dbPTM

THBG_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	THBG_HUMAN
UniProt AC	P05543
Protein Name	Thyroxine-binding globulin
Gene Name	SERPINA7
Organism	Homo sapiens (Human).
Sequence Length	415
Subcellular Localization	Secreted.
Protein Description	Major thyroid hormone transport protein in serum..
Protein Sequence	MSPFLYLVLLVLGLHATIHCASPEGKVTACHSSQPNATLYKMSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLICSLNFPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQDLKPNTIMVLVNYIHFKAQWANPFDPSKTEDSSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVLPKEGQMESVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLHIGEKGTEAAAVPEVELSDQPENTFLHPIIQIDRSFMLLILERSTRSILFLGKVVNPTEA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
36	N-linked_Glycosylation	ACHSSQPNATLYKMS EEECCCCCCEEEEEE	37.61	19838169
36	N-linked_Glycosylation	ACHSSQPNATLYKMS EEECCCCCCEEEEEE	37.61	16335952
38	Phosphorylation	HSSQPNATLYKMSSI ECCCCCCEEEEEECC	36.94	-
40	Phosphorylation	SQPNATLYKMSSINA CCCCCEEEEEECCCC	10.57	-
54	Phosphorylation	ADFAFNLYRRFTVET CCEEEEEEECCEEEC	10.80	26074081
58	Phosphorylation	FNLYRRFTVETPDKN EEEEECCEEECCCCC	18.67	26074081
99	N-linked_Glycosylation	IVETLGFNLTDTPMV HHHHHCCCCCCCCCE	39.99	3094014
99	N-linked_Glycosylation	IVETLGFNLTDTPMV HHHHHCCCCCCCCCE	39.99	3094014
164	Phosphorylation	EVFSTDFSNISAAKQ EEECCCCCCHHHHHH	35.74	28674419
165	N-linked_Glycosylation	VFSTDFSNISAAKQE EECCCCCCHHHHHHH	32.03	3094014
165	N-linked_Glycosylation	VFSTDFSNISAAKQE EECCCCCCHHHHHHH	32.03	16335952
175	Phosphorylation	AAKQEINSHVEMQTK HHHHHHHHHCCHHCC	34.27	-
181	Phosphorylation	NSHVEMQTKGKVVGL HHHCCHHCCCCEEEE	40.22	-
253	N-linked_Glycosylation	HLVDMELNCTVLQMD HHHHHHCCCEEEECC	13.20	3094014
253	N-linked_Glycosylation	HLVDMELNCTVLQMD HHHHHHCCCEEEECC	13.20	3094014
373	O-linked_Glycosylation	AVPEVELSDQPENTF ECCCEECCCCCCCCC	22.24	OGP
390	Phosphorylation	PIIQIDRSFMLLILE EEEEECHHHHHHHHC	15.97	22617229
399	Phosphorylation	MLLILERSTRSILFL HHHHHCCCCCEEEEE	20.85	23403867
400	Phosphorylation	LLILERSTRSILFLG HHHHCCCCCEEEEEE	34.36	23403867
402	Phosphorylation	ILERSTRSILFLGKV HHCCCCCEEEEEEEE	24.59	23403867
411	N-linked_Glycosylation	LFLGKVVNPTEA--- EEEEEECCCCCC---	40.54	3094014
411	N-linked_Glycosylation	LFLGKVVNPTEA--- EEEEEECCCCCC---	40.54	3094014

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 THBG_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of THBG_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
Oops, there are no SNP-PTM records of THBG_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TGO1_HUMAN	MIA3	physical	26186194
RTL8C_HUMAN	FAM127A	physical	26186194
DYR2_HUMAN	DHFRL1	physical	26186194
ERF_HUMAN	ERF	physical	26186194
DYR2_HUMAN	DHFRL1	physical	28514442
RTL8C_HUMAN	FAM127A	physical	28514442
TGO1_HUMAN	MIA3	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
314200	Thyroxine-binding globulin deficiency (TBG deficiency)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00451	Levothyroxine
DB00279	Liothyronine
DB01583	Liotrix

Regulatory Network of THBG_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Enrichment of glycopeptides for glycan structure and attachment siteidentification."; Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,Brinkmalm G., Larson G.; Nat. Methods 6:809-811(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-36, STRUCTURE OFCARBOHYDRATES, AND MASS SPECTROMETRY.	19838169 [Abstract]
"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-36 AND ASN-165, AND MASSSPECTROMETRY.	16335952 [Abstract]