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Q12797 (ASPH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aspartyl/asparaginyl beta-hydroxylase

EC=1.14.11.16
Alternative name(s):
Aspartate beta-hydroxylase
Short name=ASP beta-hydroxylase
Peptide-aspartate beta-dioxygenase
Gene names
Name:ASPH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length758 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Isoform 1:specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins. Ref.13

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. Ref.13

Catalytic activity

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

Cofactor

Iron By similarity.

Subunit structure

Monomer By similarity. Isoform 8 interacts with ORAI1 and STIM1. Ref.13

Subcellular location

Isoform 1: Endoplasmic reticulum membrane; Single-pass type II membrane protein Ref.5.

Isoform 8: Endoplasmic reticulum membrane; Single-pass type II membrane protein Ref.5.

Tissue specificity

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). Ref.5

Sequence similarities

Belongs to the aspartyl/asparaginyl beta-hydroxylase family.

Contains 4 TPR repeats.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal-anchor
TPR repeat
Transmembrane
Transmembrane helix
   LigandCalcium
Iron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of cysteine-type endopeptidase activity

Inferred from direct assay PubMed 18387192. Source: BHF-UCL

activation of store-operated calcium channel activity

Inferred from direct assay Ref.13. Source: UniProtKB

calcium ion transmembrane transport

Inferred from direct assay PubMed 21062895. Source: UniProtKB

cellular response to calcium ion

Inferred from direct assay PubMed 21062895. Source: UniProtKB

detection of calcium ion

Traceable author statement PubMed 22123818. Source: BHF-UCL

face morphogenesis

Inferred from electronic annotation. Source: Ensembl

limb morphogenesis

Inferred from electronic annotation. Source: Ensembl

muscle contraction

Traceable author statement Ref.3. Source: ProtInc

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

palate development

Inferred from electronic annotation. Source: Ensembl

pattern specification process

Inferred from electronic annotation. Source: Ensembl

peptidyl-aspartic acid hydroxylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of calcium ion transport into cytosol

Inferred from direct assay PubMed 21062895. Source: UniProtKB

positive regulation of intracellular protein transport

Inferred from direct assay Ref.13. Source: UniProtKB

positive regulation of proteolysis

Inferred from direct assay PubMed 18387192. Source: BHF-UCL

positive regulation of ryanodine-sensitive calcium-release channel activity

Traceable author statement PubMed 15041652PubMed 19567751. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.13. Source: UniProtKB

regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion

Inferred from sequence or structural similarity PubMed 17400717. Source: BHF-UCL

regulation of cell communication by electrical coupling

Traceable author statement PubMed 22123818. Source: BHF-UCL

regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity

Inferred from direct assay PubMed 21062895. Source: UniProtKB

regulation of protein depolymerization

Inferred from electronic annotation. Source: Ensembl

regulation of protein stability

Inferred from electronic annotation. Source: Ensembl

regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum

Traceable author statement PubMed 15041652. Source: BHF-UCL

regulation of ryanodine-sensitive calcium-release channel activity

Traceable author statement PubMed 22123818. Source: BHF-UCL

response to ATP

Inferred from direct assay PubMed 21062895. Source: UniProtKB

   Cellular_componentcalcium channel complex

Traceable author statement PubMed 19403607. Source: BHF-UCL

cortical endoplasmic reticulum

Inferred from direct assay PubMed 21062895Ref.13. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay. Source: HPA

endoplasmic reticulum membrane

Non-traceable author statement Ref.5. Source: UniProtKB

integral component of endoplasmic reticulum membrane

Inferred from direct assay Ref.13. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

junctional sarcoplasmic reticulum membrane

Traceable author statement PubMed 17569730. Source: BHF-UCL

plasma membrane

Inferred from direct assay PubMed 21062895. Source: UniProtKB

sarcoplasmic reticulum lumen

Traceable author statement PubMed 22123818. Source: BHF-UCL

sarcoplasmic reticulum membrane

Traceable author statement PubMed 19403607. Source: BHF-UCL

   Molecular_functioncalcium ion binding

Inferred from direct assay Ref.13. Source: UniProtKB

electron carrier activity

Traceable author statement Ref.1. Source: UniProtKB

ion channel binding

Traceable author statement PubMed 19567751. Source: BHF-UCL

peptide-aspartate beta-dioxygenase activity

Traceable author statement Ref.5. Source: ProtInc

protein binding

Inferred from physical interaction Ref.13PubMed 21062895. Source: UniProtKB

structural constituent of muscle

Traceable author statement Ref.5. Source: ProtInc

structural molecule activity

Traceable author statement Ref.5. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 10 isoforms produced by alternative splicing. [Align] [Select]

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.
Isoform 1 (identifier: Q12797-1)

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.
Isoform 2 (identifier: Q12797-2)

The sequence of this isoform differs from the canonical sequence as follows:
     312-313: ET → DT
     314-758: Missing.
Isoform 3 (identifier: Q12797-3)

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.
Isoform 4 (identifier: Q12797-4)

Also known as: Junctin-2;

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.
Isoform 5 (identifier: Q12797-5)

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.
Isoform 10 (identifier: Q12797-10)

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MAQRKNAKSSGNSSSSGSGSGSTSAGSSSPGARR → MAEDK
Isoform 6 (identifier: Q12797-6)

The sequence of this isoform differs from the canonical sequence as follows:
     164-206: Missing.
     312-313: ET → DT
     314-758: Missing.
Isoform 7 (identifier: Q12797-7)

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.
Isoform 8 (identifier: Q12797-8)

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.
Isoform 9 (identifier: Q12797-9)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 758758Aspartyl/asparaginyl beta-hydroxylase
PRO_0000064706

Regions

Topological domain1 – 5353Cytoplasmic Potential
Transmembrane54 – 7421Helical; Signal-anchor for type II membrane protein; Potential
Topological domain75 – 758684Lumenal Potential
Repeat341 – 37434TPR 1
Repeat454 – 48734TPR 2
Repeat489 – 52133TPR 3
Repeat525 – 55733TPR 4
Calcium binding90 – 10213 Probable
Region688 – 69032-oxoglutarate binding
Compositional bias9 – 2921Ser-rich
Compositional bias111 – 312202Glu-rich
Compositional bias323 – 33210Poly-Lys

Sites

Metal binding6791Iron Probable
Metal binding7251Iron Probable
Binding site62512-oxoglutarate
Binding site66812-oxoglutarate
Binding site73512-oxoglutarate

Amino acid modifications

Glycosylation4521N-linked (GlcNAc...) Ref.14
Glycosylation7061N-linked (GlcNAc...) Potential
Disulfide bond641 ↔ 648 Ref.15

Natural variations

Alternative sequence1 – 3434MAQRK…PGARR → MAEDK in isoform 3, isoform 4, isoform 5, isoform 8, isoform 9 and isoform 10.
VSP_039165
Alternative sequence841L → LAKAKDFRYNLSEVLQ in isoform 3, isoform 5, isoform 7, isoform 8 and isoform 9.
VSP_039166
Alternative sequence108 – 239132GLKER…NPDSS → EGPSGVAKRKTKAKVKELTK EELKKEKEKPESRKESKNEE RKKGKKEDVRKDKKIADADL SRKESPKGKKDREKEKVDLE KSAKTKENRKKSTNMKDVSS KMASRDKDDRKESRSSTRYA HLTKGNTQKRNG in isoform 3 and isoform 4.
VSP_039167
Alternative sequence110 – 18879KERST…DEFLM → TKDGSNENIDSLEEVLNILA EESSDWFYGFLSFLYDIMTP FEMLEEEEEESETADGVDGT SQNEGVQGKTCVILDLHNQ in isoform 7.
VSP_044235
Alternative sequence164 – 20643Missing in isoform 6 and isoform 9.
VSP_044236
Alternative sequence189 – 758570Missing in isoform 7.
VSP_044237
Alternative sequence240 – 758519Missing in isoform 3 and isoform 4.
VSP_039168
Alternative sequence2641Missing in isoform 5.
VSP_044238
Alternative sequence312 – 3132ET → DT in isoform 2, isoform 5, isoform 6, isoform 8 and isoform 9.
VSP_039169
Alternative sequence314 – 758445Missing in isoform 2, isoform 5, isoform 6, isoform 8 and isoform 9.
VSP_039170
Natural variant3541R → M.
Corresponds to variant rs6995412 [ dbSNP | Ensembl ].
VAR_053781

Experimental info

Mutagenesis91 – 933DAD → AAA: Increase in cytoplasmic Ca(2+) via activation of endogenous CRAC channels. Ref.13
Sequence conflict5191D → N in BAG65166. Ref.7
Sequence conflict5651Y → I in AAA82108. Ref.1
Sequence conflict575 – 5773WWT → CG in AAA82108. Ref.1
Sequence conflict5851E → Q in AAA82108. Ref.1
Sequence conflict5991D → Y in BAG65166. Ref.7
Sequence conflict7091K → R in AAB50779. Ref.2
Sequence conflict7341F → L in BAG65166. Ref.7

Secondary structure

......................................... 758
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 17, 2007. Version 3.
Checksum: 4AE56D1D8DF0AF0C

FASTA75885,863
        10         20         30         40         50         60 
MAQRKNAKSS GNSSSSGSGS GSTSAGSSSP GARRETKHGG HKNGRKGGLS GTSFFTWFMV 

        70         80         90        100        110        120 
IALLGVWTSV AVVWFDLVDY EEVLGKLGIY DADGDGDFDV DDAKVLLGLK ERSTSEPAVP 

       130        140        150        160        170        180 
PEEAEPHTEP EEQVPVEAEP QNIEDEAKEQ IQSLLHEMVH AEHVEGEDLQ QEDGPTGEPQ 

       190        200        210        220        230        240 
QEDDEFLMAT DVDDRFETLE PEVSHEETEH SYHVEETVSQ DCNQDMEEMM SEQENPDSSE 

       250        260        270        280        290        300 
PVVEDERLHH DTDDVTYQVY EEQAVYEPLE NEGIEITEVT APPEDNPVED SQVIVEEVSI 

       310        320        330        340        350        360 
FPVEEQQEVP PETNRKTDDP EQKAKVKKKK PKLLNKFDKT IKAELDAAEK LRKRGKIEEA 

       370        380        390        400        410        420 
VNAFKELVRK YPQSPRARYG KAQCEDDLAE KRRSNEVLRG AIETYQEVAS LPDVPADLLK 

       430        440        450        460        470        480 
LSLKRRSDRQ QFLGHMRGSL LTLQRLVQLF PNDTSLKNDL GVGYLLIGDN DNAKKVYEEV 

       490        500        510        520        530        540 
LSVTPNDGFA KVHYGFILKA QNKIAESIPY LKEGIESGDP GTDDGRFYFH LGDAMQRVGN 

       550        560        570        580        590        600 
KEAYKWYELG HKRGHFASVW QRSLYNVNGL KAQPWWTPKE TGYTELVKSL ERNWKLIRDE 

       610        620        630        640        650        660 
GLAVMDKAKG LFLPEDENLR EKGDWSQFTL WQQGRRNENA CKGAPKTCTL LEKFPETTGC 

       670        680        690        700        710        720 
RRGQIKYSIM HPGTHVWPHT GPTNCRLRMH LGLVIPKEGC KIRCANETKT WEEGKVLIFD 

       730        740        750 
DSFEHEVWQD ASSFRLIFIV DVWHPELTPQ QRRSLPAI 

« Hide

Isoform 2 [UniParc].

Checksum: 7885A18B81CD6D0D
Show »

FASTA31334,646
Isoform 3 (Junctin-1) (Cardiac junctin) [UniParc].

Checksum: 27D331DD6D88E0D3
Show »

FASTA22525,560
Isoform 4 (Junctin-2) [UniParc].

Checksum: 8E7C39D69F2B22C7
Show »

FASTA21023,796
Isoform 5 [UniParc].

Checksum: B28D921E5021348B
Show »

FASTA29833,744
Isoform 10 [UniParc].

Checksum: EA17281494828D62
Show »

FASTA72983,268
Isoform 6 [UniParc].

Checksum: 8551773C7272202A
Show »

FASTA27029,757
Isoform 7 [UniParc].

Checksum: 3EC728B1E417091C
Show »

FASTA20321,963
Isoform 8 (Junctate) [UniParc].

Checksum: 658F88C34EC2CA37
Show »

FASTA29933,815
Isoform 9 [UniParc].

Checksum: 8C892EC3D1AE1BCC
Show »

FASTA25628,926

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
[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]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS34898.1. [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]
PIRI38423.
RefSeqNP_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]
UniGeneHs.332422.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3RCQX-ray2.05A562-758[»]
ProteinModelPortalQ12797.
SMRQ12797. Positions 348-386, 431-485, 562-758.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106936. 8 interactions.
IntActQ12797. 5 interactions.
STRING9606.ENSP00000368767.

Chemistry

DrugBankDB00128. L-Aspartic Acid.
DB00139. Succinic acid.

PTM databases

PhosphoSiteQ12797.

Polymorphism databases

DMDM145559444.

Proteomic databases

MaxQBQ12797.
PaxDbQ12797.
PRIDEQ12797.

Protocols and materials databases

DNASU444.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356457; ENSP00000348841; ENSG00000198363. [Q12797-2]
ENST00000379449; ENSP00000368762; ENSG00000198363. [Q12797-7]
ENST00000379454; ENSP00000368767; ENSG00000198363. [Q12797-1]
ENST00000389204; ENSP00000373856; ENSG00000198363. [Q12797-3]
ENST00000445642; ENSP00000394013; ENSG00000198363. [Q12797-8]
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]
GeneID444.
KEGGhsa:444.
UCSCuc003xuj.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

CTD444.
GeneCardsGC08M062465.
HGNCHGNC:757. ASPH.
HPAHPA055161.
HPA057838.
HPA059303.
MIM600582. gene.
neXtProtNX_Q12797.
PharmGKBPA25056.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3555.
HOVERGENHBG004290.
InParanoidQ12797.
KOK00476.
OMARNENACK.
OrthoDBEOG715Q44.
PhylomeDBQ12797.
TreeFamTF312799.

Gene expression databases

ArrayExpressQ12797.
BgeeQ12797.
CleanExHS_ASPH.
GenevestigatorQ12797.

Family and domain databases

Gene3D1.25.40.10. 1 hit.
2.60.120.330. 1 hit.
InterProIPR007943. Asp-B-hydro/Triadin_dom.
IPR007803. Asp_Arg_Pro-Hydrxlase.
IPR027443. IPNS-like.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]
PfamPF05279. Asp-B-Hydro_N. 1 hit.
PF05118. Asp_Arg_Hydrox. 1 hit.
[Graphical view]
PROSITEPS50005. TPR. 2 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSASPH. human.
EvolutionaryTraceQ12797.
GeneWikiASPH.
GenomeRNAi444.
NextBio1859.
PROQ12797.
SOURCESearch...

Entry information

Entry nameASPH_HUMAN
AccessionPrimary (citable) accession number: Q12797
Secondary accession number(s): A6NDF4 expand/collapse secondary AC list , A6NHI2, B4DIC9, B4E2K4, B7ZM95, E5RGP5, F5H667, Q6NXR7, Q8TB28, Q9H291, Q9H2C4, Q9NRI0, Q9NRI1, Q9Y4J0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 17, 2007
Last modified: July 9, 2014
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM