ID   ASPH_HUMAN              Reviewed;         758 AA.
AC   Q12797; A6NHI2; Q9Y4J0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 3.
DT   04-NOV-2008, entry version 79.
DE   RecName: Full=Aspartyl/asparaginyl beta-hydroxylase;
DE            EC=1.14.11.16;
DE   AltName: Full=Aspartate beta-hydroxylase;
DE            Short=ASP beta-hydroxylase;
DE   AltName: Full=Peptide-aspartate beta-dioxygenase;
GN   Name=ASPH;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=95121937; PubMed=7821814; DOI=10.1016/0378-1119(94)90460-X;
RA   Korioth F., Gieffers C., Frey J.;
RT   "Cloning and characterization of the human gene encoding aspartyl
RT   beta-hydroxylase.";
RL   Gene 150:395-399(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96420598; PubMed=8823296;
RA   Lavaissiere L., Jia S., Nishiyama M., de la Monte S., Stern A.M.,
RA   Wands J.R., Friedman P.A.;
RT   "Overexpression of human aspartyl(asparaginyl)beta-hydroxylase in
RT   hepatocellular carcinoma and cholangiocarcinoma.";
RL   J. Clin. Invest. 98:1313-1323(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
RA   Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
RA   Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA   Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
RA   Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
RA   DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
RA   Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
RA   Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
RA   O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
RA   Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
RA   Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
RA   Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
RA   Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
RA   Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Epithelium;
RX   PubMed=15302935; DOI=10.1073/pnas.0404720101;
RA   Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,
RA   Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
RT   "Large-scale characterization of HeLa cell nuclear phosphoproteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
CC   -!- FUNCTION: Specifically hydroxylates an Asp or Asn residue in
CC       certain epidermal growth factor-like (EGF) domains of a number of
CC       proteins.
CC   -!- CATALYTIC ACTIVITY: Peptide L-aspartate + 2-oxoglutarate + O(2) =
CC       peptide 3-hydroxy-L-aspartate + succinate + CO(2).
CC   -!- COFACTOR: Iron.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       type II membrane protein.
CC   -!- TISSUE SPECIFICITY: Detected in all tissues tested.
CC   -!- SIMILARITY: Belongs to the aspartyl/asparaginyl beta-hydroxylase
CC       family.
CC   -!- SIMILARITY: Contains 4 TPR repeats.
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DR   EMBL; U03109; AAA82108.1; -; mRNA.
DR   EMBL; S83325; AAB50779.1; -; mRNA.
DR   EMBL; AC067881; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471068; EAW86848.1; -; Genomic_DNA.
DR   PIR; I38423; I38423.
DR   RefSeq; NP_004309.2; -.
DR   UniGene; Hs.622998; -.
DR   PhosphoSite; Q12797; -.
DR   Ensembl; ENSG00000198363; Homo sapiens.
DR   GeneID; 444; -.
DR   KEGG; hsa:444; -.
DR   H-InvDB; HIX0034267; -.
DR   HGNC; HGNC:757; ASPH.
DR   MIM; 600582; gene.
DR   PharmGKB; PA25056; -.
DR   HOVERGEN; Q12797; -.
DR   DrugBank; DB00128; L-Aspartic Acid.
DR   DrugBank; DB00139; Succinic acid.
DR   NextBio; 1859; -.
DR   ArrayExpress; Q12797; -.
DR   CleanEx; HS_ASPH; -.
DR   GermOnline; ENSG00000198363; Homo sapiens.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:ProtInc.
DR   GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
DR   GO; GO:0009055; F:electron carrier activity; TAS:UniProtKB.
DR   GO; GO:0004597; F:peptide-aspartate beta-dioxygenase activity; TAS:ProtInc.
DR   GO; GO:0008307; F:structural constituent of muscle; TAS:ProtInc.
DR   GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
DR   InterPro; IPR007943; Asp-B-hydro_N.
DR   InterPro; IPR007803; Asp_Arg_Hydrox.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR013026; TPR_region.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1.
DR   Pfam; PF05279; Asp-B-Hydro_N; 1.
DR   Pfam; PF05118; Asp_Arg_Hydrox; 1.
DR   PROSITE; PS50005; TPR; 2.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   Dioxygenase; Endoplasmic reticulum; Glycoprotein; Iron; Membrane;
KW   Oxidoreductase; Phosphoprotein; Repeat; Signal-anchor; TPR repeat;
KW   Transmembrane.
FT   CHAIN         1    758       Aspartyl/asparaginyl beta-hydroxylase.
FT                                /FTId=PRO_0000064706.
FT   TOPO_DOM      1     53       Cytoplasmic (Potential).
FT   TRANSMEM     54     74       Signal-anchor for type II membrane
FT                                protein (Potential).
FT   TOPO_DOM     75    758       Lumenal (Potential).
FT   REPEAT      341    374       TPR 1.
FT   REPEAT      454    487       TPR 2.
FT   REPEAT      489    521       TPR 3.
FT   REPEAT      525    557       TPR 4.
FT   COMPBIAS      9     29       Ser-rich.
FT   COMPBIAS    111    312       Glu-rich.
FT   COMPBIAS    323    332       Poly-Lys.
FT   MOD_RES      29     29       Phosphoserine.
FT   CARBOHYD    452    452       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    706    706       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    565    565       Y -> I (in Ref. 1; AAA82108).
FT   CONFLICT    575    577       WWT -> CG (in Ref. 1; AAA82108).
FT   CONFLICT    585    585       E -> Q (in Ref. 1; AAA82108).
FT   CONFLICT    709    709       K -> R (in Ref. 2; AAB50779).
SQ   SEQUENCE   758 AA;  85863 MW;  4AE56D1D8DF0AF0C CRC64;
     MAQRKNAKSS GNSSSSGSGS GSTSAGSSSP GARRETKHGG HKNGRKGGLS GTSFFTWFMV
     IALLGVWTSV AVVWFDLVDY EEVLGKLGIY DADGDGDFDV DDAKVLLGLK ERSTSEPAVP
     PEEAEPHTEP EEQVPVEAEP QNIEDEAKEQ IQSLLHEMVH AEHVEGEDLQ QEDGPTGEPQ
     QEDDEFLMAT DVDDRFETLE PEVSHEETEH SYHVEETVSQ DCNQDMEEMM SEQENPDSSE
     PVVEDERLHH DTDDVTYQVY EEQAVYEPLE NEGIEITEVT APPEDNPVED SQVIVEEVSI
     FPVEEQQEVP PETNRKTDDP EQKAKVKKKK PKLLNKFDKT IKAELDAAEK LRKRGKIEEA
     VNAFKELVRK YPQSPRARYG KAQCEDDLAE KRRSNEVLRG AIETYQEVAS LPDVPADLLK
     LSLKRRSDRQ QFLGHMRGSL LTLQRLVQLF PNDTSLKNDL GVGYLLIGDN DNAKKVYEEV
     LSVTPNDGFA KVHYGFILKA QNKIAESIPY LKEGIESGDP GTDDGRFYFH LGDAMQRVGN
     KEAYKWYELG HKRGHFASVW QRSLYNVNGL KAQPWWTPKE TGYTELVKSL ERNWKLIRDE
     GLAVMDKAKG LFLPEDENLR EKGDWSQFTL WQQGRRNENA CKGAPKTCTL LEKFPETTGC
     RRGQIKYSIM HPGTHVWPHT GPTNCRLRMH LGLVIPKEGC KIRCANETKT WEEGKVLIFD
     DSFEHEVWQD ASSFRLIFIV DVWHPELTPQ QRRSLPAI
//