PAPS2_HUMAN
ID PAPS2_HUMAN Reviewed; 614 AA.
AC O95340; Q9BZL2; Q9P0G6; Q9UHM1; Q9UKD3; Q9UP30;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2002, sequence version 2.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2 {ECO:0000305|PubMed:23824674};
DE Short=PAPS synthase 2;
DE Short=PAPSS 2;
DE AltName: Full=Sulfurylase kinase 2;
DE Short=SK 2;
DE Short=SK2;
DE Includes:
DE RecName: Full=Sulfate adenylyltransferase {ECO:0000305|PubMed:23824674};
DE EC=2.7.7.4 {ECO:0000305|PubMed:11773860, ECO:0000305|PubMed:19474428, ECO:0000305|PubMed:23824674, ECO:0000305|PubMed:25594860};
DE AltName: Full=ATP-sulfurylase;
DE AltName: Full=Sulfate adenylate transferase;
DE Short=SAT;
DE Includes:
DE RecName: Full=Adenylyl-sulfate kinase {ECO:0000305|PubMed:23824674};
DE EC=2.7.1.25 {ECO:0000305|PubMed:11773860, ECO:0000305|PubMed:19474428, ECO:0000305|PubMed:23824674, ECO:0000305|PubMed:25594860};
DE AltName: Full=3'-phosphoadenosine-5'-phosphosulfate synthase;
DE AltName: Full=APS kinase;
DE AltName: Full=Adenosine-5'-phosphosulfate 3'-phosphotransferase;
DE AltName: Full=Adenylylsulfate 3'-phosphotransferase;
GN Name=PAPSS2; Synonyms=ATPSK2;
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 A), FUNCTION, AND INVOLVEMENT IN BCYM4.
RC TISSUE=Fetal cartilage;
RX PubMed=9771708; DOI=10.1038/2458;
RA ul Haque M.F., King L.M., Krakow D., Cantor R.M., Rusiniak M.E.,
RA Swank R.T., Superti-Furga A., Haque S., Abbas H., Ahmad W., Ahmad M.,
RA Cohn D.H.;
RT "Mutations in orthologous genes in human spondyloepimetaphyseal dysplasia
RT and the brachymorphic mouse.";
RL Nat. Genet. 20:157-162(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RA Franzon V.L., Gibson M.A., Hatzinikolas G., Cleary E.G., Woolatt E.,
RA Sutherland G.R.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RA Fuda H., Shimizu C., Strott C.A.;
RT "Human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase:
RT differential expression of isoforms and effect of polymorphisms on
RT activity.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
RX PubMed=10679223; DOI=10.1006/bbrc.2000.2123;
RA Xu Z.-H., Otterness D.M., Freimuth R.R., Carlini E.J., Wood T.C.,
RA Mitchell S., Moon E., Kim U.-J., Xu J.-P., Siciliano M.J.,
RA Weinshilboum R.M.;
RT "Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 (PAPSS1) and
RT PAPSS2: gene cloning, characterization and chromosomal localization.";
RL Biochem. Biophys. Res. Commun. 268:437-444(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RC TISSUE=Liver;
RX PubMed=10559207; DOI=10.1074/jbc.274.47.33306;
RA Kurima K., Singh B., Schwartz N.B.;
RT "Genomic organization of the mouse and human genes encoding the ATP
RT sulfurylase/adenosine 5'-phosphosulfate kinase isoform SK2.";
RL J. Biol. Chem. 274:33306-33312(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RA Venkatachalam K.V., Fuda H., Strott C.A.;
RT "3'-phosphoadenosine 5'-phosphosulfate synthase 2b isoform.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC TISSUE=Colon;
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 [8]
RP INVOLVEMENT IN BCYM4.
RX PubMed=9714015;
RX DOI=10.1002/(sici)1096-8628(19980806)78:5<468::aid-ajmg13>3.0.co;2-d;
RA Ahmad M., Haque M.F., Ahmad W., Abbas H., Haque S., Krakow D., Rimoin D.L.,
RA Lachman R.S., Cohn D.H.;
RT "Distinct, autosomal recessive form of spondyloepimetaphyseal dysplasia
RT segregating in an inbred Pakistani kindred.";
RL Am. J. Med. Genet. 78:468-473(1998).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, VARIANT BCYM4 ARG-48,
RP CHARACTERIZATION OF VARIANT BCYM4 ARG-48, AND TISSUE SPECIFICITY.
RX PubMed=19474428; DOI=10.1056/nejmoa0810489;
RA Noordam C., Dhir V., McNelis J.C., Schlereth F., Hanley N.A., Krone N.,
RA Smeitink J.A., Smeets R., Sweep F.C., Claahsen-van der Grinten H.L.,
RA Arlt W.;
RT "Inactivating PAPSS2 mutations in a patient with premature pubarche.";
RL N. Engl. J. Med. 360:2310-2318(2009).
RN [10]
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 [11]
RP 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., 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 [12]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 21-218 IN COMPLEX WITH ATP.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the kinase domain of PAPSS 2.";
RL Submitted (SEP-2005) to the PDB data bank.
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, VARIANTS LYS-10; LEU-281; MET-291
RP AND LYS-432, AND CHARACTERIZATION OF VARIANTS LYS-10 AND MET-291.
RX PubMed=11773860; DOI=10.1097/00008571-200201000-00003;
RA Xu Z.-H., Freimuth R.R., Eckloff B., Wieben E., Weinshilboum R.M.;
RT "Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 2 (PAPSS2)
RT pharmacogenetics: gene resequencing, genetic polymorphisms and functional
RT characterization of variant allozymes.";
RL Pharmacogenetics 12:11-21(2002).
RN [14]
RP INVOLVEMENT IN BCYM4.
RX PubMed=23633440; DOI=10.1002/ajmg.a.35906;
RA Tueysuez B., Yilmaz S., Guel E., Kolb L., Bilguvar K., Evliyaoglu O.,
RA Guenel M.;
RT "Spondyloepimetaphyseal dysplasia Pakistani type: expansion of the
RT phenotype.";
RL Am. J. Med. Genet. A 161A:1300-1308(2013).
RN [15]
RP VARIANTS BCYM4 TYR-43 AND GLN-76, CHARACTERIZATION OF VARIANTS BCYM4 TYR-43
RP AND GLN-76, VARIANT LYS-183, CHARACTERIZATION OF VARIANT LYS-183, FUNCTION,
RP CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=23824674; DOI=10.1002/humu.22377;
RA Iida A., Simsek-Kiper P.O., Mizumoto S., Hoshino T., Elcioglu N.,
RA Horemuzova E., Geiberger S., Yesil G., Kayserili H., Utine G.E.,
RA Boduroglu K., Watanabe S., Ohashi H., Alanay Y., Sugahara K., Nishimura G.,
RA Ikegawa S.;
RT "Clinical and radiographic features of the autosomal recessive form of
RT brachyolmia caused by PAPSS2 mutations.";
RL Hum. Mutat. 34:1381-1386(2013).
RN [16]
RP VARIANT BCYM4 ASP-270, CHARACTERIZATION OF VARIANTS BCYM4 ARG-48 AND
RP ASP-270, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=25594860; DOI=10.1210/jc.2014-3556;
RA Oostdijk W., Idkowiak J., Mueller J.W., House P.J., Taylor A.E.,
RA O'Reilly M.W., Hughes B.A., de Vries M.C., Kant S.G., Santen G.W.,
RA Verkerk A.J., Uitterlinden A.G., Wit J.M., Losekoot M., Arlt W.;
RT "PAPSS2 deficiency causes androgen excess via impaired DHEA sulfation - in
RT vitro and in vivo studies in a family harboring two novel PAPSS2
RT mutations.";
RL J. Clin. Endocrinol. Metab. 2015:JC20143556-JC20143556(2015).
CC -!- FUNCTION: Bifunctional enzyme with both ATP sulfurylase and APS kinase
CC activity, which mediates two steps in the sulfate activation pathway.
CC The first step is the transfer of a sulfate group to ATP to yield
CC adenosine 5'-phosphosulfate (APS), and the second step is the transfer
CC of a phosphate group from ATP to APS yielding 3'-
CC phosphoadenylylsulfate/PAPS, the activated sulfate donor used by
CC sulfotransferases (PubMed:19474428, PubMed:11773860, PubMed:23824674,
CC PubMed:25594860). In mammals, PAPS is the sole source of sulfate while
CC APS appears to only be an intermediate in the sulfate-activation
CC pathway (PubMed:19474428, PubMed:11773860, PubMed:23824674,
CC PubMed:25594860). Plays indirectly an important role in skeletogenesis
CC during postnatal growth (PubMed:9771708). {ECO:0000269|PubMed:11773860,
CC ECO:0000269|PubMed:19474428, ECO:0000269|PubMed:23824674,
CC ECO:0000269|PubMed:25594860, ECO:0000269|PubMed:9771708}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate +
CC diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58243; EC=2.7.7.4; Evidence={ECO:0000305|PubMed:11773860,
CC ECO:0000305|PubMed:19474428, ECO:0000305|PubMed:23824674,
CC ECO:0000305|PubMed:25594860};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18134;
CC Evidence={ECO:0000305|PubMed:19474428};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate
CC + ADP + H(+); Xref=Rhea:RHEA:24152, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:456216; EC=2.7.1.25;
CC Evidence={ECO:0000305|PubMed:11773860, ECO:0000305|PubMed:19474428,
CC ECO:0000305|PubMed:23824674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24153;
CC Evidence={ECO:0000305|PubMed:19474428};
CC -!- PATHWAY: Sulfur metabolism; sulfate assimilation.
CC {ECO:0000269|PubMed:11773860, ECO:0000269|PubMed:19474428,
CC ECO:0000269|PubMed:23824674, ECO:0000269|PubMed:25594860}.
CC -!- INTERACTION:
CC O95340; Q96LK0: CEP19; NbExp=6; IntAct=EBI-1053912, EBI-741885;
CC O95340; O75031: HSF2BP; NbExp=3; IntAct=EBI-1053912, EBI-7116203;
CC O95340; Q96CV9: OPTN; NbExp=3; IntAct=EBI-1053912, EBI-748974;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=O95340-1; Sequence=Displayed;
CC Name=B;
CC IsoId=O95340-2; Sequence=VSP_001259;
CC -!- TISSUE SPECIFICITY: Expressed in cartilage and adrenal gland.
CC {ECO:0000269|PubMed:19474428}.
CC -!- DISEASE: Brachyolmia type 4 with mild epiphyseal and metaphyseal
CC changes (BCYM4) [MIM:612847]: A form of brachyolmia, a clinically and
CC genetically heterogeneous skeletal dysplasia primarily affecting the
CC spine and characterized by a short trunk, short stature, and
CC platyspondyly. BCYM4 is an autosomal recessive form with mild
CC epiphyseal and metaphyseal changes. Clinical features include short
CC stature evidenced at birth, short and bowed lower limbs, mild
CC brachydactyly, kyphoscoliosis, abnormal gait, enlarged knee joints.
CC Some BCYM4 patients may manifest premature pubarche and
CC hyperandrogenism associated with skeletal dysplasia and short stature.
CC {ECO:0000269|PubMed:19474428, ECO:0000269|PubMed:23633440,
CC ECO:0000269|PubMed:23824674, ECO:0000269|PubMed:25594860,
CC ECO:0000269|PubMed:9714015, ECO:0000269|PubMed:9771708}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: In the N-terminal section; belongs to the APS kinase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the sulfate
CC adenylyltransferase family. {ECO:0000305}.
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DR EMBL; AF091242; AAC64583.1; -; mRNA.
DR EMBL; AF074331; AAD38423.1; -; mRNA.
DR EMBL; AF313907; AAK00296.1; -; mRNA.
DR EMBL; AF160509; AAF40307.2; -; Genomic_DNA.
DR EMBL; AF160503; AAF40307.2; JOINED; Genomic_DNA.
DR EMBL; AF160504; AAF40307.2; JOINED; Genomic_DNA.
DR EMBL; AF160505; AAF40307.2; JOINED; Genomic_DNA.
DR EMBL; AF160506; AAF40307.2; JOINED; Genomic_DNA.
DR EMBL; AF160507; AAF40307.2; JOINED; Genomic_DNA.
DR EMBL; AF160508; AAF40307.2; JOINED; Genomic_DNA.
DR EMBL; AF173365; AAF12761.1; -; mRNA.
DR EMBL; AF150754; AAF20366.2; -; mRNA.
DR EMBL; BC009894; AAH09894.1; -; mRNA.
DR CCDS; CCDS44453.1; -. [O95340-2]
DR CCDS; CCDS7385.1; -. [O95340-1]
DR RefSeq; NP_001015880.1; NM_001015880.1. [O95340-2]
DR RefSeq; NP_004661.2; NM_004670.3. [O95340-1]
DR PDB; 2AX4; X-ray; 2.50 A; A/B/C/D=21-218.
DR PDB; 7FH3; X-ray; 1.80 A; A/B=223-614.
DR PDB; 7FHA; X-ray; 2.00 A; A/B=223-614.
DR PDBsum; 2AX4; -.
DR PDBsum; 7FH3; -.
DR PDBsum; 7FHA; -.
DR AlphaFoldDB; O95340; -.
DR SMR; O95340; -.
DR BioGRID; 114521; 41.
DR IntAct; O95340; 8.
DR STRING; 9606.ENSP00000406157; -.
DR BindingDB; O95340; -.
DR ChEMBL; CHEMBL4105790; -.
DR GlyGen; O95340; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95340; -.
DR MetOSite; O95340; -.
DR PhosphoSitePlus; O95340; -.
DR SwissPalm; O95340; -.
DR BioMuta; PAPSS2; -.
DR EPD; O95340; -.
DR jPOST; O95340; -.
DR MassIVE; O95340; -.
DR MaxQB; O95340; -.
DR PaxDb; O95340; -.
DR PeptideAtlas; O95340; -.
DR PRIDE; O95340; -.
DR ProteomicsDB; 50808; -. [O95340-1]
DR ProteomicsDB; 50809; -. [O95340-2]
DR TopDownProteomics; O95340-1; -. [O95340-1]
DR Antibodypedia; 30161; 253 antibodies from 25 providers.
DR DNASU; 9060; -.
DR Ensembl; ENST00000361175.8; ENSP00000354436.4; ENSG00000198682.13. [O95340-1]
DR Ensembl; ENST00000456849.2; ENSP00000406157.1; ENSG00000198682.13. [O95340-2]
DR GeneID; 9060; -.
DR KEGG; hsa:9060; -.
DR MANE-Select; ENST00000456849.2; ENSP00000406157.1; NM_001015880.2; NP_001015880.1. [O95340-2]
DR UCSC; uc001kew.4; human. [O95340-1]
DR CTD; 9060; -.
DR DisGeNET; 9060; -.
DR GeneCards; PAPSS2; -.
DR HGNC; HGNC:8604; PAPSS2.
DR HPA; ENSG00000198682; Tissue enhanced (adrenal).
DR MalaCards; PAPSS2; -.
DR MIM; 603005; gene.
DR MIM; 612847; phenotype.
DR neXtProt; NX_O95340; -.
DR OpenTargets; ENSG00000198682; -.
DR Orphanet; 448242; Autosomal recessive brachyolmia.
DR Orphanet; 93282; Spondyloepimetaphyseal dysplasia, PAPSS2 type.
DR PharmGKB; PA383; -.
DR VEuPathDB; HostDB:ENSG00000198682; -.
DR eggNOG; KOG4238; Eukaryota.
DR GeneTree; ENSGT00390000009613; -.
DR HOGENOM; CLU_009463_3_0_1; -.
DR OMA; DQMYERP; -.
DR OrthoDB; 528280at2759; -.
DR PhylomeDB; O95340; -.
DR TreeFam; TF313143; -.
DR BioCyc; MetaCyc:HS07544-MON; -.
DR BRENDA; 2.7.1.25; 2681.
DR BRENDA; 2.7.7.4; 2681.
DR PathwayCommons; O95340; -.
DR Reactome; R-HSA-174362; Transport and synthesis of PAPS.
DR Reactome; R-HSA-2408550; Metabolism of ingested H2SeO4 and H2SeO3 into H2Se.
DR Reactome; R-HSA-3560796; Defective PAPSS2 causes SEMD-PA.
DR SABIO-RK; O95340; -.
DR SignaLink; O95340; -.
DR UniPathway; UPA00097; -.
DR BioGRID-ORCS; 9060; 13 hits in 1071 CRISPR screens.
DR ChiTaRS; PAPSS2; human.
DR EvolutionaryTrace; O95340; -.
DR GeneWiki; PAPSS2; -.
DR GenomeRNAi; 9060; -.
DR Pharos; O95340; Tbio.
DR PRO; PR:O95340; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O95340; protein.
DR Bgee; ENSG00000198682; Expressed in tibia and 187 other tissues.
DR ExpressionAtlas; O95340; baseline and differential.
DR Genevisible; O95340; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; ISS:UniProtKB.
DR GO; GO:0050428; P:3'-phosphoadenosine 5'-phosphosulfate biosynthetic process; IMP:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; IEA:Ensembl.
DR GO; GO:0060348; P:bone development; IEA:Ensembl.
DR GO; GO:0042445; P:hormone metabolic process; IMP:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0000103; P:sulfate assimilation; IMP:UniProtKB.
DR CDD; cd02027; APSK; 1.
DR CDD; cd00517; ATPS; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR InterPro; IPR002891; APS_kinase.
DR InterPro; IPR025980; ATP-Sase_PUA-like_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR024951; Sulfurylase_cat_dom.
DR InterPro; IPR002650; Sulphate_adenylyltransferase.
DR Pfam; PF01747; ATP-sulfurylase; 1.
DR Pfam; PF14306; PUA_2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00455; apsK; 1.
DR TIGRFAMs; TIGR00339; sopT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Disease variant; Dwarfism;
KW Kinase; Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..614
FT /note="Bifunctional 3'-phosphoadenosine 5'-phosphosulfate
FT synthase 2"
FT /id="PRO_0000105961"
FT REGION 1..215
FT /note="Adenylyl-sulfate kinase"
FT /evidence="ECO:0000305"
FT REGION 224..614
FT /note="Sulfate adenylyltransferase"
FT /evidence="ECO:0000305"
FT BINDING 52..57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:2AX4"
FT BINDING 79..82
FT /ligand="adenosine 5'-phosphosulfate"
FT /ligand_id="ChEBI:CHEBI:58243"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 91
FT /ligand="adenosine 5'-phosphosulfate"
FT /ligand_id="ChEBI:CHEBI:58243"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 96..99
FT /ligand="adenosine 5'-phosphosulfate"
FT /ligand_id="ChEBI:CHEBI:58243"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 122..123
FT /ligand="adenosine 5'-phosphosulfate"
FT /ligand_id="ChEBI:CHEBI:58243"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 161
FT /ligand="adenosine 5'-phosphosulfate"
FT /ligand_id="ChEBI:CHEBI:58243"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 174..175
FT /ligand="adenosine 5'-phosphosulfate"
FT /ligand_id="ChEBI:CHEBI:58243"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:2AX4"
FT BINDING 409..412
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 511..515
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 553
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT VAR_SEQ 288
FT /note="D -> DGMALP (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10559207, ECO:0000303|Ref.6"
FT /id="VSP_001259"
FT VARIANT 10
FT /note="E -> K (decreased sulfate assimilation;
FT dbSNP:rs17173698)"
FT /evidence="ECO:0000269|PubMed:11773860"
FT /id="VAR_029136"
FT VARIANT 43
FT /note="C -> Y (in BCYM4; reduced 3'-phosphoadenosine 5'-
FT phosphosulfate biosynthetic process)"
FT /evidence="ECO:0000269|PubMed:23824674"
FT /id="VAR_073026"
FT VARIANT 48
FT /note="T -> R (in BCYM4; patient with premature pubarche
FT and hyperandrogenism; decreased sulfate assimilation;
FT increases ubiquitin-dependent protein instability;
FT dbSNP:rs121908951)"
FT /evidence="ECO:0000269|PubMed:19474428,
FT ECO:0000269|PubMed:25594860"
FT /id="VAR_063049"
FT VARIANT 76
FT /note="L -> Q (in BCYM4; reduced 3'-phosphoadenosine 5'-
FT phosphosulfate biosynthetic process)"
FT /evidence="ECO:0000269|PubMed:23824674"
FT /id="VAR_073027"
FT VARIANT 183
FT /note="E -> K (no effect on 3'-phosphoadenosine 5'-
FT phosphosulfate biosynthetic process; dbSNP:rs774709274)"
FT /evidence="ECO:0000269|PubMed:23824674"
FT /id="VAR_073028"
FT VARIANT 270
FT /note="G -> D (in BCYM4; increases ubiquitin-dependent
FT protein instability; dbSNP:rs138943074)"
FT /evidence="ECO:0000269|PubMed:25594860"
FT /id="VAR_073029"
FT VARIANT 281
FT /note="M -> L (in dbSNP:rs45624631)"
FT /evidence="ECO:0000269|PubMed:11773860"
FT /id="VAR_029137"
FT VARIANT 291
FT /note="V -> M (decreased sulfate assimilation;
FT dbSNP:rs45467596)"
FT /evidence="ECO:0000269|PubMed:11773860"
FT /id="VAR_022077"
FT VARIANT 432
FT /note="R -> K (in dbSNP:rs17129133)"
FT /evidence="ECO:0000269|PubMed:11773860"
FT /id="VAR_029138"
FT CONFLICT 166
FT /note="R -> K (in Ref. 2; AAD38423)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="E -> G (in Ref. 3; AAK00296)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="R -> C (in Ref. 1; AAC64583)"
FT /evidence="ECO:0000305"
FT CONFLICT 567
FT /note="P -> L (in Ref. 2; AAD38423)"
FT /evidence="ECO:0000305"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:2AX4"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:2AX4"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:2AX4"
FT HELIX 55..68
FT /evidence="ECO:0007829|PDB:2AX4"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:2AX4"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:2AX4"
FT TURN 82..88
FT /evidence="ECO:0007829|PDB:2AX4"
FT HELIX 93..112
FT /evidence="ECO:0007829|PDB:2AX4"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:2AX4"
FT HELIX 126..138
FT /evidence="ECO:0007829|PDB:2AX4"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:2AX4"
FT HELIX 152..158
FT /evidence="ECO:0007829|PDB:2AX4"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:2AX4"
FT HELIX 163..168
FT /evidence="ECO:0007829|PDB:2AX4"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:2AX4"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:2AX4"
FT HELIX 199..212
FT /evidence="ECO:0007829|PDB:2AX4"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:7FH3"
FT HELIX 234..241
FT /evidence="ECO:0007829|PDB:7FH3"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:7FH3"
FT HELIX 251..261
FT /evidence="ECO:0007829|PDB:7FH3"
FT TURN 262..267
FT /evidence="ECO:0007829|PDB:7FH3"
FT HELIX 274..283
FT /evidence="ECO:0007829|PDB:7FH3"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:7FHA"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:7FH3"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:7FH3"
FT HELIX 304..310
FT /evidence="ECO:0007829|PDB:7FH3"
FT STRAND 314..320
FT /evidence="ECO:0007829|PDB:7FH3"
FT STRAND 323..335
FT /evidence="ECO:0007829|PDB:7FH3"
FT HELIX 338..346
FT /evidence="ECO:0007829|PDB:7FH3"
FT HELIX 354..360
FT /evidence="ECO:0007829|PDB:7FH3"
FT STRAND 364..375
FT /evidence="ECO:0007829|PDB:7FH3"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:7FH3"
FT HELIX 390..399
FT /evidence="ECO:0007829|PDB:7FH3"
FT STRAND 403..412
FT /evidence="ECO:0007829|PDB:7FH3"
FT HELIX 416..431
FT /evidence="ECO:0007829|PDB:7FH3"
FT STRAND 437..444
FT /evidence="ECO:0007829|PDB:7FH3"
FT HELIX 455..467
FT /evidence="ECO:0007829|PDB:7FH3"
FT HELIX 473..475
FT /evidence="ECO:0007829|PDB:7FH3"
FT STRAND 476..478
FT /evidence="ECO:0007829|PDB:7FH3"
FT HELIX 489..502
FT /evidence="ECO:0007829|PDB:7FH3"
FT STRAND 506..509
FT /evidence="ECO:0007829|PDB:7FH3"
FT TURN 520..522
FT /evidence="ECO:0007829|PDB:7FH3"
FT STRAND 524..527
FT /evidence="ECO:0007829|PDB:7FH3"
FT HELIX 531..538
FT /evidence="ECO:0007829|PDB:7FH3"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:7FH3"
FT STRAND 553..556
FT /evidence="ECO:0007829|PDB:7FH3"
FT TURN 557..560
FT /evidence="ECO:0007829|PDB:7FH3"
FT STRAND 561..564
FT /evidence="ECO:0007829|PDB:7FH3"
FT HELIX 567..572
FT /evidence="ECO:0007829|PDB:7FH3"
FT HELIX 578..586
FT /evidence="ECO:0007829|PDB:7FH3"
FT HELIX 598..610
FT /evidence="ECO:0007829|PDB:7FH3"
SQ SEQUENCE 614 AA; 69501 MW; 52F4B6D972DDA91E CRC64;
MSGIKKQKTE NQQKSTNVVY QAHHVSRNKR GQVVGTRGGF RGCTVWLTGL SGAGKTTISF
ALEEYLVSHA IPCYSLDGDN VRHGLNRNLG FSPGDREENI RRIAEVAKLF ADAGLVCITS
FISPFAKDRE NARKIHESAG LPFFEIFVDA PLNICESRDV KGLYKRARAG EIKGFTGIDS
DYEKPETPER VLKTNLSTVS DCVHQVVELL QEQNIVPYTI IKDIHELFVP ENKLDHVRAE
AETLPSLSIT KLDLQWVQVL SEGWATPLKG FMREKEYLQV MHFDTLLDDG VINMSIPIVL
PVSAEDKTRL EGCSKFVLAH GGRRVAILRD AEFYEHRKEE RCSRVWGTTC TKHPHIKMVM
ESGDWLVGGD LQVLEKIRWN DGLDQYRLTP LELKQKCKEM NADAVFAFQL RNPVHNGHAL
LMQDTRRRLL ERGYKHPVLL LHPLGGWTKD DDVPLDWRMK QHAAVLEEGV LDPKSTIVAI
FPSPMLYAGP TEVQWHCRSR MIAGANFYIV GRDPAGMPHP ETKKDLYEPT HGGKVLSMAP
GLTSVEIIPF RVAAYNKAKK AMDFYDPARH NEFDFISGTR MRKLAREGEN PPDGFMAPKA
WKVLTDYYRS LEKN
