ST6B1_HUMAN
ID ST6B1_HUMAN Reviewed; 303 AA.
AC Q6IMI4; B2RTS7;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Sulfotransferase 6B1;
DE Short=ST6B1;
DE AltName: Full=Thyroxine sulfotransferase;
DE EC=2.8.2.n2 {ECO:0000250|UniProtKB:P0CC03};
GN Name=SULT6B1;
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 32-303, AND VARIANT PHE-150.
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 IDENTIFICATION (ISOFORMS 1 AND 2), AND ALTERNATIVE SPLICING.
RX PubMed=14676822; DOI=10.1038/sj.tpj.6500223;
RA Freimuth R.R., Wiepert M., Chute C.G., Wieben E.D., Weinshilboum R.M.;
RT "Human cytosolic sulfotransferase database mining: identification of seven
RT novel genes and pseudogenes.";
RL Pharmacogenomics J. 4:54-65(2004).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=19505954; DOI=10.1093/jb/mvp087;
RA Takahashi S., Sakakibara Y., Mishiro E., Kouriki H., Nobe R., Kurogi K.,
RA Yasuda S., Liu M.C., Suiko M.;
RT "Molecular cloning, expression and characterization of a novel mouse SULT6
RT cytosolic sulfotransferase.";
RL J. Biochem. 146:399-405(2009).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the sulfate conjugation of
CC thyroxine. Involved in the metabolism of thyroxine (By similarity).
CC {ECO:0000250|UniProtKB:P0CC03}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + thyroxine = adenosine 3',5'-
CC bisphosphate + H(+) + thyroxine sulfate; Xref=Rhea:RHEA:26422,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:58910, ChEBI:CHEBI:305790; EC=2.8.2.n2;
CC Evidence={ECO:0000250|UniProtKB:P0CC03};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P0CC03}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q6IMI4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6IMI4-2; Sequence=VSP_013111;
CC -!- TISSUE SPECIFICITY: Specifically expressed in kidney and testis.
CC {ECO:0000269|PubMed:19505954}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI40798.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=DAA01772.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC007899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC140797; AAI40798.1; ALT_INIT; mRNA.
DR EMBL; BK001437; DAA01772.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_001027549.1; NM_001032377.1.
DR AlphaFoldDB; Q6IMI4; -.
DR SMR; Q6IMI4; -.
DR BioGRID; 133902; 8.
DR STRING; 9606.ENSP00000384950; -.
DR DrugBank; DB12471; Ibrexafungerp.
DR DrugBank; DB00968; Methyldopa.
DR DrugBank; DB00960; Pindolol.
DR DrugBank; DB00871; Terbutaline.
DR iPTMnet; Q6IMI4; -.
DR PhosphoSitePlus; Q6IMI4; -.
DR BioMuta; SULT6B1; -.
DR DMDM; 269849654; -.
DR PaxDb; Q6IMI4; -.
DR PeptideAtlas; Q6IMI4; -.
DR PRIDE; Q6IMI4; -.
DR ProteomicsDB; 66427; -. [Q6IMI4-1]
DR Antibodypedia; 29393; 25 antibodies from 14 providers.
DR DNASU; 391365; -.
DR Ensembl; ENST00000535679.6; ENSP00000444081.1; ENSG00000138068.12. [Q6IMI4-1]
DR GeneID; 391365; -.
DR KEGG; hsa:391365; -.
DR MANE-Select; ENST00000535679.6; ENSP00000444081.1; NM_001367551.1; NP_001354480.1.
DR UCSC; uc002rpu.4; human. [Q6IMI4-1]
DR CTD; 391365; -.
DR GeneCards; SULT6B1; -.
DR HGNC; HGNC:33433; SULT6B1.
DR HPA; ENSG00000138068; Tissue enhanced (brain, testis).
DR MIM; 617152; gene.
DR neXtProt; NX_Q6IMI4; -.
DR VEuPathDB; HostDB:ENSG00000138068; -.
DR eggNOG; KOG1584; Eukaryota.
DR GeneTree; ENSGT00940000159084; -.
DR InParanoid; Q6IMI4; -.
DR OMA; HLFFTYQ; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; Q6IMI4; -.
DR TreeFam; TF321745; -.
DR BRENDA; 2.8.2.2; 2681.
DR PathwayCommons; Q6IMI4; -.
DR Reactome; R-HSA-156584; Cytosolic sulfonation of small molecules.
DR BioGRID-ORCS; 391365; 18 hits in 1057 CRISPR screens.
DR GenomeRNAi; 391365; -.
DR Pharos; Q6IMI4; Tdark.
DR PRO; PR:Q6IMI4; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q6IMI4; protein.
DR Bgee; ENSG00000138068; Expressed in apex of heart and 67 other tissues.
DR ExpressionAtlas; Q6IMI4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0051923; P:sulfation; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..303
FT /note="Sulfotransferase 6B1"
FT /id="PRO_0000085171"
FT ACT_SITE 118
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 65..70
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 140
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 148
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 203
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 237..242
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 259..261
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT VAR_SEQ 105..208
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_013111"
FT VARIANT 61
FT /note="A -> T (in dbSNP:rs45552433)"
FT /id="VAR_052522"
FT VARIANT 75
FT /note="V -> D (in dbSNP:rs45626240)"
FT /id="VAR_052523"
FT VARIANT 88
FT /note="K -> E (in dbSNP:rs45493492)"
FT /id="VAR_052524"
FT VARIANT 150
FT /note="L -> F (in dbSNP:rs10205833)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_059853"
FT VARIANT 167
FT /note="E -> V (in dbSNP:rs7425881)"
FT /id="VAR_052525"
FT VARIANT 181
FT /note="R -> S (in dbSNP:rs45439591)"
FT /id="VAR_052526"
FT VARIANT 296
FT /note="K -> R (in dbSNP:rs45495394)"
FT /id="VAR_052527"
SQ SEQUENCE 303 AA; 34919 MW; 4FE556266BD2C7A7 CRC64;
MADKSKFIEY IDEALEKSKE TALSHLFFTY QGIPYPITMC TSETFQALDT FEARHDDIVL
ASYPKCGSNW ILHIVSELIY AVSKKKYKYP EFPVLECGDS EKYQRMKGFP SPRILATHLH
YDKLPGSIFE NKAKILVIFR NPKDTAVSFL HFHNDVPDIP SYGSWDEFFR QFMKGQVSWG
RYFDFAINWN KHLDGDNVKF ILYEDLKENL AAGIKQIAEF LGFFLTGEQI QTISVQSTFQ
AMRAKSQDTH GAVGPFLFRK GEVGDWKNLF SEIQNQEMDE KFKECLAGTS LGAKLKYESY
CQG
