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ASPH aspartate beta-hydroxylase [ Homo sapiens (human) ]

Gene ID: 444, updated on 16-Nov-2022

Summary

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Official Symbol
ASPHprovided by HGNC
Official Full Name
aspartate beta-hydroxylaseprovided by HGNC
Primary source
HGNC:HGNC:757
See related
Ensembl:ENSG00000198363 MIM:600582; AllianceGenome:HGNC:757
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Homo sapiens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as
AAH; BAH; HAAH; JCTN; FDLAB; junctin; CASQ2BP1
Summary
This gene is thought to play an important role in calcium homeostasis. The gene is expressed from two promoters and undergoes extensive alternative splicing. The encoded set of proteins share varying amounts of overlap near their N-termini but have substantial variations in their C-terminal domains resulting in distinct functional properties. The longest isoforms (a and f) include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the epidermal growth factor (EGF)-like domains of some proteins, including protein C, coagulation factors VII, IX, and X, and the complement factors C1R and C1S. Other isoforms differ primarily in the C-terminal sequence and lack the hydroxylase domain, and some have been localized to the endoplasmic and sarcoplasmic reticulum. Some of these isoforms are found in complexes with calsequestrin, triadin, and the ryanodine receptor, and have been shown to regulate calcium release from the sarcoplasmic reticulum. Some isoforms have been implicated in metastasis. [provided by RefSeq, Sep 2009]
Expression
Broad expression in fat (RPKM 85.5), adrenal (RPKM 27.8) and 21 other tissues See more
Orthologs
mouse all
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Genomic context

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See ASPH in Genome Data Viewer
Location:
8q12.3
Exon count:
33
Annotation release Status Assembly Chr Location
110 current GRCh38.p14 (GCF_000001405.40) 8 NC_000008.11 (61500556..61714592, complement)
110 current T2T-CHM13v2.0 (GCF_009914755.1) 8 NC_060932.1 (61924301..62138323, complement)
105.20220307 previous assembly GRCh37.p13 (GCF_000001405.25) 8 NC_000008.10 (62413115..62627151, complement)

Chromosome 8 - NC_000008.11Genomic Context describing neighboring genes Neighboring gene clavesin 1 Neighboring gene uncharacterized LOC105375870 Neighboring gene Sharpr-MPRA regulatory region 11405 Neighboring gene keratin 8 pseudogene 3 Neighboring gene RN7SK pseudogene 97 Neighboring gene P300/CBP strongly-dependent group 1 enhancer GRCh37_chr8:62634171-62635370 Neighboring gene microRNA 4470

Genomic regions, transcripts, and products

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Go to nucleotide: Graphics FASTA GenBank

Expression

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  • Project title: HPA RNA-seq normal tissues
  • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
  • BioProject: PRJEB4337
  • Publication: PMID 24309898
  • Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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Related articles in PubMed

  1. Traboulsi syndrome caused by mutations in ASPH: An autosomal recessive disorder with overlapping features of Marfan syndrome. Jones G, et al. Eur J Med Genet, 2022 Oct. PMID 35918038
  2. Overexpression of Human Aspartyl (Asparaginyl) β-hydroxylase in NSCLC: Its Diagnostic Value by Means of Exosomes of Bronchoalveolar Lavage. Zhu H, et al. Appl Immunohistochem Mol Morphol, 2021 Nov-Dec 01. PMID 34433181
  3. Expanding the clinical spectrum and management of Traboulsi syndrome: report on two siblings homozygous for a novel pathogenic variant in ASPH. Van Hoorde T, et al. Ophthalmic Genet, 2021 Aug. PMID 34018898
  4. Human Oxygenase Variants Employing a Single Protein FeII Ligand Are Catalytically Active. Brasnett A, et al. Angew Chem Int Ed Engl, 2021 Jun 21. PMID 33887099, Free PMC Article
  5. Characterization of the Relationship Between the Expression of Aspartate β-Hydroxylase and the Pathological Characteristics of Breast Cancer. Zhang Y, et al. Med Sci Monit, 2020 Dec 31. PMID 33380715, Free PMC Article

See all (141) citations in PubMed

See citations in PubMed for homologs of this gene provided by HomoloGene

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Traboulsi syndrome caused by mutations in ASPH: An autosomal recessive disorder with overlapping features of Marfan syndrome.
    Title: Traboulsi syndrome caused by mutations in ASPH: An autosomal recessive disorder with overlapping features of Marfan syndrome.
  2. Overexpression of Human Aspartyl (Asparaginyl) beta-hydroxylase in NSCLC: Its Diagnostic Value by Means of Exosomes of Bronchoalveolar Lavage.
    Title: Overexpression of Human Aspartyl (Asparaginyl) β-hydroxylase in NSCLC: Its Diagnostic Value by Means of Exosomes of Bronchoalveolar Lavage.
  3. Expanding the clinical spectrum and management of Traboulsi syndrome: report on two siblings homozygous for a novel pathogenic variant in ASPH.
    Title: Expanding the clinical spectrum and management of Traboulsi syndrome: report on two siblings homozygous for a novel pathogenic variant in <i>ASPH</i>.
  4. Human Oxygenase Variants Employing a Single Protein Fe(II) Ligand Are Catalytically Active.
    Title: Human Oxygenase Variants Employing a Single Protein Fe<sup>II</sup> Ligand Are Catalytically Active.
  5. A novel mutation in the aspartate beta-hydroxylase (ASPH) gene is associated with a rare form of Traboulsi syndrome.
    Title: A novel mutation in the aspartate beta-hydroxylase (<i>ASPH</i>) gene is associated with a rare form of Traboulsi syndrome.
  6. Diverse molecular functions of aspartate betahydroxylase in cancer (Review).
    Title: Diverse molecular functions of aspartate β‑hydroxylase in cancer (Review).
  7. Aspartate beta-hydroxylase targeting in castration-resistant prostate cancer modulates the NOTCH/HIF1alpha/GSK3beta crosstalk.
    Title: Aspartate β-hydroxylase targeting in castration-resistant prostate cancer modulates the NOTCH/HIF1α/GSK3β crosstalk.
  8. Characterization of the Relationship Between the Expression of Aspartate beta-Hydroxylase and the Pathological Characteristics of Breast Cancer.
    Title: Characterization of the Relationship Between the Expression of Aspartate β-Hydroxylase and the Pathological Characteristics of Breast Cancer.
  9. Kinetic parameters of human aspartate/asparagine-beta-hydroxylase suggest that it has a possible function in oxygen sensing.
    Title: Kinetic parameters of human aspartate/asparagine-β-hydroxylase suggest that it has a possible function in oxygen sensing.
  10. High ASPH expression is associated with pancreatic ductal adenocarcinoma metastasisthrough activation of SRC signaling pathway.
    Title: Aspartate β-hydroxylase promotes pancreatic ductal adenocarcinoma metastasis through activation of SRC signaling pathway.
Submit: New GeneRIF Correction See all GeneRIFs (37)

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

Genotypes

HIV-1 interactions

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Protein interactions

Protein Gene Interaction Pubs
Envelope surface glycoprotein gp160, precursor env HIV-1 gp160 interacts with ASPH; predicted interaction to be within the endoplasmic reticulum PubMed

Go to the HIV-1, Human Interaction Database

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 GOA

Function Evidence Code Pubs
enables calcium ion binding NAS
Non-traceable Author Statement
more info
 PubMed 
enables electron transfer activity TAS
Traceable Author Statement
more info
 PubMed 
enables peptidyl-aspartic acid 3-dioxygenase activity IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables structural constituent of muscle TAS
Traceable Author Statement
more info
 PubMed 
enables structural molecule activity TAS
Traceable Author Statement
more info
 PubMed 
Process Evidence Code Pubs
involved_in activation of cysteine-type endopeptidase activity IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in cell population proliferation IEA
Inferred from Electronic Annotation
more info
  
involved_in electron transport chain IEA
Inferred from Electronic Annotation
more info
  
involved_in face morphogenesis IEA
Inferred from Electronic Annotation
more info
  
involved_in limb morphogenesis IEA
Inferred from Electronic Annotation
more info
  
involved_in muscle contraction TAS
Traceable Author Statement
more info
 PubMed 
involved_in negative regulation of cell population proliferation IEA
Inferred from Electronic Annotation
more info
  
involved_in pattern specification process IEA
Inferred from Electronic Annotation
more info
  
involved_in peptidyl-aspartic acid hydroxylation IBA
Inferred from Biological aspect of Ancestor
more info
 PubMed 
involved_in positive regulation of proteolysis IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in regulation of protein depolymerization IEA
Inferred from Electronic Annotation
more info
  
involved_in regulation of protein stability IEA
Inferred from Electronic Annotation
more info
  
involved_in roof of mouth development IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
located_in cortical endoplasmic reticulum IDA
Inferred from Direct Assay
more info
 PubMed 
is_active_in endoplasmic reticulum IBA
Inferred from Biological aspect of Ancestor
more info
 PubMed 
located_in endoplasmic reticulum IDA
Inferred from Direct Assay
more info
  
located_in endoplasmic reticulum membrane NAS
Non-traceable Author Statement
more info
 PubMed 
located_in endoplasmic reticulum membrane TAS
Traceable Author Statement
more info
  
located_in plasma membrane IDA
Inferred from Direct Assay
more info
 PubMed 
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
A beta H-J-J
ASP beta-hydroxylase
cardiac junctin
humbug
junctate
peptide-aspartate beta-dioxygenase
NP_001158222.1
NP_001158223.1
NP_001158224.1
NP_001158225.1
NP_001158226.1
NP_001158227.1
NP_001158228.1
NP_004309.2
NP_064549.1
NP_115855.1
NP_115856.1
NP_115857.1
XP_005251292.1
XP_005251293.1
XP_005251296.1
XP_005251297.1
XP_005251299.1
XP_005251300.1
XP_005251301.1
XP_005251303.1
XP_005251304.1
XP_016868908.1
XP_016868909.1
XP_016868911.1
XP_016868915.1
XP_016868916.1
XP_016868917.1
XP_016868918.1
XP_016868919.1
XP_016868920.1
XP_016868923.1
XP_016868924.1
XP_016868926.1
XP_016868927.1
XP_016868928.1
XP_016868929.1
XP_016868933.1
XP_016868934.1
XP_016868935.1
XP_016868936.1
XP_024302925.1
XP_024302926.1
XP_024302927.1
XP_047277741.1
XP_047277742.1
XP_047277744.1
XP_047277745.1
XP_047277746.1
XP_047277747.1
XP_047277748.1
XP_047277749.1

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.

Genomic

  1. NG_013210.1 RefSeqGene

    Range
    5049..219085
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001164750.2 → NP_001158222.1  aspartyl/asparaginyl beta-hydroxylase isoform 6

    Status: REVIEWED

    Description
    Transcript Variant: This variant (6) represents use of an alternate promoter and 5' UTR and uses a distinct start codon, compared to variant 1. The resulting isoform (f) has a shorter and distinct N-terminus, compared to isoform a. This isoform includes the beta-hydroxylase domain found in isoform a and is likely to have catalytic activity.
    Source sequence(s)
    AC090094, AF339775, AK304314, BC025236, DN993915, S83325
    Consensus CDS
    CCDS55234.1
    UniProtKB/Swiss-Prot
    Q12797
    Related
    ENSP00000437864.1, ENST00000541428.5
    Conserved Domains (5) summary
    TIGR02795
    Location:313 → 426
    tol_pal_ybgF; tol-pal system protein YbgF
    pfam05279
    Location:14 → 281
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region
    sd00006
    Location:429 → 453
    TPR; TPR repeat [structural motif]
    pfam05118
    Location:562 → 715
    Asp_Arg_Hydrox; Aspartyl/Asparaginyl beta-hydroxylase
    pfam13428
    Location:316 → 355
    TPR_14; Tetratricopeptide repeat

  2. NM_001164751.2 → NP_001158223.1  aspartyl/asparaginyl beta-hydroxylase isoform 7

    See identical proteins and their annotated locations for NP_001158223.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (7) represents use of an alternate promoter and 5' UTR and uses a distinct start codon, uses a distinct 3' splice pattern that lacks many coding exons, includes an alternate in-frame exon and uses an alternate in-frame splice site, compared to variant 1. The resulting isoform (g) has a shorter and distinct N-terminus a substantially shorter and distinct C-terminus, and several internal differences, compared to isoform a. This isoform is similar to isoform b, which is also known as junctate.
    Source sequence(s)
    AC067881, BC144362, BU623111, DN993915
    Consensus CDS
    CCDS55236.1
    UniProtKB/Swiss-Prot
    Q12797
    Related
    ENSP00000430245.1, ENST00000517903.5
    Conserved Domains (1) summary
    pfam05279
    Location:14 → 295
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  3. NM_001164752.2 → NP_001158224.1  aspartyl/asparaginyl beta-hydroxylase isoform 8

    See identical proteins and their annotated locations for NP_001158224.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (8) represents use of an alternate promoter and 5' UTR and uses a distinct start codon, uses a distinct 3' splice pattern that lacks many coding exons, includes an alternate in-frame exon, lacks an alternate in-frame exon, and uses an alternate in-frame splice site, compared to variant 1. The resulting isoform (h) has a shorter and distinct N-terminus a substantially shorter and distinct C-terminus, and several internal differences, compared to isoform a. This isoform is similar to isoform b, which is also known as junctate.
    Source sequence(s)
    AC067881, BC144363, BU623111, DN993915
    UniProtKB/TrEMBL
    B7ZM96
    Conserved Domains (1) summary
    pfam05279
    Location:14 → 276
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  4. NM_001164753.2 → NP_001158225.1  aspartyl/asparaginyl beta-hydroxylase isoform 9

    See identical proteins and their annotated locations for NP_001158225.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (9) represents use of an alternate promoter and 5' UTR and uses a distinct start codon, uses a distinct 3' splice pattern that lacks many coding exons, includes an alternate in-frame exon, and lacks an alternate in-frame exon, compared to variant 1. The resulting isoform (i) has a shorter and distinct N-terminus a substantially shorter and distinct C-terminus, and several internal differences, compared to isoform a. This isoform is similar to isoform b, which is also known as junctate.
    Source sequence(s)
    AC067881, AK295528, BU623111, DN993915
    Consensus CDS
    CCDS55235.1
    UniProtKB/Swiss-Prot
    Q12797
    Related
    ENSP00000429160.1, ENST00000522835.5
    Conserved Domains (1) summary
    pfam05279
    Location:14 → 253
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  5. NM_001164754.2 → NP_001158226.1  aspartyl/asparaginyl beta-hydroxylase isoform 10

    Status: REVIEWED

    Description
    Transcript Variant: This variant (10) lacks an alternate in-frame exon and uses a distinct 3' splice pattern that lacks many coding exons, compared to variant 1. The resulting isoform (j) lacks an internal segment and has a substantially shorter and distinct C-terminus, compared to isoform a.
    Source sequence(s)
    AC067881, AK298577, BU623111, DA136318
    Consensus CDS
    CCDS75746.1
    UniProtKB/TrEMBL
    B4DQ07
    Related
    ENSP00000394013.4, ENST00000445642.6
    Conserved Domains (1) summary
    pfam05279
    Location:43 → 291
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  6. NM_001164755.2 → NP_001158227.1  aspartyl/asparaginyl beta-hydroxylase isoform 11

    See identical proteins and their annotated locations for NP_001158227.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (11) lacks an alternate in-frame exon and uses a distinct 3' splice pattern that lacks many coding exons, compared to variant 1. The resulting isoform (k) lacks an internal segment and has a substantially shorter and distinct C-terminus, compared to isoform a.
    Source sequence(s)
    AC067881, BC025236, BU623111
    Consensus CDS
    CCDS55237.1
    UniProtKB/Swiss-Prot
    Q12797
    Related
    ENSP00000429286.1, ENST00000518068.5
    Conserved Domains (1) summary
    pfam05279
    Location:43 → 267
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  7. NM_001164756.2 → NP_001158228.1  aspartyl/asparaginyl beta-hydroxylase isoform 12

    See identical proteins and their annotated locations for NP_001158228.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (12) includes an alternate in-frame exon and uses a distinct 3' splice pattern that lacks many coding exons, compared to variant 1. The resulting isoform (l) includes an alternate segment and has a substantially shorter and distinct C-terminus, compared to isoform a.
    Source sequence(s)
    BC066929, BU741737, DA136318
    Consensus CDS
    CCDS55238.1
    UniProtKB/Swiss-Prot
    Q12797
    Related
    ENSP00000368762.5, ENST00000379449.11
    Conserved Domains (1) summary
    pfam05279
    Location:43 → 146
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  8. NM_001413844.1 → NP_001400773.1  aspartyl/asparaginyl beta-hydroxylase isoform 13

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  9. NM_001413845.1 → NP_001400774.1  aspartyl/asparaginyl beta-hydroxylase isoform 14

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  10. NM_001413846.1 → NP_001400775.1  aspartyl/asparaginyl beta-hydroxylase isoform 15

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  11. NM_001413847.1 → NP_001400776.1  aspartyl/asparaginyl beta-hydroxylase isoform 16

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  12. NM_001413848.1 → NP_001400777.1  aspartyl/asparaginyl beta-hydroxylase isoform 17

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  13. NM_001413849.1 → NP_001400778.1  aspartyl/asparaginyl beta-hydroxylase isoform 1

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  14. NM_001413850.1 → NP_001400779.1  aspartyl/asparaginyl beta-hydroxylase isoform 18

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  15. NM_001413851.1 → NP_001400780.1  aspartyl/asparaginyl beta-hydroxylase isoform 18

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  16. NM_001413852.1 → NP_001400781.1  aspartyl/asparaginyl beta-hydroxylase isoform 19

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  17. NM_001413853.1 → NP_001400782.1  aspartyl/asparaginyl beta-hydroxylase isoform 20

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  18. NM_001413854.1 → NP_001400783.1  aspartyl/asparaginyl beta-hydroxylase isoform 21

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  19. NM_001413855.1 → NP_001400784.1  aspartyl/asparaginyl beta-hydroxylase isoform 21

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  20. NM_001413856.1 → NP_001400785.1  aspartyl/asparaginyl beta-hydroxylase isoform 21

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  21. NM_001413857.1 → NP_001400786.1  aspartyl/asparaginyl beta-hydroxylase isoform 22

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  22. NM_001413858.1 → NP_001400787.1  aspartyl/asparaginyl beta-hydroxylase isoform 23

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  23. NM_001413859.1 → NP_001400788.1  aspartyl/asparaginyl beta-hydroxylase isoform 23

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  24. NM_001413860.1 → NP_001400789.1  aspartyl/asparaginyl beta-hydroxylase isoform 24

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  25. NM_001413861.1 → NP_001400790.1  aspartyl/asparaginyl beta-hydroxylase isoform 25

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  26. NM_001413862.1 → NP_001400791.1  aspartyl/asparaginyl beta-hydroxylase isoform 26

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  27. NM_001413863.1 → NP_001400792.1  aspartyl/asparaginyl beta-hydroxylase isoform 27

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  28. NM_001413864.1 → NP_001400793.1  aspartyl/asparaginyl beta-hydroxylase isoform 6

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  29. NM_001413865.1 → NP_001400794.1  aspartyl/asparaginyl beta-hydroxylase isoform 6

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  30. NM_001413866.1 → NP_001400795.1  aspartyl/asparaginyl beta-hydroxylase isoform 6

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  31. NM_001413867.1 → NP_001400796.1  aspartyl/asparaginyl beta-hydroxylase isoform 28

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  32. NM_001413868.1 → NP_001400797.1  aspartyl/asparaginyl beta-hydroxylase isoform 28

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  33. NM_001413869.1 → NP_001400798.1  aspartyl/asparaginyl beta-hydroxylase isoform 29

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  34. NM_001413870.1 → NP_001400799.1  aspartyl/asparaginyl beta-hydroxylase isoform 30

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  35. NM_001413871.1 → NP_001400800.1  aspartyl/asparaginyl beta-hydroxylase isoform 31

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  36. NM_001413872.1 → NP_001400801.1  aspartyl/asparaginyl beta-hydroxylase isoform 31

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  37. NM_001413873.1 → NP_001400802.1  aspartyl/asparaginyl beta-hydroxylase isoform 32

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  38. NM_001413874.1 → NP_001400803.1  aspartyl/asparaginyl beta-hydroxylase isoform 33

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  39. NM_001413875.1 → NP_001400804.1  aspartyl/asparaginyl beta-hydroxylase isoform 34

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  40. NM_001413876.1 → NP_001400805.1  aspartyl/asparaginyl beta-hydroxylase isoform 35

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  41. NM_001413877.1 → NP_001400806.1  aspartyl/asparaginyl beta-hydroxylase isoform 35

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  42. NM_001413878.1 → NP_001400807.1  aspartyl/asparaginyl beta-hydroxylase isoform 36

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  43. NM_001413879.1 → NP_001400808.1  aspartyl/asparaginyl beta-hydroxylase isoform 37

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  44. NM_001413880.1 → NP_001400809.1  aspartyl/asparaginyl beta-hydroxylase isoform 38

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  45. NM_001413881.1 → NP_001400810.1  aspartyl/asparaginyl beta-hydroxylase isoform 39

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  46. NM_001413882.1 → NP_001400811.1  aspartyl/asparaginyl beta-hydroxylase isoform 40

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  47. NM_001413883.1 → NP_001400812.1  aspartyl/asparaginyl beta-hydroxylase isoform 41

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  48. NM_001413884.1 → NP_001400813.1  aspartyl/asparaginyl beta-hydroxylase isoform 42

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  49. NM_001413885.1 → NP_001400814.1  aspartyl/asparaginyl beta-hydroxylase isoform 43

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  50. NM_001413886.1 → NP_001400815.1  aspartyl/asparaginyl beta-hydroxylase isoform 44

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  51. NM_001413887.1 → NP_001400816.1  aspartyl/asparaginyl beta-hydroxylase isoform 44

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  52. NM_001413888.1 → NP_001400817.1  aspartyl/asparaginyl beta-hydroxylase isoform 45

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  53. NM_001413889.1 → NP_001400818.1  aspartyl/asparaginyl beta-hydroxylase isoform 46

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  54. NM_001413890.1 → NP_001400819.1  aspartyl/asparaginyl beta-hydroxylase isoform 47

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  55. NM_001413891.1 → NP_001400820.1  aspartyl/asparaginyl beta-hydroxylase isoform 48

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  56. NM_001413893.1 → NP_001400822.1  aspartyl/asparaginyl beta-hydroxylase isoform 49

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  57. NM_001413894.1 → NP_001400823.1  aspartyl/asparaginyl beta-hydroxylase isoform 50

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  58. NM_001413895.1 → NP_001400824.1  aspartyl/asparaginyl beta-hydroxylase isoform 51

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  59. NM_001413896.1 → NP_001400825.1  aspartyl/asparaginyl beta-hydroxylase isoform 52

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  60. NM_001413897.1 → NP_001400826.1  aspartyl/asparaginyl beta-hydroxylase isoform 53

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  61. NM_001413898.1 → NP_001400827.1  aspartyl/asparaginyl beta-hydroxylase isoform 54

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  62. NM_001413899.1 → NP_001400828.1  aspartyl/asparaginyl beta-hydroxylase isoform 55

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  63. NM_001413900.1 → NP_001400829.1  aspartyl/asparaginyl beta-hydroxylase isoform 56

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  64. NM_001413901.1 → NP_001400830.1  aspartyl/asparaginyl beta-hydroxylase isoform 58

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  65. NM_001413902.1 → NP_001400831.1  aspartyl/asparaginyl beta-hydroxylase isoform 2

    Status: REVIEWED

    Source sequence(s)
    AC067881

  66. NM_001413903.1 → NP_001400832.1  aspartyl/asparaginyl beta-hydroxylase isoform 59

    Status: REVIEWED

    Source sequence(s)
    AC067881

  67. NM_001413904.1 → NP_001400833.1  aspartyl/asparaginyl beta-hydroxylase isoform 60

    Status: REVIEWED

    Source sequence(s)
    AC067881

  68. NM_001413905.1 → NP_001400834.1  aspartyl/asparaginyl beta-hydroxylase isoform 61

    Status: REVIEWED

    Source sequence(s)
    AC067881

  69. NM_001413906.1 → NP_001400835.1  aspartyl/asparaginyl beta-hydroxylase isoform 62

    Status: REVIEWED

    Source sequence(s)
    AC067881

  70. NM_001413907.1 → NP_001400836.1  aspartyl/asparaginyl beta-hydroxylase isoform 63

    Status: REVIEWED

    Source sequence(s)
    AC067881

  71. NM_001413908.1 → NP_001400837.1  aspartyl/asparaginyl beta-hydroxylase isoform 64

    Status: REVIEWED

    Source sequence(s)
    AC067881

  72. NM_001413909.1 → NP_001400838.1  aspartyl/asparaginyl beta-hydroxylase isoform 57

    Status: REVIEWED

    Source sequence(s)
    AC067881, AC090094

  73. NM_004318.4 → NP_004309.2  aspartyl/asparaginyl beta-hydroxylase isoform 1

    See identical proteins and their annotated locations for NP_004309.2

    Status: REVIEWED

    Description
    Transcript Variant: This variant (1) represents the longest transcript and encodes the longest isoform. The distinct C-terminus of this isoform has enzymatic activity which hydroxylates the beta carbon of aspartic acid or asparagine residues in certain epidermal growth factor-like domains of proteins such as protein C, coagulation factors VII, IX, and X, and the complement factors C1R and C1S. This variant is widely expressed among heart, placenta, skeletal muscle, kidney, and lung tissues.
    Source sequence(s)
    AC067881, AC090094, S83325, U03109
    Consensus CDS
    CCDS34898.1
    UniProtKB/Swiss-Prot
    Q12797, Q9Y4J0
    Related
    ENSP00000368767.4, ENST00000379454.9
    Conserved Domains (5) summary
    TIGR02795
    Location:342 → 455
    tol_pal_ybgF; tol-pal system protein YbgF
    pfam05279
    Location:43 → 310
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region
    sd00006
    Location:458 → 482
    TPR; TPR repeat [structural motif]
    pfam05118
    Location:591 → 744
    Asp_Arg_Hydrox; Aspartyl/Asparaginyl beta-hydroxylase
    pfam13428
    Location:345 → 384
    TPR_14; Tetratricopeptide repeat

  74. NM_020164.5 → NP_064549.1  aspartyl/asparaginyl beta-hydroxylase isoform 5

    See identical proteins and their annotated locations for NP_064549.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (5) represents use of an alternate promoter and 5' UTR, uses a distinct start codon, includes an alternate in-frame exon, and uses a distinct 3' splice pattern that lacks many coding exons, compared to variant 1. The encoded isoform (e) has a slightly shorter and distinct N-terminus and some overlap with the N-terminus of isoform a. This isoform lacks the catalytic domain and enzymatic function of isoform a. This isoform has also been referred to as junctin isoform 1 and forms a complex with calsequestrin, triadin, and the ryanodine receptor by direct interaction at the C-terminal part of the molecule. This protein appears to stabilize the complex and plays a crucial role in the regulation of calcium release from the sarcoplasmic reticulum. This variant is expressed in cardiac and skeletal muscle.
    Source sequence(s)
    AC067881, AF224469, BX102882, DN993915
    Consensus CDS
    CCDS34900.1
    UniProtKB/Swiss-Prot
    Q12797
    Related
    ENSP00000373856.4, ENST00000389204.9
    Conserved Domains (1) summary
    pfam05279
    Location:14 → 205
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  75. NM_032466.4 → NP_115855.1  aspartyl/asparaginyl beta-hydroxylase isoform 3

    See identical proteins and their annotated locations for NP_115855.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (3) uses a distinct 3' splice pattern that lacks many coding exons, compared to variant 1. The encoded isoform (c), also known as humbug, is identical to the N-terminal and central region of isoform a. Because this transcript variant lacks the alternative 3' terminal exon which encodes a catalytic domain for isoform a, isoform c is considered a noncatalytic isoform. This variant is widely expressed among heart, placenta, skeletal muscle, kidney, and lung tissues.
    Source sequence(s)
    AC067881, AF289489, BC025236, BU623111
    Consensus CDS
    CCDS43742.1
    UniProtKB/Swiss-Prot
    Q12797
    Related
    ENSP00000348841.5, ENST00000356457.9
    Conserved Domains (1) summary
    pfam05279
    Location:43 → 310
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  76. NM_032467.4 → NP_115856.1  aspartyl/asparaginyl beta-hydroxylase isoform 4

    See identical proteins and their annotated locations for NP_115856.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (4) represents use of an alternate promoter and 5' UTR, uses a distinct start codon, and uses a distinct 3' splice pattern that lacks many coding exons, compared to variant 1. The encoded isoform (d) has a slightly shorter and distinct N-terminus and some overlap with the N-terminus of isoform a, but lacks the catalytic domain and enzymatic function of isoform a. This isoform has also been referred to as junctin and forms a complex with calsequestrin, triadin, and the ryanodine receptor by direct interaction at the C-terminal part of the molecule. This protein appears to stabilize the complex and plays a crucial role in the regulation of calcium release from the sarcoplasmic reticulum. This variant is expressed in cardiac and skeletal muscle.
    Source sequence(s)
    AC067881, AF224468, BX102882, DN993915
    Consensus CDS
    CCDS34899.1
    UniProtKB/Swiss-Prot
    Q12797
    Related
    ENSP00000436188.1, ENST00000522603.5
    Conserved Domains (1) summary
    pfam05279
    Location:14 → 190
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  77. NM_032468.5 → NP_115857.1  aspartyl/asparaginyl beta-hydroxylase isoform 2

    See identical proteins and their annotated locations for NP_115857.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (2) represents use of an alternate promoter and 5' UTR, uses a distinct start codon, includes an alternate in-frame exon, and uses a distinct 3' splice pattern that lacks many coding exons, compared to variant 1. The encoded isoform (b) shares residues with the central region of isoform a. This isoform lacks the catalytic domain and enzymatic function of isoform a. Isoform b has also been referred to as junctate and is located in both the endoplasmic and sarcoplasmic reticulum. Calcium binding properties of this isoform suggest an active role in the calcium storage and release process in the endoplasmic reticulum. This variant is expressed in heart, brain, pancreas, placenta, lung, liver, kidney, and skeletal muscle tissues.
    Source sequence(s)
    AC067881, AF306765, BU623111, DN993915
    Consensus CDS
    CCDS47866.1
    UniProtKB/Swiss-Prot
    Q12797
    Related
    ENSP00000429954.2, ENST00000517847.7
    Conserved Domains (1) summary
    pfam05279
    Location:14 → 296
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 110 details...Open this link in a new tab

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

Reference GRCh38.p14 Primary Assembly

Genomic

  1. NC_000008.11 Reference GRCh38.p14 Primary Assembly

    Range
    61500556..61714592 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_047421790.1 → XP_047277746.1  aspartyl/asparaginyl beta-hydroxylase isoform X28

  2. XM_005251246.4 → XP_005251303.1  aspartyl/asparaginyl beta-hydroxylase isoform X27

    Conserved Domains (5) summary
    TIGR02795
    Location:299 → 412
    tol_pal_ybgF; tol-pal system protein YbgF
    pfam05279
    Location:43 → 267
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region
    sd00006
    Location:415 → 439
    TPR; TPR repeat [structural motif]
    pfam05118
    Location:548 → 701
    Asp_Arg_Hydrox; Aspartyl/Asparaginyl beta-hydroxylase
    pfam13428
    Location:302 → 341
    TPR_14; Tetratricopeptide repeat

  3. XM_017013437.3 → XP_016868926.1  aspartyl/asparaginyl beta-hydroxylase isoform X19

  4. XM_047421789.1 → XP_047277745.1  aspartyl/asparaginyl beta-hydroxylase isoform X21

  5. XM_005251242.4 → XP_005251299.1  aspartyl/asparaginyl beta-hydroxylase isoform X20

    Conserved Domains (5) summary
    TIGR02795
    Location:323 → 436
    tol_pal_ybgF; tol-pal system protein YbgF
    pfam05279
    Location:43 → 291
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region
    sd00006
    Location:439 → 463
    TPR; TPR repeat [structural motif]
    pfam05118
    Location:572 → 725
    Asp_Arg_Hydrox; Aspartyl/Asparaginyl beta-hydroxylase
    pfam13428
    Location:326 → 365
    TPR_14; Tetratricopeptide repeat

  6. XM_017013428.3 → XP_016868917.1  aspartyl/asparaginyl beta-hydroxylase isoform X8

  7. XM_017013429.3 → XP_016868918.1  aspartyl/asparaginyl beta-hydroxylase isoform X11

  8. XM_047421788.1 → XP_047277744.1  aspartyl/asparaginyl beta-hydroxylase isoform X18

  9. XM_017013422.3 → XP_016868911.1  aspartyl/asparaginyl beta-hydroxylase isoform X3

  10. XM_005251247.3 → XP_005251304.1  aspartyl/asparaginyl beta-hydroxylase isoform X29

    Conserved Domains (5) summary
    TIGR02795
    Location:295 → 408
    tol_pal_ybgF; tol-pal system protein YbgF
    pfam05279
    Location:43 → 263
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region
    sd00006
    Location:411 → 435
    TPR; TPR repeat [structural motif]
    pfam05118
    Location:544 → 697
    Asp_Arg_Hydrox; Aspartyl/Asparaginyl beta-hydroxylase
    pfam13428
    Location:298 → 337
    TPR_14; Tetratricopeptide repeat

  11. XM_017013438.2 → XP_016868927.1  aspartyl/asparaginyl beta-hydroxylase isoform X23

  12. XM_005251243.3 → XP_005251300.1  aspartyl/asparaginyl beta-hydroxylase isoform X22

    Conserved Domains (5) summary
    TIGR02795
    Location:314 → 427
    tol_pal_ybgF; tol-pal system protein YbgF
    pfam05279
    Location:43 → 282
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region
    sd00006
    Location:430 → 454
    TPR; TPR repeat [structural motif]
    pfam05118
    Location:563 → 716
    Asp_Arg_Hydrox; Aspartyl/Asparaginyl beta-hydroxylase
    pfam13428
    Location:317 → 356
    TPR_14; Tetratricopeptide repeat

  13. XM_017013430.2 → XP_016868919.1  aspartyl/asparaginyl beta-hydroxylase isoform X12

  14. XM_017013434.2 → XP_016868923.1  aspartyl/asparaginyl beta-hydroxylase isoform X15

  15. XM_005251239.3 → XP_005251296.1  aspartyl/asparaginyl beta-hydroxylase isoform X14

    Conserved Domains (5) summary
    TIGR02795
    Location:338 → 451
    tol_pal_ybgF; tol-pal system protein YbgF
    pfam05279
    Location:43 → 306
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region
    sd00006
    Location:454 → 478
    TPR; TPR repeat [structural motif]
    pfam05118
    Location:587 → 740
    Asp_Arg_Hydrox; Aspartyl/Asparaginyl beta-hydroxylase
    pfam13428
    Location:341 → 380
    TPR_14; Tetratricopeptide repeat

  16. XM_047421785.1 → XP_047277741.1  aspartyl/asparaginyl beta-hydroxylase isoform X9

  17. XM_005251236.3 → XP_005251293.1  aspartyl/asparaginyl beta-hydroxylase isoform X5

    Conserved Domains (5) summary
    TIGR02795
    Location:356 → 469
    tol_pal_ybgF; tol-pal system protein YbgF
    pfam05279
    Location:43 → 324
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region
    sd00006
    Location:472 → 496
    TPR; TPR repeat [structural motif]
    pfam05118
    Location:605 → 758
    Asp_Arg_Hydrox; Aspartyl/Asparaginyl beta-hydroxylase
    pfam13428
    Location:359 → 398
    TPR_14; Tetratricopeptide repeat

  18. XM_017013420.2 → XP_016868909.1  aspartyl/asparaginyl beta-hydroxylase isoform X2

  19. XM_047421786.1 → XP_047277742.1  aspartyl/asparaginyl beta-hydroxylase isoform X10

  20. XM_005251235.3 → XP_005251292.1  aspartyl/asparaginyl beta-hydroxylase isoform X4

    Conserved Domains (5) summary
    TIGR02795
    Location:357 → 470
    tol_pal_ybgF; tol-pal system protein YbgF
    pfam05279
    Location:43 → 325
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region
    sd00006
    Location:473 → 497
    TPR; TPR repeat [structural motif]
    pfam05118
    Location:606 → 759
    Asp_Arg_Hydrox; Aspartyl/Asparaginyl beta-hydroxylase
    pfam13428
    Location:360 → 399
    TPR_14; Tetratricopeptide repeat

  21. XM_017013419.2 → XP_016868908.1  aspartyl/asparaginyl beta-hydroxylase isoform X1

  22. XM_017013444.2 → XP_016868933.1  aspartyl/asparaginyl beta-hydroxylase isoform X31

  23. XM_047421791.1 → XP_047277747.1  aspartyl/asparaginyl beta-hydroxylase isoform X30

  24. XM_017013439.2 → XP_016868928.1  aspartyl/asparaginyl beta-hydroxylase isoform X24

  25. XM_017013431.2 → XP_016868920.1  aspartyl/asparaginyl beta-hydroxylase isoform X13

  26. XM_017013440.2 → XP_016868929.1  aspartyl/asparaginyl beta-hydroxylase isoform X25

  27. XM_005251244.2 → XP_005251301.1  aspartyl/asparaginyl beta-hydroxylase isoform X26

    Conserved Domains (5) summary
    TIGR02795
    Location:308 → 421
    tol_pal_ybgF; tol-pal system protein YbgF
    pfam05279
    Location:14 → 276
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region
    sd00006
    Location:424 → 448
    TPR; TPR repeat [structural motif]
    pfam05118
    Location:557 → 710
    Asp_Arg_Hydrox; Aspartyl/Asparaginyl beta-hydroxylase
    pfam13428
    Location:311 → 350
    TPR_14; Tetratricopeptide repeat

  28. XM_017013435.2 → XP_016868924.1  aspartyl/asparaginyl beta-hydroxylase isoform X16

  29. XM_017013427.2 → XP_016868916.1  aspartyl/asparaginyl beta-hydroxylase isoform X7

  30. XM_005251240.2 → XP_005251297.1  aspartyl/asparaginyl beta-hydroxylase isoform X17

    Conserved Domains (5) summary
    TIGR02795
    Location:328 → 441
    tol_pal_ybgF; tol-pal system protein YbgF
    pfam05279
    Location:14 → 296
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region
    sd00006
    Location:444 → 468
    TPR; TPR repeat [structural motif]
    pfam05118
    Location:577 → 730
    Asp_Arg_Hydrox; Aspartyl/Asparaginyl beta-hydroxylase
    pfam13428
    Location:331 → 370
    TPR_14; Tetratricopeptide repeat

  31. XM_017013426.2 → XP_016868915.1  aspartyl/asparaginyl beta-hydroxylase isoform X6

  32. XM_047421793.1 → XP_047277749.1  aspartyl/asparaginyl beta-hydroxylase isoform X35

  33. XM_047421792.1 → XP_047277748.1  aspartyl/asparaginyl beta-hydroxylase isoform X33

  34. XM_024447157.2 → XP_024302925.1  aspartyl/asparaginyl beta-hydroxylase isoform X32

    Conserved Domains (1) summary
    pfam05279
    Location:43 → 310
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  35. XM_024447158.2 → XP_024302926.1  aspartyl/asparaginyl beta-hydroxylase isoform X34

    Conserved Domains (1) summary
    pfam05279
    Location:14 → 281
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  36. XM_017013447.2 → XP_016868936.1  aspartyl/asparaginyl beta-hydroxylase isoform X38

    Related
    ENSP00000427877.1, ENST00000518306.5

  37. XM_017013446.2 → XP_016868935.1  aspartyl/asparaginyl beta-hydroxylase isoform X37

  38. XM_017013445.2 → XP_016868934.1  aspartyl/asparaginyl beta-hydroxylase isoform X36

  39. XM_024447159.2 → XP_024302927.1  aspartyl/asparaginyl beta-hydroxylase isoform X39

    UniProtKB/TrEMBL
    G3XAN5
    Related
    ENSP00000428060.1, ENST00000517661.5
    Conserved Domains (1) summary
    pfam05279
    Location:14 → 117
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

Alternate T2T-CHM13v2.0

Genomic

  1. NC_060932.1 Alternate T2T-CHM13v2.0

    Range
    61924301..62138323 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
Q12797.3 GenPept UniProtKB/Swiss-Prot:Q12797

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