dbPTM

A1AG1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	A1AG1_HUMAN
UniProt AC	P02763
Protein Name	Alpha-1-acid glycoprotein 1
Gene Name	ORM1
Organism	Homo sapiens (Human).
Sequence Length	201
Subcellular Localization	Secreted.
Protein Description	Functions as transport protein in the blood stream. Binds various ligands in the interior of its beta-barrel domain. Also binds synthetic drugs and influences their distribution and availability in the body. Appears to function in modulating the activity of the immune system during the acute-phase reaction..
Protein Sequence	MALSWVLTVLSLLPLLEAQIPLCANLVPVPITNATLDQITGKWFYIASAFRNEEYNKSVQEIQATFFYFTPNKTEDTIFLREYQTRQDQCIYNTTYLNVQRENGTISRYVGGQEHFAHLLILRDTKTYMLAFDVNDEKNWGLSVYADKPETTKEQLGEFYEALDCLRIPKSDVVYTDWKKDKCEPLEKQHEKERKQEEGES

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
19	Pyrrolidone_carboxylic_acid	LLPLLEAQIPLCANL HHHHHHCCCCCCCCC	28.58	-
19	Pyrrolidone_carboxylic_acid	LLPLLEAQIPLCANL HHHHHHCCCCCCCCC	28.58	4711474
19	Pyrrolidone_carboxylic_acid	LLPLLEAQIPLCANL HHHHHHCCCCCCCCC	28.58	4711474
33	N-linked_Glycosylation	LVPVPITNATLDQIT CCEEECCCCCHHHHC	31.48	15084671
33	N-linked_Glycosylation	LVPVPITNATLDQIT CCEEECCCCCHHHHC	31.48	1567356
56	N-linked_Glycosylation	AFRNEEYNKSVQEIQ HHCCHHHHHHHHHCE	33.15	1567356
56	N-linked_Glycosylation	AFRNEEYNKSVQEIQ HHCCHHHHHHHHHCE	33.15	16335952
65	Phosphorylation	SVQEIQATFFYFTPN HHHHCEEEEEEECCC	9.63	25627689
72	N-linked_Glycosylation	TFFYFTPNKTEDTIF EEEEECCCCCCCEEE	61.90	18638581
72	N-linked_Glycosylation	TFFYFTPNKTEDTIF EEEEECCCCCCCEEE	61.90	1567356
74	Phosphorylation	FYFTPNKTEDTIFLR EEECCCCCCCEEEEE	45.81	26657352
77	Phosphorylation	TPNKTEDTIFLREYQ CCCCCCCEEEEEEEE	13.85	26657352
83	Phosphorylation	DTIFLREYQTRQDQC CEEEEEEEECCCCEE	14.57	26657352
93	N-linked_Glycosylation	RQDQCIYNTTYLNVQ CCCEEEEEEEEEEEE	13.16	15084671
93	N-linked_Glycosylation	RQDQCIYNTTYLNVQ CCCEEEEEEEEEEEE	13.16	15084671
103	N-linked_Glycosylation	YLNVQRENGTISRYV EEEEEEECCCEEEEE	55.91	18638581
103	N-linked_Glycosylation	YLNVQRENGTISRYV EEEEEEECCCEEEEE	55.91	1567356
109	Phosphorylation	ENGTISRYVGGQEHF ECCCEEEEECCHHHE	9.17	-
109	Nitration	ENGTISRYVGGQEHF ECCCEEEEECCHHHE	9.17	-
170	Glycation	LDCLRIPKSDVVYTD HHHHCCCHHHCEEEC	57.84	-
170	Acetylation	LDCLRIPKSDVVYTD HHHHCCCHHHCEEEC	57.84	27178108
175	Phosphorylation	IPKSDVVYTDWKKDK CCHHHCEEECCCCCC	9.99	-
179	Acetylation	DVVYTDWKKDKCEPL HCEEECCCCCCCHHH	54.63	27178108

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 A1AG1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of A1AG1_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 A1AG1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
P63_HUMAN	TP63	physical	21988832
CCGL_HUMAN	TMEM37	physical	21988832
A1AG2_HUMAN	ORM2	physical	28514442
PTGDS_HUMAN	PTGDS	physical	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 A1AG1_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD."; Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.; Mol. Cell. Proteomics 0:0-0(2011). Cited for: GLYCOSYLATION AT ASN-33, STRUCTURE OF CARBOHYDRATES, AND MASSSPECTROMETRY.	22171320 [Abstract]
"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-33 AND ASN-72, STRUCTUREOF CARBOHYDRATES, AND MASS SPECTROMETRY.	19838169 [Abstract]
"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-93 AND ASN-103, AND MASSSPECTROMETRY.	19159218 [Abstract]
"Identification of N-linked glycoproteins in human saliva byglycoprotein capture and mass spectrometry."; Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,Loo J.A.; J. Proteome Res. 5:1493-1503(2006). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-93, AND MASS SPECTROMETRY.	16740002 [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-33; ASN-56; ASN-72; ASN-93AND ASN-103, AND MASS SPECTROMETRY.	16335952 [Abstract]
"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-33; ASN-56; ASN-72; ASN-93AND ASN-103, AND MASS SPECTROMETRY.	14760718 [Abstract]
"A proteomic analysis of human bile."; Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.; Mol. Cell. Proteomics 3:715-728(2004). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33 AND ASN-93, AND MASSSPECTROMETRY.	15084671 [Abstract]
"A new strategy for identification of N-glycosylated proteins andunambiguous assignment of their glycosylation sites using HILICenrichment and partial deglycosylation."; Hagglund P., Bunkenborg J., Elortza F., Jensen O.N., Roepstorff P.; J. Proteome Res. 3:556-566(2004). Cited for: GLYCOSYLATION AT ASN-33; ASN-72 AND ASN-93, AND MASS SPECTROMETRY.	15253437 [Abstract]
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry."; Zhang H., Li X.-J., Martin D.B., Aebersold R.; Nat. Biotechnol. 21:660-666(2003). Cited for: GLYCOSYLATION AT ASN-33.	12754519 [Abstract]
"Analysis of the five glycosylation sites of human alpha 1-acidglycoprotein."; Treuheit M.J., Costello C.E., Halsall H.B.; Biochem. J. 283:105-112(1992). Cited for: GLYCOSYLATION AT ASN-33; ASN-56; ASN-72; ASN-93 AND ASN-103.	1567356 [Abstract]
"The disulfide bonds of alpha1-acid glycoprotein."; Schmid K., Buergi W., Collins J.H., Nanno S.; Biochemistry 13:2694-2697(1974). Cited for: DISULFIDE BONDS.	4603214 [Abstract]
Pyrrolidone carboxylic acid
Reference	PubMed
"Structure of alpha 1-acid glycoprotein. The complete amino acidsequence, multiple amino acid substitutions, and homology with theimmunoglobulins."; Schmid K., Kaufmann H., Isemura S., Bauer F., Emura J., Motoyama T.,Ishiguro M., Nanno S.; Biochemistry 12:2711-2724(1973). Cited for: PROTEIN SEQUENCE OF 19-129.	4711474 [Abstract]