dbPTM

A1AG2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	A1AG2_HUMAN
UniProt AC	P19652
Protein Name	Alpha-1-acid glycoprotein 2
Gene Name	ORM2
Organism	Homo sapiens (Human).
Sequence Length	201
Subcellular Localization	Secreted.
Protein Description	Functions as transport protein in the blood stream. Binds various hydrophobic ligands in the interior of its beta-barrel domain. Also binds synthetic drugs and influences their distribution and availability. Appears to function in modulating the activity of the immune system during the acute-phase reaction..
Protein Sequence	MALSWVLTVLSLLPLLEAQIPLCANLVPVPITNATLDRITGKWFYIASAFRNEEYNKSVQEIQATFFYFTPNKTEDTIFLREYQTRQNQCFYNSSYLNVQRENGTVSRYEGGREHVAHLLFLRDTKTLMFGSYLDDEKNWGLSFYADKPETTKEQLGEFYEALDCLCIPRSDVMYTDWKKDKCEPLEKQHEKERKQEEGES

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MALSWVLTVLS ----CHHHHHHHHHH	12.95	24043423
8	Phosphorylation	MALSWVLTVLSLLPL CHHHHHHHHHHHHHH	15.13	24043423
11	Phosphorylation	SWVLTVLSLLPLLEA HHHHHHHHHHHHHHC	24.43	24043423
19	Pyrrolidone_carboxylic_acid	LLPLLEAQIPLCANL HHHHHHCCCCCCCCC	28.58	15253437
19	Pyrrolidone_carboxylic_acid	LLPLLEAQIPLCANL HHHHHHCCCCCCCCC	28.58	15253437
19	Pyrrolidone_carboxylic_acid	LLPLLEAQIPLCANL HHHHHHCCCCCCCCC	28.58	-
32	Phosphorylation	NLVPVPITNATLDRI CCCEEECCCCCHHHH	16.84	24043423
33	N-linked_Glycosylation	LVPVPITNATLDRIT CCEEECCCCCHHHHC	31.48	22171320
33	N-linked_Glycosylation	LVPVPITNATLDRIT CCEEECCCCCHHHHC	31.48	22171320
35	Phosphorylation	PVPITNATLDRITGK EEECCCCCHHHHCCC	31.12	24043423
40	Phosphorylation	NATLDRITGKWFYIA CCCHHHHCCCEEEHH	33.33	24043423
45	Nitration	RITGKWFYIASAFRN HHCCCEEEHHHHHCC	8.41	-
55	Nitration	SAFRNEEYNKSVQEI HHHCCHHHHHHHHHC	23.01	-
56	N-linked_Glycosylation	AFRNEEYNKSVQEIQ HHCCHHHHHHHHHCC	33.15	1567356
56	N-linked_Glycosylation	AFRNEEYNKSVQEIQ HHCCHHHHHHHHHCC	33.15	4711474
65	Phosphorylation	SVQEIQATFFYFTPN HHHHCCEEEEEECCC	9.63	25627689
68	Nitration	EIQATFFYFTPNKTE HCCEEEEEECCCCCC	11.44	-
72	N-linked_Glycosylation	TFFYFTPNKTEDTIF EEEEECCCCCCCEEE	61.90	1567356
72	N-linked_Glycosylation	TFFYFTPNKTEDTIF EEEEECCCCCCCEEE	61.90	18638581
93	N-linked_Glycosylation	RQNQCFYNSSYLNVQ CCCCCCCCCCCEEEE	12.29	18638581
93	N-linked_Glycosylation	RQNQCFYNSSYLNVQ CCCCCCCCCCCEEEE	12.29	1567356
96	Nitration	QCFYNSSYLNVQREN CCCCCCCCEEEEEEC	11.34	-
98	N-linked_Glycosylation	FYNSSYLNVQRENGT CCCCCCEEEEEECCC	21.46	17623646
98	N-linked_Glycosylation	FYNSSYLNVQRENGT CCCCCCEEEEEECCC	21.46	17623646
103	N-linked_Glycosylation	YLNVQRENGTVSRYE CEEEEEECCCEEEEC	54.33	4711474
103	N-linked_Glycosylation	YLNVQRENGTVSRYE CEEEEEECCCEEEEC	54.33	1567356
109	Nitration	ENGTVSRYEGGREHV ECCCEEEECCCHHEE	16.06	-
132	Phosphorylation	TKTLMFGSYLDDEKN CCEEEECCEECCCCC	15.97	24043423
133	Nitration	KTLMFGSYLDDEKNW CEEEECCEECCCCCC	17.96	-
133	Phosphorylation	KTLMFGSYLDDEKNW CEEEECCEECCCCCC	17.96	24043423
145	Nitration	KNWGLSFYADKPETT CCCCCEEECCCCCCC	15.54	-
160	Nitration	KEQLGEFYEALDCLC HHHHHHHHHHHHHEE	8.94	-
175	Nitration	IPRSDVMYTDWKKDK EEHHHCCCCCCCCCC	11.03	-
179	Acetylation	DVMYTDWKKDKCEPL HCCCCCCCCCCCHHH	54.63	30586329
188	Glycation	DKCEPLEKQHEKERK CCCHHHHHHHHHHHH	65.72	-

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 A1AG2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of A1AG2_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 A1AG2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
STK3_HUMAN	STK3	physical	21988832
PRDX6_HUMAN	PRDX6	physical	21988832

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 A1AG2_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, STRUCTURE OFCARBOHYDRATES, 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-33; ASN-56; ASN-93 ANDASN-103, AND MASS SPECTROMETRY.	19159218 [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 ANDASN-93, 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 MASS SPECTROMETRY.	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: PYROGLUTAMATE FORMATION AT GLN-19, GLYCOSYLATION AT ASN-33 AND ASN-93,AND MASS SPECTROMETRY.	15253437 [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]