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P04278

- SHBG_HUMAN

UniProt

P04278 - SHBG_HUMAN

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Protein

Sex hormone-binding globulin

Gene
SHBG
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. androgen binding Source: ProtInc

GO - Biological processi

  1. primary spermatocyte growth Source: Ensembl
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: 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
Complete GO annotation...

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...)CAR_000174
Disulfide bondi193 ↔ 2171 Publication
Disulfide bondi362 ↔ 3901 Publication
Glycosylationi380 – 3801N-linked (GlcNAc...)3 Publications
Glycosylationi396 – 3961N-linked (GlcNAc...)1 Publication

Post-translational modificationi

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

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.

Miscellaneous databases

EvolutionaryTraceiP04278.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

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.

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. VSP_006090Add
BLAST
Alternative sequencei186 – 20318Missing in isoform 5. VSP_045376Add
BLAST
Alternative sequencei239 – 353115Missing in isoform 4. VSP_045358Add
BLAST
Alternative sequencei285 – 2939KVVLSSGSG → EKTLPPLFA in isoform 2 and isoform 3. VSP_006091
Alternative sequencei294 – 402109Missing in isoform 2 and isoform 3. VSP_006092Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221R → Q in CAA28987. 1 Publication
Sequence conflicti334 – 3341A → L in AAC18778. 1 Publication
Sequence conflicti336 – 3361L → S in AAC18778. 1 Publication

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

« 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: September 3, 2014
This is version 152 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

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