dbPTM

RAGE_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RAGE_HUMAN
UniProt AC	Q15109
Protein Name	Advanced glycosylation end product-specific receptor
Gene Name	AGER
Organism	Homo sapiens (Human).
Sequence Length	404
Subcellular Localization	Isoform 1: Cell membrane Single-pass type I membrane protein. Isoform 2: Secreted. Isoform 10: Cell membrane Single-pass type I membrane protein .
Protein Description	Mediates interactions of advanced glycosylation end products (AGE). These are nonenzymatically glycosylated proteins which accumulate in vascular tissue in aging and at an accelerated rate in diabetes. Acts as a mediator of both acute and chronic vascular inflammation in conditions such as atherosclerosis and in particular as a complication of diabetes. AGE/RAGE signaling plays an important role in regulating the production/expression of TNF-alpha, oxidative stress, and endothelial dysfunction in type 2 diabetes. Interaction with S100A12 on endothelium, mononuclear phagocytes, and lymphocytes triggers cellular activation, with generation of key proinflammatory mediators. Interaction with S100B after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling (By similarity). Receptor for amyloid beta peptide. Contributes to the translocation of amyloid-beta peptide (ABPP) across the cell membrane from the extracellular to the intracellular space in cortical neurons. ABPP-initiated RAGE signaling, especially stimulation of p38 mitogen-activated protein kinase (MAPK), has the capacity to drive a transport system delivering ABPP as a complex with RAGE to the intraneuronal space. Can also bind oligonucleotides..
Protein Sequence	MAAGTAVGAWVLVLSLWGAVVGAQNITARIGEPLVLKCKGAPKKPPQRLEWKLNTGRTEAWKVLSPQGGGPWDSVARVLPNGSLFLPAVGIQDEGIFRCQAMNRNGKETKSNYRVRVYQIPGKPEIVDSASELTAGVPNKVGTCVSEGSYPAGTLSWHLDGKPLVPNEKGVSVKEQTRRHPETGLFTLQSELMVTPARGGDPRPTFSCSFSPGLPRHRALRTAPIQPRVWEPVPLEEVQLVVEPEGGAVAPGGTVTLTCEVPAQPSPQIHWMKDGVPLPLPPSPVLILPEIGPQDQGTYSCVATHSSHGPQESRAVSISIIEPGEEGPTAGSVGGSGLGTLALALGILGGLGTAALLIGVILWQRRQRRGEERKAPENQEEEEERAELNQSEEPEAGESSTGGP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
25	N-linked_Glycosylation	GAVVGAQNITARIGE HHHHCCCCHHHCCCC	32.80	UniProtKB CARBOHYD
81	N-linked_Glycosylation	SVARVLPNGSLFLPA HHEEECCCCCEEECC	48.82	UniProtKB CARBOHYD
148 (in isoform 4)	Phosphorylation	-	25.60	23911959
148 (in isoform 6)	Phosphorylation	-	25.60	23911959
177	Phosphorylation	GVSVKEQTRRHPETG CCCHHHHHHCCCCCC	30.66	24719451
187	Phosphorylation	HPETGLFTLQSELMV CCCCCCEEECEEEEE	29.00	24719451
195	Phosphorylation	LQSELMVTPARGGDP ECEEEEECCCCCCCC	9.39	24719451
271 (in isoform 2)	Phosphorylation	-	9.35	16674116
278 (in isoform 9)	Phosphorylation	-	6.72	-
291 (in isoform 9)	Phosphorylation	-	10.35	-
391	Phosphorylation	ERAELNQSEEPEAGE HHHHHHCCCCCCCCC	42.74	21829704
399	Phosphorylation	EEPEAGESSTGGP-- CCCCCCCCCCCCC--	32.08	23911959
400	Phosphorylation	EPEAGESSTGGP--- CCCCCCCCCCCC---	27.11	23911959

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
391	S	Phosphorylation	Kinase	ATM	Q13315	PSP
391	S	Phosphorylation	Kinase	PKCZ	Q05513	PSP

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SC61B_HUMAN	SEC61B	physical	10601334
A4_HUMAN	APP	physical	21832049
NRP1_HUMAN	NRP1	physical	26186194
CSTF2_HUMAN	CSTF2	physical	26186194

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 RAGE_HUMAN

Related Literatures of Post-Translational Modification