NGAL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NGAL_HUMAN
• UniProt AC: P80188
• Protein Name: Neutrophil gelatinase-associated lipocalin
• Gene Name: LCN2
• Organism: Homo sapiens (Human).
• Sequence Length: 198
• Subcellular Localization: Secreted . Upon binding to the SLC22A17 (24p3R) receptor, it is internalized.
• Protein Description: Iron-trafficking protein involved in multiple processes such as apoptosis, innate immunity and renal development. Binds iron through association with 2,5-dihydroxybenzoic acid (2,5-DHBA), a siderophore that shares structural similarities with bacterial enterobactin, and delivers or removes iron from the cell, depending on the context. Iron-bound form (holo-24p3) is internalized following binding to the SLC22A17 (24p3R) receptor, leading to release of iron and subsequent increase of intracellular iron concentration. In contrast, association of the iron-free form (apo-24p3) with the SLC22A17 (24p3R) receptor is followed by association with an intracellular siderophore, iron chelation and iron transfer to the extracellular medium, thereby reducing intracellular iron concentration. Involved in apoptosis due to interleukin-3 (IL3) deprivation: iron-loaded form increases intracellular iron concentration without promoting apoptosis, while iron-free form decreases intracellular iron levels, inducing expression of the proapoptotic protein BCL2L11/BIM, resulting in apoptosis. Involved in innate immunity, possibly by sequestrating iron, leading to limit bacterial growth..
• Protein Sequence: MPLGLLWLGLALLGALHAQAQDSTSDLIPAPPLSKVPLQQNFQDNQFQGKWYVVGLAGNAILREDKDPQKMYATIYELKEDKSYNVTSVLFRKKKCDYWIRTFVPGCQPGEFTLGNIKSYPGLTSYLVRVVSTNYNQHAMVFFKKVSQNREYFKITLYGRTKELTSELKENFIRFSKSLGLPENHIVFPVPIDQCIDG

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	GALHAQAQDSTSDLI HHHHHHHCCCCCCCC	32.86	7683678
21	Pyrrolidone_carboxylic_acid	GALHAQAQDSTSDLI HHHHHHHCCCCCCCC	32.86	-
21	Pyrrolidone_carboxylic_acid	GALHAQAQDSTSDLI HHHHHHHCCCCCCCC	32.86	7683678
23	Phosphorylation	LHAQAQDSTSDLIPA HHHHHCCCCCCCCCC	20.10	24505115
72	Phosphorylation	DKDPQKMYATIYELK CCCHHHHEEEEEECC	13.97	-
76	Phosphorylation	QKMYATIYELKEDKS HHHEEEEEECCCCCC	15.74	-
79	2-Hydroxyisobutyrylation	YATIYELKEDKSYNV EEEEEECCCCCCCCE	52.51	-
83	Phosphorylation	YELKEDKSYNVTSVL EECCCCCCCCEEEEE	33.97	23403867
84	Phosphorylation	ELKEDKSYNVTSVLF ECCCCCCCCEEEEEE	21.28	23403867
85	N-linked_Glycosylation	LKEDKSYNVTSVLFR CCCCCCCCEEEEEEE	37.37	15084671
85	N-linked_Glycosylation	LKEDKSYNVTSVLFR CCCCCCCCEEEEEEE	37.37	15084671
87	Phosphorylation	EDKSYNVTSVLFRKK CCCCCCEEEEEEEEC	14.96	23403867
88	Phosphorylation	DKSYNVTSVLFRKKK CCCCCEEEEEEEECC	16.73	23403867
126	Phosphorylation	SYPGLTSYLVRVVST CCCCCEEEEEEEEEC	12.18	-
132	Phosphorylation	SYLVRVVSTNYNQHA EEEEEEEECCCCCEE	14.21	30631047
133	Phosphorylation	YLVRVVSTNYNQHAM EEEEEEECCCCCEEE	30.07	-
154	Acetylation	SQNREYFKITLYGRT HHCCCEEEEEEECCH	33.60	25038526

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NGAL_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 NGAL_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NGAL_HUMAN	LCN2	physical	7683678

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

"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-85, AND MASS SPECTROMETRY.
PubMed: 19159218

"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-85, 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-85, AND MASS SPECTROMETRY.
PubMed: 16335952

"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-85, AND MASS SPECTROMETRY.
PubMed: 15084671

"Isolation and primary structure of NGAL, a novel protein associatedwith human neutrophil gelatinase.";
Kjeldsen L., Johnsen A.H., Sengelov H., Borregaard N.;
J. Biol. Chem. 268:10425-10432(1993).
Cited for: PROTEIN SEQUENCE OF 21-198.
PubMed: 7683678

Pyrrolidone carboxylic acid

"Isolation and primary structure of NGAL, a novel protein associatedwith human neutrophil gelatinase.";
Kjeldsen L., Johnsen A.H., Sengelov H., Borregaard N.;
J. Biol. Chem. 268:10425-10432(1993).
Cited for: PROTEIN SEQUENCE OF 21-198.
PubMed: 7683678