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Asph aspartate-beta-hydroxylase [ Mus musculus (house mouse) ]

Gene ID: 65973, updated on 2-Nov-2024

Summary

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Official Symbol
Asphprovided by MGI
Official Full Name
aspartate-beta-hydroxylaseprovided by MGI
Primary source
MGI:MGI:1914186
See related
Ensembl:ENSMUSG00000028207 AllianceGenome:MGI:1914186
Gene type
protein coding
RefSeq status
VALIDATED
Organism
Mus musculus
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as
BAH; cI-37; 2310005F16Rik; 3110001L23Rik
Summary
Predicted to enable calcium ion binding activity and peptidyl-aspartic acid 3-dioxygenase activity. Involved in regulation of protein depolymerization and regulation of protein stability. Acts upstream of or within several processes, including face morphogenesis; limb morphogenesis; and peptidyl-aspartic acid hydroxylation. Located in cytoplasm. Is expressed in several structures, including cerebellum; eye; face; heart; and limb. Human ortholog(s) of this gene implicated in cholangiocarcinoma. Orthologous to human ASPH (aspartate beta-hydroxylase). [provided by Alliance of Genome Resources, Nov 2024]
Expression
Ubiquitous expression in cerebellum adult (RPKM 12.3), heart adult (RPKM 7.8) and 24 other tissues See more
Orthologs
human all
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Genomic context

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See Asph in Genome Data Viewer
Location:
4 A1; 4 4.17 cM
Exon count:
30
Annotation release Status Assembly Chr Location
RS_2024_02 current GRCm39 (GCF_000001635.27) 4 NC_000070.7 (9449085..9669344, complement)
108.20200622 previous assembly GRCm38.p6 (GCF_000001635.26) 4 NC_000070.6 (9449085..9669344, complement)

Chromosome 4 - NC_000070.7Genomic Context describing neighboring genes Neighboring gene clavesin 1 Neighboring gene STARR-seq mESC enhancer starr_09537 Neighboring gene predicted gene 11816 Neighboring gene predicted gene, 57727 Neighboring gene STARR-seq mESC enhancer starr_09538 Neighboring gene NIMA (never in mitosis gene a)-related expressed kinase 2 pseudogene Neighboring gene STARR-positive B cell enhancer mm9_chr4:9557799-9558100 Neighboring gene STARR-positive B cell enhancer ABC_E2685 Neighboring gene STARR-seq mESC enhancer starr_09540 Neighboring gene STARR-seq mESC enhancer starr_09542 Neighboring gene predicted gene, 24152 Neighboring gene STARR-seq mESC enhancer starr_09543 Neighboring gene predicted gene, 34947

Genomic regions, transcripts, and products

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Go to nucleotide: Graphics FASTA GenBank

Expression

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  • Project title: Mouse ENCODE transcriptome data Mouse ENCODE transcriptome data
  • Description: RNA profiling data sets generated by the Mouse ENCODE project.
  • BioProject: PRJNA66167
  • Publication: PMID 25409824
  • Analysis date: n/a

Bibliography

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Related articles in PubMed

  1. Molecular cloning and characterization of mouse cardiac junctate isoforms. Hong CS, et al. Biochem Biophys Res Commun, 2001 Dec 14. PMID 11735129
  2. Cardiac remodeling and atrial fibrillation in transgenic mice overexpressing junctin. Hong CS, et al. FASEB J, 2002 Aug. PMID 12154005
  3. Orexin neurons as conditional glucosensors: paradoxical regulation of sugar sensing by intracellular fuels. Venner A, et al. J Physiol, 2011 Dec 1. PMID 22005675, Free PMC Article
  4. Overexpression of junctin causes adaptive changes in cardiac myocyte Ca(2+) signaling. Kirchhefer U, et al. Cell Calcium, 2006 Feb. PMID 16289269
  5. Sarcoplasmic reticulum calcium overloading in junctin deficiency enhances cardiac contractility but increases ventricular automaticity. Yuan Q, et al. Circulation, 2007 Jan 23. PMID 17224479

See all (60) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. INPP5F translocates into cytoplasm and interacts with ASPH to promote tumor growth in hepatocellular carcinoma.
    Title: INPP5F translocates into cytoplasm and interacts with ASPH to promote tumor growth in hepatocellular carcinoma.
  2. Results predict that junctin ablation, or mutations that alter its structural attributes, may mimic the etiology of catecholaminergic polymorphic ventricular tachycardia by causing enhanced diastolic Ca2+ leak in the presence of beta-adrenergic activation.
    Title: Dual role of junctin in the regulation of ryanodine receptors and calcium release in cardiac ventricular myocytes.
  3. in skeletal muscle the disruption of Tdn/CASQ link has a more profound effect on jSR architecture and myoplasmic Ca(2+) regulation than Jct/CASQ association.
    Title: Triadin/Junctin double null mouse reveals a differential role for Triadin and Junctin in anchoring CASQ to the jSR and regulating Ca(2+) homeostasis.
  4. Ca(2+) and JNT-dependent disassembly of the CSQ2 polymer
    Title: Role of Junctin protein interactions in cellular dynamics of calsequestrin polymer upon calcium perturbation.
  5. junctate may play an important role in the regulation of sarcoplasmic reticulum Ca(2+) cycling through the interaction with SERCA2a in the murine heart.
    Title: Characterization of junctate-SERCA2a interaction in murine cardiomyocyte.
  6. analysis of aspartyl (asparaginyl) beta-hydroxylase monoclonal antibodies
    Title: Monoclonal antibodies against human aspartyl (asparaginyl) beta-hydroxylase developed by DNA immunization.
  7. Partial downregulation of junctin enhances cardiac calcium cycling without eliciting ventricular arrhythmias in mice.
    Title: Partial downregulation of junctin enhances cardiac calcium cycling without eliciting ventricular arrhythmias in mice.
  8. involved in maintaining sarcoplasmic reticulum Ca2+ store size in skeletal myotubes
    Title: Altered stored calcium release in skeletal myotubes deficient of triadin and junctin.
  9. Junctate-1 in the heart is closely linked to the homeostasis of E-C coupling proteins and a sustained increase of junctate-1 expression leads to a severe cardiac remodeling and arrhythmias.
    Title: Overexpression of junctate induces cardiac hypertrophy and arrhythmia via altered calcium handling.
  10. Data suggest that junctate over-expression is associated with an increase in the sarcoplasmic reticulum Ca2+ storage capacity and releasable Ca2+ content and support a physiological role for junctate in intracellular Ca2+ homeostasis.
    Title: Increased Ca2+ storage capacity of the skeletal muscle sarcoplasmic reticulum of transgenic mice over-expressing membrane bound calcium binding protein junctate.
Submit: New GeneRIF Correction See all GeneRIFs (16)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics  (MGI)
  • Endonuclease-mediated (3) 
  • Targeted (2)  1 citation

Pathways from PubChem

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Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Markers

Homology

Gene Ontology Provided by MGI

Function Evidence Code Pubs
enables calcium ion binding ISO
Inferred from Sequence Orthology
more info
  
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables peptidyl-aspartic acid 3-dioxygenase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables peptidyl-aspartic acid 3-dioxygenase activity ISS
Inferred from Sequence or Structural Similarity
more info
 PubMed 
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
Process Evidence Code Pubs
involved_in activation of cysteine-type endopeptidase activity IEA
Inferred from Electronic Annotation
more info
  
involved_in activation of cysteine-type endopeptidase activity ISO
Inferred from Sequence Orthology
more info
  
involved_in activation of store-operated calcium channel activity ISO
Inferred from Sequence Orthology
more info
  
involved_in calcium ion homeostasis ISO
Inferred from Sequence Orthology
more info
  
involved_in calcium ion transmembrane transport ISO
Inferred from Sequence Orthology
more info
  
acts_upstream_of cell population proliferation IGI
Inferred from Genetic Interaction
more info
 PubMed 
involved_in cellular response to calcium ion ISO
Inferred from Sequence Orthology
more info
  
acts_upstream_of_or_within face morphogenesis IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within limb morphogenesis IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within negative regulation of cell population proliferation IGI
Inferred from Genetic Interaction
more info
 PubMed 
acts_upstream_of_or_within pattern specification process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within peptidyl-aspartic acid hydroxylation IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in peptidyl-aspartic acid hydroxylation IEA
Inferred from Electronic Annotation
more info
  
involved_in positive regulation of DNA-templated transcription ISO
Inferred from Sequence Orthology
more info
  
involved_in positive regulation of calcium ion transport into cytosol ISO
Inferred from Sequence Orthology
more info
  
involved_in positive regulation of intracellular protein transport ISO
Inferred from Sequence Orthology
more info
  
involved_in positive regulation of proteolysis ISO
Inferred from Sequence Orthology
more info
  
involved_in regulation of cytosolic calcium ion concentration IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in regulation of cytosolic calcium ion concentration IEA
Inferred from Electronic Annotation
more info
  
involved_in regulation of cytosolic calcium ion concentration ISO
Inferred from Sequence Orthology
more info
  
involved_in regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity ISO
Inferred from Sequence Orthology
more info
  
involved_in regulation of protein depolymerization IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in regulation of protein stability IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in response to ATP ISO
Inferred from Sequence Orthology
more info
  
acts_upstream_of_or_within roof of mouth development IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
located_in cortical endoplasmic reticulum IEA
Inferred from Electronic Annotation
more info
  
located_in cortical endoplasmic reticulum ISO
Inferred from Sequence Orthology
more info
  
located_in cytoplasm IDA
Inferred from Direct Assay
more info
 PubMed 
is_active_in endoplasmic reticulum IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in endoplasmic reticulum ISO
Inferred from Sequence Orthology
more info
  
located_in endoplasmic reticulum membrane ISO
Inferred from Sequence Orthology
more info
  
located_in membrane ISS
Inferred from Sequence or Structural Similarity
more info
 PubMed 
located_in plasma membrane IEA
Inferred from Electronic Annotation
more info
  
located_in plasma membrane ISO
Inferred from Sequence Orthology
more info
  
located_in sarcoplasmic reticulum membrane IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
aspartyl/asparaginyl beta-hydroxylase
Names
ASP beta-hydroxylase
aspartly beta-hydroxylase
aspartyl beta-hydroxylase Humbug
calsequestrin-binding protein
jumbug
junctate
junctin
peptide-aspartate beta-dioxygenase
NP_001171320.1
NP_001171321.1
NP_001171322.1
NP_001171323.1
NP_001171324.1
NP_001171325.1
NP_001171326.1
NP_001171327.1
NP_001277296.1
NP_075553.2
NP_598484.2
XP_006538222.1
XP_017175829.1
XP_017175830.1
XP_017175831.1
XP_017175832.1
XP_017175833.1
XP_017175834.1
XP_036020189.1
XP_036020190.1
XP_036020191.1
XP_036020192.1
XP_036020193.1
XP_036020194.1
XP_036020195.1
XP_036020196.1

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_001177849.1 → NP_001171320.1  aspartyl/asparaginyl beta-hydroxylase isoform 3

    Status: VALIDATED

    Description
    Transcript Variant: This variant lacks an alternate, in-frame coding exon, compared to variant 1. The resulting protein (isoform 3) is shorter when it is compared to isoform 1.
    Source sequence(s)
    AK035735, AK049506, AL671970, BY268464
    Consensus CDS
    CCDS51114.1
    UniProtKB/TrEMBL
    A2AL85, Q8BQK0
    Related
    ENSMUSP00000103977.3, ENSMUST00000108340.9
    Conserved Domains (5) summary
    pfam05279
    Location:63 → 290
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region
    sd00006
    Location:425 → 449
    TPR; TPR repeat [structural motif]
    pfam05118
    Location:558 → 711
    Asp_Arg_Hydrox; Aspartyl/Asparaginyl beta-hydroxylase
    pfam13428
    Location:312 → 351
    TPR_14; Tetratricopeptide repeat
    pfam13432
    Location:312 → 382
    TPR_16; Tetratricopeptide repeat

  2. NM_001177850.1 → NP_001171321.1  aspartyl/asparaginyl beta-hydroxylase isoform 4

    See identical proteins and their annotated locations for NP_001171321.1

    Status: VALIDATED

    Description
    Transcript Variant: This variant (4) lacks much of the 3' coding region and contains a different segment for its 3' coding and UTR segments, compared to variant 1. The resulting protein (isoform 4) has a shorter and distinct C-terminus when it is compared to isoform 1.
    Source sequence(s)
    AK030293, AK160984, BP767098, BY268464
    Consensus CDS
    CCDS51116.1
    UniProtKB/TrEMBL
    A2AL81, Q9EQ65
    Related
    ENSMUSP00000081978.5, ENSMUST00000084915.11
    Conserved Domains (1) summary
    pfam05279
    Location:63 → 307
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  3. NM_001177851.1 → NP_001171322.1  aspartyl/asparaginyl beta-hydroxylase isoform 5

    See identical proteins and their annotated locations for NP_001171322.1

    Status: VALIDATED

    Description
    Transcript Variant: This variant (5) lacks an alternate, in-frame exon, much of the 3' coding region and contains a different segment for its 3' coding and UTR segments, compared to variant 1. The resulting protein (isoform 5) has a shorter and distinct C-terminus when it is compared to isoform 1.
    Source sequence(s)
    AK160984, BP767098, BY268464
    Consensus CDS
    CCDS51115.1
    UniProtKB/TrEMBL
    Q3TU40, Q91WG6
    Related
    ENSMUSP00000103974.2, ENSMUST00000108337.8
    Conserved Domains (1) summary
    pfam05279
    Location:63 → 291
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  4. NM_001177852.1 → NP_001171323.1  aspartyl/asparaginyl beta-hydroxylase isoform 6

    Status: VALIDATED

    Description
    Transcript Variant: This variant (6) has multiple differences which result in distinct UTRs and coding end regions, compared to variant 1. The resulting protein (isoform 6) is shorter and has distinct N- and C-termini when it is compared to isoform 1.
    Source sequence(s)
    AK030293, AK030694, AK160984, AL773548, BP767098
    Consensus CDS
    CCDS51112.1
    UniProtKB/TrEMBL
    A2AL75, Q920F9
    Related
    ENSMUSP00000103971.2, ENSMUST00000108334.8
    Conserved Domains (1) summary
    pfam05279
    Location:25 → 269
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  5. NM_001177853.1 → NP_001171324.1  aspartyl/asparaginyl beta-hydroxylase isoform 7

    Status: VALIDATED

    Description
    Transcript Variant: This variant (7) has multiple differences which result in distinct UTRs and coding end regions, compared to variant 1. The resulting protein (isoform 7) is shorter and has distinct N- and C-termini when it is compared to isoform 1.
    Source sequence(s)
    AK030293, AK030694, AK160984, AL773548, BP767098
    Consensus CDS
    CCDS51113.1
    UniProtKB/TrEMBL
    A2AL76, Q920F8
    Related
    ENSMUSP00000103970.2, ENSMUST00000108333.8
    Conserved Domains (1) summary
    pfam05279
    Location:25 → 258
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  6. NM_001177854.1 → NP_001171325.1  aspartyl/asparaginyl beta-hydroxylase isoform 9

    Status: VALIDATED

    Description
    Transcript Variant: This variant (9) has multiple differences which result in distinct UTRs and coding end regions, compared to variant 1. The resulting protein (isoform 9) is shorter and has distinct N- and C-termini when it is compared to isoform 1.
    Source sequence(s)
    AK030293, AK030694, AK160984, AL773548, BP767098
    Consensus CDS
    CCDS51111.1
    UniProtKB/TrEMBL
    A2AL74, Q920F7
    Related
    ENSMUSP00000103972.2, ENSMUST00000108335.8
    Conserved Domains (1) summary
    pfam05279
    Location:25 → 212
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  7. NM_001177855.1 → NP_001171326.1  aspartyl/asparaginyl beta-hydroxylase isoform 8

    Status: VALIDATED

    Description
    Transcript Variant: This variant (8) lacks much of the 3' coding region and contains different segments for its 3' coding and UTR segments, compared to variant 1. The resulting protein (isoform 8) has a shorter and distinct C-terminus when it is compared to isoform 1.
    Source sequence(s)
    AK009170, AK030293, AK030694, BY268464
    Consensus CDS
    CCDS51117.1
    UniProtKB/TrEMBL
    A2AL78, Q8CH79
    Related
    ENSMUSP00000049018.7, ENSMUST00000038564.13
    Conserved Domains (1) summary
    pfam05279
    Location:63 → 225
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  8. NM_001177856.1 → NP_001171327.1  aspartyl/asparaginyl beta-hydroxylase isoform 10

    See identical proteins and their annotated locations for NP_001171327.1

    Status: VALIDATED

    Description
    Transcript Variant: This variant (10) has multiple differences which result in a distinct 3' coding region and 3' UTR, compared to variant 1. The resulting protein (isoform 10) is shorter and has a distinct C-terminus when it is compared to isoform 1.
    Source sequence(s)
    AK032420, BC061098, BQ176256, BY268464
    Consensus CDS
    CCDS51118.1
    UniProtKB/TrEMBL
    A2AL79
    Related
    ENSMUSP00000116899.2, ENSMUST00000146441.8
    Conserved Domains (1) summary
    pfam05279
    Location:63 → 155
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  9. NM_001290367.1 → NP_001277296.1  aspartyl/asparaginyl beta-hydroxylase isoform 11

    See identical proteins and their annotated locations for NP_001277296.1

    Status: VALIDATED

    Description
    Transcript Variant: This variant (11) differs in the 5' UTR and 5' coding region, initiates translation at a downstream start codon and lacks an alternate in-frame exon in the 5' coding region, compared to variant 1. It encodes isoform 11, which is shorter than isoform 1.
    Source sequence(s)
    AK030293, AK035735, AL671970
    Consensus CDS
    CCDS71341.1
    UniProtKB/TrEMBL
    Q8BQK0, Q8CBM2
    Related
    ENSMUSP00000103976.2, ENSMUST00000108339.8
    Conserved Domains (5) summary
    pfam05279
    Location:1 → 223
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region
    sd00006
    Location:358 → 382
    TPR; TPR repeat [structural motif]
    pfam05118
    Location:491 → 644
    Asp_Arg_Hydrox; Aspartyl/Asparaginyl beta-hydroxylase
    pfam13428
    Location:245 → 284
    TPR_14; Tetratricopeptide repeat
    pfam13432
    Location:245 → 315
    TPR_16; Tetratricopeptide repeat

  10. NM_023066.3 → NP_075553.2  aspartyl/asparaginyl beta-hydroxylase isoform 1

    See identical proteins and their annotated locations for NP_075553.2

    Status: VALIDATED

    Description
    Transcript Variant: This variant (1) represents the longest transcript and it encodes the longest protein (isoform 1).
    Source sequence(s)
    AK030293, AL671970, BY268464
    Consensus CDS
    CCDS38690.1
    UniProtKB/Swiss-Prot
    Q6P8S1, Q8BSY0, Q9EPA6, Q9EQ64
    UniProtKB/TrEMBL
    Q8BQK0
    Related
    ENSMUSP00000077273.7, ENSMUST00000078139.13
    Conserved Domains (5) summary
    pfam05279
    Location:63 → 306
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region
    sd00006
    Location:441 → 465
    TPR; TPR repeat [structural motif]
    pfam05118
    Location:574 → 727
    Asp_Arg_Hydrox; Aspartyl/Asparaginyl beta-hydroxylase
    pfam13428
    Location:328 → 367
    TPR_14; Tetratricopeptide repeat
    pfam13432
    Location:328 → 398
    TPR_16; Tetratricopeptide repeat

  11. NM_133723.2 → NP_598484.2  aspartyl/asparaginyl beta-hydroxylase isoform 2

    See identical proteins and their annotated locations for NP_598484.2

    Status: VALIDATED

    Description
    Transcript Variant: This variant (2) has multiple differences which result in distinct UTRs and coding end regions, compared to variant 1. The resulting protein (isoform 2) is shorter and has distinct N- and C-termini when it is compared to isoform 1.
    Source sequence(s)
    AK009170, AK030694, AL773548
    Consensus CDS
    CCDS17959.1
    UniProtKB/TrEMBL
    Q8CH79, Q9CR06
    Related
    ENSMUSP00000100069.4, ENSMUST00000103004.10
    Conserved Domains (1) summary
    pfam05279
    Location:25 → 187
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCm39 C57BL/6J

Genomic

  1. NC_000070.7 Reference GRCm39 C57BL/6J

    Range
    9449085..9669344 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_036164303.1 → XP_036020196.1  aspartyl/asparaginyl beta-hydroxylase isoform X10

    Conserved Domains (1) summary
    pfam05279
    Location:1 → 300
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  2. XM_036164302.1 → XP_036020195.1  aspartyl/asparaginyl beta-hydroxylase isoform X8

    Conserved Domains (1) summary
    pfam05279
    Location:1 → 315
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  3. XM_017320344.3 → XP_017175833.1  aspartyl/asparaginyl beta-hydroxylase isoform X13

    UniProtKB/TrEMBL
    Q9EQ65
    Conserved Domains (1) summary
    pfam05279
    Location:63 → 282
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  4. XM_036164297.1 → XP_036020190.1  aspartyl/asparaginyl beta-hydroxylase isoform X2

    UniProtKB/TrEMBL
    Q9EQ65
    Conserved Domains (1) summary
    pfam05279
    Location:63 → 367
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  5. XM_017320342.1 → XP_017175831.1  aspartyl/asparaginyl beta-hydroxylase isoform X11

    UniProtKB/TrEMBL
    Q9EQ65
    Conserved Domains (1) summary
    pfam05279
    Location:63 → 297
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  6. XM_017320341.1 → XP_017175830.1  aspartyl/asparaginyl beta-hydroxylase isoform X9

    UniProtKB/TrEMBL
    Q91WG6
    Conserved Domains (1) summary
    pfam05279
    Location:63 → 306
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  7. XM_017320340.1 → XP_017175829.1  aspartyl/asparaginyl beta-hydroxylase isoform X7

    UniProtKB/TrEMBL
    Q9EQ65
    Conserved Domains (1) summary
    pfam05279
    Location:63 → 322
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  8. XM_036164299.1 → XP_036020192.1  aspartyl/asparaginyl beta-hydroxylase isoform X4

    Conserved Domains (1) summary
    pfam05279
    Location:63 → 357
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  9. XM_036164298.1 → XP_036020191.1  aspartyl/asparaginyl beta-hydroxylase isoform X3

    Conserved Domains (1) summary
    pfam05279
    Location:63 → 366
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  10. XM_036164296.1 → XP_036020189.1  aspartyl/asparaginyl beta-hydroxylase isoform X1

    UniProtKB/TrEMBL
    Q9EQ65
    Conserved Domains (1) summary
    pfam05279
    Location:63 → 382
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  11. XM_036164300.1 → XP_036020193.1  aspartyl/asparaginyl beta-hydroxylase isoform X5

    Conserved Domains (1) summary
    pfam05279
    Location:25 → 344
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  12. XM_036164301.1 → XP_036020194.1  aspartyl/asparaginyl beta-hydroxylase isoform X6

    UniProtKB/TrEMBL
    Q920F9
    Conserved Domains (1) summary
    pfam05279
    Location:25 → 329
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  13. XM_017320343.3 → XP_017175832.1  aspartyl/asparaginyl beta-hydroxylase isoform X12

    UniProtKB/TrEMBL
    Q920F9
    Conserved Domains (1) summary
    pfam05279
    Location:25 → 284
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  14. XM_006538159.4 → XP_006538222.1  aspartyl/asparaginyl beta-hydroxylase isoform X14

    UniProtKB/TrEMBL
    Q8CH79
    Conserved Domains (1) summary
    pfam05279
    Location:25 → 202
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  15. XM_017320345.3 → XP_017175834.1  aspartyl/asparaginyl beta-hydroxylase isoform X15

    Conserved Domains (1) summary
    pfam05279
    Location:25 → 117
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region
Nucleotide Protein Strain
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
Q8BSY0.1 GenPept UniProtKB/Swiss-Prot:Q8BSY0

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