SHBG_HUMAN
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 03-AUG-2022, entry version 207.
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="http://atlasgeneticsoncology.org/Genes/SHBGID42286ch17p13.html";
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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 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.
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; 62.
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 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; P04278; -.
DR PeptideAtlas; P04278; -.
DR PRIDE; P04278; -.
DR ProteomicsDB; 20405; -.
DR ProteomicsDB; 2543; -.
DR ProteomicsDB; 27033; -.
DR ProteomicsDB; 46697; -.
DR ProteomicsDB; 51697; -. [P04278-1]
DR ProteomicsDB; 51698; -. [P04278-2]
DR Antibodypedia; 24226; 736 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; 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 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; NLSMPWE; -.
DR PhylomeDB; P04278; -.
DR TreeFam; TF334367; -.
DR PathwayCommons; P04278; -.
DR SignaLink; P04278; -.
DR BioGRID-ORCS; 6462; 15 hits in 1068 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 112 other tissues.
DR ExpressionAtlas; P04278; baseline and differential.
DR Genevisible; P04278; HS.
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 InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF00054; Laminin_G_1; 1.
DR SMART; SM00282; LamG; 1.
DR SUPFAM; SSF49899; SSF49899; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
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
