dbPTM

LRP10_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LRP10_HUMAN
UniProt AC	Q7Z4F1
Protein Name	Low-density lipoprotein receptor-related protein 10
Gene Name	LRP10
Organism	Homo sapiens (Human).
Sequence Length	713
Subcellular Localization	Membrane Single-pass type I membrane protein . Membrane, coated pit.
Protein Description	Probable receptor, which is involved in the internalization of lipophilic molecules and/or signal transduction. May be involved in the uptake of lipoprotein APOE in liver (By similarity)..
Protein Sequence	MLLATLLLLLLGGALAHPDRIIFPNHACEDPPAVLLEVQGTLQRPLVRDSRTSPANCTWLILGSKEQTVTIRFQKLHLACGSERLTLRSPLQPLISLCEAPPSPLQLPGGNVTITYSYAGARAPMGQGFLLSYSQDWLMCLQEEFQCLNHRCVSAVQRCDGVDACGDGSDEAGCSSDPFPGLTPRPVPSLPCNVTLEDFYGVFSSPGYTHLASVSHPQSCHWLLDPHDGRRLAVRFTALDLGFGDAVHVYDGPGPPESSRLLRSLTHFSNGKAVTVETLSGQAVVSYHTVAWSNGRGFNATYHVRGYCLPWDRPCGLGSGLGAGEGLGERCYSEAQRCDGSWDCADGTDEEDCPGCPPGHFPCGAAGTSGATACYLPADRCNYQTFCADGADERRCRHCQPGNFRCRDEKCVYETWVCDGQPDCADGSDEWDCSYVLPRKVITAAVIGSLVCGLLLVIALGCTCKLYAIRTQEYSIFAPLSRMEAEIVQQQAPPSYGQLIAQGAIPPVEDFPTENPNDNSVLGNLRSLLQILRQDMTPGGGPGARRRQRGRLMRRLVRRLRRWGLLPRTNTPARASEARSQVTPSAAPLEALDGGTGPAREGGAVGGQDGEQAPPLPIKAPLPSASTSPAPTTVPEAPGPLPSLPLEPSLLSGVVQALRGRLLPSLGPPGPTRSPPGPHTAVLALEDEDDVLLVPLAEPGVWVAEAEDEPLLT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
56	N-linked_Glycosylation	DSRTSPANCTWLILG CCCCCCCCEEEEEEC	27.43	UniProtKB CARBOHYD
58	Phosphorylation	RTSPANCTWLILGSK CCCCCCEEEEEECCC	24.10	-
64	Phosphorylation	CTWLILGSKEQTVTI EEEEEECCCCEEEEE	29.58	-
70	Phosphorylation	GSKEQTVTIRFQKLH CCCCEEEEEEEEEHH	15.15	24719451
82	Phosphorylation	KLHLACGSERLTLRS EHHHHCCCCEEECCC	21.30	-
111	N-linked_Glycosylation	PLQLPGGNVTITYSY CCCCCCCCEEEEEEE	33.40	UniProtKB CARBOHYD
183	Phosphorylation	SDPFPGLTPRPVPSL CCCCCCCCCCCCCCC	24.14	24719451
193	N-linked_Glycosylation	PVPSLPCNVTLEDFY CCCCCCCCEEHHHHE	28.06	UniProtKB CARBOHYD
299	N-linked_Glycosylation	WSNGRGFNATYHVRG EECCCCCEEEEEEEC	33.91	UniProtKB CARBOHYD
443	Phosphorylation	VLPRKVITAAVIGSL ECCHHHHHHHHHHHH	16.14	30175587
467	Phosphorylation	LGCTCKLYAIRTQEY HHCCEEHHHHHCCCE	5.86	30175587
471	Phosphorylation	CKLYAIRTQEYSIFA EEHHHHHCCCEEEEE	21.46	21945579
474	Phosphorylation	YAIRTQEYSIFAPLS HHHHCCCEEEEEEHH	9.39	21945579
475	Phosphorylation	AIRTQEYSIFAPLSR HHHCCCEEEEEEHHH	15.52	21945579
537	Phosphorylation	QILRQDMTPGGGPGA HHHHCCCCCCCCCCH	27.37	21815630
569	Phosphorylation	RWGLLPRTNTPARAS HCCCCCCCCCCHHHH	41.31	23403867
571	Phosphorylation	GLLPRTNTPARASEA CCCCCCCCCHHHHHH	20.08	23403867
576	Phosphorylation	TNTPARASEARSQVT CCCCHHHHHHHHCCC	26.66	-
580	Phosphorylation	ARASEARSQVTPSAA HHHHHHHHCCCCCCC	35.73	22199227
583	Phosphorylation	SEARSQVTPSAAPLE HHHHHCCCCCCCCHH	12.14	26055452
585	Phosphorylation	ARSQVTPSAAPLEAL HHHCCCCCCCCHHHH	27.91	21815630
596	Phosphorylation	LEALDGGTGPAREGG HHHHCCCCCCCCCCC	45.59	26055452
619	Ubiquitination	QAPPLPIKAPLPSAS CCCCCCCCCCCCCCC	41.85	23503661
624	Phosphorylation	PIKAPLPSASTSPAP CCCCCCCCCCCCCCC	42.40	22199227
626	Phosphorylation	KAPLPSASTSPAPTT CCCCCCCCCCCCCCC	33.48	22199227
627	Phosphorylation	APLPSASTSPAPTTV CCCCCCCCCCCCCCC	38.15	29496963
627	Ubiquitination	APLPSASTSPAPTTV CCCCCCCCCCCCCCC	38.15	23503661
628	Phosphorylation	PLPSASTSPAPTTVP CCCCCCCCCCCCCCC	19.30	29496963
632	Phosphorylation	ASTSPAPTTVPEAPG CCCCCCCCCCCCCCC	42.40	29496963
633	Phosphorylation	STSPAPTTVPEAPGP CCCCCCCCCCCCCCC	32.76	29496963
665	Phosphorylation	LRGRLLPSLGPPGPT HHCCCCCCCCCCCCC	46.02	23312004

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
Oops, there are no upstream regulatory protein records of LRP10_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LRP10_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 LRP10_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of LRP10_HUMAN !!

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 LRP10_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-583 AND THR-596, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-583, AND MASSSPECTROMETRY.	18691976 [Abstract]