Sign in to NCBI
Format

Send to:

Choose Destination

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

Gene ID: 444, updated on 2-Mar-2021

Summary

Go to the top of the page Help
Official Symbol
ASPHprovided by HGNC
Official Full Name
aspartate beta-hydroxylaseprovided by HGNC
Primary source
HGNC:HGNC:757
See related
Ensembl:ENSG00000198363 MIM:600582
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
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help
See ASPH in Genome Data Viewer
Location:
8q12.3
Exon count:
33
Annotation release Status Assembly Chr Location
109.20210226 current GRCh38.p13 (GCF_000001405.39) 8 NC_000008.11 (61500556..61714609, complement)
105.20201022 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 nucleophosmin 1 pseudogene 6 Neighboring gene uncharacterized LOC105375870 Neighboring gene keratin 8 pseudogene 3 Neighboring gene RN7SK pseudogene 97 Neighboring gene CAGE-defined mid-level expression enhancer upstream of ASPH Neighboring gene microRNA 4470

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to nucleotide: Graphics FASTA GenBank

Expression

Go to the top of the page Help
  • 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

Go to the top of the pageHelp

Related articles in PubMed

  1. Kinetic parameters of human aspartate/asparagine-β-hydroxylase suggest that it has a possible function in oxygen sensing. Brewitz L, et al. J Biol Chem, 2020 Jun 5. PMID 32107312, Free PMC Article
  2. Aspartate β-hydroxylase promotes pancreatic ductal adenocarcinoma metastasis through activation of SRC signaling pathway. Ogawa K, et al. J Hematol Oncol, 2019 Dec 30. PMID 31888763, Free PMC Article
  3. Labyrinthin, The Tumor Marker Recognized By MCA 44-3A6: A Case For Pan-Tumor Markers As Targets To Treat Cancer. Radosevich JA, et al. Onco Targets Ther, 2019. PMID 31807015, Free PMC Article
  4. ASPH-notch Axis guided Exosomal delivery of Prometastatic Secretome renders breast Cancer multi-organ metastasis. Lin Q, et al. Mol Cancer, 2019 Nov 7. PMID 31694640, Free PMC Article
  5. Aspartate/asparagine-β-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern. Pfeffer I, et al. Nat Commun, 2019 Oct 28. PMID 31659163, Free PMC Article

See all (109) 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. 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.
  2. 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.
  3. ASPH-Notch axis guides particularly selective exosomes to potentiate multifaceted metastasis. ASPH's pro-oncogenic/pro-metastatic properties are essential for breast cancer development/progression, revealing a potential target for therapy.
    Title: ASPH-notch Axis guided Exosomal delivery of Prometastatic Secretome renders breast Cancer multi-organ metastasis.
  4. We report the 14th individual with Traboulsi syndrome and a novel homozygous deletion variant in exon 22 of ASPH gene associated with the phenotype.
    Title: A novel 5 bp homozygous deletion mutation in ASPH gene associates with Traboulsi syndrome.
  5. An unexpected Cys3-4 disulfide bonding pattern is observed in the epidermal growth factor-like domains of AspH.
    Title: Aspartate/asparagine-β-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern.
  6. Expression of aspartate beta-hydroxylase (ASPH) promoted direct protein interaction between RB1, cyclin-dependent kinases, and cyclins.
    Title: Aspartate beta-hydroxylase promotes cholangiocarcinoma progression by modulating RB1 phosphorylation.
  7. The mRNA expression and promoter methylation rate of ASPH gene may play a role in the development and progression of breast cancer.
    Title: [Expression of <i>ASPH</i> Gene in Invasive Breast Cancer and Its Clinical Significance in Promoter Methylation].
  8. the role of FTH1 in the FIH control of HIF-1 activity, is reported.
    Title: Ferritin heavy chain controls the HIF-driven hypoxic response by activating the asparaginyl hydroxylase FIH.
  9. the hydroxylase activity of ASPH affected HCC metastasis through interacting with vimentin and regulating EMT. As such, ASPH might be a promising therapeutic target of HCC.
    Title: Hydroxylase Activity of ASPH Promotes Hepatocellular Carcinoma Metastasis Through Epithelial-to-Mesenchymal Transition Pathway.
  10. Higher levels of HAAH/humbug mRNA were found in the hepatocellular carcinoma tissues relative to the adjacent cancerfree tissue.
    Title: Evaluation of HAAH/humbug quantitative detection in the diagnosis of hepatocellular carcinoma.
Submit: New GeneRIF Correction See all GeneRIFs (29)

Phenotypes

Go to the top of the page Help

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

Review eQTL and phenotype association data in this region using PheGenI

Variation

Go to the top of the page Help

See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

Genotypes

HIV-1 interactions

Go to the top of the page Help

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

Go to the top of the page

Interactions

Go to the top of the page Help
Products Interactant Other Gene Complex Source Pubs Description

General gene information

Go to the top of the page Help

Markers

Homology

Gene Ontology Provided by GOA

Function Evidence Code Pubs
calcium ion binding NAS
Non-traceable Author Statement
more info
 PubMed 
electron transfer activity TAS
Traceable Author Statement
more info
 PubMed 
peptide-aspartate beta-dioxygenase activity IBA
Inferred from Biological aspect of Ancestor
more info
 PubMed 
peptidyl-aspartic acid 3-dioxygenase activity IEA
Inferred from Electronic Annotation
more info
  
protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
structural constituent of muscle TAS
Traceable Author Statement
more info
 PubMed 
structural molecule activity TAS
Traceable Author Statement
more info
 PubMed 
Process Evidence Code Pubs
activation of cysteine-type endopeptidase activity IDA
Inferred from Direct Assay
more info
 PubMed 
electron transport chain IEA
Inferred from Electronic Annotation
more info
  
ion transmembrane transport TAS
Traceable Author Statement
more info
  
muscle contraction TAS
Traceable Author Statement
more info
 PubMed 
peptidyl-aspartic acid hydroxylation IBA
Inferred from Biological aspect of Ancestor
more info
 PubMed 
positive regulation of proteolysis IDA
Inferred from Direct Assay
more info
 PubMed 
protein phosphopantetheinylation IEA
Inferred from Electronic Annotation
more info
  
regulation of cardiac conduction TAS
Traceable Author Statement
more info
  
Component Evidence Code Pubs
cortical endoplasmic reticulum IDA
Inferred from Direct Assay
more info
 PubMed 
endoplasmic reticulum IBA
Inferred from Biological aspect of Ancestor
more info
 PubMed 
endoplasmic reticulum IDA
Inferred from Direct Assay
more info
  
endoplasmic reticulum membrane NAS
Non-traceable Author Statement
more info
 PubMed 
endoplasmic reticulum membrane TAS
Traceable Author Statement
more info
  
integral component of membrane IEA
Inferred from Electronic Annotation
more info
  
plasma membrane IDA
Inferred from Direct Assay
more info
 PubMed 
sarcoplasmic reticulum membrane IEA
Inferred from Electronic Annotation
more info
  

General protein information

Go to the top of the page Help
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_016868910.1
XP_016868911.1
XP_016868913.1
XP_016868914.1
XP_016868915.1
XP_016868916.1
XP_016868917.1
XP_016868918.1
XP_016868919.1
XP_016868920.1
XP_016868921.1
XP_016868922.1
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_024302923.1
XP_024302924.1
XP_024302925.1
XP_024302926.1
XP_024302927.1

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

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 f

    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 g

    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 h

    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 i

    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 j

    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 k

    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 l

    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, ENST00000379449.10
    Conserved Domains (1) summary
    pfam05279
    Location:43 → 146
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  8. NM_004318.4 → NP_004309.2  aspartyl/asparaginyl beta-hydroxylase isoform a

    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
    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

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

    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, ENST00000389204.8
    Conserved Domains (1) summary
    pfam05279
    Location:14 → 205
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

  10. NM_032466.4 → NP_115855.1  aspartyl/asparaginyl beta-hydroxylase isoform c

    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

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

    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

  12. NM_032468.5 → NP_115857.1  aspartyl/asparaginyl beta-hydroxylase isoform b

    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, ENST00000517847.6
    Conserved Domains (1) summary
    pfam05279
    Location:14 → 296
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region

RefSeqs of Annotated Genomes: Homo sapiens Updated Annotation Release 109.20210226

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

Reference GRCh38.p13 Primary Assembly

Genomic

  1. NC_000008.11 Reference GRCh38.p13 Primary Assembly

    Range
    61500556..61714609 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_005251247.2 → XP_005251304.1  aspartyl/asparaginyl beta-hydroxylase isoform X31

    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

  2. XM_024447155.1 → XP_024302923.1  aspartyl/asparaginyl beta-hydroxylase isoform X23

    Conserved Domains (5) summary
    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 → 724
    Asp_Arg_Hydrox; Aspartyl/Asparaginyl beta-hydroxylase
    cl26250
    Location:295 → 408
    TPR_6; Tetratricopeptide repeat
    cl27017
    Location:318 → 506
    YfgC; Putative Zn-dependent protease, contains TPR repeats [General function prediction only]

  3. XM_017013438.1 → XP_016868927.1  aspartyl/asparaginyl beta-hydroxylase isoform X26

  4. XM_017013432.1 → XP_016868921.1  aspartyl/asparaginyl beta-hydroxylase isoform X15

  5. XM_005251243.2 → XP_005251300.1  aspartyl/asparaginyl beta-hydroxylase isoform X25

    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

  6. XM_017013430.1 → XP_016868919.1  aspartyl/asparaginyl beta-hydroxylase isoform X13

  7. XM_017013434.1 → XP_016868923.1  aspartyl/asparaginyl beta-hydroxylase isoform X18

  8. XM_005251239.2 → XP_005251296.1  aspartyl/asparaginyl beta-hydroxylase isoform X17

    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

  9. XM_017013425.1 → XP_016868914.1  aspartyl/asparaginyl beta-hydroxylase isoform X6

  10. XM_017013421.1 → XP_016868910.1  aspartyl/asparaginyl beta-hydroxylase isoform X3

  11. XM_005251236.2 → XP_005251293.1  aspartyl/asparaginyl beta-hydroxylase isoform X8

    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

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

  13. XM_005251235.2 → XP_005251292.1  aspartyl/asparaginyl beta-hydroxylase isoform X7

    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

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

  15. XM_005251246.3 → XP_005251303.1  aspartyl/asparaginyl beta-hydroxylase isoform X30

    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

  16. XM_017013437.2 → XP_016868926.1  aspartyl/asparaginyl beta-hydroxylase isoform X21

  17. XM_005251242.3 → XP_005251299.1  aspartyl/asparaginyl beta-hydroxylase isoform X22

    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

  18. XM_017013428.2 → XP_016868917.1  aspartyl/asparaginyl beta-hydroxylase isoform X11

  19. XM_017013429.2 → XP_016868918.1  aspartyl/asparaginyl beta-hydroxylase isoform X12

  20. XM_017013424.2 → XP_016868913.1  aspartyl/asparaginyl beta-hydroxylase isoform X5

  21. XM_017013422.2 → XP_016868911.1  aspartyl/asparaginyl beta-hydroxylase isoform X4

  22. XM_017013440.1 → XP_016868929.1  aspartyl/asparaginyl beta-hydroxylase isoform X28

  23. XM_005251244.1 → XP_005251301.1  aspartyl/asparaginyl beta-hydroxylase isoform X29

    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

  24. XM_017013435.1 → XP_016868924.1  aspartyl/asparaginyl beta-hydroxylase isoform X19

  25. XM_017013427.1 → XP_016868916.1  aspartyl/asparaginyl beta-hydroxylase isoform X10

  26. XM_005251240.1 → XP_005251297.1  aspartyl/asparaginyl beta-hydroxylase isoform X20

    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

  27. XM_017013426.1 → XP_016868915.1  aspartyl/asparaginyl beta-hydroxylase isoform X9

  28. XM_017013444.1 → XP_016868933.1  aspartyl/asparaginyl beta-hydroxylase isoform X32

  29. XM_024447156.1 → XP_024302924.1  aspartyl/asparaginyl beta-hydroxylase isoform X24

    Conserved Domains (5) summary
    pfam05279
    Location:14 → 262
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region
    sd00006
    Location:410 → 434
    TPR; TPR repeat [structural motif]
    pfam05118
    Location:543 → 723
    Asp_Arg_Hydrox; Aspartyl/Asparaginyl beta-hydroxylase
    cl26250
    Location:294 → 407
    TPR_6; Tetratricopeptide repeat
    cl27017
    Location:317 → 505
    YfgC; Putative Zn-dependent protease, contains TPR repeats [General function prediction only]

  30. XM_017013439.1 → XP_016868928.1  aspartyl/asparaginyl beta-hydroxylase isoform X27

  31. XM_017013433.1 → XP_016868922.1  aspartyl/asparaginyl beta-hydroxylase isoform X16

  32. XM_017013431.1 → XP_016868920.1  aspartyl/asparaginyl beta-hydroxylase isoform X14

  33. XM_024447157.1 → XP_024302925.1  aspartyl/asparaginyl beta-hydroxylase isoform X33

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

  34. XM_024447158.1 → 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

  35. XM_017013447.1 → XP_016868936.1  aspartyl/asparaginyl beta-hydroxylase isoform X37

    Related
    ENSP00000427877.1, ENST00000518306.5

  36. XM_017013446.1 → XP_016868935.1  aspartyl/asparaginyl beta-hydroxylase isoform X36

  37. XM_017013445.1 → XP_016868934.1  aspartyl/asparaginyl beta-hydroxylase isoform X35

  38. XM_024447159.1 → XP_024302927.1  aspartyl/asparaginyl beta-hydroxylase isoform X38

    Related
    ENSP00000428060.1, ENST00000517661.5
    Conserved Domains (1) summary
    pfam05279
    Location:14 → 117
    Asp-B-Hydro_N; Aspartyl beta-hydroxylase N-terminal region
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
Q12797.3 GenPept UniProtKB/Swiss-Prot:Q12797

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

Chemical Information
Molecular Biology Databases
Research Materials
Tools
Miscellaneous
You are here: NCBI > Genes & Expression > Gene
Support Center