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UniProtKB/Swiss-Prot entry Q8BSY0


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ASPH_MOUSE
Primary accession number Q8BSY0
Secondary accession number Q9EPA6
Integrated into Swiss-Prot on October 31, 2006
Sequence was last modified on March 1, 2003 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 50)
Name and origin of the protein
Protein name Aspartyl/asparaginyl beta-hydroxylase
Synonyms EC 1.14.11.16
Aspartate beta-hydroxylase
ASP beta-hydroxylase
Peptide-aspartate beta-dioxygenase
Gene name
Name: Asph
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/c;
TISSUE=Liver;
DOI=10.1074/jbc.M006753200; PubMed=10956665 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Aspartyl beta -hydroxylase (Asph) and an evolutionarily conserved isoform of Asph missing the catalytic domain share exons with junctin.";
J. Biol. Chem. 275:39543-39554(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF289486; AAG40808.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF289487; AAG40809.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK030293; BAC26882.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_075553.2; -.
UniGene Mm.239247
3D structure databases
HSSP P04573; 1C7V. [HSSP ENTRY / PDB]
ModBase Q8BSY0.
PTM databases
PhosphoSite Q8BSY0; -.
Organism-specific databases
MGI MGI:1914186; Asph.
Gene expression databases
ArrayExpress Q8BSY0; -.
CleanEx MM_ASPH; -.
GermOnline ENSMUSG00000028207; Mus musculus.
Ontologies
GO
GO:0030176; Cellular component: integral to endoplasmic reticulum membrane (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0016702; Molecular function: oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen (inferred from electronic annotation from UniProtKB-KW).
GO:0004597; Molecular function: peptide-aspartate beta-dioxygenase activity (inferred from electronic annotation from InterPro).
GO:0060325; Biological process: face morphogenesis (inferred from mutant phenotype from MGI).
GO:0035108; Biological process: limb morphogenesis (inferred from mutant phenotype from MGI).
GO:0008285; Biological process: negative regulation of cell proliferation (inferred from genetic interaction from MGI).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0060021; Biological process: palate development (inferred from mutant phenotype from MGI).
GO:0007389; Biological process: pattern specification process (inferred from mutant phenotype from MGI).
GO:0042264; Biological process: peptidyl-aspartic acid hydroxylation (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR007943; Asp-B-hydro_N.
IPR007803; Asp_Arg_Hydrox.
IPR011990; TPR-like_helical.
IPR013026; TPR_region.
Graphical view of domain structure.
Gene3D G3DSA:1.25.40.10; TPR-like_helical; 1.
Pfam PF05279; Asp-B-Hydro_N; 1.
PF05118; Asp_Arg_Hydrox; 1.
Pfam graphical view of domain structure.
PROSITE PS50005; TPR; 2.
PS50293; TPR_REGION; 1.
PROSITE graphical view of domain structure (profiles).
Proteomics databases
PRIDE Q8BSY0; -.
Genome annotation databases
Ensembl ENSMUSG00000028207; Mus musculus. [Contig view]
GeneID 65973; -.
KEGG mmu:65973; -.
Phylogenomic databases
HOVERGEN Q8BSY0; -.
Other
NextBio 320434; -.
SOURCE Asph; Mus musculus.
ProtoNet Q8BSY0.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Dioxygenase; Endoplasmic reticulum; Glycoprotein; Iron; Membrane; Oxidoreductase; Phosphoprotein; Repeat; Signal-anchor; TPR repeat; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   741  741     Aspartyl/asparaginyl beta-hydroxylase. PRO_0000254161
TOPO_DOM   1    62  62     Cytoplasmic (Potential). 
TRANSMEM   63    83  21     Signal-anchor for type II membrane protein (Potential). 
TOPO_DOM   84   741  658     Lumenal (Potential). 
REPEAT   324   357  34     TPR 1. 
REPEAT   365   398  34     TPR 2. 
REPEAT   437   470  34     TPR 3. 
REPEAT   472   504  33     TPR 4. 
REPEAT   508   540  33     TPR 5. 
COMPBIAS   9    61  53     Gly-rich. 
COMPBIAS   14    38  25     Ser-rich. 
COMPBIAS   310   315  6     Poly-Lys. 
MOD_RES   38    38        Phosphoserine (By similarity). 
CARBOHYD   453   453        N-linked (GlcNAc...) (Potential). 
CARBOHYD   689   689        N-linked (GlcNAc...) (Potential). 
CONFLICT   131   132        Missing (in Ref. 1; AAG40808/AAG40809). 
CONFLICT   279   279        A -> E (in Ref. 1; AAG40808/AAG40809). 
Sequence information
Length: 741 AA [This is the length of the unprocessed precursor] Molecular weight: 83042 Da [This is the MW of the unprocessed precursor] CRC64: 0660A6A5E34418C8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAPRKNAKGG GGNSSSSGSG SGSGSGSPST GSSGSSSSPG ARREAKHGGH KNGRRGGISG 

        70         80         90        100        110        120 
GSFFTWFMVI ALLGVWTSVA VVWFDLVDYE EVLGKLGVYD ADGDGDFDVD DAKVLLGLKE 

       130        140        150        160        170        180 
RSPSERTFPP EEEAETHAEL EEQAPEGADI QNVEDEVKEQ IQSLLQESVH TDHDLEADGL 

       190        200        210        220        230        240 
AGEPQPEVED FLTVTDSDDR FEDLEPGTVH EEIEDTYHVE DTASQNHPND MEEMTNEQEN 

       250        260        270        280        290        300 
SDPSEAVTDA GVLLPHAEEV RHQDYDEPVY EPSEHEGVAI SDNTIDDSSI ISEEINVASV 

       310        320        330        340        350        360 
EEQQDTPPVK KKKPKLLNKF DKTIKAELDA AEKLRKRGKI EEAVNAFEEL VRKYPQSPRA 

       370        380        390        400        410        420 
RYGKAQCEDD LAEKQRSNEV LRRAIETYQE AADLPDAPTD LVKLSLKRRS ERQQFLGHMR 

       430        440        450        460        470        480 
GSLLTLQRLV QLFPSDTTLK NDLGVGYLLL GDNDSAKKVY EEVLNVTPND GFAKVHYGFI 

       490        500        510        520        530        540 
LKAQNKISES IPYLKEGIES GDPGTDDGRF YFHLGDAMQR VGNKEAYKWY ELGHKRGHFA 

       550        560        570        580        590        600 
SVWQRSLYNV NGLKAQPWWT PRETGYTELV KSLERNWKLI RDEGLMVMDK AKGLFLPEDE 

       610        620        630        640        650        660 
NLREKGDWSQ FTLWQQGRKN ENACKGAPKT CALLEKFSET TGCRRGQIKY SIMHPGTHVW 

       670        680        690        700        710        720 
PHTGPTNCRL RMHLGLVIPK EGCKIRCANE TRTWEEGKVL IFDDSFEHEV WQDASSFRLI 

       730        740 
FIVDVWHPEL TPQQRRSLPA I 

Q8BSY0 in FASTA format

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