NPCL1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NPCL1_HUMAN
• UniProt AC: Q9UHC9
• Protein Name: NPC1-like intracellular cholesterol transporter 1 {ECO:0000312|HGNC:HGNC:7898}
• Gene Name: NPC1L1 {ECO:0000312|HGNC:HGNC:7898}
• Organism: Homo sapiens (Human).
• Sequence Length: 1359
• Subcellular Localization: Apical cell membrane ; Multi-pass membrane protein . Cell membrane; Multi-pass membrane protein. Cytoplasmic vesicle membrane ; Multi-pass membrane protein . Subfractionation of brush border membranes from proximal enterocytes suggests considerable a
• Protein Description: Plays a major role in cholesterol homeostasis. Is critical for the uptake of cholesterol across the plasma membrane of the intestinal enterocyte. Is the direct molecular target of ezetimibe, a drug that inhibits cholesterol absorption. Lack of activity leads to multiple lipid transport defects. The protein may have a function in the transport of multiple lipids and their homeostasis, and may play a critical role in regulating lipid metabolism. Acts as a negative regulator of NPC2 and down-regulates its expression and secretion by inhibiting its maturation and accelerating its degradation..
• Protein Sequence: MAEAGLRGWLLWALLLRLAQSEPYTTIHQPGYCAFYDECGKNPELSGSLMTLSNVSCLSNTPARKITGDHLILLQKICPRLYTGPNTQACCSAKQLVSLEASLSITKALLTRCPACSDNFVNLHCHNTCSPNQSLFINVTRVAQLGAGQLPAVVAYEAFYQHSFAEQSYDSCSRVRVPAAATLAVGTMCGVYGSALCNAQRWLNFQGDTGNGLAPLDITFHLLEPGQAVGSGIQPLNEGVARCNESQGDDVATCSCQDCAASCPAIARPQALDSTFYLGQMPGSLVLIIILCSVFAVVTILLVGFRVAPARDKSKMVDPKKGTSLSDKLSFSTHTLLGQFFQGWGTWVASWPLTILVLSVIPVVALAAGLVFTELTTDPVELWSAPNSQARSEKAFHDQHFGPFFRTNQVILTAPNRSSYRYDSLLLGPKNFSGILDLDLLLELLELQERLRHLQVWSPEAQRNISLQDICYAPLNPDNTSLYDCCINSLLQYFQNNRTLLLLTANQTLMGQTSQVDWKDHFLYCANAPLTFKDGTALALSCMADYGAPVFPFLAIGGYKGKDYSEAEALIMTFSLNNYPAGDPRLAQAKLWEEAFLEEMRAFQRRMAGMFQVTFMAERSLEDEINRTTAEDLPIFATSYIVIFLYISLALGSYSSWSRVMVDSKATLGLGGVAVVLGAVMAAMGFFSYLGIRSSLVILQVVPFLVLSVGADNIFIFVLEYQRLPRRPGEPREVHIGRALGRVAPSMLLCSLSEAICFFLGALTPMPAVRTFALTSGLAVILDFLLQMSAFVALLSLDSKRQEASRLDVCCCVKPQELPPPGQGEGLLLGFFQKAYAPFLLHWITRGVVLLLFLALFGVSLYSMCHISVGLDQELALPKDSYLLDYFLFLNRYFEVGAPVYFVTTLGYNFSSEAGMNAICSSAGCNNFSFTQKIQYATEFPEQSYLAIPASSWVDDFIDWLTPSSCCRLYISGPNKDKFCPSTVNSLNCLKNCMSITMGSVRPSVEQFHKYLPWFLNDRPNIKCPKGGLAAYSTSVNLTSDGQVLDTVAILSPRLEYSGTISAHCNLYLLDSTSRFMAYHKPLKNSQDYTEALRAARELAANITADLRKVPGTDPAFEVFPYTITNVFYEQYLTILPEGLFMLSLCLVPTFAVSCLLLGLDLRSGLLNLLSIVMILVDTVGFMALWGISYNAVSLINLVSAVGMSVEFVSHITRSFAISTKPTWLERAKEATISMGSAVFAGVAMTNLPGILVLGLAKAQLIQIFFFRLNLLITLLGLLHGLVFLPVILSYVGPDVNPALALEQKRAEEAVAAVMVASCPNHPSRVSTADNIYVNHSFEGSIKGAGAISNFLPNNGRQF

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
54	N-linked_Glycosylation	GSLMTLSNVSCLSNT CEEEEECCCHHHCCC	32.60	21525977
56	Phosphorylation	LMTLSNVSCLSNTPA EEEECCCHHHCCCCC	17.37	-
104	Phosphorylation	VSLEASLSITKALLT HCHHHHHHHHHHHHH	26.22	24719451
132	N-linked_Glycosylation	CHNTCSPNQSLFINV ECCCCCCCCEEEEEE	27.98	UniProtKB CARBOHYD
138	N-linked_Glycosylation	PNQSLFINVTRVAQL CCCEEEEEEEEEHHC	23.05	21525977
244	N-linked_Glycosylation	NEGVARCNESQGDDV CHHHHCCCCCCCCCC	46.53	UniProtKB CARBOHYD
413	Phosphorylation	RTNQVILTAPNRSSY CCCCEEEECCCCCCC	29.01	30622161
416	N-linked_Glycosylation	QVILTAPNRSSYRYD CEEEECCCCCCCCCC	54.74	UniProtKB CARBOHYD
418	Phosphorylation	ILTAPNRSSYRYDSL EEECCCCCCCCCCEE	38.06	30622161
419	Phosphorylation	LTAPNRSSYRYDSLL EECCCCCCCCCCEEE	15.47	30622161
420	Phosphorylation	TAPNRSSYRYDSLLL ECCCCCCCCCCEEEC	17.90	30622161
431	N-linked_Glycosylation	SLLLGPKNFSGILDL EEECCCCCCCCCCCH	39.18	UniProtKB CARBOHYD
433	Phosphorylation	LLGPKNFSGILDLDL ECCCCCCCCCCCHHH	34.03	-
464	N-linked_Glycosylation	WSPEAQRNISLQDIC CCHHHHHCCCHHHHE	19.00	UniProtKB CARBOHYD
479	N-linked_Glycosylation	YAPLNPDNTSLYDCC ECCCCCCCCHHHHHH	32.59	UniProtKB CARBOHYD
497	N-linked_Glycosylation	LLQYFQNNRTLLLLT HHHHHHCCCEEEEEE	27.77	UniProtKB CARBOHYD
506	N-linked_Glycosylation	TLLLLTANQTLMGQT EEEEEEECCCCCCCC	30.08	UniProtKB CARBOHYD
626	N-linked_Glycosylation	RSLEDEINRTTAEDL CCHHHHHHHCCHHHC	32.95	UniProtKB CARBOHYD
658	Phosphorylation	LGSYSSWSRVMVDSK HCCCCCCCCCCCCCC	19.56	-
664	Phosphorylation	WSRVMVDSKATLGLG CCCCCCCCCCCCCCH	16.87	19053533
667	Phosphorylation	VMVDSKATLGLGGVA CCCCCCCCCCCHHHH	25.70	19053533
1052	Phosphorylation	LDTVAILSPRLEYSG EEEEEEECCCCEECC	11.23	24719451
1205	Phosphorylation	LVSAVGMSVEFVSHI HHHHCCCCHHHHHHH	16.74	-
1232	Phosphorylation	LERAKEATISMGSAV HHHHHHHEECCCCHH	18.06	-
1349	Phosphorylation	IKGAGAISNFLPNNG CCCCCHHHHCCCCCC	22.46	30622161

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

Oops, there are no upstream regulatory protein records of NPCL1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NPCL1_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of NPCL1_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of NPCL1_HUMAN !!

Drug and Disease Associations

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