LBP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LBP_HUMAN
• UniProt AC: P18428
• Protein Name: Lipopolysaccharide-binding protein
• Gene Name: LBP
• Organism: Homo sapiens (Human).
• Sequence Length: 481
• Subcellular Localization: Secreted . Cytoplasmic granule membrane . Membrane-associated in polymorphonuclear Leukocytes (PMN) granules.
• Protein Description: Plays a role in the innate immune response. Binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria. [PubMed: 7517398]
• Protein Sequence: MGALARALPSILLALLLTSTPEALGANPGLVARITDKGLQYAAQEGLLALQSELLRITLPDFTGDLRIPHVGRGRYEFHSLNIHSCELLHSALRPVPGQGLSLSISDSSIRVQGRWKVRKSFFKLQGSFDVSVKGISISVNLLLGSESSGRPTVTASSCSSDIADVEVDMSGDLGWLLNLFHNQIESKFQKVLESRICEMIQKSVSSDLQPYLQTLPVTTEIDSFADIDYSLVEAPRATAQMLEVMFKGEIFHRNHRSPVTLLAAVMSLPEEHNKMVYFAISDYVFNTASLVYHEEGYLNFSITDDMIPPDSNIRLTTKSFRPFVPRLARLYPNMNLELQGSVPSAPLLNFSPGNLSVDPYMEIDAFVLLPSSSKEPVFRLSVATNVSATLTFNTSKITGFLKPGKVKVELKESKVGLFNAELLEALLNYYILNTFYPKFNDKLAEGFPLPLLKRVQLYDLGLQIHKDFLFLGANVQYMRV

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
300	N-linked_Glycosylation	YHEEGYLNFSITDDM EEECCEECEEECCCC	21.82	UniProtKB CARBOHYD
355	N-linked_Glycosylation	LLNFSPGNLSVDPYM CCCCCCCCCCCCCCC	32.31	UniProtKB CARBOHYD
386	N-linked_Glycosylation	FRLSVATNVSATLTF EEEEEEECEEEEEEE	18.93	UniProtKB CARBOHYD
394	N-linked_Glycosylation	VSATLTFNTSKITGF EEEEEEEECCCCCCE	37.90	19159218
414	Phosphorylation	VKVELKESKVGLFNA EEEEEECCCCCCCCH	30.93	23612710
454	Acetylation	GFPLPLLKRVQLYDL CCCCCHHEEEEHHHC	59.20	30589847

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LBP_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 LBP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FHR1_HUMAN	CFHR1	physical	8663389
APOA1_HUMAN	APOA1	physical	8663389
SMAD3_HUMAN	SMAD3	physical	21988832
PSA3_HUMAN	PSMA3	physical	21988832
SET1A_HUMAN	SETD1A	physical	21988832
PRDX4_HUMAN	PRDX4	physical	21988832
TRA2A_HUMAN	TRA2A	physical	21988832
P5CR3_HUMAN	PYCRL	physical	21988832
T22D4_HUMAN	TSC22D4	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

"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-394, AND MASSSPECTROMETRY.
PubMed: 19159218