ASPH1_HUMAN
ID ASPH1_HUMAN Reviewed; 390 AA.
AC Q5U4P2; A0AVE3; B7ZLZ3; Q8IW63; Q8N316; Q96H00;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Aspartate beta-hydroxylase domain-containing protein 1;
DE EC=1.14.11.-;
GN Name=ASPHD1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Colon, and Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the aspartyl/asparaginyl beta-hydroxylase
CC family. {ECO:0000305}.
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DR EMBL; AC120114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009033; AAH09033.1; -; mRNA.
DR EMBL; BC029136; AAH29136.3; -; mRNA.
DR EMBL; BC040933; AAH40933.3; -; mRNA.
DR EMBL; BC085011; AAH85011.1; -; mRNA.
DR EMBL; BC126319; AAI26320.1; -; mRNA.
DR EMBL; BC126321; AAI26322.1; -; mRNA.
DR EMBL; BC144152; AAI44153.1; -; mRNA.
DR CCDS; CCDS10660.1; -.
DR RefSeq; NP_859069.2; NM_181718.3.
DR AlphaFoldDB; Q5U4P2; -.
DR SMR; Q5U4P2; -.
DR BioGRID; 129003; 6.
DR IntAct; Q5U4P2; 1.
DR MINT; Q5U4P2; -.
DR STRING; 9606.ENSP00000311447; -.
DR iPTMnet; Q5U4P2; -.
DR PhosphoSitePlus; Q5U4P2; -.
DR BioMuta; ASPHD1; -.
DR DMDM; 215274179; -.
DR EPD; Q5U4P2; -.
DR jPOST; Q5U4P2; -.
DR MassIVE; Q5U4P2; -.
DR MaxQB; Q5U4P2; -.
DR PaxDb; Q5U4P2; -.
DR PeptideAtlas; Q5U4P2; -.
DR PRIDE; Q5U4P2; -.
DR ProteomicsDB; 65227; -.
DR Antibodypedia; 26891; 55 antibodies from 13 providers.
DR DNASU; 253982; -.
DR Ensembl; ENST00000308748.10; ENSP00000311447.5; ENSG00000174939.11.
DR Ensembl; ENST00000414952.6; ENSP00000388036.2; ENSG00000174939.11.
DR Ensembl; ENST00000566693.1; ENSP00000456801.1; ENSG00000174939.11.
DR GeneID; 253982; -.
DR KEGG; hsa:253982; -.
DR MANE-Select; ENST00000308748.10; ENSP00000311447.5; NM_181718.4; NP_859069.2.
DR UCSC; uc002dut.4; human.
DR CTD; 253982; -.
DR DisGeNET; 253982; -.
DR GeneCards; ASPHD1; -.
DR HGNC; HGNC:27380; ASPHD1.
DR HPA; ENSG00000174939; Group enriched (brain, choroid plexus, pituitary gland).
DR neXtProt; NX_Q5U4P2; -.
DR OpenTargets; ENSG00000174939; -.
DR PharmGKB; PA143485313; -.
DR VEuPathDB; HostDB:ENSG00000174939; -.
DR eggNOG; KOG3696; Eukaryota.
DR GeneTree; ENSGT00940000161676; -.
DR HOGENOM; CLU_059279_3_0_1; -.
DR InParanoid; Q5U4P2; -.
DR OMA; GQGNWGL; -.
DR OrthoDB; 1324479at2759; -.
DR PhylomeDB; Q5U4P2; -.
DR TreeFam; TF312799; -.
DR PathwayCommons; Q5U4P2; -.
DR SignaLink; Q5U4P2; -.
DR BioGRID-ORCS; 253982; 16 hits in 1075 CRISPR screens.
DR ChiTaRS; ASPHD1; human.
DR GenomeRNAi; 253982; -.
DR Pharos; Q5U4P2; Tdark.
DR PRO; PR:Q5U4P2; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q5U4P2; protein.
DR Bgee; ENSG00000174939; Expressed in C1 segment of cervical spinal cord and 147 other tissues.
DR ExpressionAtlas; Q5U4P2; baseline and differential.
DR Genevisible; Q5U4P2; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0018193; P:peptidyl-amino acid modification; IEA:InterPro.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR007803; Asp/Arg/Pro-Hydrxlase.
DR InterPro; IPR027443; IPNS-like_sf.
DR Pfam; PF05118; Asp_Arg_Hydrox; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Membrane; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..390
FT /note="Aspartate beta-hydroxylase domain-containing protein
FT 1"
FT /id="PRO_0000254595"
FT TOPO_DOM 1..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..390
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT CONFLICT 172
FT /note="G -> GG (in Ref. 2; AAI44153)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 41128 MW; 072163A74E3A23BF CRC64;
MKEGRGSFSV ERGPRKERET AQSGMWKGNS PAGSQGAAME GTGGELGGQG NWGPEDAPGL
LARASLIMLP WPLPLASSAL TLLFGALTSL FLWYCYRLGS QDMQALGAGS RAGGVRGGPV
GCSEAGGPSP GGPGDPGEGP RTEGLVSRRL RAYARRYSWA GMGRVRRAAQ GGPGPGRGPG
VLGIQRPGLL FLPDLPSAPF VPRDAQRHDV ELLESSFPAI LRDFGAVSWD FSGTTPPPRG
WSPPLAPGCY QLLLYQAGRC QPSNCRRCPG AYRALRGLRS FMSANTFGNA GFSVLLPGAR
LEGRCGPTNA RVRCHLGLKI PPGCELVVGG EPQCWAEGHC LLVDDSFLHT VAHNGSPEDG
PRVVFIVDLW HPNVAGAERQ ALDFVFAPDP
