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

Summary

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

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_000070.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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.
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.
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.
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.
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.
analysis of aspartyl (asparaginyl) beta-hydroxylase monoclonal antibodies
Title: Monoclonal antibodies against human aspartyl (asparaginyl) beta-hydroxylase developed by DNA immunization.
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.
involved in maintaining sarcoplasmic reticulum Ca2+ store size in skeletal myotubes
Title: Altered stored calcium release in skeletal myotubes deficient of triadin and junctin.
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.
Data suggest that junctate over-expression is associated with an increase in the sarcoplasmic reticulum Ca2+ storage capacity and releasable Ca2+ content and support a physiological role for junctate in intracellular Ca2+ homeostasis.
Title: Increased Ca2+ storage capacity of the skeletal muscle sarcoplasmic reticulum of transgenic mice over-expressing membrane bound calcium binding protein junctate.

Submit: New GeneRIF Correction See all GeneRIFs (16)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (3)
Targeted (2) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

D4Mit263 (e-PCR), detects polymorphism
- UniSTS:130052

Asph (e-PCR), detects polymorphism
- UniSTS:472877

D10Mit157.2 (e-PCR), detects polymorphism
- UniSTS:126061

NoName (e-PCR)
- UniSTS:234865

D4Mit181 (e-PCR), detects polymorphism
- UniSTS:129962

AI848629 (e-PCR)
- UniSTS:165310

RH125437 (e-PCR)
- UniSTS:162258

Asph (e-PCR), detects polymorphism
- UniSTS:507348

Trdn (e-PCR), detects polymorphism
- UniSTS:507353

AW261690 (e-PCR)
- UniSTS:185571

RH126745 (e-PCR)
- UniSTS:207595

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables calcium ion binding	ISO Inferred from Sequence Orthology more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables peptidyl-aspartic acid 3-dioxygenase activity	IBA Inferred from Biological aspect of Ancestor more info
enables peptidyl-aspartic acid 3-dioxygenase activity	ISS Inferred from Sequence or Structural Similarity more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in activation of cysteine-type endopeptidase activity	ISO Inferred from Sequence Orthology more info
involved_in activation of store-operated calcium channel activity	ISO Inferred from Sequence Orthology more info
involved_in calcium ion homeostasis	ISO Inferred from Sequence Orthology more info
involved_in calcium ion transmembrane transport	ISO Inferred from Sequence Orthology more info
acts_upstream_of cell population proliferation	IGI Inferred from Genetic Interaction more info	PubMed
involved_in cellular response to calcium ion	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within face morphogenesis	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within limb morphogenesis	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within negative regulation of cell population proliferation	IGI Inferred from Genetic Interaction more info	PubMed
acts_upstream_of_or_within pattern specification process	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within peptidyl-aspartic acid hydroxylation	IDA Inferred from Direct Assay more info	PubMed
involved_in 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	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of proteolysis	ISO Inferred from Sequence Orthology more info
involved_in regulation of cytosolic calcium ion concentration	IBA Inferred from Biological aspect of Ancestor more info
involved_in regulation of cytosolic calcium ion concentration	IEA Inferred from Electronic Annotation more info
involved_in regulation of cytosolic calcium ion concentration	ISO Inferred from Sequence Orthology more info
involved_in regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity	ISO Inferred from Sequence Orthology more info
involved_in regulation of protein depolymerization	IDA Inferred from Direct Assay more info	PubMed
involved_in regulation of protein stability	IDA Inferred from Direct Assay more info	PubMed
involved_in response to ATP	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within roof of mouth development	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cortical endoplasmic reticulum	IEA Inferred from Electronic Annotation more info
located_in cortical endoplasmic reticulum	ISO Inferred from Sequence Orthology more info
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
is_active_in endoplasmic reticulum	IBA Inferred from Biological aspect of Ancestor more info
located_in endoplasmic reticulum	ISO Inferred from Sequence Orthology more info
located_in endoplasmic reticulum membrane	ISO Inferred from Sequence Orthology more info
located_in membrane	ISS Inferred from Sequence or Structural Similarity more info	PubMed
located_in plasma membrane	IEA Inferred from Electronic Annotation more info
located_in plasma membrane	ISO Inferred from Sequence Orthology more info
located_in sarcoplasmic reticulum membrane	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: aspartyl/asparaginyl beta-hydroxylase

Names: ASP beta-hydroxylase; aspartly beta-hydroxylase; aspartyl beta-hydroxylase Humbug; calsequestrin-binding protein; jumbug; junctate; junctin; peptide-aspartate beta-dioxygenase

NP_001171320.1

EC 1.14.11.16

NP_001171321.1

EC 1.14.11.16

NP_001171322.1

EC 1.14.11.16

NP_001171323.1

EC 1.14.11.16

NP_001171324.1

EC 1.14.11.16

NP_001171325.1

EC 1.14.11.16

NP_001171326.1

EC 1.14.11.16

NP_001171327.1

EC 1.14.11.16

NP_001277296.1

EC 1.14.11.16

NP_075553.2

EC 1.14.11.16

NP_598484.2

EC 1.14.11.16

XP_006538222.1

EC 1.14.11.16

XP_017175829.1

EC 1.14.11.16

XP_017175830.1

EC 1.14.11.16

XP_017175831.1

EC 1.14.11.16

XP_017175832.1

EC 1.14.11.16

XP_017175833.1

EC 1.14.11.16

XP_017175834.1

EC 1.14.11.16

XP_036020189.1

EC 1.14.11.16

XP_036020190.1

EC 1.14.11.16

XP_036020191.1

EC 1.14.11.16

XP_036020192.1

EC 1.14.11.16

XP_036020193.1

EC 1.14.11.16

XP_036020194.1

EC 1.14.11.16

XP_036020195.1

EC 1.14.11.16

XP_036020196.1

EC 1.14.11.16

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)

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
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
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
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
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
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
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
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
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
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
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

NC_000070.7 Reference GRCm39 C57BL/6J

Range

9449085..9669344 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

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
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
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
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
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
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
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
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
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
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
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
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
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
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
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