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

    Gene ID: 65973, updated on 5-Mar-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 eye; face; heart; limb; and trunk. Human ortholog(s) of this gene implicated in cholangiocarcinoma. Orthologous to human ASPH (aspartate beta-hydroxylase). [provided by Alliance of Genome Resources, Apr 2022]
    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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    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
    • 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. Dual role of junctin in the regulation of ryanodine receptors and calcium release in cardiac ventricular myocytes. Altschafl BA, et al. J Physiol, 2011 Dec 15. PMID 22025663, Free PMC Article
    2. 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
    3. Partial downregulation of junctin enhances cardiac calcium cycling without eliciting ventricular arrhythmias in mice. Yuan Q, et al. Am J Physiol Heart Circ Physiol, 2009 May. PMID 19286959, Free PMC Article
    4. Overexpression of junctate induces cardiac hypertrophy and arrhythmia via altered calcium handling. Hong CS, et al. J Mol Cell Cardiol, 2008 Apr. PMID 18353357
    5. Multiple functions of junctin and junctate, two distinct isoforms of aspartyl beta-hydroxylase. Hong CS, et al. Biochem Biophys Res Commun, 2007 Oct 12. PMID 17706594

    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)
    • Targeted (2)  1 citation
    • Endonuclease-mediated (2) 

    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 dioxygenase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables oxidoreductase activity IEA
    Inferred from Electronic Annotation
    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 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 
    involved_in peptidyl-amino acid modification IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in peptidyl-aspartic acid hydroxylation IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within peptidyl-aspartic acid hydroxylation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    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 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 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 ISO
    Inferred from Sequence Orthology
    more info
    		  
    located_in sarcoplasmic reticulum 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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