BPNT1_HUMAN
ID BPNT1_HUMAN Reviewed; 308 AA.
AC O95861; A8K7C8; B4DPS5; B4DUS9; D3DTA9; Q8WVL5; Q9UGJ3;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=3'(2'),5'-bisphosphate nucleotidase 1;
DE EC=3.1.3.7;
DE AltName: Full=Bisphosphate 3'-nucleotidase 1;
DE AltName: Full=PAP-inositol 1,4-phosphatase;
DE Short=PIP;
GN Name=BPNT1;
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 [MRNA] (ISOFORM 1), FUNCTION, ACTIVITY REGULATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=10224133; DOI=10.1074/jbc.274.19.13619;
RA Spiegelberg B.D., Xiong J.-P., Smith J.J., Gu R.F., York J.D.;
RT "Cloning and characterization of a mammalian lithium-sensitive bisphosphate
RT 3'-nucleotidase inhibited by inositol 1,4-bisphosphate.";
RL J. Biol. Chem. 274:13619-13628(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=B-cell;
RA Yenush L., Gil-Mascarell M., Serrano R., Rodriguez P.L.;
RT "Hydrolysis of inositol-1,4-bisphosphate by human and yeast lithium
RT sensitive 3'-phosphoadenosine 5'-phosphate nucleotidases.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Skeletal muscle;
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
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., Buerckstuemmer T.,
RA 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122, AND IDENTIFICATION BY
RP 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., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
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., Ayoub D.,
RA 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 [14]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 6-308 IN COMPLEX WITH MAGNESIUM
RP IONS AND AMP.
RG Structural genomics consortium (SGC);
RT "Human 3'(2'), 5'-bisphosphate nucleotidase 1 (BPNT1) in complex with AMP,
RT PO4 and magnesium.";
RL Submitted (APR-2009) to the PDB data bank.
CC -!- FUNCTION: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to
CC adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine
CC 5'- phosphate (PAP) to AMP. Has 1000-fold lower activity towards
CC inositol 1,4-bisphosphate (Ins(1,4)P2) and inositol 1,3,4-trisphosphate
CC (Ins(1,3,4)P3), but does not hydrolyze Ins(1)P, Ins(3,4)P2,
CC Ins(1,3,4,5)P4 or InsP6. {ECO:0000269|PubMed:10224133}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 3',5'-bisphosphate + H2O = AMP + phosphate;
CC Xref=Rhea:RHEA:10040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; EC=3.1.3.7;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Uncompetitive inhibition by micromolar
CC concentrations of lithium. Competitive inhibition by inositol 1,4-
CC bisphosphate. {ECO:0000269|PubMed:10224133}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O95861-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95861-2; Sequence=VSP_009937;
CC Name=3;
CC IsoId=O95861-3; Sequence=VSP_054807;
CC Name=4;
CC IsoId=O95861-4; Sequence=VSP_054808;
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney, liver, pancreas and
CC heart. Detected at lower levels in brain, placenta, lung and skeletal
CC muscle. {ECO:0000269|PubMed:10224133}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; AF125042; AAD17329.1; -; mRNA.
DR EMBL; AJ249339; CAB65115.1; -; mRNA.
DR EMBL; AK291943; BAF84632.1; -; mRNA.
DR EMBL; AK298476; BAG60687.1; -; mRNA.
DR EMBL; AK300777; BAG62441.1; -; mRNA.
DR EMBL; AC103590; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471100; EAW93306.1; -; Genomic_DNA.
DR EMBL; CH471100; EAW93308.1; -; Genomic_DNA.
DR EMBL; BC017801; AAH17801.1; -; mRNA.
DR CCDS; CCDS41469.1; -. [O95861-1]
DR CCDS; CCDS65787.1; -. [O95861-3]
DR CCDS; CCDS65788.1; -. [O95861-4]
DR RefSeq; NP_001273078.1; NM_001286149.1. [O95861-3]
DR RefSeq; NP_001273079.1; NM_001286150.1. [O95861-4]
DR RefSeq; NP_001273080.1; NM_001286151.1. [O95861-3]
DR RefSeq; NP_006076.4; NM_006085.5. [O95861-1]
DR RefSeq; XP_005273057.1; XM_005273000.4. [O95861-1]
DR RefSeq; XP_016855532.1; XM_017000043.1. [O95861-4]
DR PDB; 2WEF; X-ray; 1.80 A; A=6-308.
DR PDBsum; 2WEF; -.
DR AlphaFoldDB; O95861; -.
DR SMR; O95861; -.
DR BioGRID; 115653; 66.
DR IntAct; O95861; 53.
DR STRING; 9606.ENSP00000446828; -.
DR DEPOD; BPNT1; -.
DR GlyGen; O95861; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95861; -.
DR MetOSite; O95861; -.
DR PhosphoSitePlus; O95861; -.
DR BioMuta; BPNT1; -.
DR REPRODUCTION-2DPAGE; IPI00410214; -.
DR EPD; O95861; -.
DR jPOST; O95861; -.
DR MassIVE; O95861; -.
DR MaxQB; O95861; -.
DR PaxDb; O95861; -.
DR PeptideAtlas; O95861; -.
DR PRIDE; O95861; -.
DR ProteomicsDB; 4810; -.
DR ProteomicsDB; 51094; -. [O95861-1]
DR ProteomicsDB; 51095; -. [O95861-2]
DR ProteomicsDB; 5212; -.
DR Antibodypedia; 34625; 226 antibodies from 29 providers.
DR DNASU; 10380; -.
DR Ensembl; ENST00000322067.12; ENSP00000318852.7; ENSG00000162813.18. [O95861-1]
DR Ensembl; ENST00000414869.6; ENSP00000410348.2; ENSG00000162813.18. [O95861-4]
DR Ensembl; ENST00000469520.6; ENSP00000446828.1; ENSG00000162813.18. [O95861-1]
DR Ensembl; ENST00000544404.5; ENSP00000444398.1; ENSG00000162813.18. [O95861-3]
DR GeneID; 10380; -.
DR KEGG; hsa:10380; -.
DR MANE-Select; ENST00000322067.12; ENSP00000318852.7; NM_006085.6; NP_006076.4.
DR UCSC; uc010puh.3; human. [O95861-1]
DR CTD; 10380; -.
DR DisGeNET; 10380; -.
DR GeneCards; BPNT1; -.
DR HGNC; HGNC:1096; BPNT1.
DR HPA; ENSG00000162813; Low tissue specificity.
DR MIM; 604053; gene.
DR neXtProt; NX_O95861; -.
DR OpenTargets; ENSG00000162813; -.
DR PharmGKB; PA25407; -.
DR VEuPathDB; HostDB:ENSG00000162813; -.
DR eggNOG; KOG3099; Eukaryota.
DR GeneTree; ENSGT00940000157359; -.
DR HOGENOM; CLU_034742_2_0_1; -.
DR OMA; QTEADRC; -.
DR OrthoDB; 1096950at2759; -.
DR PhylomeDB; O95861; -.
DR TreeFam; TF314300; -.
DR BRENDA; 3.1.3.7; 2681.
DR PathwayCommons; O95861; -.
DR Reactome; R-HSA-156584; Cytosolic sulfonation of small molecules.
DR SignaLink; O95861; -.
DR BioGRID-ORCS; 10380; 24 hits in 1077 CRISPR screens.
DR ChiTaRS; BPNT1; human.
DR EvolutionaryTrace; O95861; -.
DR GenomeRNAi; 10380; -.
DR Pharos; O95861; Tbio.
DR PRO; PR:O95861; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O95861; protein.
DR Bgee; ENSG00000162813; Expressed in islet of Langerhans and 168 other tissues.
DR ExpressionAtlas; O95861; baseline and differential.
DR Genevisible; O95861; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; TAS:Reactome.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR Pfam; PF00459; Inositol_P; 1.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Hydrolase; Lithium;
KW Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..308
FT /note="3'(2'),5'-bisphosphate nucleotidase 1"
FT /id="PRO_0000142527"
FT BINDING 74
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 117
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 119..122
FT /ligand="substrate"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 120
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 195..198
FT /ligand="substrate"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 247
FT /ligand="substrate"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 122
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 244
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0S1"
FT VAR_SEQ 1..55
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054807"
FT VAR_SEQ 76..111
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054808"
FT VAR_SEQ 277..308
FT /note="KHMNSAGVLATLRNYDYYASRVPESIKNALVP -> SHRTWPKPDFFRAQFF
FT LESHSCFSRNFKNVSTPIKNIYDVIIYAYETDL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009937"
FT CONFLICT 221
FT /note="A -> V (in Ref. 6; AAH17801)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="G -> S (in Ref. 2; CAB65115)"
FT /evidence="ECO:0000305"
FT HELIX 7..32
FT /evidence="ECO:0007829|PDB:2WEF"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:2WEF"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:2WEF"
FT HELIX 49..65
FT /evidence="ECO:0007829|PDB:2WEF"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:2WEF"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:2WEF"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:2WEF"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:2WEF"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:2WEF"
FT STRAND 112..120
FT /evidence="ECO:0007829|PDB:2WEF"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:2WEF"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:2WEF"
FT STRAND 134..141
FT /evidence="ECO:0007829|PDB:2WEF"
FT STRAND 144..152
FT /evidence="ECO:0007829|PDB:2WEF"
FT TURN 153..158
FT /evidence="ECO:0007829|PDB:2WEF"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:2WEF"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:2WEF"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:2WEF"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:2WEF"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:2WEF"
FT HELIX 201..208
FT /evidence="ECO:0007829|PDB:2WEF"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:2WEF"
FT HELIX 221..229
FT /evidence="ECO:0007829|PDB:2WEF"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:2WEF"
FT HELIX 245..257
FT /evidence="ECO:0007829|PDB:2WEF"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:2WEF"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:2WEF"
FT HELIX 291..295
FT /evidence="ECO:0007829|PDB:2WEF"
FT HELIX 300..305
FT /evidence="ECO:0007829|PDB:2WEF"
SQ SEQUENCE 308 AA; 33392 MW; A5952F5E31C8CFCB CRC64;
MASSNTVLMR LVASAYSIAQ KAGMIVRRVI AEGDLGIVEK TCATDLQTKA DRLAQMSICS
SLARKFPKLT IIGEEDLPSE EVDQELIEDS QWEEILKQPC PSQYSAIKEE DLVVWVDPLD
GTKEYTEGLL DNVTVLIGIA YEGKAIAGVI NQPYYNYEAG PDAVLGRTIW GVLGLGAFGF
QLKEVPAGKH IITTTRSHSN KLVTDCVAAM NPDAVLRVGG AGNKIIQLIE GKASAYVFAS
PGCKKWDTCA PEVILHAVGG KLTDIHGNVL QYHKDVKHMN SAGVLATLRN YDYYASRVPE
SIKNALVP
