GenomeNet

Database: UniProt
Entry: Q9UBQ7
LinkDB: Q9UBQ7
Original site: Q9UBQ7 
ID   GRHPR_HUMAN             Reviewed;         328 AA.
AC   Q9UBQ7; Q5T945; Q9H3E9; Q9H636; Q9UKX1;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   13-FEB-2019, entry version 172.
DE   RecName: Full=Glyoxylate reductase/hydroxypyruvate reductase;
DE            EC=1.1.1.79;
DE            EC=1.1.1.81;
GN   Name=GRHPR; Synonyms=GLXR; ORFNames=MSTP035;
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] (ISOFORM 1), AND SUBUNIT.
RC   TISSUE=Liver;
RX   PubMed=10524214; DOI=10.1016/S0167-4781(99)00105-0;
RA   Rumsby G., Cregeen D.P.;
RT   "Identification and expression of a cDNA for human
RT   hydroxypyruvate/glyoxylate reductase.";
RL   Biochim. Biophys. Acta 1446:383-388(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND INVOLVEMENT
RP   IN HP2.
RC   TISSUE=Liver;
RX   PubMed=10484776; DOI=10.1093/hmg/8.11.2063;
RA   Cramer S.D., Ferree P.M., Lin K., Milliner D.S., Holmes R.P.;
RT   "The gene encoding hydroxypyruvate reductase (GRHPR) is mutated in
RT   patients with primary hyperoxaluria type II.";
RL   Hum. Mol. Genet. 8:2063-2069(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Aorta;
RA   Liu B., Liu Y.Q., Wang X.Y., Zhao B., Sheng H., Zhao X.W., Liu S.,
RA   Xu Y.Y., Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J.,
RA   Cao H.Q., Zhao Y., Liu L.S., Ding J.F., Gao R.L., Wu Q.Y., Qiang B.Q.,
RA   Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.;
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Small intestine, and Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA   Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA   Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA   Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA   Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA   Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA   Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA   Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA   Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA   Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA   Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA   McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA   Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA   Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA   Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA   Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA   Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA   Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA   Rogers J., Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Kidney;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 45-328 (ISOFORM 1), AND TISSUE
RP   SPECIFICITY.
RX   PubMed=10679197; DOI=10.1006/bbrc.2000.2122;
RA   Huang T., Yang W., Pereira A.C., Craigen W.J., Shih V.E.;
RT   "Cloning and characterization of a putative human D-2-hydroxyacid
RT   dehydrogenase in chromosome 9q.";
RL   Biochem. Biophys. Res. Commun. 268:298-301(2000).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-272 AND THR-298,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA   Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH NADP AND
RP   SUBSTRATE, AND SUBUNIT.
RX   PubMed=16756993; DOI=10.1016/j.jmb.2006.05.018;
RA   Booth M.P.S., Conners R., Rumsby G., Brady R.L.;
RT   "Structural basis of substrate specificity in human glyoxylate
RT   reductase/hydroxypyruvate reductase.";
RL   J. Mol. Biol. 360:178-189(2006).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 2-328.
RG   Center for eukaryotic structural genomics (CESG);
RT   "Crystal structure of a glyoxylate/hydroxypyruvate reductase from Homo
RT   sapiens.";
RL   Submitted (FEB-2009) to the PDB data bank.
CC   -!- FUNCTION: Enzyme with hydroxy-pyruvate reductase, glyoxylate
CC       reductase and D-glycerate dehydrogenase enzymatic activities.
CC       Reduces hydroxypyruvate to D-glycerate, glyoxylate to glycolate
CC       oxidizes D-glycerate to hydroxypyruvate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycolate + NADP(+) = glyoxylate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:10992, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805,
CC         ChEBI:CHEBI:36655, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.79;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-glycerate + NAD(+) = 3-hydroxypyruvate + H(+) + NADH;
CC         Xref=Rhea:RHEA:17905, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC         ChEBI:CHEBI:17180, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.81;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-glycerate + NADP(+) = 3-hydroxypyruvate + H(+) +
CC         NADPH; Xref=Rhea:RHEA:18657, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16659, ChEBI:CHEBI:17180, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.1.1.81;
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10524214,
CC       ECO:0000269|PubMed:16756993}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9UBQ7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UBQ7-2; Sequence=VSP_057016, VSP_057017, VSP_057018;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Most abundantly expressed in the
CC       liver. {ECO:0000269|PubMed:10679197}.
CC   -!- DISEASE: Hyperoxaluria primary 2 (HP2) [MIM:260000]: A disorder
CC       characterized by elevated urinary excretion of oxalate and L-
CC       glycerate, progressive tissue accumulation of insoluble calcium
CC       oxalate, nephrolithiasis, nephrocalcinosis, and end-stage renal
CC       disease. {ECO:0000269|PubMed:10484776}. Note=The disease is caused
CC       by mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD54066.1; Type=Frameshift; Positions=109, 137; Evidence={ECO:0000305};
CC       Sequence=AAG39286.1; Type=Frameshift; Positions=237; Evidence={ECO:0000305};
DR   EMBL; AF134895; AAF00111.1; -; mRNA.
DR   EMBL; AF146018; AAD45886.1; -; mRNA.
DR   EMBL; AF146689; AAD46517.1; -; Genomic_DNA.
DR   EMBL; AF113215; AAG39286.1; ALT_FRAME; mRNA.
DR   EMBL; AK026287; BAB15430.1; -; mRNA.
DR   EMBL; AK315690; BAG38053.1; -; mRNA.
DR   EMBL; AL158155; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471071; EAW58284.1; -; Genomic_DNA.
DR   EMBL; CH471071; EAW58285.1; -; Genomic_DNA.
DR   EMBL; BC000605; AAH00605.1; -; mRNA.
DR   EMBL; AF113251; AAD54066.1; ALT_FRAME; mRNA.
DR   CCDS; CCDS6609.1; -. [Q9UBQ7-1]
DR   PIR; JC7190; JC7190.
DR   RefSeq; NP_036335.1; NM_012203.1. [Q9UBQ7-1]
DR   UniGene; Hs.155742; -.
DR   PDB; 2GCG; X-ray; 2.20 A; A/B/C/D=1-328.
DR   PDB; 2H1S; X-ray; 2.45 A; A/B/C/D=2-328.
DR   PDB; 2Q50; X-ray; 2.45 A; A/B/C/D=2-328.
DR   PDB; 2WWR; X-ray; 2.82 A; A/B/C/D=1-328.
DR   PDBsum; 2GCG; -.
DR   PDBsum; 2H1S; -.
DR   PDBsum; 2Q50; -.
DR   PDBsum; 2WWR; -.
DR   ProteinModelPortal; Q9UBQ7; -.
DR   SMR; Q9UBQ7; -.
DR   BioGrid; 114781; 37.
DR   IntAct; Q9UBQ7; 5.
DR   STRING; 9606.ENSP00000313432; -.
DR   iPTMnet; Q9UBQ7; -.
DR   PhosphoSitePlus; Q9UBQ7; -.
DR   SwissPalm; Q9UBQ7; -.
DR   BioMuta; GRHPR; -.
DR   DMDM; 47116943; -.
DR   REPRODUCTION-2DPAGE; IPI00037448; -.
DR   UCD-2DPAGE; Q9UBQ7; -.
DR   EPD; Q9UBQ7; -.
DR   jPOST; Q9UBQ7; -.
DR   PaxDb; Q9UBQ7; -.
DR   PeptideAtlas; Q9UBQ7; -.
DR   PRIDE; Q9UBQ7; -.
DR   ProteomicsDB; 84034; -.
DR   DNASU; 9380; -.
DR   Ensembl; ENST00000318158; ENSP00000313432; ENSG00000137106. [Q9UBQ7-1]
DR   Ensembl; ENST00000494290; ENSP00000432021; ENSG00000137106. [Q9UBQ7-2]
DR   GeneID; 9380; -.
DR   KEGG; hsa:9380; -.
DR   UCSC; uc003zzu.2; human. [Q9UBQ7-1]
DR   CTD; 9380; -.
DR   DisGeNET; 9380; -.
DR   EuPathDB; HostDB:ENSG00000137106.17; -.
DR   GeneCards; GRHPR; -.
DR   GeneReviews; GRHPR; -.
DR   HGNC; HGNC:4570; GRHPR.
DR   HPA; HPA022971; -.
DR   MalaCards; GRHPR; -.
DR   MIM; 260000; phenotype.
DR   MIM; 604296; gene.
DR   neXtProt; NX_Q9UBQ7; -.
DR   OpenTargets; ENSG00000137106; -.
DR   Orphanet; 93599; Primary hyperoxaluria type 2.
DR   PharmGKB; PA28965; -.
DR   eggNOG; KOG0069; Eukaryota.
DR   eggNOG; COG1052; LUCA.
DR   GeneTree; ENSGT00940000158578; -.
DR   HOGENOM; HOG000136702; -.
DR   HOVERGEN; HBG051838; -.
DR   InParanoid; Q9UBQ7; -.
DR   KO; K00049; -.
DR   OMA; KWIAHNG; -.
DR   OrthoDB; 1378766at2759; -.
DR   PhylomeDB; Q9UBQ7; -.
DR   TreeFam; TF324791; -.
DR   BioCyc; MetaCyc:HS06275-MONOMER; -.
DR   Reactome; R-HSA-389661; Glyoxylate metabolism and glycine degradation.
DR   SABIO-RK; Q9UBQ7; -.
DR   ChiTaRS; GRHPR; human.
DR   EvolutionaryTrace; Q9UBQ7; -.
DR   GeneWiki; GRHPR; -.
DR   GenomeRNAi; 9380; -.
DR   PRO; PR:Q9UBQ7; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   Bgee; ENSG00000137106; Expressed in 237 organ(s), highest expression level in liver.
DR   ExpressionAtlas; Q9UBQ7; baseline and differential.
DR   Genevisible; Q9UBQ7; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
DR   GO; GO:0031406; F:carboxylic acid binding; IEA:Ensembl.
DR   GO; GO:0008465; F:glycerate dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0030267; F:glyoxylate reductase (NADP) activity; IDA:UniProtKB.
DR   GO; GO:0016618; F:hydroxypyruvate reductase activity; IDA:UniProtKB.
DR   GO; GO:0051287; F:NAD binding; TAS:UniProtKB.
DR   GO; GO:0070402; F:NADPH binding; IDA:UniProtKB.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
DR   GO; GO:0043648; P:dicarboxylic acid metabolic process; IEA:Ensembl.
DR   GO; GO:0007588; P:excretion; IMP:UniProtKB.
DR   GO; GO:0046487; P:glyoxylate metabolic process; IDA:UniProtKB.
DR   GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
DR   GO; GO:0051259; P:protein complex oligomerization; IDA:UniProtKB.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Complete proteome; NADP;
KW   Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome.
FT   CHAIN         1    328       Glyoxylate reductase/hydroxypyruvate
FT                                reductase.
FT                                /FTId=PRO_0000075944.
FT   NP_BIND     162    164       NADP. {ECO:0000269|PubMed:16756993}.
FT   NP_BIND     185    188       NADP. {ECO:0000269|PubMed:16756993}.
FT   REGION       83     84       Substrate binding.
FT                                {ECO:0000269|PubMed:16756993}.
FT   REGION      293    296       Substrate binding.
FT                                {ECO:0000269|PubMed:16756993}.
FT   ACT_SITE    293    293       Proton donor.
FT                                {ECO:0000305|PubMed:16756993}.
FT   BINDING     217    217       NADP. {ECO:0000269|PubMed:16756993}.
FT   BINDING     243    243       NADP; via carbonyl oxygen.
FT                                {ECO:0000269|PubMed:16756993}.
FT   BINDING     245    245       Substrate. {ECO:0000269|PubMed:16756993}.
FT   BINDING     269    269       Substrate. {ECO:0000269|PubMed:16756993}.
FT   BINDING     295    295       NADP; via amide nitrogen.
FT                                {ECO:0000269|PubMed:16756993}.
FT   SITE        274    274       Raises pKa of active site His.
FT                                {ECO:0000305|PubMed:16756993}.
FT   MOD_RES      36     36       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     272    272       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     298    298       Phosphothreonine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   VAR_SEQ       1     21       MRPVRLMKVFVTRRIPAEGRV -> MLGGVPTLCGTGNETW
FT                                TLLAL (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_057016.
FT   VAR_SEQ      22    164       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_057017.
FT   VAR_SEQ     246    328       GDVVNQDDLYQALASGKIAAAGLDVTSPEPLPTNHPLLTLK
FT                                NCVILPHIGSATHRTRNTMSLLAANNLLAGLRGEPMPSELK
FT                                L -> YPRATLPSKPGEEPSPLLPSGDFLPRGLLVRPQAEL
FT                                AGFHKPNNQLRNSWEYTRPPYREEEPSEWAWPVCFSAVAPT
FT                                RRGLAHSSVASGSVPREPLQAHYPPPQRAGLEDLKGPLEAA
FT                                SHTAEPGFVWLWFSDTLNLMLLGGQTLKLTWS (in
FT                                isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_057018.
FT   VARIANT     170    170       R -> Q (in dbSNP:rs12002324).
FT                                /FTId=VAR_032762.
FT   STRAND        7     13       {ECO:0000244|PDB:2GCG}.
FT   HELIX        17     25       {ECO:0000244|PDB:2GCG}.
FT   STRAND       29     33       {ECO:0000244|PDB:2GCG}.
FT   STRAND       36     38       {ECO:0000244|PDB:2GCG}.
FT   HELIX        42     49       {ECO:0000244|PDB:2GCG}.
FT   STRAND       53     57       {ECO:0000244|PDB:2GCG}.
FT   HELIX        65     71       {ECO:0000244|PDB:2GCG}.
FT   STRAND       77     83       {ECO:0000244|PDB:2GCG}.
FT   HELIX        90     95       {ECO:0000244|PDB:2GCG}.
FT   STRAND       99    101       {ECO:0000244|PDB:2GCG}.
FT   HELIX       108    123       {ECO:0000244|PDB:2GCG}.
FT   HELIX       126    134       {ECO:0000244|PDB:2GCG}.
FT   STRAND      143    146       {ECO:0000244|PDB:2Q50}.
FT   STRAND      155    159       {ECO:0000244|PDB:2GCG}.
FT   HELIX       163    172       {ECO:0000244|PDB:2GCG}.
FT   HELIX       173    175       {ECO:0000244|PDB:2GCG}.
FT   STRAND      179    186       {ECO:0000244|PDB:2GCG}.
FT   HELIX       189    193       {ECO:0000244|PDB:2GCG}.
FT   TURN        194    196       {ECO:0000244|PDB:2GCG}.
FT   STRAND      197    199       {ECO:0000244|PDB:2Q50}.
FT   HELIX       202    208       {ECO:0000244|PDB:2GCG}.
FT   STRAND      210    214       {ECO:0000244|PDB:2GCG}.
FT   TURN        220    224       {ECO:0000244|PDB:2GCG}.
FT   HELIX       228    233       {ECO:0000244|PDB:2GCG}.
FT   STRAND      239    242       {ECO:0000244|PDB:2GCG}.
FT   HELIX       246    248       {ECO:0000244|PDB:2GCG}.
FT   HELIX       251    259       {ECO:0000244|PDB:2GCG}.
FT   STRAND      262    269       {ECO:0000244|PDB:2GCG}.
FT   STRAND      272    275       {ECO:0000244|PDB:2GCG}.
FT   HELIX       281    284       {ECO:0000244|PDB:2GCG}.
FT   STRAND      288    290       {ECO:0000244|PDB:2GCG}.
FT   HELIX       299    318       {ECO:0000244|PDB:2GCG}.
SQ   SEQUENCE   328 AA;  35668 MW;  68A0E311AA4E5650 CRC64;
     MRPVRLMKVF VTRRIPAEGR VALARAADCE VEQWDSDEPI PAKELERGVA GAHGLLCLLS
     DHVDKRILDA AGANLKVIST MSVGIDHLAL DEIKKRGIRV GYTPDVLTDT TAELAVSLLL
     TTCRRLPEAI EEVKNGGWTS WKPLWLCGYG LTQSTVGIIG LGRIGQAIAR RLKPFGVQRF
     LYTGRQPRPE EAAEFQAEFV STPELAAQSD FIVVACSLTP ATEGLCNKDF FQKMKETAVF
     INISRGDVVN QDDLYQALAS GKIAAAGLDV TSPEPLPTNH PLLTLKNCVI LPHIGSATHR
     TRNTMSLLAA NNLLAGLRGE PMPSELKL
//
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