CBG_HUMAN - dbPTM
CBG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CBG_HUMAN
UniProt AC P08185
Protein Name Corticosteroid-binding globulin
Gene Name SERPINA6
Organism Homo sapiens (Human).
Sequence Length 405
Subcellular Localization Secreted.
Protein Description Major transport protein for glucocorticoids and progestins in the blood of almost all vertebrate species..
Protein Sequence MPLLLYTCLLWLPTSGLWTVQAMDPNAAYVNMSNHHRGLASANVDFAFSLYKHLVALSPKKNIFISPVSISMALAMLSLGTCGHTRAQLLQGLGFNLTERSETEIHQGFQHLHQLFAKSDTSLEMTMGNALFLDGSLELLESFSADIKHYYESEVLAMNFQDWATASRQINSYVKNKTQGKIVDLFSGLDSPAILVLVNYIFFKGTWTQPFDLASTREENFYVDETTVVKVPMMLQSSTISYLHDSELPCQLVQMNYVGNGTVFFILPDKGKMNTVIAALSRDTINRWSAGLTSSQVDLYIPKVTISGVYDLGDVLEEMGIADLFTNQANFSRITQDAQLKSSKVVHKAVLQLNEEGVDTAGSTGVTLNLTSKPIILRFNQPFIIMIFDHFTWSSLFLARVMNPV
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
6Phosphorylation--MPLLLYTCLLWLP
--CCCHHHHHHHHCC		8.7224043423
7Phosphorylation-MPLLLYTCLLWLPT
-CCCHHHHHHHHCCC		9.1724043423
14PhosphorylationTCLLWLPTSGLWTVQ
HHHHHCCCCCCEEEE		33.0024043423
15PhosphorylationCLLWLPTSGLWTVQA
HHHHCCCCCCEEEEE		29.9224043423
19PhosphorylationLPTSGLWTVQAMDPN
CCCCCCEEEEECCCC		14.0524043423
29PhosphorylationAMDPNAAYVNMSNHH
ECCCCCEEECCCCCC		7.0224043423
31N-linked_GlycosylationDPNAAYVNMSNHHRG
CCCCEEECCCCCCCC		18.588180202
31N-linked_GlycosylationDPNAAYVNMSNHHRG
CCCCEEECCCCCCCC		18.5816335952
33PhosphorylationNAAYVNMSNHHRGLA
CCEEECCCCCCCCCH		28.0124043423
58PhosphorylationYKHLVALSPKKNIFI
HHHHHHHCCCCCEEE		25.5724719451
66PhosphorylationPKKNIFISPVSISMA
CCCCEEECCHHHHHH		14.43-
78PhosphorylationSMALAMLSLGTCGHT
HHHHHHHHHCCCHHH		16.21-
96N-linked_GlycosylationLLQGLGFNLTERSET
HHHHCCCCCCCCCCH		44.238180202
96N-linked_GlycosylationLLQGLGFNLTERSET
HHHHCCCCCCCCCCH		44.238180202
176N-linked_GlycosylationQINSYVKNKTQGKIV
HHHHHHCCCCCCCEE		42.438180202
176N-linked_GlycosylationQINSYVKNKTQGKIV
HHHHHHCCCCCCCEE		42.438180202
208PhosphorylationIFFKGTWTQPFDLAS
ECCCCCCCCCCCCCC		26.6324505115
260N-linked_GlycosylationVQMNYVGNGTVFFIL
EEEEEECCCEEEEEC		32.688180202
260N-linked_GlycosylationVQMNYVGNGTVFFIL
EEEEEECCCEEEEEC		32.688180202
330N-linked_GlycosylationDLFTNQANFSRITQD
HHHCCCCCHHHHCCC		26.1816335952
330N-linked_GlycosylationDLFTNQANFSRITQD
HHHCCCCCHHHHCCC		26.188180202
360PhosphorylationLNEEGVDTAGSTGVT
HCCCCCCCCCCCCCE		30.4326270265
363PhosphorylationEGVDTAGSTGVTLNL
CCCCCCCCCCCEEEC		21.3726270265
364O-linked_GlycosylationGVDTAGSTGVTLNLT
CCCCCCCCCCEEECC		34.45OGP
364PhosphorylationGVDTAGSTGVTLNLT
CCCCCCCCCCEEECC		34.4526270265
367PhosphorylationTAGSTGVTLNLTSKP
CCCCCCCEEECCCCC		15.9826270265
369N-linked_GlycosylationGSTGVTLNLTSKPII
CCCCCEEECCCCCEE		31.7216335952
369N-linked_GlycosylationGSTGVTLNLTSKPII
CCCCCEEECCCCCEE		31.7216335952
371PhosphorylationTGVTLNLTSKPIILR
CCCEEECCCCCEEEE		33.3626270265
372PhosphorylationGVTLNLTSKPIILRF
CCEEECCCCCEEEEC		39.3326270265
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 CBG_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
260NGlycosylation

-
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

Oops, there are no SNP-PTM records of CBG_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SC65_HUMANP3H4physical
26186194
COCH_HUMANCOCHphysical
26186194
AMD_HUMANPAMphysical
26186194
CO4A2_HUMANCOL4A2physical
26186194
PEDF_HUMANSERPINF1physical
26186194
DYR2_HUMANDHFRL1physical
26186194
WRB_HUMANWRBphysical
26186194
DPB1_HUMANHLA-DPB1physical
26186194
DYR2_HUMANDHFRL1physical
28514442
COCH_HUMANCOCHphysical
28514442
AMD_HUMANPAMphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
611489Corticosteroid-binding globulin deficiency (CBG deficiency)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00240Alclometasone
DB00394Beclomethasone
DB01410Ciclesonide
DB00663Flumethasone Pivalate
DB00180Flunisolide
DB00591Fluocinolone Acetonide
DB01047Fluocinonide
DB00324Fluorometholone
DB00846Flurandrenolide
DB00588Fluticasone Propionate
DB00596Halobetasol Propionate
DB00253Medrysone
DB00648Mitotane
DB01384Paramethasone
DB00860Prednisolone
DB00896Rimexolone
DB00620Triamcinolone
Regulatory Network of CBG_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-96 AND ASN-330, 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-31; ASN-96; ASN-330 ANDASN-369, AND MASS SPECTROMETRY.
"Screening for N-glycosylated proteins by liquid chromatography massspectrometry.";
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
Proteomics 4:454-465(2004).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-96, AND MASS SPECTROMETRY.

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