ARH_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ARH_MOUSE
• UniProt AC: Q8C142
• Protein Name: Low density lipoprotein receptor adapter protein 1 {ECO:0000305}
• Gene Name: Ldlrap1 {ECO:0000312|MGI:MGI:2140175}
• Organism: Mus musculus (Mouse).
• Sequence Length: 308
• Subcellular Localization: Cytoplasm .
• Protein Description: Adapter protein (clathrin-associated sorting protein (CLASP)) required for efficient endocytosis of the LDL receptor (LDLR) in polarized cells such as hepatocytes and lymphocytes, but not in non-polarized cells (fibroblasts). May be required for LDL binding and internalization but not for receptor clustering in coated pits. May facilitate the endocytocis of LDLR and LDLR-LDL complexes from coated pits by stabilizing the interaction between the receptor and the structural components of the pits. May also be involved in the internalization of other LDLR family members. Binds to phosphoinositides, which regulate clathrin bud assembly at the cell surface. Required for trafficking of LRP2 to the endocytic recycling compartment which is necessary for LRP2 proteolysis, releasing a tail fragment which translocates to the nucleus and mediates transcriptional repression (By similarity)..
• Protein Sequence: MDALKSAGRALIRSPSLAKQSWAGGRHRKLPENWTDTRETLLEGMVFSLKYLGMTLVERPKGEELSAAAVKRIVATAKASGKKLQKVTLKVSPRGIILTDSLTSQLIENVSIYRISYCTADKMHDKVFAYIAQSQQNESLECHAFLCTKRKVAQAVTLTVAQAFKVAFEFWQVSKEEKEKREKANQEGGDVPGTRRDSTPSLKTLVATGNLLDLEEVAKAPLSTVSANTNNVDETPRPQVLGNNSVVWELDDGLDEAFSRLAQSRTNPQVLDTGLSAQDIHYAQCLSPTDWDKPDSSGIDQDDDVFTF

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
1	Acetylation	-------MDALKSAG -------CHHHHHHH	6.49	-
14	Phosphorylation	AGRALIRSPSLAKQS HHHHHHHCHHHHHCC	16.31	26824392
16	Phosphorylation	RALIRSPSLAKQSWA HHHHHCHHHHHCCCC	42.05	22942356
19	Ubiquitination	IRSPSLAKQSWAGGR HHCHHHHHCCCCCCC	50.59	22790023
194	Phosphorylation	EGGDVPGTRRDSTPS CCCCCCCCCCCCCCC	19.23	26239621
198	Phosphorylation	VPGTRRDSTPSLKTL CCCCCCCCCCCHHHH	40.17	25521595
199	Phosphorylation	PGTRRDSTPSLKTLV CCCCCCCCCCHHHHH	22.61	25521595
201	Phosphorylation	TRRDSTPSLKTLVAT CCCCCCCCHHHHHHH	42.46	27087446
204	Phosphorylation	DSTPSLKTLVATGNL CCCCCHHHHHHHCCC	31.58	22817900
245	Phosphorylation	PQVLGNNSVVWELDD CCCCCCCCEEEEECC	23.27	30352176

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

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

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Oops, there are no PPI records of ARH_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, AND MASSSPECTROMETRY.
PubMed: 19367708

"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, AND MASSSPECTROMETRY.
PubMed: 18630941