ZA2G_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ZA2G_HUMAN
• UniProt AC: P25311
• Protein Name: Zinc-alpha-2-glycoprotein
• Gene Name: AZGP1
• Organism: Homo sapiens (Human).
• Sequence Length: 298
• Subcellular Localization: Secreted.
• Protein Description: Stimulates lipid degradation in adipocytes and causes the extensive fat losses associated with some advanced cancers. May bind polyunsaturated fatty acids..
• Protein Sequence: MVRMVPVLLSLLLLLGPAVPQENQDGRYSLTYIYTGLSKHVEDVPAFQALGSLNDLQFFRYNSKDRKSQPMGLWRQVEGMEDWKQDSQLQKAREDIFMETLKDIVEYYNDSNGSHVLQGRFGCEIENNRSSGAFWKYYYDGKDYIEFNKEIPAWVPFDPAAQITKQKWEAEPVYVQRAKAYLEEECPATLRKYLKYSKNILDRQDPPSVVVTSHQAPGEKKKLKCLAYDFYPGKIDVHWTRAGEVQEPELRGDVLHNGNGTYQSWVVVAVPPQDTAPYSCHVQHSSLAQPLVVPWEAS

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
21	Pyrrolidone_carboxylic_acid	LLGPAVPQENQDGRY HHCCCCCCCCCCCCE	56.53	-
21	Pyrrolidone_carboxylic_acid	LLGPAVPQENQDGRY HHCCCCCCCCCCCCE	56.53	3422450
21	Pyrrolidone_carboxylic_acid	LLGPAVPQENQDGRY HHCCCCCCCCCCCCE	56.53	3422450
107	Phosphorylation	TLKDIVEYYNDSNGS HHHHHHHHHHCCCCC	9.18	22817900
109	N-linked_Glycosylation	KDIVEYYNDSNGSHV HHHHHHHHCCCCCEE	45.38	18780401
112	N-linked_Glycosylation	VEYYNDSNGSHVLQG HHHHHCCCCCEEEEE	59.87	18780401
128	N-linked_Glycosylation	FGCEIENNRSSGAFW EEEEEECCCCCCCEE	32.21	22171320
208	Phosphorylation	LDRQDPPSVVVTSHQ CCCCCCCCEEEECCC	32.69	26657352
212	Phosphorylation	DPPSVVVTSHQAPGE CCCCEEEECCCCCCC	14.64	26657352
213	Phosphorylation	PPSVVVTSHQAPGEK CCCEEEECCCCCCCC	11.29	26657352
259	N-linked_Glycosylation	GDVLHNGNGTYQSWV CCEEECCCCCEEEEE	44.97	18930737

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ZA2G_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ZA2G_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ZA2G_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NUF2_HUMAN	NUF2	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.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Crystal structure of the novel complex formed between zinc alpha2-glycoprotein (ZAG) and prolactin-inducible protein (PIP) from humanseminal plasma.";
Hassan M.I., Bilgrami S., Kumar V., Singh N., Yadav S., Kaur P.,Singh T.P.;
J. Mol. Biol. 384:663-672(2008).
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 32-149 IN COMPLEX WITH PIP,DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-259.
PubMed: 18930737

"Crystallographic studies of ligand binding by Zn-alpha2-glycoprotein.";
Delker S.L., West A.P. Jr., McDermott L., Kennedy M.W., Bjorkman P.J.;
J. Struct. Biol. 148:205-213(2004).
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 21-298, DISULFIDE BONDS, ANDGLYCOSYLATION AT ASN-128 AND ASN-259.
PubMed: 15477100

"Crystal structure of human ZAG, a fat-depleting factor related to MHCmolecules.";
Sanchez L.M., Chirino A.J., Bjorkman P.J.;
Science 283:1914-1919(1999).
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), DISULFIDE BONDS, ANDGLYCOSYLATION AT ASN-109; ASN-128 AND ASN-259.
PubMed: 10206894

"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-128, STRUCTURE OF CARBOHYDRATES, AND MASSSPECTROMETRY.
PubMed: 22171320

"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-109; ASN-112 AND ASN-128,AND MASS SPECTROMETRY.
PubMed: 19159218

"Identification of N-linked glycoproteins in human milk by hydrophilicinteraction liquid chromatography and mass spectrometry.";
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
Proteomics 8:3833-3847(2008).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-109; ASN-112 AND ASN-128,AND MASS SPECTROMETRY.
PubMed: 18780401

"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-109; ASN-112 AND ASN-128,AND MASS SPECTROMETRY.
PubMed: 16740002

"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-112, AND MASSSPECTROMETRY.
PubMed: 16335952

"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-112 AND ASN-128, AND MASSSPECTROMETRY.
PubMed: 14760718

"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-128, AND MASSSPECTROMETRY.
PubMed: 15084671