SHBG_HUMAN - dbPTM
SHBG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SHBG_HUMAN
UniProt AC P04278
Protein Name Sex hormone-binding globulin
Gene Name SHBG
Organism Homo sapiens (Human).
Sequence Length 402
Subcellular Localization Secreted. In testis, it is synthesized by the Sertoli cells, secreted into the lumen of the seminiferous tubule and transported to the epididymis..
Protein Description 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..
Protein Sequence MESRGPLATSRLLLLLLLLLLRHTRQGWALRPVLPTQSAHDPPAVHLSNGPGQEPIAVMTFDLTKITKTSSSFEVRTWDPEGVIFYGDTNPKDDWFMLGLRDGRPEIQLHNHWAQLTVGAGPRLDDGRWHQVEVKMEGDSVLLEVDGEEVLRLRQVSGPLTSKRHPIMRIALGGLLFPASNLRLPLVPALDGCLRRDSWLDKQAEISASAPTSLRSCDVESNPGIFLPPGTQAEFNLRDIPQPHAEPWAFSLDLGLKQAAGSGHLLALGTPENPSWLSLHLQDQKVVLSSGSGPGLDLPLVLGLPLQLKLSMSRVVLSQGSKMKALALPPLGLAPLLNLWAKPQGRLFLGALPGEDSSTSFCLNGLWAQGQRLDVDQALNRSHEIWTHSCPQSPGNGTDASH
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
3Phosphorylation-----MESRGPLATS
-----CCCCCHHHHH		41.04-
36O-linked_GlycosylationALRPVLPTQSAHDPP
CCCCCCCCCCCCCCC		30.873542030
72PhosphorylationKITKTSSSFEVRTWD
EEEECCCCEEEEEEC		25.78-
86PhosphorylationDPEGVIFYGDTNPKD
CCCCEEEECCCCCCC		11.7217322306
161PhosphorylationRQVSGPLTSKRHPIM
EEECCCCCCCCCCCC		35.02-
162PhosphorylationQVSGPLTSKRHPIMR
EECCCCCCCCCCCCH		35.06-
207PhosphorylationLDKQAEISASAPTSL
HHHHCEECCCCCCCH		14.0029083192
209PhosphorylationKQAEISASAPTSLRS
HHCEECCCCCCCHHC		28.1729083192
212PhosphorylationEISASAPTSLRSCDV
EECCCCCCCHHCCCC		39.8629083192
380N-linked_GlycosylationLDVDQALNRSHEIWT
CCHHHHHHCCCCCEE		46.5618638581
380N-linked_GlycosylationLDVDQALNRSHEIWT
CCHHHHHHCCCCCEE		46.5616335952
396N-linked_GlycosylationSCPQSPGNGTDASH-
CCCCCCCCCCCCCC-		54.283542030
396N-linked_GlycosylationSCPQSPGNGTDASH-
CCCCCCCCCCCCCC-		54.2817623646
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of SHBG_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SHBG_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference
72Phosphorylation69 (3)P ⇒ Q;Lrs6258
  • Testosterone levels
21998597
22829776
120N-linked Glycosylation127 (7)P ⇒ L;Qrs6258
  • Testosterone levels
21998597
22829776
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UIF_HUMANFYTTD1physical
15862967
HYI_HUMANHYIphysical
15862967
RMD5B_HUMANRMND5Bphysical
15862967
HDHD5_HUMANCECR5physical
15862967
ALDR_HUMANAKR1B1physical
15862967
DHSO_HUMANSORDphysical
15862967
CATD_HUMANCTSDphysical
15862967
KLK4_HUMANKLK4physical
15862967
PPAP_HUMANACPPphysical
15862967
PA24A_HUMANPLA2G4Aphysical
15862967
ZA2G_HUMANAZGP1physical
15862967
KAD2_HUMANAK2physical
15862967
KPYM_HUMANPKMphysical
15862967
ATPA_HUMANATP5A1physical
15862967
ACPH_HUMANAPEHphysical
15862967
SHBG_HUMANSHBGphysical
15862967
APOD_HUMANAPODphysical
15862967
A2MG_HUMANA2Mphysical
15862967
SORCN_HUMANSRIphysical
15862967
TINAL_HUMANTINAGL1physical
15862967
PTGDS_HUMANPTGDSphysical
15862967
MT1F_HUMANMT1Fphysical
15862967
MT1G_HUMANMT1Gphysical
15862967
MT2_HUMANMT2Aphysical
15862967
UBE3A_HUMANUBE3Aphysical
15862967
UBE2O_HUMANUBE2Ophysical
15862967
PACN2_HUMANPACSIN2physical
15862967
SEM3F_HUMANSEMA3Fphysical
15862967
PLP2_HUMANPLP2physical
15862967
G6PT1_HUMANSLC37A4physical
15862967
FLOT1_HUMANFLOT1physical
15862967
CD177_HUMANCD177physical
15862967
CLD4_HUMANCLDN4physical
15862967
MPU1_HUMANMPDU1physical
15862967
AP1B1_HUMANAP1B1physical
15862967
AP2A1_HUMANAP2A1physical
15862967
ACTA_HUMANACTA2physical
15862967
ACTB_HUMANACTBphysical
15862967
ACTH_HUMANACTG2physical
15862967
CO1A2_HUMANCOL1A2physical
15862967
DEST_HUMANDSTNphysical
15862967
DESM_HUMANDESphysical
15862967
PPIP1_HUMANPSTPIP1physical
15862967
FLNA_HUMANFLNAphysical
15862967
NOMO1_HUMANNOMO1physical
15862967
EF1A1_HUMANEEF1A1physical
15862967
EIF3E_HUMANEIF3Ephysical
15862967
SRF_HUMANSRFphysical
15862967
MAD4_HUMANMXD4physical
15862967
ABC3C_HUMANAPOBEC3Cphysical
15862967
RU17_HUMANSNRNP70physical
15862967
DDX3Y_HUMANDDX3Yphysical
15862967
GBB2_HUMANGNB2physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SHBG_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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).
Cited for: VARIANT ASN-356, AND GLYCOSYLATION AT ASN-356.
"Glycoproteomics analysis of human liver tissue by combination ofmultiple 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).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-380, AND MASSSPECTROMETRY.
"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).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-380, AND MASSSPECTROMETRY.
"Amino acid sequence of the sex steroid binding protein of human bloodplasma.";
Walsh K.A., Titani K., Takio K., Kumar S., Hayes R., Petra P.H.;
Biochemistry 25:7584-7590(1986).
Cited for: PROTEIN SEQUENCE OF 30-402.

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