LY96_HUMAN - dbPTM
LY96_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LY96_HUMAN
UniProt AC Q9Y6Y9
Protein Name Lymphocyte antigen 96
Gene Name LY96
Organism Homo sapiens (Human).
Sequence Length 160
Subcellular Localization Secreted, extracellular space . Secreted . Retained in the extracellular space at the cell surface by interaction with TLR4 (PubMed:10359581).
Protein Description Binds bacterial lipopolysaccharide (LPS). [PubMed: 17803912]
Protein Sequence MLPFLFFSTLFSSIFTEAQKQYWVCNSSDASISYTYCDKMQYPISINVNPCIELKRSKGLLHIFYIPRRDLKQLYFNLYITVNTMNLPKRKEVICRGSDDDYSFCRALKGETVNTTISFSFKGIKFSKGKYKCVVEAISGSPEEMLFCLEFVILHQPNSN
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 Orthologous
Protein Cluster
22PhosphorylationFTEAQKQYWVCNSSD
HHHHHHHEEEECCCC
13.57-
26N-linked_GlycosylationQKQYWVCNSSDASIS
HHHEEEECCCCCEEE
34.6217569869
42PhosphorylationTYCDKMQYPISINVN
EECCCCCCEEEEEEC
10.0725002506
45PhosphorylationDKMQYPISINVNPCI
CCCCCEEEEEECCCE
12.0125002506
114N-linked_GlycosylationALKGETVNTTISFSF
HHCCCEECEEEEEEE
38.6417569869
120PhosphorylationVNTTISFSFKGIKFS
ECEEEEEEECCCEEC
21.1824719451
131PhosphorylationIKFSKGKYKCVVEAI
CEECCCEEEEEEEEC
20.49-

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
22YPhosphorylationKinaseLYNP07948
PSP
131YPhosphorylationKinaseLYNP07948
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LY96_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 LY96_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TLR4_HUMANTLR4physical
11976338

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 LY96_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Crystal structures of human MD-2 and its complex with antiendotoxiclipid IVa.";
Ohto U., Fukase K., Miyake K., Satow Y.;
Science 316:1632-1634(2007).
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 17-160 IN COMPLEX WITH LIPIDIV-A, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-26 AND ASN-114.

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