dbPTM

VLDLR_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	VLDLR_HUMAN
UniProt AC	P98155
Protein Name	Very low-density lipoprotein receptor
Gene Name	VLDLR
Organism	Homo sapiens (Human).
Sequence Length	873
Subcellular Localization	Membrane Single-pass type I membrane protein. Membrane, clathrin-coated pit Single-pass type I membrane protein.
Protein Description	Binds VLDL and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits. Binding to Reelin induces tyrosine phosphorylation of Dab1 and modulation of Tau phosphorylation (By similarity)..
Protein Sequence	MGTSALWALWLLLALCWAPRESGATGTGRKAKCEPSQFQCTNGRCITLLWKCDGDEDCVDGSDEKNCVKKTCAESDFVCNNGQCVPSRWKCDGDPDCEDGSDESPEQCHMRTCRIHEISCGAHSTQCIPVSWRCDGENDCDSGEDEENCGNITCSPDEFTCSSGRCISRNFVCNGQDDCSDGSDELDCAPPTCGAHEFQCSTSSCIPISWVCDDDADCSDQSDESLEQCGRQPVIHTKCPASEIQCGSGECIHKKWRCDGDPDCKDGSDEVNCPSRTCRPDQFECEDGSCIHGSRQCNGIRDCVDGSDEVNCKNVNQCLGPGKFKCRSGECIDISKVCNQEQDCRDWSDEPLKECHINECLVNNGGCSHICKDLVIGYECDCAAGFELIDRKTCGDIDECQNPGICSQICINLKGGYKCECSRGYQMDLATGVCKAVGKEPSLIFTNRRDIRKIGLERKEYIQLVEQLRNTVALDADIAAQKLFWADLSQKAIFSASIDDKVGRHVKMIDNVYNPAAIAVDWVYKTIYWTDAASKTISVATLDGTKRKFLFNSDLREPASIAVDPLSGFVYWSDWGEPAKIEKAGMNGFDRRPLVTADIQWPNGITLDLIKSRLYWLDSKLHMLSSVDLNGQDRRIVLKSLEFLAHPLALTIFEDRVYWIDGENEAVYGANKFTGSELATLVNNLNDAQDIIVYHELVQPSGKNWCEEDMENGGCEYLCLPAPQINDHSPKYTCSCPSGYNVEENGRDCQSTATTVTYSETKDTNTTEISATSGLVPGGINVTTAVSEVSVPPKGTSAAWAILPLLLLVMAAVGGYLMWRNWQHKNMKSMNFDNPVYLKTTEEDLSIDIGRHSASVGHTYPAISVVSTDDDLA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
71	O-linked_Glycosylation	EKNCVKKTCAESDFV CCCEEEHHHHCCCEE	15.95	55825159
151	N-linked_Glycosylation	EDEENCGNITCSPDE CCCCCCCCCEECCCC	28.70	UniProtKB CARBOHYD
153	O-linked_Glycosylation	EENCGNITCSPDEFT CCCCCCCEECCCCEE	15.78	OGP
192	O-linked_Glycosylation	ELDCAPPTCGAHEFQ CCCCCCCCCCCCEEE	23.63	OGP
277	O-linked_Glycosylation	EVNCPSRTCRPDQFE CCCCCCCCCCCCCEE	19.73	55823601
524	Phosphorylation	AIAVDWVYKTIYWTD HHHHHEEHHHHCCCC	9.73	-
759	Phosphorylation	TATTVTYSETKDTNT CCEEEEEECCCCCCC	29.44	-
765	N-linked_Glycosylation	YSETKDTNTTEISAT EECCCCCCCCEEEEC	55.95	UniProtKB CARBOHYD
781	N-linked_Glycosylation	GLVPGGINVTTAVSE CCCCCCEEEEEEEEE	28.49	UniProtKB CARBOHYD
800 (in isoform 2)	Ubiquitination	-	5.42	21890473
828 (in isoform 1)	Ubiquitination	-	56.82	21890473
828	Ubiquitination	NWQHKNMKSMNFDNP CCCCCCCCCCCCCCC	56.82	21890473
837	Phosphorylation	MNFDNPVYLKTTEED CCCCCCEEEEECCCC	12.07	21945579
839	Ubiquitination	FDNPVYLKTTEEDLS CCCCEEEEECCCCEE	35.40	20427281
846	Phosphorylation	KTTEEDLSIDIGRHS EECCCCEEEECCCCC	30.45	30576142
853	Phosphorylation	SIDIGRHSASVGHTY EEECCCCCCCCCCCC	22.37	28450419
855	Phosphorylation	DIGRHSASVGHTYPA ECCCCCCCCCCCCCC	31.48	28450419
859	Phosphorylation	HSASVGHTYPAISVV CCCCCCCCCCCEEEE	25.85	28450419
860	Phosphorylation	SASVGHTYPAISVVS CCCCCCCCCCEEEEE	5.74	25884760
864	Phosphorylation	GHTYPAISVVSTDDD CCCCCCEEEEECCCC	20.69	26437602
867	Phosphorylation	YPAISVVSTDDDLA- CCCEEEEECCCCCC-	24.78	22617229
868	Phosphorylation	PAISVVSTDDDLA-- CCEEEEECCCCCC--	31.66	30576142

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
-	K	Ubiquitination	E3 ubiquitin ligase	MYLIP	Q8WY64	PMID:20427281

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
839	K	ubiquitylation		20427281
Ubiquitinated at Lys-839 by MYLIP leading to degradation.

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 VLDLR_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DAB1_HUMAN	DAB1	physical	10827173
SNX17_HUMAN	SNX17	physical	12169628
MYLIP_HUMAN	MYLIP	physical	21734303
RELN_HUMAN	RELN	physical	10571240
CLUS_MOUSE	Clu	physical	12824284

Drug and Disease Associations

Kegg Disease
H01204	Cerebellar ataxia, mental retardation (MR), and dysequilibrium syndrome (CAMRQ)
OMIM Disease
224050	Cerebellar ataxia, mental retardation, and dysequilibrium syndrome 1 (CAMRQ1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of VLDLR_HUMAN

Related Literatures of Post-Translational Modification

Ubiquitylation
Reference	PubMed
"The E3 ubiquitin ligase IDOL induces the degradation of the lowdensity lipoprotein receptor family members VLDLR and ApoER2."; Hong C., Duit S., Jalonen P., Out R., Scheer L., Sorrentino V.,Boyadjian R., Rodenburg K.W., Foley E., Korhonen L., Lindholm D.,Nimpf J., van Berkel T.J., Tontonoz P., Zelcer N.; J. Biol. Chem. 285:19720-19726(2010). Cited for: UBIQUITINATION AT LYS-839 BY MYLIP, GLYCOSYLATION, AND MUTAGENESIS OFLYS-825; LYS-828 AND LYS-839.	20427281 [Abstract]

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