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Protein

Sex hormone-binding globulin

Gene

SHBG

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • androgen binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

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 Componenti: 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

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35745.

Chemistry

DrugBankiDB01406. Danazol.
DB00858. Drostanolone.
DB00783. Estradiol.
DB04574. Estropipate.
DB01185. Fluoxymesterone.
DB00741. Hydrocortisone.
DB06710. Methyltestosterone.
DB00648. Mitotane.
DB00717. Norethindrone.
DB00421. Spironolactone.
DB00624. Testosterone.
DB05275. transdermal testosterone gel.

Polymorphism and mutation databases

BioMutaiSHBG.
DMDMi134907.

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 ↔ 217PROSITE-ProRule annotation1 Publication
Disulfide bondi362 ↔ 390PROSITE-ProRule annotation1 Publication
Glycosylationi380 – 3801N-linked (GlcNAc...)3 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

BgeeiP04278.
CleanExiHS_SHBG.
ExpressionAtlasiP04278. baseline and differential.
GenevisibleiP04278. HS.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi112359. 55 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 – 474Combined sources
Beta strandi56 – 627Combined sources
Helixi63 – 653Combined sources
Beta strandi70 – 789Combined sources
Beta strandi80 – 9011Combined sources
Turni91 – 933Combined sources
Beta strandi94 – 1018Combined sources
Beta strandi104 – 11310Combined sources
Beta strandi115 – 1195Combined sources
Beta strandi126 – 1283Combined sources
Beta strandi130 – 1378Combined sources
Beta strandi140 – 1456Combined sources
Beta strandi148 – 1536Combined sources
Helixi160 – 1623Combined sources
Beta strandi167 – 1748Combined sources
Helixi179 – 1813Combined sources
Beta strandi182 – 1843Combined sources
Beta strandi192 – 2009Combined sources
Helixi202 – 2043Combined sources
Beta strandi205 – 2095Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00530000063339.
HOGENOMiHOG000285982.
HOVERGENiHBG017800.
InParanoidiP04278.
OMAiEIQLHNH.
PhylomeDBiP04278.
TreeFamiTF334367.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
InterProiIPR013320. ConA-like_dom.
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. AlignAdd to basket

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

        10         20         30         40         50
MESRGPLATS RLLLLLLLLL LRHTRQGWAL RPVLPTQSAH DPPAVHLSNG
60 70 80 90 100
PGQEPIAVMT FDLTKITKTS SSFEVRTWDP EGVIFYGDTN PKDDWFMLGL
110 120 130 140 150
RDGRPEIQLH NHWAQLTVGA GPRLDDGRWH QVEVKMEGDS VLLEVDGEEV
160 170 180 190 200
LRLRQVSGPL TSKRHPIMRI ALGGLLFPAS NLRLPLVPAL DGCLRRDSWL
210 220 230 240 250
DKQAEISASA PTSLRSCDVE SNPGIFLPPG TQAEFNLRDI PQPHAEPWAF
260 270 280 290 300
SLDLGLKQAA GSGHLLALGT PENPSWLSLH LQDQKVVLSS GSGPGLDLPL
310 320 330 340 350
VLGLPLQLKL SMSRVVLSQG SKMKALALPP LGLAPLLNLW AKPQGRLFLG
360 370 380 390 400
ALPGEDSSTS FCLNGLWAQG QRLDVDQALN RSHEIWTHSC PQSPGNGTDA

SH
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. Curated

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; 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:
EMBLi
GenBanki
DDBJi
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.
ENST00000416273; ENSP00000388867; ENSG00000129214. [P04278-3]
ENST00000441599; ENSP00000393426; ENSG00000129214. [P04278-4]
ENST00000575903; ENSP00000458973; ENSG00000129214. [P04278-5]
GeneIDi6462.
KEGGihsa:6462.
UCSCiuc002gie.2. human. [P04278-1]

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi112359. 55 interactions.
IntActiP04278. 2 interactions.
STRINGi9606.ENSP00000369816.

Chemistry

BindingDBiP04278.
ChEMBLiCHEMBL3305.
DrugBankiDB01406. Danazol.
DB00858. Drostanolone.
DB00783. Estradiol.
DB04574. Estropipate.
DB01185. Fluoxymesterone.
DB00741. Hydrocortisone.
DB06710. Methyltestosterone.
DB00648. Mitotane.
DB00717. Norethindrone.
DB00421. Spironolactone.
DB00624. Testosterone.
DB05275. transdermal testosterone gel.

PTM databases

UniCarbKBiP04278.

Polymorphism and mutation databases

BioMutaiSHBG.
DMDMi134907.

Proteomic databases

PaxDbiP04278.
PeptideAtlasiP04278.
PRIDEiP04278.

Protocols and materials databases

DNASUi6462.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6462.
GeneCardsiGC17P007523.
HGNCiHGNC:10839. SHBG.
MIMi182205. gene.
neXtProtiNX_P04278.
PharmGKBiPA35745.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG39525.
GeneTreeiENSGT00530000063339.
HOGENOMiHOG000285982.
HOVERGENiHBG017800.
InParanoidiP04278.
OMAiEIQLHNH.
PhylomeDBiP04278.
TreeFamiTF334367.

Miscellaneous databases

ChiTaRSiSHBG. human.
EvolutionaryTraceiP04278.
GeneWikiiSex_hormone-binding_globulin.
GenomeRNAii6462.
NextBioi25109.
PROiP04278.
SOURCEiSearch...

Gene expression databases

BgeeiP04278.
CleanExiHS_SHBG.
ExpressionAtlasiP04278. baseline and differential.
GenevisibleiP04278. HS.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
InterProiIPR013320. ConA-like_dom.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 161 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.