Q12797 (ASPH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	758 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
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 component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal-anchor TPR repeat Transmembrane Transmembrane helix
Ligand	Calcium Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
PTM	Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation 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: Compara limb morphogenesis Inferred from electronic annotation. Source: Compara muscle contraction Traceable author statement Ref.3. Source: ProtInc negative regulation of cell proliferation Inferred from electronic annotation. Source: Compara palate development Inferred from electronic annotation. Source: Compara pattern specification process Inferred from electronic annotation. Source: Compara peptidyl-aspartic acid hydroxylation Inferred from electronic annotation. Source: Compara 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-dependent 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 response to ATP Inferred from direct assay PubMed 21062895. Source: UniProtKB
Cellular_component	calcium channel complex Traceable author statement PubMed 19403607. Source: BHF-UCL cortical endoplasmic reticulum Inferred from direct assay PubMed 21062895Ref.13. Source: UniProtKB endoplasmic reticulum membrane Non-traceable author statement Ref.5. Source: UniProtKB integral to endoplasmic reticulum membrane Inferred from direct assay Ref.13. Source: UniProtKB integral to 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
Molecular_function	calcium 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 oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW peptide-aspartate beta-dioxygenase activity Traceable author statement Ref.5. Source: ProtInc structural constituent of muscle Traceable author statement Ref.5. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 9 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 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 758

758

Aspartyl/asparaginyl beta-hydroxylase

PRO_0000064706

Regions

Topological domain

1 – 53

53

Cytoplasmic Potential

Transmembrane

54 – 74

21

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

75 – 758

684

Lumenal Potential

Repeat

341 – 374

34

TPR 1

Repeat

454 – 487

34

TPR 2

Repeat

489 – 521

33

TPR 3

Repeat

525 – 557

33

TPR 4

Calcium binding

90 – 102

13

Probable

Compositional bias

9 – 29

21

Ser-rich

Compositional bias

111 – 312

202

Glu-rich

Compositional bias

323 – 332

10

Poly-Lys

Amino acid modifications

Glycosylation

452

1

N-linked (GlcNAc...) Ref.14

Glycosylation

706

1

N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence

1 – 34

34

MAQRK…PGARR → MAEDK in isoform 3, isoform 4, isoform 5, isoform 8 and isoform 9.

VSP_039165

Alternative sequence

84

1

L → LAKAKDFRYNLSEVLQ in isoform 3, isoform 5, isoform 7, isoform 8 and isoform 9.

VSP_039166

Alternative sequence

108 – 239

132

GLKER…NPDSS → EGPSGVAKRKTKAKVKELTK EELKKEKEKPESRKESKNEE RKKGKKEDVRKDKKIADADL SRKESPKGKKDREKEKVDLE KSAKTKENRKKSTNMKDVSS KMASRDKDDRKESRSSTRYA HLTKGNTQKRNG in isoform 3 and isoform 4.

VSP_039167

Alternative sequence

110 – 188

79

KERST…DEFLM → TKDGSNENIDSLEEVLNILA EESSDWFYGFLSFLYDIMTP FEMLEEEEEESETADGVDGT SQNEGVQGKTCVILDLHNQ in isoform 7.

VSP_044235

Alternative sequence

164 – 206

43

Missing in isoform 6 and isoform 9.

VSP_044236

Alternative sequence

189 – 758

570

Missing in isoform 7.

VSP_044237

Alternative sequence

240 – 758

519

Missing in isoform 3 and isoform 4.

VSP_039168

Alternative sequence

264

1

Missing in isoform 5.

VSP_044238

Alternative sequence

312 – 313

2

ET → DT in isoform 2, isoform 5, isoform 6, isoform 8 and isoform 9.

VSP_039169

Alternative sequence

314 – 758

445

Missing in isoform 2, isoform 5, isoform 6, isoform 8 and isoform 9.

VSP_039170

Natural variant

354

1

R → M.
Corresponds to variant rs6995412 [ dbSNP | Ensembl ].

VAR_053781

Experimental info

Mutagenesis

91 – 93

3

DAD → AAA: Increase in cytoplasmic Ca(2+) via activation of endogenous CRAC channels. Ref.13

Sequence conflict

565

1

Y → I in AAA82108. Ref.1

Sequence conflict

575 – 577

3

WWT → CG in AAA82108. Ref.1

Sequence conflict

585

1

E → Q in AAA82108. Ref.1

Sequence conflict

709

1

K → R in AAB50779. Ref.2

Secondary structure

1

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758

Helix Strand Turn

Details...

Beta strand

574 – 576

3

Helix

578 – 581

4

Helix

584 – 592

9

Helix

594 – 604

11

Turn

607 – 610

4

Beta strand

620 – 623

4

Beta strand

625 – 632

8

Helix

638 – 643

6

Helix

645 – 651

7

Helix

655 – 658

4

Beta strand

664 – 670

7

Beta strand

674 – 679

6

Beta strand

686 – 694

9

Beta strand

697 – 704

8

Beta strand

707 – 709

3

Beta strand

716 – 719

4

Beta strand

725 – 729

5

Beta strand

731 – 733

3

Beta strand

735 – 743

9

Helix

749 – 754

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 17, 2007. Version 3. Checksum: 4AE56D1D8DF0AF0C	FASTA	758	85,863
	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
	Isoform 2 [UniParc]. Checksum: 7885A18B81CD6D0D	FASTA	313	34,646
	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 FPVEEQQEVP PDT
	Isoform 3 (Junctin-1) (Cardiac junctin) [UniParc]. Checksum: 27D331DD6D88E0D3	FASTA	225	25,560
	10 20 30 40 50 60 MAEDKETKHG GHKNGRKGGL SGTSFFTWFM VIALLGVWTS VAVVWFDLVD YEEVLAKAKD 70 80 90 100 110 120 FRYNLSEVLQ GKLGIYDADG DGDFDVDDAK VLLEGPSGVA KRKTKAKVKE LTKEELKKEK 130 140 150 160 170 180 EKPESRKESK NEERKKGKKE DVRKDKKIAD ADLSRKESPK GKKDREKEKV DLEKSAKTKE 190 200 210 220 NRKKSTNMKD VSSKMASRDK DDRKESRSST RYAHLTKGNT QKRNG
	Isoform 4 (Junctin-2) [UniParc]. Checksum: 8E7C39D69F2B22C7	FASTA	210	23,796
	10 20 30 40 50 60 MAEDKETKHG GHKNGRKGGL SGTSFFTWFM VIALLGVWTS VAVVWFDLVD YEEVLGKLGI 70 80 90 100 110 120 YDADGDGDFD VDDAKVLLEG PSGVAKRKTK AKVKELTKEE LKKEKEKPES RKESKNEERK 130 140 150 160 170 180 KGKKEDVRKD KKIADADLSR KESPKGKKDR EKEKVDLEKS AKTKENRKKS TNMKDVSSKM 190 200 210 ASRDKDDRKE SRSSTRYAHL TKGNTQKRNG
	Isoform 5 [UniParc]. Checksum: B28D921E5021348B	FASTA	298	33,744
	10 20 30 40 50 60 MAEDKETKHG GHKNGRKGGL SGTSFFTWFM VIALLGVWTS VAVVWFDLVD YEEVLAKAKD 70 80 90 100 110 120 FRYNLSEVLQ GKLGIYDADG DGDFDVDDAK VLLGLKERST SEPAVPPEEA EPHTEPEEQV 130 140 150 160 170 180 PVEAEPQNIE DEAKEQIQSL LHEMVHAEHV EGEDLQQEDG PTGEPQQEDD EFLMATDVDD 190 200 210 220 230 240 RFETLEPEVS HEETEHSYHV EETVSQDCNQ DMEEMMSEQE NPDSSEPVVE DERLHHDTDD 250 260 270 280 290 VTYQVYEEQV YEPLENEGIE ITEVTAPPED NPVEDSQVIV EEVSIFPVEE QQEVPPDT
	Isoform 6 [UniParc]. Checksum: 8551773C7272202A	FASTA	270	29,757
	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 AEHETEHSYH VEETVSQDCN 190 200 210 220 230 240 QDMEEMMSEQ ENPDSSEPVV EDERLHHDTD DVTYQVYEEQ AVYEPLENEG IEITEVTAPP 250 260 270 EDNPVEDSQV IVEEVSIFPV EEQQEVPPDT
	Isoform 7 [UniParc]. Checksum: 3EC728B1E417091C	FASTA	203	21,963
	10 20 30 40 50 60 MAQRKNAKSS GNSSSSGSGS GSTSAGSSSP GARRETKHGG HKNGRKGGLS GTSFFTWFMV 70 80 90 100 110 120 IALLGVWTSV AVVWFDLVDY EEVLAKAKDF RYNLSEVLQG KLGIYDADGD GDFDVDDAKV 130 140 150 160 170 180 LLGLTKDGSN ENIDSLEEVL NILAEESSDW FYGFLSFLYD IMTPFEMLEE EEEESETADG 190 200 VDGTSQNEGV QGKTCVILDL HNQ
	Isoform 8 (Junctate) [UniParc]. Checksum: 658F88C34EC2CA37	FASTA	299	33,815
	10 20 30 40 50 60 MAEDKETKHG GHKNGRKGGL SGTSFFTWFM VIALLGVWTS VAVVWFDLVD YEEVLAKAKD 70 80 90 100 110 120 FRYNLSEVLQ GKLGIYDADG DGDFDVDDAK VLLGLKERST SEPAVPPEEA EPHTEPEEQV 130 140 150 160 170 180 PVEAEPQNIE DEAKEQIQSL LHEMVHAEHV EGEDLQQEDG PTGEPQQEDD EFLMATDVDD 190 200 210 220 230 240 RFETLEPEVS HEETEHSYHV EETVSQDCNQ DMEEMMSEQE NPDSSEPVVE DERLHHDTDD 250 260 270 280 290 VTYQVYEEQA VYEPLENEGI EITEVTAPPE DNPVEDSQVI VEEVSIFPVE EQQEVPPDT
	Isoform 9 [UniParc]. Checksum: 8C892EC3D1AE1BCC	FASTA	256	28,926
	10 20 30 40 50 60 MAEDKETKHG GHKNGRKGGL SGTSFFTWFM VIALLGVWTS VAVVWFDLVD YEEVLAKAKD 70 80 90 100 110 120 FRYNLSEVLQ GKLGIYDADG DGDFDVDDAK VLLGLKERST SEPAVPPEEA EPHTEPEEQV 130 140 150 160 170 180 PVEAEPQNIE DEAKEQIQSL LHEMVHAEHE TEHSYHVEET VSQDCNQDME EMMSEQENPD 190 200 210 220 230 240 SSEPVVEDER LHHDTDDVTY QVYEEQAVYE PLENEGIEIT EVTAPPEDNP VEDSQVIVEE 250 VSIFPVEEQQ EVPPDT

References

	« Hide 'large scale' referencesShow '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. , 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] (ISOFORM 9). Tissue: Hippocampus.
[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]	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. , 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), MASS SPECTROMETRY. Tissue: Liver.
+	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.
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.

IPI

IPI00024572.
IPI00032449.
IPI00032450.
IPI00294834.

PIR

I38423.

RefSeq

NP_001158222.1. NM_001164750.1.
NP_001158223.1. NM_001164751.1.
NP_001158225.1. NM_001164753.1.
NP_001158227.1. NM_001164755.1.
NP_001158228.1. NM_001164756.1.
NP_004309.2. NM_004318.3.
NP_064549.1. NM_020164.4.
NP_115855.1. NM_032466.3.
NP_115856.1. NM_032467.3.
NP_115857.1. NM_032468.4.

UniGene

Hs.332422.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3RCQ	X-ray	2.05	A	562-758	[»]

ProteinModelPortal

Q12797.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q12797. 4 interactions.

STRING

9606.ENSP00000368767.

PTM databases

PhosphoSite

Q12797.

Polymorphism databases

DMDM

145559444.

Proteomic databases

PaxDb

Q12797.

PRIDE

Q12797.

Protocols and materials databases

DNASU

444.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000356457; ENSP00000348841; ENSG00000198363.
ENST00000379449; ENSP00000368762; ENSG00000198363.
ENST00000379454; ENSP00000368767; ENSG00000198363.
ENST00000389204; ENSP00000373856; ENSG00000198363.
ENST00000445642; ENSP00000394013; ENSG00000198363.
ENST00000517847; ENSP00000429954; ENSG00000198363.
ENST00000517903; ENSP00000430245; ENSG00000198363.
ENST00000518068; ENSP00000429286; ENSG00000198363.
ENST00000522603; ENSP00000436188; ENSG00000198363.
ENST00000522835; ENSP00000429160; ENSG00000198363.

GeneID

444.

KEGG

hsa:444.

UCSC

uc003xuj.3. human.
uc003xul.3. human.
uc003xum.3. human.
uc003xun.3. human.
uc003xur.3. human.
uc011lei.2. human.
uc011lej.2. human.
uc011lel.2. human.
uc011lem.2. human.

Organism-specific databases

CTD

444.

GeneCards

GC08M062465.

HGNC

HGNC:757. ASPH.

MIM

600582. gene.

neXtProt

NX_Q12797.

PharmGKB

PA25056.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG3555.

HOVERGEN

HBG004290.

InParanoid

Q12797.

KO

K00476.

OMA

FPNDTSL.

OrthoDB

EOG42FSK2.

Gene expression databases

ArrayExpress

Q12797.

Bgee

Q12797.

CleanEx

HS_ASPH.

Genevestigator

Q12797.

GermOnline

ENSG00000198363. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.10. 1 hit.
2.60.120.330. 1 hit.

InterPro

IPR007943. Asp-B-hydro/Triadin_dom.
IPR007803. Asp_Arg_b-Hydrxlase.
IPR027443. IPNS-like.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]

Pfam

PF05279. Asp-B-Hydro_N. 1 hit.
PF05118. Asp_Arg_Hydrox. 1 hit.
[Graphical view]

PROSITE

PS50005. TPR. 2 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ASPH. human.

DrugBank

DB00128. L-Aspartic Acid.
DB00139. Succinic acid.

EvolutionaryTrace

Q12797.

GenomeRNAi

444.

NextBio

1859.

SOURCE

Search...

Entry information

Entry name

ASPH_HUMAN

Accession

Primary (citable) accession number: Q12797
Secondary accession number(s): A6NDF4 , A6NHI2, B4DIC9, B7ZM95, E5RGP5, 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:	May 29, 2013
This is version 129 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.