ID   SHBG_HUMAN              Reviewed;         402 AA.
AC   P04278; B0FWH4; B4DYU0; E9PGW1; F5H5Z8; I3L1N7; P14689; Q16616; Q3MIL0;
AC   Q6ISD2;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 2.
DT   27-MAR-2024, entry version 216.
DE   RecName: Full=Sex hormone-binding globulin {ECO:0000305};
DE            Short=SHBG;
DE   AltName: Full=Sex steroid-binding protein;
DE            Short=SBP;
DE   AltName: Full=Testis-specific androgen-binding protein;
DE            Short=ABP;
DE   AltName: Full=Testosterone-estradiol-binding globulin;
DE            Short=TeBG;
DE   AltName: Full=Testosterone-estrogen-binding globulin;
DE   Flags: Precursor;
GN   Name=SHBG {ECO:0000312|HGNC:HGNC:10839};
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 [GENOMIC DNA], NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2),
RP   AND ALTERNATIVE SPLICING.
RC   TISSUE=Testis;
RX   PubMed=2587256; DOI=10.1093/nar/17.22.9245;
RA   Gershagen S., Lundwall A., Fernlund P.;
RT   "Characterization of the human sex hormone binding globulin (SHBG) gene and
RT   demonstration of two transcripts in both liver and testis.";
RL   Nucleic Acids Res. 17:9245-9258(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   TISSUE=Testis;
RX   PubMed=2608061; DOI=10.1210/mend-3-11-1869;
RA   Hammond G.L., Underhill D.A., Rykse H.M., Smith C.L.;
RT   "The human sex hormone-binding globulin gene contains exons for androgen-
RT   binding protein and two other testicular messenger RNAs.";
RL   Mol. Endocrinol. 3:1869-1876(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX   PubMed=15028279; DOI=10.1016/j.ygeno.2003.09.023;
RA   Jin P., Fu G.K., Wilson A.D., Yang J., Chien D., Hawkins P.R., Au-Young J.,
RA   Stuve L.L.;
RT   "PCR isolation and cloning of novel splice variant mRNAs from known drug
RT   target genes.";
RL   Genomics 83:566-571(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 22-402 (ISOFORM 1).
RC   TISSUE=Liver;
RX   PubMed=3569533; DOI=10.1016/0014-5793(87)80121-7;
RA   Hammond G.L., Underhill D.A., Smith C.L., Goping I.S., Harley M.J.,
RA   Musto N.A., Cheng C.Y., Bardin C.W.;
RT   "The cDNA-deduced primary structure of human sex hormone-binding globulin
RT   and location of its steroid-binding domain.";
RL   FEBS Lett. 215:100-104(1987).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 28-402 (ISOFORM 4).
RC   TISSUE=Liver;
RA   Kahn S.M., Nakhla A.M., Hryb D.J., Rosner W., Romas N.A.;
RT   "Human sex hormone-binding globulin gene transcript expression in liver,
RT   prostate, breast, testis, and brain- multiple promoters and complex
RT   alternative splicing.";
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 47-402 (ISOFORM 1).
RC   TISSUE=Liver;
RX   PubMed=2956126; DOI=10.1016/0014-5793(87)80890-6;
RA   Gershagen S., Fernlund P., Lundwall A.;
RT   "A cDNA coding for human sex hormone binding globulin. Homology to vitamin
RT   K-dependent protein S.";
RL   FEBS Lett. 220:129-135(1987).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 121-402 (ISOFORM 1).
RC   TISSUE=Liver;
RX   PubMed=2956125; DOI=10.1016/0014-5793(87)80261-2;
RA   Que B.G., Petra P.H.;
RT   "Characterization of a cDNA coding for sex steroid-binding protein of human
RT   plasma.";
RL   FEBS Lett. 219:405-409(1987).
RN   [11]
RP   PROTEIN SEQUENCE OF 30-54.
RX   PubMed=3702459; DOI=10.1016/0022-4731(86)90442-5;
RA   Hammond G.L., Robinson P.A., Sugino H., Ward D.N., Finne J.;
RT   "Physicochemical characteristics of human sex hormone binding globulin:
RT   evidence for two identical subunits.";
RL   J. Steroid Biochem. 24:815-824(1986).
RN   [12]
RP   PROTEIN SEQUENCE OF 30-402.
RX   PubMed=3542030; DOI=10.1021/bi00371a048;
RA   Walsh K.A., Titani K., Takio K., Kumar S., Hayes R., Petra P.H.;
RT   "Amino acid sequence of the sex steroid binding protein of human blood
RT   plasma.";
RL   Biochemistry 25:7584-7590(1986).
RN   [13]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-380.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA   Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [14]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-380.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [15]
RP   VARIANT ASN-356, CHARACTERIZATION OF VARIANT ASN-356, AND GLYCOSYLATION.
RX   PubMed=1400872; DOI=10.1210/jcem.75.4.1400872;
RA   Power S.G.A., Bocchinfuso W.P., Pallesen M., Warmels-Rodenhiser S.,
RA   Van Baelen H., Hammond G.L.;
RT   "Molecular analyses of a human sex hormone-binding globulin variant:
RT   evidence for an additional carbohydrate chain.";
RL   J. Clin. Endocrinol. Metab. 75:1066-1070(1992).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 42-211.
RX   PubMed=10675319; DOI=10.1093/emboj/19.4.504;
RA   Grishkovskaya I., Avvakumov G.V., Sklenar G., Dales D., Hammond G.L.,
RA   Muller Y.A.;
RT   "Crystal structure of human sex hormone-binding globulin: steroid transport
RT   by a laminin G-like domain.";
RL   EMBO J. 19:504-512(2000).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 42-218.
RX   PubMed=12065592; DOI=10.1074/jbc.m203999200;
RA   Grishkovskaya I., Avvakumov G.V., Hammond G.L., Catalano M.G., Muller Y.A.;
RT   "Steroid ligands bind human sex hormone-binding globulin in specific
RT   orientations and produce distinct changes in protein conformation.";
RL   J. Biol. Chem. 277:32086-32093(2002).
RN   [18]
RP   VARIANT ASN-356.
RX   PubMed=7714097; DOI=10.1210/jcem.80.4.7714097;
RA   Hardy D.O., Carino C., Catterall J.F., Larrea F.;
RT   "Molecular characterization of a genetic variant of the steroid hormone-
RT   binding globulin gene in heterozygous subjects.";
RL   J. Clin. Endocrinol. Metab. 80:1253-1256(1995).
RN   [19]
RP   VARIANTS HIS-25 AND ASN-356.
RX   PubMed=10391209; DOI=10.1038/10290;
RA   Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA   Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA   Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA   Lander E.S.;
RT   "Characterization of single-nucleotide polymorphisms in coding regions of
RT   human genes.";
RL   Nat. Genet. 22:231-238(1999).
RN   [20]
RP   ERRATUM OF PUBMED:10391209.
RA   Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA   Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA   Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA   Lander E.S.;
RL   Nat. Genet. 23:373-373(1999).
CC   -!- FUNCTION: Functions as an androgen transport protein, but may also be
CC       involved in receptor mediated processes. Each dimer binds one molecule
CC       of steroid. Specific for 5-alpha-dihydrotestosterone, testosterone, and
CC       17-beta-estradiol. Regulates the plasma metabolic clearance rate of
CC       steroid hormones by controlling their plasma concentration.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=In testis, it is
CC       synthesized by the Sertoli cells, secreted into the lumen of the
CC       seminiferous tubule and transported to the epididymis. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=1; Synonyms=SHBG, SHBGr-1;
CC         IsoId=P04278-1; Sequence=Displayed;
CC       Name=2; Synonyms=Sex hormone binding globulin-gene-related protein
CC       (SHBGgrp), SHBGr-2;
CC         IsoId=P04278-2; Sequence=VSP_061578, VSP_006091, VSP_006092;
CC       Name=3;
CC         IsoId=P04278-3; Sequence=VSP_006091, VSP_006092;
CC       Name=4;
CC         IsoId=P04278-4; Sequence=VSP_045358;
CC       Name=5;
CC         IsoId=P04278-5; Sequence=VSP_045376;
CC   -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are present in liver and
CC       testis.
CC   -!- PTM: Variant Asn-356 contains one N-linked (GlcNAc...) at position 356.
CC       {ECO:0000269|PubMed:1400872, ECO:0000269|PubMed:16335952,
CC       ECO:0000269|PubMed:19159218}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA29309.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAA34400.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Androgen-binding protein entry;
CC       URL="https://en.wikipedia.org/wiki/Androgen-binding_protein";
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/42286/SHBG";
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DR   EMBL; X16349; CAA34398.1; -; Genomic_DNA.
DR   EMBL; X16350; CAA34399.1; -; Genomic_DNA.
DR   EMBL; X16351; CAA34400.1; ALT_INIT; mRNA.
DR   EMBL; M31651; AAC18778.1; -; Genomic_DNA.
DR   EMBL; CD013955; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK302603; BAG63852.1; -; mRNA.
DR   EMBL; AC007421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC069597; AAH69597.1; -; mRNA.
DR   EMBL; BC101785; AAI01786.1; -; mRNA.
DR   EMBL; BC112186; AAI12187.1; -; mRNA.
DR   EMBL; X05403; CAA28987.1; -; mRNA.
DR   EMBL; EU352661; ABY67999.1; -; mRNA.
DR   EMBL; X05885; CAA29309.1; ALT_FRAME; mRNA.
DR   EMBL; X05792; CAA29234.1; -; mRNA.
DR   CCDS; CCDS11117.1; -. [P04278-1]
DR   CCDS; CCDS54082.1; -. [P04278-3]
DR   CCDS; CCDS54083.1; -. [P04278-4]
DR   CCDS; CCDS58513.1; -. [P04278-5]
DR   CCDS; CCDS73962.1; -. [P04278-2]
DR   PIR; S09606; BOHUS.
DR   RefSeq; NP_001031.2; NM_001040.4. [P04278-1]
DR   RefSeq; NP_001139751.1; NM_001146279.2. [P04278-5]
DR   RefSeq; NP_001139752.1; NM_001146280.2. [P04278-3]
DR   RefSeq; NP_001139753.1; NM_001146281.2. [P04278-4]
DR   RefSeq; NP_001276042.1; NM_001289113.1.
DR   RefSeq; NP_001276043.1; NM_001289114.1.
DR   RefSeq; NP_001276044.1; NM_001289115.1. [P04278-2]
DR   RefSeq; NP_001276045.1; NM_001289116.1.
DR   PDB; 1D2S; X-ray; 1.55 A; A=42-217.
DR   PDB; 1F5F; X-ray; 1.70 A; A=30-234.
DR   PDB; 1KDK; X-ray; 1.70 A; A=41-217.
DR   PDB; 1KDM; X-ray; 2.35 A; A=41-217.
DR   PDB; 1LHN; X-ray; 2.00 A; A=30-218.
DR   PDB; 1LHO; X-ray; 2.00 A; A=30-218.
DR   PDB; 1LHU; X-ray; 1.80 A; A=30-218.
DR   PDB; 1LHV; X-ray; 2.00 A; A=30-218.
DR   PDB; 1LHW; X-ray; 1.75 A; A=30-218.
DR   PDB; 6PYA; X-ray; 1.71 A; A=30-234.
DR   PDB; 6PYB; X-ray; 1.80 A; A=30-234.
DR   PDB; 6PYF; X-ray; 1.73 A; A=30-234.
DR   PDB; 6ULB; X-ray; 1.75 A; A=30-234.
DR   PDBsum; 1D2S; -.
DR   PDBsum; 1F5F; -.
DR   PDBsum; 1KDK; -.
DR   PDBsum; 1KDM; -.
DR   PDBsum; 1LHN; -.
DR   PDBsum; 1LHO; -.
DR   PDBsum; 1LHU; -.
DR   PDBsum; 1LHV; -.
DR   PDBsum; 1LHW; -.
DR   PDBsum; 6PYA; -.
DR   PDBsum; 6PYB; -.
DR   PDBsum; 6PYF; -.
DR   PDBsum; 6ULB; -.
DR   AlphaFoldDB; P04278; -.
DR   SMR; P04278; -.
DR   BioGRID; 112359; 64.
DR   IntAct; P04278; 5.
DR   STRING; 9606.ENSP00000369816; -.
DR   BindingDB; P04278; -.
DR   ChEMBL; CHEMBL3305; -.
DR   DrugBank; DB02342; 2-Methoxyestradiol.
DR   DrugBank; DB04429; 4'-Hydroxyflavanone.
DR   DrugBank; DB03882; 5-Alpha-Androstane-3-Beta,17beta-Diol.
DR   DrugBank; DB03926; 5alpha-androstane-3beta,17alpha-diol.
DR   DrugBank; DB04468; Afimoxifene.
DR   DrugBank; DB00882; Clomifene.
DR   DrugBank; DB00286; Conjugated estrogens.
DR   DrugBank; DB01406; Danazol.
DR   DrugBank; DB00080; Daptomycin.
DR   DrugBank; DB00304; Desogestrel.
DR   DrugBank; DB00890; Dienestrol.
DR   DrugBank; DB00255; Diethylstilbestrol.
DR   DrugBank; DB11221; Dioxybenzone.
DR   DrugBank; DB00858; Drostanolone.
DR   DrugBank; DB11674; Equol.
DR   DrugBank; DB00783; Estradiol.
DR   DrugBank; DB13952; Estradiol acetate.
DR   DrugBank; DB13953; Estradiol benzoate.
DR   DrugBank; DB13954; Estradiol cypionate.
DR   DrugBank; DB13955; Estradiol dienanthate.
DR   DrugBank; DB13956; Estradiol valerate.
DR   DrugBank; DB04573; Estriol.
DR   DrugBank; DB14641; Estriol tripropionate.
DR   DrugBank; DB00655; Estrone.
DR   DrugBank; DB04574; Estrone sulfate.
DR   DrugBank; DB00977; Ethinylestradiol.
DR   DrugBank; DB00294; Etonogestrel.
DR   DrugBank; DB15690; Fluoroestradiol F-18.
DR   DrugBank; DB01185; Fluoxymesterone.
DR   DrugBank; DB01645; Genistein.
DR   DrugBank; DB11619; Gestrinone.
DR   DrugBank; DB01094; Hesperetin.
DR   DrugBank; DB00741; Hydrocortisone.
DR   DrugBank; DB14538; Hydrocortisone aceponate.
DR   DrugBank; DB14539; Hydrocortisone acetate.
DR   DrugBank; DB14540; Hydrocortisone butyrate.
DR   DrugBank; DB14541; Hydrocortisone cypionate.
DR   DrugBank; DB14542; Hydrocortisone phosphate.
DR   DrugBank; DB14543; Hydrocortisone probutate.
DR   DrugBank; DB14544; Hydrocortisone valerate.
DR   DrugBank; DB01026; Ketoconazole.
DR   DrugBank; DB00367; Levonorgestrel.
DR   DrugBank; DB00179; Masoprocol.
DR   DrugBank; DB09124; Medrogestone.
DR   DrugBank; DB06710; Methyltestosterone.
DR   DrugBank; DB00648; Mitotane.
DR   DrugBank; DB08804; Nandrolone decanoate.
DR   DrugBank; DB03467; Naringenin.
DR   DrugBank; DB00717; Norethisterone.
DR   DrugBank; DB09371; Norethynodrel.
DR   DrugBank; DB00957; Norgestimate.
DR   DrugBank; DB06412; Oxymetholone.
DR   DrugBank; DB04824; Phenolphthalein.
DR   DrugBank; DB00396; Progesterone.
DR   DrugBank; DB04216; Quercetin.
DR   DrugBank; DB00421; Spironolactone.
DR   DrugBank; DB02901; Stanolone.
DR   DrugBank; DB13951; Stanolone acetate.
DR   DrugBank; DB00675; Tamoxifen.
DR   DrugBank; DB00624; Testosterone.
DR   DrugBank; DB13943; Testosterone cypionate.
DR   DrugBank; DB13944; Testosterone enanthate.
DR   DrugBank; DB01420; Testosterone propionate.
DR   DrugBank; DB13946; Testosterone undecanoate.
DR   DrugBank; DB00539; Toremifene.
DR   DrugBank; DB11478; Zeranol.
DR   DrugBank; DB01593; Zinc.
DR   DrugBank; DB14487; Zinc acetate.
DR   DrugBank; DB14533; Zinc chloride.
DR   DrugBank; DB14548; Zinc sulfate, unspecified form.
DR   DrugCentral; P04278; -.
DR   MoonDB; P04278; Predicted.
DR   GlyConnect; 562; 5 N-Linked glycans (2 sites), 3 O-Linked glycans (1 site).
DR   GlyCosmos; P04278; 3 sites, 18 glycans.
DR   GlyGen; P04278; 4 sites, 12 N-linked glycans (3 sites), 6 O-linked glycans (1 site).
DR   iPTMnet; P04278; -.
DR   PhosphoSitePlus; P04278; -.
DR   BioMuta; SHBG; -.
DR   DMDM; 134907; -.
DR   jPOST; P04278; -.
DR   MassIVE; P04278; -.
DR   PaxDb; 9606-ENSP00000369816; -.
DR   PeptideAtlas; P04278; -.
DR   ProteomicsDB; 20405; -.
DR   ProteomicsDB; 2543; -.
DR   ProteomicsDB; 27033; -.
DR   ProteomicsDB; 46697; -.
DR   ProteomicsDB; 51697; -. [P04278-1]
DR   ProteomicsDB; 51698; -. [P04278-2]
DR   ProteomicsDB; 5547; -.
DR   Antibodypedia; 24226; 819 antibodies from 36 providers.
DR   DNASU; 6462; -.
DR   Ensembl; ENST00000380450.9; ENSP00000369816.4; ENSG00000129214.15. [P04278-1]
DR   Ensembl; ENST00000416273.7; ENSP00000388867.3; ENSG00000129214.15. [P04278-3]
DR   Ensembl; ENST00000441599.6; ENSP00000393426.2; ENSG00000129214.15. [P04278-4]
DR   Ensembl; ENST00000574539.5; ENSP00000458181.1; ENSG00000129214.15. [P04278-2]
DR   Ensembl; ENST00000575903.5; ENSP00000458973.1; ENSG00000129214.15. [P04278-5]
DR   GeneID; 6462; -.
DR   KEGG; hsa:6462; -.
DR   MANE-Select; ENST00000380450.9; ENSP00000369816.4; NM_001040.5; NP_001031.2.
DR   UCSC; uc002gie.4; human. [P04278-1]
DR   AGR; HGNC:10839; -.
DR   CTD; 6462; -.
DR   DisGeNET; 6462; -.
DR   GeneCards; SHBG; -.
DR   HGNC; HGNC:10839; SHBG.
DR   HPA; ENSG00000129214; Tissue enriched (liver).
DR   MIM; 182205; gene.
DR   neXtProt; NX_P04278; -.
DR   OpenTargets; ENSG00000129214; -.
DR   PharmGKB; PA35745; -.
DR   VEuPathDB; HostDB:ENSG00000129214; -.
DR   eggNOG; KOG3927; Eukaryota.
DR   GeneTree; ENSGT00940000154035; -.
DR   HOGENOM; CLU_087489_0_0_1; -.
DR   InParanoid; P04278; -.
DR   OMA; FPLMQIS; -.
DR   OrthoDB; 5316510at2759; -.
DR   PhylomeDB; P04278; -.
DR   TreeFam; TF334367; -.
DR   PathwayCommons; P04278; -.
DR   SignaLink; P04278; -.
DR   BioGRID-ORCS; 6462; 19 hits in 1146 CRISPR screens.
DR   ChiTaRS; SHBG; human.
DR   EvolutionaryTrace; P04278; -.
DR   GeneWiki; Sex_hormone-binding_globulin; -.
DR   GenomeRNAi; 6462; -.
DR   Pharos; P04278; Tchem.
DR   PRO; PR:P04278; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; P04278; Protein.
DR   Bgee; ENSG00000129214; Expressed in right lobe of liver and 113 other cell types or tissues.
DR   ExpressionAtlas; P04278; baseline and differential.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR   GO; GO:0005497; F:androgen binding; TAS:ProtInc.
DR   GO; GO:0005496; F:steroid binding; IBA:GO_Central.
DR   CDD; cd00110; LamG; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001791; Laminin_G.
DR   PANTHER; PTHR24040; LAMININ G-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24040:SF3; SEX HORMONE-BINDING GLOBULIN; 1.
DR   Pfam; PF00054; Laminin_G_1; 1.
DR   SMART; SM00282; LamG; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 1.
DR   Genevisible; P04278; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Lipid-binding; Reference proteome; Repeat;
KW   Secreted; Signal; Steroid-binding.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000269|PubMed:3542030,
FT                   ECO:0000269|PubMed:3702459"
FT   CHAIN           30..402
FT                   /note="Sex hormone-binding globulin"
FT                   /evidence="ECO:0000269|PubMed:3542030"
FT                   /id="PRO_0000032557"
FT   DOMAIN          45..217
FT                   /note="Laminin G-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          224..390
FT                   /note="Laminin G-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   CARBOHYD        36
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:1400872"
FT                   /id="CAR_000174"
FT   CARBOHYD        380
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:3542030"
FT   CARBOHYD        396
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:1400872,
FT                   ECO:0000269|PubMed:3542030"
FT   DISULFID        193..217
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122,
FT                   ECO:0000269|PubMed:3542030"
FT   DISULFID        362..390
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122,
FT                   ECO:0000269|PubMed:3542030"
FT   VAR_SEQ         1..58
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_061578"
FT   VAR_SEQ         186..203
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_045376"
FT   VAR_SEQ         239..353
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|Ref.8"
FT                   /id="VSP_045358"
FT   VAR_SEQ         285..293
FT                   /note="KVVLSSGSG -> EKTLPPLFA (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15028279"
FT                   /id="VSP_006091"
FT   VAR_SEQ         294..402
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15028279"
FT                   /id="VSP_006092"
FT   VARIANT         22
FT                   /note="R -> H (in dbSNP:rs9282845)"
FT                   /id="VAR_022002"
FT   VARIANT         25
FT                   /note="R -> H (in dbSNP:rs6260)"
FT                   /evidence="ECO:0000269|PubMed:10391209"
FT                   /id="VAR_013946"
FT   VARIANT         185
FT                   /note="P -> L (in dbSNP:rs6258)"
FT                   /id="VAR_016182"
FT   VARIANT         356
FT                   /note="D -> N (generates a N-glycosylation site;
FT                   dbSNP:rs6259)"
FT                   /evidence="ECO:0000269|PubMed:10391209,
FT                   ECO:0000269|PubMed:1400872, ECO:0000269|PubMed:7714097"
FT                   /id="VAR_013129"
FT   CONFLICT        22
FT                   /note="R -> Q (in Ref. 6; CAA28987)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        334
FT                   /note="A -> L (in Ref. 2; AAC18778)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        336
FT                   /note="L -> S (in Ref. 2; AAC18778)"
FT                   /evidence="ECO:0000305"
FT   STRAND          44..47
FT                   /evidence="ECO:0007829|PDB:1D2S"
FT   STRAND          50..52
FT                   /evidence="ECO:0007829|PDB:6PYA"
FT   STRAND          56..62
FT                   /evidence="ECO:0007829|PDB:1D2S"
FT   HELIX           63..65
FT                   /evidence="ECO:0007829|PDB:1D2S"
FT   STRAND          70..78
FT                   /evidence="ECO:0007829|PDB:1D2S"
FT   STRAND          80..90
FT                   /evidence="ECO:0007829|PDB:1D2S"
FT   TURN            91..93
FT                   /evidence="ECO:0007829|PDB:1D2S"
FT   STRAND          94..101
FT                   /evidence="ECO:0007829|PDB:1D2S"
FT   STRAND          104..113
FT                   /evidence="ECO:0007829|PDB:1D2S"
FT   STRAND          115..119
FT                   /evidence="ECO:0007829|PDB:1D2S"
FT   STRAND          126..128
FT                   /evidence="ECO:0007829|PDB:1D2S"
FT   STRAND          130..137
FT                   /evidence="ECO:0007829|PDB:1D2S"
FT   STRAND          140..145
FT                   /evidence="ECO:0007829|PDB:1D2S"
FT   STRAND          148..153
FT                   /evidence="ECO:0007829|PDB:1D2S"
FT   HELIX           160..162
FT                   /evidence="ECO:0007829|PDB:6PYF"
FT   STRAND          167..174
FT                   /evidence="ECO:0007829|PDB:1D2S"
FT   HELIX           179..181
FT                   /evidence="ECO:0007829|PDB:1D2S"
FT   STRAND          182..184
FT                   /evidence="ECO:0007829|PDB:1D2S"
FT   STRAND          192..200
FT                   /evidence="ECO:0007829|PDB:1D2S"
FT   HELIX           202..204
FT                   /evidence="ECO:0007829|PDB:1D2S"
FT   STRAND          205..209
FT                   /evidence="ECO:0007829|PDB:1D2S"
FT   HELIX           211..213
FT                   /evidence="ECO:0007829|PDB:6PYA"
SQ   SEQUENCE   402 AA;  43779 MW;  5A3B1885E4E7A460 CRC64;
     MESRGPLATS RLLLLLLLLL LRHTRQGWAL RPVLPTQSAH DPPAVHLSNG PGQEPIAVMT
     FDLTKITKTS SSFEVRTWDP EGVIFYGDTN PKDDWFMLGL RDGRPEIQLH NHWAQLTVGA
     GPRLDDGRWH QVEVKMEGDS VLLEVDGEEV LRLRQVSGPL TSKRHPIMRI ALGGLLFPAS
     NLRLPLVPAL DGCLRRDSWL DKQAEISASA PTSLRSCDVE SNPGIFLPPG TQAEFNLRDI
     PQPHAEPWAF SLDLGLKQAA GSGHLLALGT PENPSWLSLH LQDQKVVLSS GSGPGLDLPL
     VLGLPLQLKL SMSRVVLSQG SKMKALALPP LGLAPLLNLW AKPQGRLFLG ALPGEDSSTS
     FCLNGLWAQG QRLDVDQALN RSHEIWTHSC PQSPGNGTDA SH
//