UniProt ID | NPC2_HUMAN | |
---|---|---|
UniProt AC | P61916 | |
Protein Name | NPC intracellular cholesterol transporter 2 {ECO:0000312|HGNC:HGNC:14537} | |
Gene Name | NPC2 {ECO:0000312|HGNC:HGNC:14537} | |
Organism | Homo sapiens (Human). | |
Sequence Length | 151 | |
Subcellular Localization | Secreted . Endoplasmic reticulum . Lysosome . | |
Protein Description | Intracellular cholesterol transporter which acts in concert with NPC1 and plays an important role in the egress of cholesterol from the endosomal/lysosomal compartment. Both NPC1 and NPC2 function as the cellular 'tag team duo' (TTD) to catalyze the mobilization of cholesterol within the multivesicular environment of the late endosome (LE) to effect egress through the limiting bilayer of the LE. NPC2 binds unesterified cholesterol that has been released from LDLs in the lumen of the late endosomes/lysosomes and transfers it to the cholesterol-binding pocket of the N-terminal domain of NPC1. Cholesterol binds to NPC1 with the hydroxyl group buried in the binding pocket and is exported from the limiting membrane of late endosomes/ lysosomes to the ER and plasma membrane by an unknown mechanism. The secreted form of NCP2 regulates biliary cholesterol secretion via stimulation of ABCG5/ABCG8-mediated cholesterol transport.. | |
Protein Sequence | MRFLAATFLLLALSTAAQAEPVQFKDCGSVDGVIKEVNVSPCPTQPCQLSKGQSYSVNVTFTSNIQSKSSKAVVHGILMGVPVPFPIPEPDGCKSGINCPIQKDKTYSYLNKLPVKSEYPSIKLVVEWQLQDDKNQSLFCWEIPVQIVSHL | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
7 | Phosphorylation | -MRFLAATFLLLALS -CHHHHHHHHHHHHH | 14.81 | 24043423 | |
14 | Phosphorylation | TFLLLALSTAAQAEP HHHHHHHHHHHHCCC | 15.47 | 24043423 | |
15 | Phosphorylation | FLLLALSTAAQAEPV HHHHHHHHHHHCCCC | 27.19 | 24043423 | |
29 | Phosphorylation | VQFKDCGSVDGVIKE CCCCCCCCCCCEEEE | 24.30 | 21712546 | |
44 | O-linked_Glycosylation | VNVSPCPTQPCQLSK EECCCCCCCCCCCCC | 52.43 | OGP | |
58 | N-linked_Glycosylation | KGQSYSVNVTFTSNI CCCEEEEEEEEECCC | 22.59 | 17018531 | |
58 | N-linked_Glycosylation | KGQSYSVNVTFTSNI CCCEEEEEEEEECCC | 22.59 | 16399764 | |
79 | Sulfoxidation | AVVHGILMGVPVPFP EEEEEEECCCCCCCC | 4.86 | 28465586 | |
93 | Glutathionylation | PIPEPDGCKSGINCP CCCCCCCCCCCCCCC | 4.06 | 22555962 | |
103 | Acetylation | GINCPIQKDKTYSYL CCCCCCCCCCCHHHH | 63.01 | 26051181 | |
103 | 2-Hydroxyisobutyrylation | GINCPIQKDKTYSYL CCCCCCCCCCCHHHH | 63.01 | - | |
105 | Ubiquitination | NCPIQKDKTYSYLNK CCCCCCCCCHHHHHC | 57.29 | - | |
105 | 2-Hydroxyisobutyrylation | NCPIQKDKTYSYLNK CCCCCCCCCHHHHHC | 57.29 | - | |
106 | Phosphorylation | CPIQKDKTYSYLNKL CCCCCCCCHHHHHCC | 28.03 | 29759185 | |
107 | Phosphorylation | PIQKDKTYSYLNKLP CCCCCCCHHHHHCCC | 10.89 | - | |
108 | Phosphorylation | IQKDKTYSYLNKLPV CCCCCCHHHHHCCCC | 28.51 | 29759185 | |
109 | Phosphorylation | QKDKTYSYLNKLPVK CCCCCHHHHHCCCCC | 12.13 | 29759185 | |
112 | Ubiquitination | KTYSYLNKLPVKSEY CCHHHHHCCCCCCCC | 52.12 | - | |
112 | 2-Hydroxyisobutyrylation | KTYSYLNKLPVKSEY CCHHHHHCCCCCCCC | 52.12 | - | |
116 | Acetylation | YLNKLPVKSEYPSIK HHHCCCCCCCCCCEE | 35.31 | - | |
117 | Phosphorylation | LNKLPVKSEYPSIKL HHCCCCCCCCCCEEE | 42.47 | 28102081 | |
119 | Phosphorylation | KLPVKSEYPSIKLVV CCCCCCCCCCEEEEE | 14.90 | 28102081 | |
121 | Phosphorylation | PVKSEYPSIKLVVEW CCCCCCCCEEEEEEE | 31.30 | 28102081 | |
135 | N-linked_Glycosylation | WQLQDDKNQSLFCWE EEECCCCCCEEEEEE | 43.60 | 16399764 | |
135 | N-linked_Glycosylation | WQLQDDKNQSLFCWE EEECCCCCCEEEEEE | 43.60 | 17018531 |
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 NPC2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NPC2_HUMAN !! |
* 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 NPC2_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
DHDDS_HUMAN | DHDDS | physical | 15110773 | |
NUD19_HUMAN | NUDT19 | physical | 22939629 | |
HXK3_HUMAN | HK3 | physical | 28514442 | |
NDKB_HUMAN | NME2 | physical | 28514442 | |
CFAB_HUMAN | CFB | physical | 28514442 | |
TTHY_HUMAN | TTR | physical | 28514442 | |
IRGQ_HUMAN | IRGQ | physical | 28514442 |
Kegg Disease | ||||||
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There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
607625 | Niemann-Pick disease C2 (NPC2) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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N-linked Glycosylation | |
Reference | PubMed |
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-135, AND MASSSPECTROMETRY. |