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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 NHGRI_mPanTro3-v2.0_pri Primary Assembly
Genomic
-
NC_072408.2 Reference NHGRI_mPanTro3-v2.0_pri Primary Assembly
- Range
-
39324876..39361221
- Download
- GenBank, FASTA, Sequence Viewer (Graphics)
mRNA and Protein(s)
-
XM_009424966.5 → XP_009423241.1 prostaglandin E synthase 3 isoform X16
See identical proteins and their annotated locations for XP_009423241.1
- UniProtKB/TrEMBL
- A0A2I3RBX3, A0A2J8Q1T7, A0A6D2X6P8, K7CHQ0
- Related
-
ENSPTRP00000062141.1
- Conserved Domains (1) summary
-
- cl00175
Location:3 → 95
- alpha-crystallin-Hsps_p23-like; alpha-crystallin domain (ACD) found in alpha-crystallin-type small heat shock proteins, and a similar domain found in p23 (a cochaperone for Hsp90) and in other p23-like proteins.
-
XM_054662984.1 → XP_054518959.1 prostaglandin E synthase 3 isoform X18
-
XM_009424960.5 → XP_009423235.1 prostaglandin E synthase 3 isoform X9
See identical proteins and their annotated locations for XP_009423235.1
- UniProtKB/TrEMBL
- A0A2I3SSV3, A0A2J8Q1U7, A0A6D2WPX8
- Related
-
ENSPTRP00000079630.1
- Conserved Domains (1) summary
-
- cd00237
Location:3 → 109
- p23; p23 binds heat shock protein (Hsp)90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis.
-
XM_009424955.5 → XP_009423230.1 prostaglandin E synthase 3 isoform X2
- UniProtKB/TrEMBL
-
K7CHQ0
- Conserved Domains (1) summary
-
- cd00237
Location:3 → 109
- p23; p23 binds heat shock protein (Hsp)90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis.
-
XM_009424963.5 → XP_009423238.1 prostaglandin E synthase 3 isoform X12
- Conserved Domains (1) summary
-
- cl00175
Location:3 → 95
- alpha-crystallin-Hsps_p23-like; alpha-crystallin domain (ACD) found in alpha-crystallin-type small heat shock proteins, and a similar domain found in p23 (a cochaperone for Hsp90) and in other p23-like proteins.
-
XM_009424956.5 → XP_009423231.1 prostaglandin E synthase 3 isoform X3
See identical proteins and their annotated locations for XP_009423231.1
- UniProtKB/TrEMBL
-
K7CHQ0
- Conserved Domains (1) summary
-
- cd00237
Location:7 → 113
- p23; p23 binds heat shock protein (Hsp)90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis.
-
XM_016923189.4 → XP_016778678.1 prostaglandin E synthase 3 isoform X21
- Conserved Domains (1) summary
-
- cl00175
Location:3 → 95
- alpha-crystallin-Hsps_p23-like; alpha-crystallin domain (ACD) found in alpha-crystallin-type small heat shock proteins, and a similar domain found in p23 (a cochaperone for Hsp90) and in other p23-like proteins.
-
XM_009424965.5 → XP_009423240.1 prostaglandin E synthase 3 isoform X14
See identical proteins and their annotated locations for XP_009423240.1
- UniProtKB/TrEMBL
-
K7CHQ0
- Conserved Domains (1) summary
-
- cl00175
Location:7 → 99
- alpha-crystallin-Hsps_p23-like; alpha-crystallin domain (ACD) found in alpha-crystallin-type small heat shock proteins, and a similar domain found in p23 (a cochaperone for Hsp90) and in other p23-like proteins.
-
XM_063784888.1 → XP_063640958.1 prostaglandin E synthase 3 isoform X5
-
XM_063784891.1 → XP_063640961.1 prostaglandin E synthase 3 isoform X13
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XM_063784893.1 → XP_063640963.1 prostaglandin E synthase 3 isoform X19
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XM_063784889.1 → XP_063640959.1 prostaglandin E synthase 3 isoform X7
-
XM_063784892.1 → XP_063640962.1 prostaglandin E synthase 3 isoform X17
-
XM_009424958.5 → XP_009423233.1 prostaglandin E synthase 3 isoform X8
- Conserved Domains (1) summary
-
- cd00237
Location:7 → 113
- p23; p23 binds heat shock protein (Hsp)90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis.
-
XM_016923188.4 → XP_016778677.1 prostaglandin E synthase 3 isoform X20
-
XM_063784887.1 → XP_063640957.1 prostaglandin E synthase 3 isoform X4
-
XM_063784890.1 → XP_063640960.1 prostaglandin E synthase 3 isoform X11
-
XM_009424954.5 → XP_009423229.1 prostaglandin E synthase 3 isoform X1
- UniProtKB/TrEMBL
-
K7CHQ0
- Conserved Domains (1) summary
-
- cd00237
Location:7 → 113
- p23; p23 binds heat shock protein (Hsp)90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis.
-
XM_009424957.5 → XP_009423232.1 prostaglandin E synthase 3 isoform X6
- Conserved Domains (1) summary
-
- cd00237
Location:7 → 113
- p23; p23 binds heat shock protein (Hsp)90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis.
-
XM_009424961.5 → XP_009423236.1 prostaglandin E synthase 3 isoform X10
- Conserved Domains (1) summary
-
- cl00175
Location:7 → 99
- alpha-crystallin-Hsps_p23-like; alpha-crystallin domain (ACD) found in alpha-crystallin-type small heat shock proteins, and a similar domain found in p23 (a cochaperone for Hsp90) and in other p23-like proteins.
-
XM_009424964.5 → XP_009423239.1 prostaglandin E synthase 3 isoform X15
- Conserved Domains (1) summary
-
- cd00237
Location:7 → 113
- p23; p23 binds heat shock protein (Hsp)90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis.