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

Summary

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

Genomic context

Location:: 8q12.3

Exon count:: 33

Annotation release	Status	Assembly	Chr	Location
109	current	GRCh38.p12 (GCF_000001405.38)	8	NC_000008.11 (61500556..61714640, complement)
105	previous assembly	GRCh37.p13 (GCF_000001405.25)	8	NC_000008.10 (62413115..62627199, complement)

Chromosome 8 - NC_000008.11 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

Go to the top of the page Help

See details

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 page Help

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

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].
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.
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.
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.
this study provides evidence that ASPH is mutated in a distinct form of syndromic ectopia lentis.
Title: Mutations in ASPH cause facial dysmorphism, lens dislocation, anterior-segment abnormalities, and spontaneous filtering blebs, or Traboulsi syndrome.
Data show that junctate (ASPH) is an interacting partner of Orai1-STIM1 complex.
Title: Junctate is a Ca2+-sensing structural component of Orai1 and stromal interaction molecule 1 (STIM1).
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.
Aspartyl-asparaginyl-beta-hydroxylase is an important, positive regulator of trophoblastic cell motility, and it's inhibition in vivo leads to impaired implantation and fetal growth, and alters Notch-signaling mechanisms.
Title: siRNA inhibition of aspartyl-asparaginyl β-hydroxylase expression impairs cell motility, Notch signaling, and fetal growth.
Low expression of AAH in the endochylema and nucleus of trephocyte may play a role in patients with missed abortion.
Title: [Expression of aspartyl-(asparaginyl) beta-hydroxylase in villi in patients with missed abortion].
analysis of aspartyl (asparaginyl) beta-hydroxylase monoclonal antibodies
Title: Monoclonal antibodies against human aspartyl (asparaginyl) beta-hydroxylase developed by DNA immunization.

Submit: New GeneRIF Correction See all GeneRIFs (23)

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

Associated conditions

Description	Tests
Facial dysmorphism, lens dislocation, anterior segment abnormalities, and spontaneous filtering blebs MedGen: C1832167 OMIM: 601552 GeneReviews: Not available	Compare labs

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)

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 BioSystems

Go to the top of the page Help

Cardiac conduction, organism-specific biosystem (from REACTOME)
Cardiac conduction, organism-specific biosystemThe normal sequence of contraction of atria and ventricles of the heart require activation of groups of cardiac cells. The mechanism must elicit rapid changes in heart rate and respond to changes in ...
Ion channel transport, organism-specific biosystem (from REACTOME)
Ion channel transport, organism-specific biosystemIon channels mediate the flow of ions across the plasma membrane of cells. They are integral membrane proteins, typically a multimer of proteins, which, when arranged in the membrane, create a pore f...
Ion homeostasis, organism-specific biosystem (from REACTOME)
Ion homeostasis, organism-specific biosystemIon channel homeostasis in relation to cardiac conduction is described in this section (Couette et al. 2006, Bartos et al. 2015).
Muscle contraction, organism-specific biosystem (from REACTOME)
Muscle contraction, organism-specific biosystemIn this module, the processes by which calcium binding triggers actin - myosin interactions and force generation in smooth and striated muscle tissues are annotated.
Stimuli-sensing channels, organism-specific biosystem (from REACTOME)
Stimuli-sensing channels, organism-specific biosystemIon channels that mediate sensations such as pain, warmth, cold, taste pressure and vision. Channels that mediate these sensations include acid-sensing ion channels (ASICs) (Wang & Xu 2011, Qadri et ...
Transmembrane transport of small molecules, organism-specific biosystem (from REACTOME)
Transmembrane transport of small molecules, organism-specific biosystem
Transmembrane transport of small molecules

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

RH91181 (e-PCR)
- UniSTS:86534

RH48484 (e-PCR)
- UniSTS:76554

RH12812 (e-PCR)
- UniSTS:58644

WI-15471 (e-PCR)
- UniSTS:31020

D8S1685 (e-PCR)
- UniSTS:154191

SHGC-32770 (e-PCR)
- UniSTS:18516

RH91152 (e-PCR)
- UniSTS:90710

SHGC-24147 (e-PCR)
- UniSTS:28511

D8S1514 (e-PCR)
- UniSTS:28512

SHGC-108120 (e-PCR)
- UniSTS:184672

D8S1596 (e-PCR)
- UniSTS:12141

A006X24 (e-PCR)
- UniSTS:17790

SHGC-142338 (e-PCR)
- UniSTS:184702

D8S1359E (e-PCR)
- UniSTS:151173

D8S1374E (e-PCR)
- UniSTS:151187

RH66780 (e-PCR)
- UniSTS:70832

NIB322 (e-PCR)
- UniSTS:69862

RH66163 (e-PCR)
- UniSTS:43751

WI-11767 (e-PCR)
- UniSTS:20973

Homology

Homologs of the ASPH gene: The ASPH gene is conserved in chimpanzee, Rhesus monkey, cow, mouse, rat, and chicken.
Orthologs from Annotation Pipeline: 215 organisms have orthologs with human gene ASPH
Orthologs

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	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
face morphogenesis	IEA Inferred from Electronic Annotation more info
ion transmembrane transport	TAS Traceable Author Statement more info
limb morphogenesis	IEA Inferred from Electronic Annotation more info
muscle contraction	TAS Traceable Author Statement more info	PubMed
negative regulation of cell proliferation	IEA Inferred from Electronic Annotation more info
pattern specification process	IEA Inferred from Electronic Annotation more info
peptidyl-aspartic acid hydroxylation	IEA Inferred from Electronic Annotation more info
positive regulation of proteolysis	IDA Inferred from Direct Assay more info	PubMed
regulation of cardiac conduction	TAS Traceable Author Statement more info
regulation of protein depolymerization	IEA Inferred from Electronic Annotation more info
regulation of protein stability	IEA Inferred from Electronic Annotation more info
roof of mouth development	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
cortical endoplasmic reticulum	IDA Inferred from Direct Assay 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

EC 1.14.11.16

NP_001158223.1

EC 1.14.11.16

NP_001158224.1

EC 1.14.11.16

NP_001158225.1

EC 1.14.11.16

NP_001158226.1

EC 1.14.11.16

NP_001158227.1

EC 1.14.11.16

NP_001158228.1

EC 1.14.11.16

NP_004309.2

EC 1.14.11.16

NP_064549.1

EC 1.14.11.16

NP_115855.1

EC 1.14.11.16

NP_115856.1

EC 1.14.11.16

NP_115857.1

EC 1.14.11.16

XP_005251292.1

EC 1.14.11.16

XP_005251293.1

EC 1.14.11.16

XP_005251296.1

EC 1.14.11.16

XP_005251297.1

EC 1.14.11.16

XP_005251299.1

EC 1.14.11.16

XP_005251300.1

EC 1.14.11.16

XP_005251301.1

EC 1.14.11.16

XP_005251303.1

EC 1.14.11.16

XP_005251304.1

EC 1.14.11.16

XP_016868908.1

EC 1.14.11.16

XP_016868909.1

EC 1.14.11.16

XP_016868910.1

EC 1.14.11.16

XP_016868911.1

EC 1.14.11.16

XP_016868913.1

EC 1.14.11.16

XP_016868914.1

EC 1.14.11.16

XP_016868915.1

EC 1.14.11.16

XP_016868916.1

EC 1.14.11.16

XP_016868917.1

EC 1.14.11.16

XP_016868918.1

EC 1.14.11.16

XP_016868919.1

EC 1.14.11.16

XP_016868920.1

EC 1.14.11.16

XP_016868921.1

EC 1.14.11.16

XP_016868922.1

EC 1.14.11.16

XP_016868923.1

EC 1.14.11.16

XP_016868924.1

EC 1.14.11.16

XP_016868926.1

EC 1.14.11.16

XP_016868927.1

EC 1.14.11.16

XP_016868928.1

EC 1.14.11.16

XP_016868929.1

EC 1.14.11.16

XP_016868933.1

EC 1.14.11.16

XP_016868934.1

EC 1.14.11.16

XP_016868935.1

EC 1.14.11.16

XP_016868936.1

EC 1.14.11.16

XP_024302923.1

EC 1.14.11.16

XP_024302924.1

EC 1.14.11.16

XP_024302925.1

EC 1.14.11.16

XP_024302926.1

EC 1.14.11.16

XP_024302927.1

EC 1.14.11.16

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

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

NG_013210.1 RefSeqGene

Range

5001..219085

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001164750.1 → 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
NM_001164751.1 → 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
NM_001164752.1 → 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
NM_001164753.1 → 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
NM_001164754.1 → 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
NM_001164755.1 → 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
NM_001164756.1 → 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, CR996516, 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
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, ENST00000379454.8

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
NM_020164.4 → 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
NM_032466.3 → 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
NM_032467.3 → 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
NM_032468.4 → 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 Annotation Release 109

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

Reference GRCh38.p12 Primary Assembly

Genomic

NC_000008.11 Reference GRCh38.p12 Primary Assembly

Range

61500556..61714640 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

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
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]
XM_017013438.1 → XP_016868927.1 aspartyl/asparaginyl beta-hydroxylase isoform X26
XM_017013432.1 → XP_016868921.1 aspartyl/asparaginyl beta-hydroxylase isoform X15
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
XM_017013430.1 → XP_016868919.1 aspartyl/asparaginyl beta-hydroxylase isoform X13
XM_017013434.1 → XP_016868923.1 aspartyl/asparaginyl beta-hydroxylase isoform X18
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
XM_017013425.1 → XP_016868914.1 aspartyl/asparaginyl beta-hydroxylase isoform X6
XM_017013421.1 → XP_016868910.1 aspartyl/asparaginyl beta-hydroxylase isoform X3
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
XM_017013420.1 → XP_016868909.1 aspartyl/asparaginyl beta-hydroxylase isoform X2
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
XM_017013419.1 → XP_016868908.1 aspartyl/asparaginyl beta-hydroxylase isoform X1
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
XM_017013437.2 → XP_016868926.1 aspartyl/asparaginyl beta-hydroxylase isoform X21
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
XM_017013428.2 → XP_016868917.1 aspartyl/asparaginyl beta-hydroxylase isoform X11
XM_017013429.2 → XP_016868918.1 aspartyl/asparaginyl beta-hydroxylase isoform X12
XM_017013424.2 → XP_016868913.1 aspartyl/asparaginyl beta-hydroxylase isoform X5
XM_017013422.2 → XP_016868911.1 aspartyl/asparaginyl beta-hydroxylase isoform X4
XM_017013440.1 → XP_016868929.1 aspartyl/asparaginyl beta-hydroxylase isoform X28
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
XM_017013435.1 → XP_016868924.1 aspartyl/asparaginyl beta-hydroxylase isoform X19
XM_017013427.1 → XP_016868916.1 aspartyl/asparaginyl beta-hydroxylase isoform X10
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
XM_017013426.1 → XP_016868915.1 aspartyl/asparaginyl beta-hydroxylase isoform X9
XM_017013444.1 → XP_016868933.1 aspartyl/asparaginyl beta-hydroxylase isoform X32
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]
XM_017013439.1 → XP_016868928.1 aspartyl/asparaginyl beta-hydroxylase isoform X27
XM_017013433.1 → XP_016868922.1 aspartyl/asparaginyl beta-hydroxylase isoform X16
XM_017013431.1 → XP_016868920.1 aspartyl/asparaginyl beta-hydroxylase isoform X14
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
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
XM_017013447.1 → XP_016868936.1 aspartyl/asparaginyl beta-hydroxylase isoform X37

Related

ENSP00000427877.1, ENST00000518306.5
XM_017013446.1 → XP_016868935.1 aspartyl/asparaginyl beta-hydroxylase isoform X36
XM_017013445.1 → XP_016868934.1 aspartyl/asparaginyl beta-hydroxylase isoform X35
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