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Protein

Aspartyl/asparaginyl beta-hydroxylase

Gene

ASPH

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Isoform 1: specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins.1 Publication
Isoform 8: membrane-bound Ca2+-sensing protein, which is a structural component of the ER-plasma membrane junctions. Isoform 8 regulates the activity of Ca(+2) released-activated Ca(+2) (CRAC) channels in T-cells.1 Publication

Catalytic activityi

Peptide L-aspartate + 2-oxoglutarate + O2 = peptide 3-hydroxy-L-aspartate + succinate + CO2.1 Publication

Cofactori

Fe cationBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei625 – 62512-oxoglutarate1 Publication
Binding sitei668 – 66812-oxoglutarate1 Publication
Metal bindingi679 – 6791IronCurated
Metal bindingi725 – 7251IronCurated
Binding sitei735 – 73512-oxoglutarate1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi90 – 102131 PublicationAdd
BLAST

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • electron carrier activity Source: UniProtKB
  • ion channel binding Source: BHF-UCL
  • peptide-aspartate beta-dioxygenase activity Source: ProtInc
  • structural constituent of muscle Source: ProtInc
  • structural molecule activity Source: ProtInc

GO - Biological processi

  • activation of cysteine-type endopeptidase activity Source: BHF-UCL
  • activation of store-operated calcium channel activity Source: UniProtKB
  • calcium ion transmembrane transport Source: UniProtKB
  • cellular response to calcium ion Source: UniProtKB
  • detection of calcium ion Source: BHF-UCL
  • face morphogenesis Source: Ensembl
  • limb morphogenesis Source: Ensembl
  • muscle contraction Source: ProtInc
  • negative regulation of cell proliferation Source: Ensembl
  • palate development Source: Ensembl
  • pattern specification process Source: Ensembl
  • peptidyl-aspartic acid hydroxylation Source: Ensembl
  • positive regulation of calcium ion transport into cytosol Source: UniProtKB
  • positive regulation of intracellular protein transport Source: UniProtKB
  • positive regulation of proteolysis Source: BHF-UCL
  • positive regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: BHF-UCL
  • regulation of cell communication by electrical coupling Source: BHF-UCL
  • regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity Source: UniProtKB
  • regulation of protein depolymerization Source: Ensembl
  • regulation of protein stability Source: Ensembl
  • regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
  • regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
  • response to ATP Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Ligandi

Calcium, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartyl/asparaginyl beta-hydroxylase (EC:1.14.11.161 Publication)
Alternative name(s):
Aspartate beta-hydroxylase
Short name:
ASP beta-hydroxylase
Peptide-aspartate beta-dioxygenase
Gene namesi
Name:ASPH
Synonyms:BAH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:757. ASPH.

Subcellular locationi

Isoform 1 :
Isoform 4 :
Isoform 8 :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5353CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei54 – 7421Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini75 – 758684LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • calcium channel complex Source: BHF-UCL
  • cortical endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum Source: HPA
  • endoplasmic reticulum membrane Source: UniProtKB
  • integral component of endoplasmic reticulum membrane Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • junctional sarcoplasmic reticulum membrane Source: BHF-UCL
  • plasma membrane Source: UniProtKB
  • sarcoplasmic reticulum lumen Source: BHF-UCL
  • sarcoplasmic reticulum membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Sarcoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

Facial dysmorphism, lens dislocation, anterior segment abnormalities, and spontaneous filtering blebs (FDLAB)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA syndrome characterized by dislocated crystalline lenses and anterior segment abnormalities in association with a distinctive facies involving flat cheeks and a beaked nose. Some affected individuals develop highly unusual non-traumatic conjunctival cysts (filtering blebs).

See also OMIM:601552
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti735 – 7351R → W in FDLAB. 1 Publication
VAR_071821

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi91 – 933DAD → AAA: Increase in cytoplasmic Ca(2+) via activation of endogenous CRAC channels. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi601552. phenotype.
PharmGKBiPA25056.

Chemistry

DrugBankiDB00128. L-Aspartic Acid.
DB00139. Succinic acid.

Polymorphism and mutation databases

BioMutaiASPH.
DMDMi145559444.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 758758Aspartyl/asparaginyl beta-hydroxylasePRO_0000064706Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141Phosphoserine1 Publication
Glycosylationi452 – 4521N-linked (GlcNAc...)
Disulfide bondi641 ↔ 6481 Publication
Glycosylationi706 – 7061N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ12797.
PaxDbiQ12797.
PRIDEiQ12797.

PTM databases

PhosphoSiteiQ12797.

Expressioni

Tissue specificityi

Isoform 1 is detected in all tissues tested. Isoform 8 is mainly expressed in pancreas, heart, brain, kidney and liver. Isoform 8 is expressed in kidney (at protein level).1 Publication

Gene expression databases

BgeeiQ12797.
CleanExiHS_ASPH.
ExpressionAtlasiQ12797. baseline and differential.
GenevisibleiQ12797. HS.

Organism-specific databases

HPAiHPA055161.
HPA059303.

Interactioni

Subunit structurei

Monomer (By similarity). Isoform 8 interacts with ORAI1 and STIM1. Isoform 4 interacts with CASQ2.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ASNA1O436813EBI-2967294,EBI-2515857

Protein-protein interaction databases

BioGridi106936. 36 interactions.
IntActiQ12797. 7 interactions.
STRINGi9606.ENSP00000368767.

Structurei

Secondary structure

1
758
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi574 – 5763Combined sources
Helixi578 – 5814Combined sources
Helixi584 – 5929Combined sources
Helixi594 – 60411Combined sources
Turni607 – 6104Combined sources
Beta strandi620 – 6234Combined sources
Beta strandi625 – 6328Combined sources
Helixi638 – 6436Combined sources
Helixi645 – 6517Combined sources
Helixi655 – 6584Combined sources
Beta strandi664 – 6707Combined sources
Beta strandi674 – 6796Combined sources
Beta strandi686 – 6949Combined sources
Beta strandi697 – 7048Combined sources
Beta strandi707 – 7093Combined sources
Beta strandi716 – 7194Combined sources
Beta strandi725 – 7295Combined sources
Beta strandi731 – 7333Combined sources
Beta strandi735 – 7439Combined sources
Helixi749 – 7546Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RCQX-ray2.05A562-758[»]
ProteinModelPortaliQ12797.
SMRiQ12797. Positions 562-758.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12797.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati341 – 37434TPR 1Add
BLAST
Repeati454 – 48734TPR 2Add
BLAST
Repeati489 – 52133TPR 3Add
BLAST
Repeati525 – 55733TPR 4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni688 – 69032-oxoglutarate binding1 Publication

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi9 – 2921Ser-richAdd
BLAST
Compositional biasi111 – 312202Glu-richAdd
BLAST
Compositional biasi323 – 33210Poly-Lys

Sequence similaritiesi

Contains 4 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal-anchor, TPR repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG3555.
GeneTreeiENSGT00530000063281.
HOGENOMiHOG000231622.
HOVERGENiHBG004290.
InParanoidiQ12797.
KOiK00476.
OMAiRNENACK.
OrthoDBiEOG715Q44.
PhylomeDBiQ12797.
TreeFamiTF312799.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
2.60.120.330. 1 hit.
InterProiIPR007943. Asp-B-hydro/Triadin_dom.
IPR007803. Asp_Arg_Pro-Hydrxlase.
IPR027443. IPNS-like.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF05279. Asp-B-Hydro_N. 1 hit.
PF05118. Asp_Arg_Hydrox. 1 hit.
[Graphical view]
PROSITEiPS50005. TPR. 2 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequences (10)i

Sequence statusi: Complete.

This entry describes 10 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Comment: 3 functionally distinct proteins are produced by alternative splicing: Aspartyl/asparaginyl beta-hydroxylase, Junctin and Junctate. Additional isoforms are produced by alternative splicing.1 Publication

Isoform 1 (identifier: Q12797-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAQRKNAKSS GNSSSSGSGS GSTSAGSSSP GARRETKHGG HKNGRKGGLS
60 70 80 90 100
GTSFFTWFMV IALLGVWTSV AVVWFDLVDY EEVLGKLGIY DADGDGDFDV
110 120 130 140 150
DDAKVLLGLK ERSTSEPAVP PEEAEPHTEP EEQVPVEAEP QNIEDEAKEQ
160 170 180 190 200
IQSLLHEMVH AEHVEGEDLQ QEDGPTGEPQ QEDDEFLMAT DVDDRFETLE
210 220 230 240 250
PEVSHEETEH SYHVEETVSQ DCNQDMEEMM SEQENPDSSE PVVEDERLHH
260 270 280 290 300
DTDDVTYQVY EEQAVYEPLE NEGIEITEVT APPEDNPVED SQVIVEEVSI
310 320 330 340 350
FPVEEQQEVP PETNRKTDDP EQKAKVKKKK PKLLNKFDKT IKAELDAAEK
360 370 380 390 400
LRKRGKIEEA VNAFKELVRK YPQSPRARYG KAQCEDDLAE KRRSNEVLRG
410 420 430 440 450
AIETYQEVAS LPDVPADLLK LSLKRRSDRQ QFLGHMRGSL LTLQRLVQLF
460 470 480 490 500
PNDTSLKNDL GVGYLLIGDN DNAKKVYEEV LSVTPNDGFA KVHYGFILKA
510 520 530 540 550
QNKIAESIPY LKEGIESGDP GTDDGRFYFH LGDAMQRVGN KEAYKWYELG
560 570 580 590 600
HKRGHFASVW QRSLYNVNGL KAQPWWTPKE TGYTELVKSL ERNWKLIRDE
610 620 630 640 650
GLAVMDKAKG LFLPEDENLR EKGDWSQFTL WQQGRRNENA CKGAPKTCTL
660 670 680 690 700
LEKFPETTGC RRGQIKYSIM HPGTHVWPHT GPTNCRLRMH LGLVIPKEGC
710 720 730 740 750
KIRCANETKT WEEGKVLIFD DSFEHEVWQD ASSFRLIFIV DVWHPELTPQ

QRRSLPAI
Length:758
Mass (Da):85,863
Last modified:April 17, 2007 - v3
Checksum:i4AE56D1D8DF0AF0C
GO
Isoform 2 (identifier: Q12797-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     312-313: ET → DT
     314-758: Missing.

Show »
Length:313
Mass (Da):34,646
Checksum:i7885A18B81CD6D0D
GO
Isoform 3 (identifier: Q12797-3) [UniParc]FASTAAdd to basket

Also known as: Junctin-1, Cardiac junctin

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MAQRKNAKSSGNSSSSGSGSGSTSAGSSSPGARR → MAEDK
     84-84: L → LAKAKDFRYNLSEVLQ
     108-239: GLKERSTSEP...MSEQENPDSS → EGPSGVAKRK...TKGNTQKRNG
     240-758: Missing.

Note: Glycosylated on Asn-64.
Show »
Length:225
Mass (Da):25,560
Checksum:i27D331DD6D88E0D3
GO
Isoform 4 (identifier: Q12797-4) [UniParc]FASTAAdd to basket

Also known as: Junctin-2, Junctin

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MAQRKNAKSSGNSSSSGSGSGSTSAGSSSPGARR → MAEDK
     108-239: GLKERSTSEP...MSEQENPDSS → EGPSGVAKRK...TKGNTQKRNG
     240-758: Missing.

Show »
Length:210
Mass (Da):23,796
Checksum:i8E7C39D69F2B22C7
GO
Isoform 5 (identifier: Q12797-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MAQRKNAKSSGNSSSSGSGSGSTSAGSSSPGARR → MAEDK
     84-84: L → LAKAKDFRYNLSEVLQ
     264-264: Missing.
     312-313: ET → DT
     314-758: Missing.

Show »
Length:298
Mass (Da):33,744
Checksum:iB28D921E5021348B
GO
Isoform 10 (identifier: Q12797-10) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MAQRKNAKSSGNSSSSGSGSGSTSAGSSSPGARR → MAEDK

Show »
Length:729
Mass (Da):83,268
Checksum:iEA17281494828D62
GO
Isoform 6 (identifier: Q12797-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     164-206: Missing.
     312-313: ET → DT
     314-758: Missing.

Show »
Length:270
Mass (Da):29,757
Checksum:i8551773C7272202A
GO
Isoform 7 (identifier: Q12797-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     84-84: L → LAKAKDFRYNLSEVLQ
     110-188: KERSTSEPAV...PQQEDDEFLM → TKDGSNENID...TCVILDLHNQ
     189-758: Missing.

Show »
Length:203
Mass (Da):21,963
Checksum:i3EC728B1E417091C
GO
Isoform 8 (identifier: Q12797-8) [UniParc]FASTAAdd to basket

Also known as: Junctate

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MAQRKNAKSSGNSSSSGSGSGSTSAGSSSPGARR → MAEDK
     84-84: L → LAKAKDFRYNLSEVLQ
     312-313: ET → DT
     314-758: Missing.

Show »
Length:299
Mass (Da):33,815
Checksum:i658F88C34EC2CA37
GO
Isoform 9 (identifier: Q12797-9) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MAQRKNAKSSGNSSSSGSGSGSTSAGSSSPGARR → MAEDK
     84-84: L → LAKAKDFRYNLSEVLQ
     164-206: Missing.
     312-313: ET → DT
     314-758: Missing.

Show »
Length:256
Mass (Da):28,926
Checksum:i8C892EC3D1AE1BCC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti519 – 5191D → N in BAG65166 (PubMed:14702039).Curated
Sequence conflicti565 – 5651Y → I in AAA82108 (PubMed:7821814).Curated
Sequence conflicti575 – 5773WWT → CG in AAA82108 (PubMed:7821814).Curated
Sequence conflicti585 – 5851E → Q in AAA82108 (PubMed:7821814).Curated
Sequence conflicti599 – 5991D → Y in BAG65166 (PubMed:14702039).Curated
Sequence conflicti709 – 7091K → R in AAB50779 (PubMed:8823296).Curated
Sequence conflicti734 – 7341F → L in BAG65166 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti354 – 3541R → M.
Corresponds to variant rs6995412 [ dbSNP | Ensembl ].
VAR_053781
Natural varianti735 – 7351R → W in FDLAB. 1 Publication
VAR_071821

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3434MAQRK…PGARR → MAEDK in isoform 3, isoform 4, isoform 5, isoform 8, isoform 9 and isoform 10. 5 PublicationsVSP_039165Add
BLAST
Alternative sequencei84 – 841L → LAKAKDFRYNLSEVLQ in isoform 3, isoform 5, isoform 7, isoform 8 and isoform 9. 5 PublicationsVSP_039166
Alternative sequencei108 – 239132GLKER…NPDSS → EGPSGVAKRKTKAKVKELTK EELKKEKEKPESRKESKNEE RKKGKKEDVRKDKKIADADL SRKESPKGKKDREKEKVDLE KSAKTKENRKKSTNMKDVSS KMASRDKDDRKESRSSTRYA HLTKGNTQKRNG in isoform 3 and isoform 4. 2 PublicationsVSP_039167Add
BLAST
Alternative sequencei110 – 18879KERST…DEFLM → TKDGSNENIDSLEEVLNILA EESSDWFYGFLSFLYDIMTP FEMLEEEEEESETADGVDGT SQNEGVQGKTCVILDLHNQ in isoform 7. 1 PublicationVSP_044235Add
BLAST
Alternative sequencei164 – 20643Missing in isoform 6 and isoform 9. 2 PublicationsVSP_044236Add
BLAST
Alternative sequencei189 – 758570Missing in isoform 7. 1 PublicationVSP_044237Add
BLAST
Alternative sequencei240 – 758519Missing in isoform 3 and isoform 4. 2 PublicationsVSP_039168Add
BLAST
Alternative sequencei264 – 2641Missing in isoform 5. 1 PublicationVSP_044238
Alternative sequencei312 – 3132ET → DT in isoform 2, isoform 5, isoform 6, isoform 8 and isoform 9. 4 PublicationsVSP_039169
Alternative sequencei314 – 758445Missing in isoform 2, isoform 5, isoform 6, isoform 8 and isoform 9. 4 PublicationsVSP_039170Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03109 mRNA. Translation: AAA82108.1.
S83325 mRNA. Translation: AAB50779.1.
AF224468 mRNA. Translation: AAF82246.1.
AF224469 mRNA. Translation: AAF82247.1.
AF289489 mRNA. Translation: AAG40811.1.
AF306765 mRNA. Translation: AAG42257.1.
AF184241 mRNA. Translation: AAG16983.1.
AK295528 mRNA. Translation: BAG58441.1.
AK304314 mRNA. Translation: BAG65166.1.
AC067881 Genomic DNA. No translation available.
AC090094 Genomic DNA. No translation available.
CH471068 Genomic DNA. Translation: EAW86841.1.
CH471068 Genomic DNA. Translation: EAW86840.1.
CH471068 Genomic DNA. Translation: EAW86847.1.
CH471068 Genomic DNA. Translation: EAW86848.1.
CH471068 Genomic DNA. Translation: EAW86849.1.
BC025236 mRNA. Translation: AAH25236.1.
BC066929 mRNA. Translation: AAH66929.1.
BC142967 mRNA. Translation: AAI42968.1.
BC144362 mRNA. Translation: AAI44363.1.
CCDSiCCDS34898.1. [Q12797-1]
CCDS34899.1. [Q12797-4]
CCDS34900.1. [Q12797-3]
CCDS43742.1. [Q12797-2]
CCDS47866.1. [Q12797-8]
CCDS55234.1. [Q12797-10]
CCDS55235.1. [Q12797-9]
CCDS55236.1. [Q12797-5]
CCDS55237.1. [Q12797-6]
CCDS55238.1. [Q12797-7]
PIRiI38423.
RefSeqiNP_001158222.1. NM_001164750.1. [Q12797-10]
NP_001158223.1. NM_001164751.1. [Q12797-5]
NP_001158225.1. NM_001164753.1. [Q12797-9]
NP_001158227.1. NM_001164755.1. [Q12797-6]
NP_001158228.1. NM_001164756.1. [Q12797-7]
NP_004309.2. NM_004318.3. [Q12797-1]
NP_064549.1. NM_020164.4. [Q12797-3]
NP_115855.1. NM_032466.3. [Q12797-2]
NP_115856.1. NM_032467.3. [Q12797-4]
NP_115857.1. NM_032468.4. [Q12797-8]
UniGeneiHs.332422.

Genome annotation databases

EnsembliENST00000356457; ENSP00000348841; ENSG00000198363. [Q12797-2]
ENST00000379449; ENSP00000368762; ENSG00000198363. [Q12797-7]
ENST00000379454; ENSP00000368767; ENSG00000198363.
ENST00000389204; ENSP00000373856; ENSG00000198363. [Q12797-3]
ENST00000517847; ENSP00000429954; ENSG00000198363. [Q12797-8]
ENST00000517903; ENSP00000430245; ENSG00000198363. [Q12797-5]
ENST00000518068; ENSP00000429286; ENSG00000198363. [Q12797-6]
ENST00000522603; ENSP00000436188; ENSG00000198363. [Q12797-4]
ENST00000522835; ENSP00000429160; ENSG00000198363. [Q12797-9]
ENST00000541428; ENSP00000437864; ENSG00000198363. [Q12797-10]
GeneIDi444.
KEGGihsa:444.
UCSCiuc003xuj.3. human. [Q12797-1]
uc003xul.3. human. [Q12797-8]
uc003xum.3. human. [Q12797-2]
uc003xun.3. human. [Q12797-6]
uc003xur.3. human. [Q12797-7]
uc011lei.2. human. [Q12797-5]
uc011lej.2. human. [Q12797-9]
uc011lel.2. human. [Q12797-3]
uc011lem.2. human. [Q12797-4]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03109 mRNA. Translation: AAA82108.1.
S83325 mRNA. Translation: AAB50779.1.
AF224468 mRNA. Translation: AAF82246.1.
AF224469 mRNA. Translation: AAF82247.1.
AF289489 mRNA. Translation: AAG40811.1.
AF306765 mRNA. Translation: AAG42257.1.
AF184241 mRNA. Translation: AAG16983.1.
AK295528 mRNA. Translation: BAG58441.1.
AK304314 mRNA. Translation: BAG65166.1.
AC067881 Genomic DNA. No translation available.
AC090094 Genomic DNA. No translation available.
CH471068 Genomic DNA. Translation: EAW86841.1.
CH471068 Genomic DNA. Translation: EAW86840.1.
CH471068 Genomic DNA. Translation: EAW86847.1.
CH471068 Genomic DNA. Translation: EAW86848.1.
CH471068 Genomic DNA. Translation: EAW86849.1.
BC025236 mRNA. Translation: AAH25236.1.
BC066929 mRNA. Translation: AAH66929.1.
BC142967 mRNA. Translation: AAI42968.1.
BC144362 mRNA. Translation: AAI44363.1.
CCDSiCCDS34898.1. [Q12797-1]
CCDS34899.1. [Q12797-4]
CCDS34900.1. [Q12797-3]
CCDS43742.1. [Q12797-2]
CCDS47866.1. [Q12797-8]
CCDS55234.1. [Q12797-10]
CCDS55235.1. [Q12797-9]
CCDS55236.1. [Q12797-5]
CCDS55237.1. [Q12797-6]
CCDS55238.1. [Q12797-7]
PIRiI38423.
RefSeqiNP_001158222.1. NM_001164750.1. [Q12797-10]
NP_001158223.1. NM_001164751.1. [Q12797-5]
NP_001158225.1. NM_001164753.1. [Q12797-9]
NP_001158227.1. NM_001164755.1. [Q12797-6]
NP_001158228.1. NM_001164756.1. [Q12797-7]
NP_004309.2. NM_004318.3. [Q12797-1]
NP_064549.1. NM_020164.4. [Q12797-3]
NP_115855.1. NM_032466.3. [Q12797-2]
NP_115856.1. NM_032467.3. [Q12797-4]
NP_115857.1. NM_032468.4. [Q12797-8]
UniGeneiHs.332422.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RCQX-ray2.05A562-758[»]
ProteinModelPortaliQ12797.
SMRiQ12797. Positions 562-758.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106936. 36 interactions.
IntActiQ12797. 7 interactions.
STRINGi9606.ENSP00000368767.

Chemistry

DrugBankiDB00128. L-Aspartic Acid.
DB00139. Succinic acid.

PTM databases

PhosphoSiteiQ12797.

Polymorphism and mutation databases

BioMutaiASPH.
DMDMi145559444.

Proteomic databases

MaxQBiQ12797.
PaxDbiQ12797.
PRIDEiQ12797.

Protocols and materials databases

DNASUi444.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000356457; ENSP00000348841; ENSG00000198363. [Q12797-2]
ENST00000379449; ENSP00000368762; ENSG00000198363. [Q12797-7]
ENST00000379454; ENSP00000368767; ENSG00000198363.
ENST00000389204; ENSP00000373856; ENSG00000198363. [Q12797-3]
ENST00000517847; ENSP00000429954; ENSG00000198363. [Q12797-8]
ENST00000517903; ENSP00000430245; ENSG00000198363. [Q12797-5]
ENST00000518068; ENSP00000429286; ENSG00000198363. [Q12797-6]
ENST00000522603; ENSP00000436188; ENSG00000198363. [Q12797-4]
ENST00000522835; ENSP00000429160; ENSG00000198363. [Q12797-9]
ENST00000541428; ENSP00000437864; ENSG00000198363. [Q12797-10]
GeneIDi444.
KEGGihsa:444.
UCSCiuc003xuj.3. human. [Q12797-1]
uc003xul.3. human. [Q12797-8]
uc003xum.3. human. [Q12797-2]
uc003xun.3. human. [Q12797-6]
uc003xur.3. human. [Q12797-7]
uc011lei.2. human. [Q12797-5]
uc011lej.2. human. [Q12797-9]
uc011lel.2. human. [Q12797-3]
uc011lem.2. human. [Q12797-4]

Organism-specific databases

CTDi444.
GeneCardsiGC08M062465.
HGNCiHGNC:757. ASPH.
HPAiHPA055161.
HPA059303.
MIMi600582. gene.
601552. phenotype.
neXtProtiNX_Q12797.
PharmGKBiPA25056.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG3555.
GeneTreeiENSGT00530000063281.
HOGENOMiHOG000231622.
HOVERGENiHBG004290.
InParanoidiQ12797.
KOiK00476.
OMAiRNENACK.
OrthoDBiEOG715Q44.
PhylomeDBiQ12797.
TreeFamiTF312799.

Miscellaneous databases

ChiTaRSiASPH. human.
EvolutionaryTraceiQ12797.
GeneWikiiASPH.
GenomeRNAii444.
NextBioi1859.
PROiQ12797.
SOURCEiSearch...

Gene expression databases

BgeeiQ12797.
CleanExiHS_ASPH.
ExpressionAtlasiQ12797. baseline and differential.
GenevisibleiQ12797. HS.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
2.60.120.330. 1 hit.
InterProiIPR007943. Asp-B-hydro/Triadin_dom.
IPR007803. Asp_Arg_Pro-Hydrxlase.
IPR027443. IPNS-like.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF05279. Asp-B-Hydro_N. 1 hit.
PF05118. Asp_Arg_Hydrox. 1 hit.
[Graphical view]
PROSITEiPS50005. TPR. 2 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the human gene encoding aspartyl beta-hydroxylase."
    Korioth F., Gieffers C., Frey J.
    Gene 150:395-399(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Overexpression of human aspartyl(asparaginyl)beta-hydroxylase in hepatocellular carcinoma and cholangiocarcinoma."
    Lavaissiere L., Jia S., Nishiyama M., de la Monte S., Stern A.M., Wands J.R., Friedman P.A.
    J. Clin. Invest. 98:1313-1323(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "cDNA cloning and characterization of human cardiac junctin."
    Lim K.Y., Hong C.-S., Kim D.H.
    Gene 255:35-42(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
    Tissue: Heart.
  4. "Aspartyl beta -hydroxylase (Asph) and an evolutionarily conserved isoform of Asph missing the catalytic domain share exons with junctin."
    Dinchuk J.E., Henderson N.L., Burn T.C., Huber R., Ho S.P., Link J., O'Neil K.T., Focht R.J., Scully M.S., Hollis J.M., Hollis G.F., Friedman P.A.
    J. Biol. Chem. 275:39543-39554(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Liver.
  5. "Molecular cloning, expression, functional characterization, chromosomal localization, and gene structure of junctate, a novel integral calcium binding protein of sarco(endo)plasmic reticulum membrane."
    Treves S., Feriotto G., Moccagatta L., Gambari R., Zorzato F.
    J. Biol. Chem. 275:39555-39568(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8), CALCIUM-BINDING, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Tissue: Muscle.
  6. "Molecular cloning of junctin from human and developing rabbit heart."
    Wetzel G.T., Ding S., Chen F.
    Mol. Genet. Metab. 69:252-258(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Tissue: Heart.
  7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 9 AND 10).
    Tissue: Hippocampus and Trachea.
  8. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5; 6 AND 7).
    Tissue: Brain and Pancreatic carcinoma.
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Junctate is a Ca2+-sensing structural component of Orai1 and stromal interaction molecule 1 (STIM1)."
    Srikanth S., Jew M., Kim K.D., Yee M.K., Abramson J., Gwack Y.
    Proc. Natl. Acad. Sci. U.S.A. 109:8682-8687(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CALCIUM-BINDING DOMAIN, INTERACTION WITH ORAI1 AND STIM1 (ISOFORM 8), MUTAGENESIS OF 91-ASP--ASP-93, SUBCELLULAR LOCATION.
  14. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-452 (ISOFORM 1), GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64 (ISOFORM 3).
    Tissue: Liver.
  15. "Calsequestrin mutant D307H exhibits depressed binding to its protein targets and a depressed response to calcium."
    Houle T.D., Ram M.L., Cala S.E.
    Cardiovasc. Res. 64:227-233(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CASQ2 (ISOFORM 4), SUBCELLULAR LOCATION.
  16. "Absence of post-translational aspartyl beta-hydroxylation of epidermal growth factor domains in mice leads to developmental defects and an increased incidence of intestinal neoplasia."
    Dinchuk J.E., Focht R.J., Kelley J.A., Henderson N.L., Zolotarjova N.I., Wynn R., Neff N.T., Link J., Huber R.M., Burn T.C., Rupar M.J., Cunningham M.R., Selling B.H., Ma J., Stern A.A., Hollis G.F., Stein R.B., Friedman P.A.
    J. Biol. Chem. 277:12970-12977(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 1), CATALYTIC ACTIVITY.
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. "Crystal structure of human aspartate beta-hydroxylase isoform A."
    Structural genomics consortium (SGC)
    Submitted (MAY-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 562-758 IN COMPLEX WITH N-OXALYOLGLYCINE AND ZINC IONS, DISULFIDE BOND.
  19. "Mutations in ASPH cause facial dysmorphism, lens dislocation, anterior-segment abnormalities, and spontaneous filtering blebs, or Traboulsi syndrome."
    Patel N., Khan A.O., Mansour A., Mohamed J.Y., Al-Assiri A., Haddad R., Jia X., Xiong Y., Megarbane A., Traboulsi E.I., Alkuraya F.S.
    Am. J. Hum. Genet. 94:755-759(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN FDLAB, VARIANT FDLAB TRP-735.

Entry informationi

Entry nameiASPH_HUMAN
AccessioniPrimary (citable) accession number: Q12797
Secondary accession number(s): A6NDF4
, A6NHI2, B4DIC9, B4E2K4, B7ZM95, E5RGP5, F5H667, Q6NXR7, Q8TB28, Q9H291, Q9H2C4, Q9NRI0, Q9NRI1, Q9Y4J0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 17, 2007
Last modified: July 22, 2015
This is version 153 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.