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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 ASM220157v2
Genomic
-
NC_058410.1 Reference ASM220157v2
- Range
-
94374322..94850476
- Download
- GenBank, FASTA, Sequence Viewer (Graphics)
mRNA and Protein(s)
-
XM_044917613.1 → XP_044773548.1 LOW QUALITY PROTEIN: dystonin
- UniProtKB/TrEMBL
-
A0A8M1MLL3
- Conserved Domains (11) summary
-
- pfam05483
Location:849 → 1481
- SCP-1; Synaptonemal complex protein 1 (SCP-1)
- smart00243
Location:7496 → 7571
- GAS2; Growth-Arrest-Specific Protein 2 Domain
- TIGR00618
Location:3447 → 4189
- sbcc; exonuclease SbcC
- smart00150
Location:820 → 911
- SPEC; Spectrin repeats
- smart00250
Location:1986 → 2022
- PLEC; Plectin repeat
- smart00935
Location:1698 → 1767
- OmpH; Outer membrane protein (OmpH-like)
- COG1196
Location:3830 → 4641
- Smc; Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]
- COG5069
Location:208 → 465
- SAC6; Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]
- cd00051
Location:7421 → 7483
- EFh; EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to ...
- cd00176
Location:6600 → 6814
- SPEC; Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; ...
- cl02488
Location:5325 → 5498
- SPEC; Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; ...