Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P04278

- SHBG_HUMAN

UniProt

P04278 - SHBG_HUMAN

Protein

Sex hormone-binding globulin

Gene

SHBG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 2 (01 Apr 1990)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Functions as an androgen transport protein, but may also be involved in receptor mediated processes. Each dimer binds one molecule of steroid. Specific for 5-alpha-dihydrotestosterone, testosterone, and 17-beta-estradiol. Regulates the plasma metabolic clearance rate of steroid hormones by controlling their plasma concentration.

    GO - Molecular functioni

    1. androgen binding Source: ProtInc

    GO - Biological processi

    1. primary spermatocyte growth Source: Ensembl

    Keywords - Ligandi

    Lipid-binding, Steroid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sex hormone-binding globulin
    Short name:
    SHBG
    Alternative name(s):
    Sex steroid-binding protein
    Short name:
    SBP
    Testis-specific androgen-binding protein
    Short name:
    ABP
    Testosterone-estradiol-binding globulin
    Short name:
    TeBG
    Testosterone-estrogen-binding globulin
    Gene namesi
    Name:SHBG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:10839. SHBG.

    Subcellular locationi

    Secreted By similarity
    Note: In testis, it is synthesized by the Sertoli cells, secreted into the lumen of the seminiferous tubule and transported to the epididymis.By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35745.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 29292 PublicationsAdd
    BLAST
    Chaini30 – 402373Sex hormone-binding globulin1 PublicationPRO_0000032557Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi36 – 361O-linked (GalNAc...)1 PublicationCAR_000174
    Disulfide bondi193 ↔ 2171 PublicationPROSITE-ProRule annotation
    Disulfide bondi362 ↔ 3901 PublicationPROSITE-ProRule annotation
    Glycosylationi380 – 3801N-linked (GlcNAc...)4 Publications
    Glycosylationi396 – 3961N-linked (GlcNAc...)2 Publications

    Post-translational modificationi

    Variant Asn-356 contains one N-linked (GlcNAc...) at position 356.3 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP04278.
    PeptideAtlasiP04278.
    PRIDEiP04278.

    PTM databases

    UniCarbKBiP04278.

    Expressioni

    Tissue specificityi

    Isoform 1 and isoform 2 are present in liver and testis.

    Gene expression databases

    ArrayExpressiP04278.
    BgeeiP04278.
    CleanExiHS_SHBG.
    GenevestigatoriP04278.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi112359. 56 interactions.
    IntActiP04278. 2 interactions.
    STRINGi9606.ENSP00000369816.

    Structurei

    Secondary structure

    1
    402
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi44 – 474
    Beta strandi56 – 627
    Helixi63 – 653
    Beta strandi70 – 789
    Beta strandi80 – 9011
    Turni91 – 933
    Beta strandi94 – 1018
    Beta strandi104 – 11310
    Beta strandi115 – 1195
    Beta strandi126 – 1283
    Beta strandi130 – 1378
    Beta strandi140 – 1456
    Beta strandi148 – 1536
    Helixi160 – 1623
    Beta strandi167 – 1748
    Helixi179 – 1813
    Beta strandi182 – 1843
    Beta strandi192 – 2009
    Helixi202 – 2043
    Beta strandi205 – 2095

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D2SX-ray1.55A42-217[»]
    1F5FX-ray1.70A30-234[»]
    1KDKX-ray1.70A41-217[»]
    1KDMX-ray2.35A41-217[»]
    1LHNX-ray2.00A30-218[»]
    1LHOX-ray2.00A30-218[»]
    1LHUX-ray1.80A30-218[»]
    1LHVX-ray2.00A30-218[»]
    1LHWX-ray1.75A30-218[»]
    ProteinModelPortaliP04278.
    SMRiP04278. Positions 32-391.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04278.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini45 – 217173Laminin G-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini224 – 390167Laminin G-like 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 2 laminin G-like domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG39525.
    HOGENOMiHOG000285982.
    HOVERGENiHBG017800.
    InParanoidiP04278.
    OMAiEIQLHNH.
    PhylomeDBiP04278.
    TreeFamiTF334367.

    Family and domain databases

    Gene3Di2.60.120.200. 2 hits.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR001791. Laminin_G.
    [Graphical view]
    PfamiPF00054. Laminin_G_1. 1 hit.
    [Graphical view]
    SMARTiSM00282. LamG. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 2 hits.
    PROSITEiPS50025. LAM_G_DOMAIN. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: P04278-1) [UniParc]FASTAAdd to Basket

    Also known as: SHBG, SHBGr-1

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MESRGPLATS RLLLLLLLLL LRHTRQGWAL RPVLPTQSAH DPPAVHLSNG    50
    PGQEPIAVMT FDLTKITKTS SSFEVRTWDP EGVIFYGDTN PKDDWFMLGL 100
    RDGRPEIQLH NHWAQLTVGA GPRLDDGRWH QVEVKMEGDS VLLEVDGEEV 150
    LRLRQVSGPL TSKRHPIMRI ALGGLLFPAS NLRLPLVPAL DGCLRRDSWL 200
    DKQAEISASA PTSLRSCDVE SNPGIFLPPG TQAEFNLRDI PQPHAEPWAF 250
    SLDLGLKQAA GSGHLLALGT PENPSWLSLH LQDQKVVLSS GSGPGLDLPL 300
    VLGLPLQLKL SMSRVVLSQG SKMKALALPP LGLAPLLNLW AKPQGRLFLG 350
    ALPGEDSSTS FCLNGLWAQG QRLDVDQALN RSHEIWTHSC PQSPGNGTDA 400
    SH 402
    Length:402
    Mass (Da):43,779
    Last modified:April 1, 1990 - v2
    Checksum:i5A3B1885E4E7A460
    GO
    Isoform 2 (identifier: P04278-2) [UniParc]FASTAAdd to Basket

    Also known as: Sex hormone binding globulin-gene-related protein (SHBGgrp), SHBGr-2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-37: MESRGPLATSRLLLLLLLLLLRHTRQGWALRPVLPTQ → PRFKGSPAVLFKLTYAVITCFSLRLTHPPRPW
         285-293: KVVLSSGSG → EKTLPPLFA
         294-402: Missing.

    Note: Incomplete sequence.

    Show »
    Length:288
    Mass (Da):31,829
    Checksum:iF5BCCF800F560461
    GO
    Isoform 3 (identifier: P04278-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         285-293: KVVLSSGSG → EKTLPPLFA
         294-402: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:293
    Mass (Da):32,363
    Checksum:iB88FA1CEE7F97A7E
    GO
    Isoform 4 (identifier: P04278-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         239-353: Missing.

    Show »
    Length:287
    Mass (Da):31,720
    Checksum:i04D30318BC6B1191
    GO
    Isoform 5 (identifier: P04278-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         186-203: Missing.

    Show »
    Length:384
    Mass (Da):41,712
    Checksum:iACAF2C28914C13D1
    GO

    Sequence cautioni

    The sequence CAA29309.1 differs from that shown. Reason: Frameshift at positions 47, 52 and 54.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 221R → Q in CAA28987. (PubMed:15489334)Curated
    Sequence conflicti334 – 3341A → L in AAC18778. (PubMed:2608061)Curated
    Sequence conflicti336 – 3361L → S in AAC18778. (PubMed:2608061)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti22 – 221R → H.
    Corresponds to variant rs9282845 [ dbSNP | Ensembl ].
    VAR_022002
    Natural varianti25 – 251R → H.1 Publication
    Corresponds to variant rs6260 [ dbSNP | Ensembl ].
    VAR_013946
    Natural varianti185 – 1851P → L.
    Corresponds to variant rs6258 [ dbSNP | Ensembl ].
    VAR_016182
    Natural varianti356 – 3561D → N Polymorphism that generates a N-glycosylation site. 3 Publications
    Corresponds to variant rs6259 [ dbSNP | Ensembl ].
    VAR_013129

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3737MESRG…VLPTQ → PRFKGSPAVLFKLTYAVITC FSLRLTHPPRPW in isoform 2. CuratedVSP_006090Add
    BLAST
    Alternative sequencei186 – 20318Missing in isoform 5. CuratedVSP_045376Add
    BLAST
    Alternative sequencei239 – 353115Missing in isoform 4. 1 PublicationVSP_045358Add
    BLAST
    Alternative sequencei285 – 2939KVVLSSGSG → EKTLPPLFA in isoform 2 and isoform 3. 1 PublicationVSP_006091
    Alternative sequencei294 – 402109Missing in isoform 2 and isoform 3. 1 PublicationVSP_006092Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16349 Genomic DNA. Translation: CAA34398.1.
    X16350 Genomic DNA. Translation: CAA34399.1.
    X16351 mRNA. Translation: CAA34400.1.
    M31651 Genomic DNA. Translation: AAC18778.1.
    CD013955 mRNA. No translation available.
    BC069597 mRNA. Translation: AAH69597.1.
    BC101785 mRNA. Translation: AAI01786.1.
    BC112186 mRNA. Translation: AAI12187.1.
    AC007421 Genomic DNA. No translation available.
    X05403 mRNA. Translation: CAA28987.1.
    EU352661 mRNA. Translation: ABY67999.1.
    X05885 mRNA. Translation: CAA29309.1. Frameshift.
    X05792 mRNA. Translation: CAA29234.1.
    CCDSiCCDS11117.1. [P04278-1]
    CCDS54082.1. [P04278-3]
    CCDS54083.1. [P04278-4]
    CCDS58513.1. [P04278-5]
    PIRiS09606. BOHUS.
    RefSeqiNP_001031.2. NM_001040.4. [P04278-1]
    NP_001139751.1. NM_001146279.2. [P04278-5]
    NP_001139752.1. NM_001146280.2. [P04278-3]
    NP_001139753.1. NM_001146281.2. [P04278-4]
    NP_001276042.1. NM_001289113.1.
    NP_001276043.1. NM_001289114.1.
    NP_001276044.1. NM_001289115.1.
    NP_001276045.1. NM_001289116.1.
    UniGeneiHs.632235.

    Genome annotation databases

    EnsembliENST00000380450; ENSP00000369816; ENSG00000129214. [P04278-1]
    ENST00000416273; ENSP00000388867; ENSG00000129214. [P04278-3]
    ENST00000441599; ENSP00000393426; ENSG00000129214. [P04278-4]
    ENST00000575903; ENSP00000458973; ENSG00000129214. [P04278-5]
    ENST00000576830; ENSP00000460219; ENSG00000129214.
    GeneIDi6462.
    KEGGihsa:6462.
    UCSCiuc002gie.2. human. [P04278-1]

    Polymorphism databases

    DMDMi134907.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Androgen-binding protein entry

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16349 Genomic DNA. Translation: CAA34398.1 .
    X16350 Genomic DNA. Translation: CAA34399.1 .
    X16351 mRNA. Translation: CAA34400.1 .
    M31651 Genomic DNA. Translation: AAC18778.1 .
    CD013955 mRNA. No translation available.
    BC069597 mRNA. Translation: AAH69597.1 .
    BC101785 mRNA. Translation: AAI01786.1 .
    BC112186 mRNA. Translation: AAI12187.1 .
    AC007421 Genomic DNA. No translation available.
    X05403 mRNA. Translation: CAA28987.1 .
    EU352661 mRNA. Translation: ABY67999.1 .
    X05885 mRNA. Translation: CAA29309.1 . Frameshift.
    X05792 mRNA. Translation: CAA29234.1 .
    CCDSi CCDS11117.1. [P04278-1 ]
    CCDS54082.1. [P04278-3 ]
    CCDS54083.1. [P04278-4 ]
    CCDS58513.1. [P04278-5 ]
    PIRi S09606. BOHUS.
    RefSeqi NP_001031.2. NM_001040.4. [P04278-1 ]
    NP_001139751.1. NM_001146279.2. [P04278-5 ]
    NP_001139752.1. NM_001146280.2. [P04278-3 ]
    NP_001139753.1. NM_001146281.2. [P04278-4 ]
    NP_001276042.1. NM_001289113.1.
    NP_001276043.1. NM_001289114.1.
    NP_001276044.1. NM_001289115.1.
    NP_001276045.1. NM_001289116.1.
    UniGenei Hs.632235.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1D2S X-ray 1.55 A 42-217 [» ]
    1F5F X-ray 1.70 A 30-234 [» ]
    1KDK X-ray 1.70 A 41-217 [» ]
    1KDM X-ray 2.35 A 41-217 [» ]
    1LHN X-ray 2.00 A 30-218 [» ]
    1LHO X-ray 2.00 A 30-218 [» ]
    1LHU X-ray 1.80 A 30-218 [» ]
    1LHV X-ray 2.00 A 30-218 [» ]
    1LHW X-ray 1.75 A 30-218 [» ]
    ProteinModelPortali P04278.
    SMRi P04278. Positions 32-391.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112359. 56 interactions.
    IntActi P04278. 2 interactions.
    STRINGi 9606.ENSP00000369816.

    Chemistry

    BindingDBi P04278.
    ChEMBLi CHEMBL3305.
    DrugBanki DB01406. Danazol.
    DB00858. Dromostanolone.
    DB00783. Estradiol.
    DB00655. Estrone.
    DB01185. Fluoxymesterone.
    DB00741. Hydrocortisone.
    DB00648. Mitotane.
    DB00717. Norethindrone.
    DB00624. Testosterone.

    PTM databases

    UniCarbKBi P04278.

    Polymorphism databases

    DMDMi 134907.

    Proteomic databases

    PaxDbi P04278.
    PeptideAtlasi P04278.
    PRIDEi P04278.

    Protocols and materials databases

    DNASUi 6462.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000380450 ; ENSP00000369816 ; ENSG00000129214 . [P04278-1 ]
    ENST00000416273 ; ENSP00000388867 ; ENSG00000129214 . [P04278-3 ]
    ENST00000441599 ; ENSP00000393426 ; ENSG00000129214 . [P04278-4 ]
    ENST00000575903 ; ENSP00000458973 ; ENSG00000129214 . [P04278-5 ]
    ENST00000576830 ; ENSP00000460219 ; ENSG00000129214 .
    GeneIDi 6462.
    KEGGi hsa:6462.
    UCSCi uc002gie.2. human. [P04278-1 ]

    Organism-specific databases

    CTDi 6462.
    GeneCardsi GC17P007519.
    HGNCi HGNC:10839. SHBG.
    MIMi 182205. gene.
    neXtProti NX_P04278.
    PharmGKBi PA35745.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG39525.
    HOGENOMi HOG000285982.
    HOVERGENi HBG017800.
    InParanoidi P04278.
    OMAi EIQLHNH.
    PhylomeDBi P04278.
    TreeFami TF334367.

    Miscellaneous databases

    ChiTaRSi SHBG. human.
    EvolutionaryTracei P04278.
    GeneWikii Sex_hormone-binding_globulin.
    GenomeRNAii 6462.
    NextBioi 25109.
    PROi P04278.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P04278.
    Bgeei P04278.
    CleanExi HS_SHBG.
    Genevestigatori P04278.

    Family and domain databases

    Gene3Di 2.60.120.200. 2 hits.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR001791. Laminin_G.
    [Graphical view ]
    Pfami PF00054. Laminin_G_1. 1 hit.
    [Graphical view ]
    SMARTi SM00282. LamG. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 2 hits.
    PROSITEi PS50025. LAM_G_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the human sex hormone binding globulin (SHBG) gene and demonstration of two transcripts in both liver and testis."
      Gershagen S., Lundwall A., Fernlund P.
      Nucleic Acids Res. 17:9245-9258(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
      Tissue: Testis.
    2. "The human sex hormone-binding globulin gene contains exons for androgen-binding protein and two other testicular messenger RNAs."
      Hammond G.L., Underhill D.A., Rykse H.M., Smith C.L.
      Mol. Endocrinol. 3:1869-1876(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
      Tissue: Testis.
    3. "PCR isolation and cloning of novel splice variant mRNAs from known drug target genes."
      Jin P., Fu G.K., Wilson A.D., Yang J., Chien D., Hawkins P.R., Au-Young J., Stuve L.L.
      Genomics 83:566-571(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Liver.
    6. "The cDNA-deduced primary structure of human sex hormone-binding globulin and location of its steroid-binding domain."
      Hammond G.L., Underhill D.A., Smith C.L., Goping I.S., Harley M.J., Musto N.A., Cheng C.Y., Bardin C.W.
      FEBS Lett. 215:100-104(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-402 (ISOFORM 1).
      Tissue: Liver.
    7. "Human sex hormone-binding globulin gene transcript expression in liver, prostate, breast, testis, and brain- multiple promoters and complex alternative splicing."
      Kahn S.M., Nakhla A.M., Hryb D.J., Rosner W., Romas N.A.
      Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 28-402 (ISOFORM 4).
      Tissue: Liver.
    8. "A cDNA coding for human sex hormone binding globulin. Homology to vitamin K-dependent protein S."
      Gershagen S., Fernlund P., Lundwall A.
      FEBS Lett. 220:129-135(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 47-402 (ISOFORM 1).
      Tissue: Liver.
    9. "Characterization of a cDNA coding for sex steroid-binding protein of human plasma."
      Que B.G., Petra P.H.
      FEBS Lett. 219:405-409(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 121-402 (ISOFORM 1).
      Tissue: Liver.
    10. "Physicochemical characteristics of human sex hormone binding globulin: evidence for two identical subunits."
      Hammond G.L., Robinson P.A., Sugino H., Ward D.N., Finne J.
      J. Steroid Biochem. 24:815-824(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 30-54.
    11. "Amino acid sequence of the sex steroid binding protein of human blood plasma."
      Walsh K.A., Titani K., Takio K., Kumar S., Hayes R., Petra P.H.
      Biochemistry 25:7584-7590(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 30-402.
    12. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-380.
      Tissue: Plasma.
    13. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-380.
      Tissue: Liver.
    14. "Molecular analyses of a human sex hormone-binding globulin variant: evidence for an additional carbohydrate chain."
      Power S.G.A., Bocchinfuso W.P., Pallesen M., Warmels-Rodenhiser S., Van Baelen H., Hammond G.L.
      J. Clin. Endocrinol. Metab. 75:1066-1070(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ASN-356, CHARACTERIZATION OF VARIANT ASN-356, GLYCOSYLATION.
    15. "Crystal structure of human sex hormone-binding globulin: steroid transport by a laminin G-like domain."
      Grishkovskaya I., Avvakumov G.V., Sklenar G., Dales D., Hammond G.L., Muller Y.A.
      EMBO J. 19:504-512(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 42-211.
    16. "Steroid ligands bind human sex hormone-binding globulin in specific orientations and produce distinct changes in protein conformation."
      Grishkovskaya I., Avvakumov G.V., Hammond G.L., Catalano M.G., Muller Y.A.
      J. Biol. Chem. 277:32086-32093(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 42-218.
    17. "Molecular characterization of a genetic variant of the steroid hormone-binding globulin gene in heterozygous subjects."
      Hardy D.O., Carino C., Catterall J.F., Larrea F.
      J. Clin. Endocrinol. Metab. 80:1253-1256(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ASN-356.
    18. Cited for: VARIANTS HIS-25 AND ASN-356.

    Entry informationi

    Entry nameiSHBG_HUMAN
    AccessioniPrimary (citable) accession number: P04278
    Secondary accession number(s): B0FWH4
    , E9PGW1, F5H5Z8, I3L1N7, P14689, Q16616, Q3MIL0, Q6ISD2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 1987
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 153 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3