binding module found in a variety of proteins as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose ...
- cl00019
Location:286 → 390
- Macro; Macro domain, a high-affinity ADP-ribose binding module found in a variety of proteins as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Some macro domains recognize poly ...
-
XM_014732852.2 → XP_014588338.1 poly [ADP-ribose] polymerase 9 isoform X3
- UniProtKB/TrEMBL
-
A0A9L0TR94
- Related
- ENSECAP00000089177.1, ENSECAT00000080811.1
- Conserved Domains (4) summary
-
- COG2110
Location:82 → 262
- YmdB; O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ribosomal structure and biogenesis]
- cd02903
Location:286 → 424
- Macro_BAL_like; Macro domain, BAL_like family. The macro domain is a high-affinity ADP-ribose binding module found in a variety of proteins as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). ...
- cd02907
Location:82 → 260
- Macro_Af1521_BAL_like; Macro domain, Af1521- and BAL-like family. The macro domain is a high-affinity ADP-ribose binding module found in a variety of proteins as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose ...
- cl00283
Location:672 → 706
- ADP_ribosyl; ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. Bacterial toxins are cytoplasmic and catalyze the transfer of a single ADP_ribose unit to eukaryotic elongation factor 2, halting protein synthesis and killing the cell. ...