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Q9UHC9 (NPCL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Niemann-Pick C1-like protein 1
Gene names
Name:NPC1L1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1359 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.12

Subunit structure

Interacts with RAB11A, MYO5B and RAB11FIP2. Interaction with RAB11A, MYO5B and RAB11FIP2 is required for proper transport to the plasma membrane upon cholesterol depletion. Interacts with NPC2. Ref.11 Ref.12

Subcellular location

Apical cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein By similarity. Cytoplasmic vesicle membrane; Multi-pass membrane protein. Note: Subfractionation of brush border membranes from proximal enterocytes suggests considerable association with the apical membrane fraction. Exists as a predominantly cell surface membrane expressed protein By similarity. According to Ref.8, localizes in a subcellular vesicular compartment rich in RAB5. Ref.8

Tissue specificity

Widely expressed. Expressed in liver. Also expressed in small intestine, pancreas, kidney, lung, pancreas, spleen, heart, gall bladder, brain, testis, stomach and muscle. Ref.1 Ref.2 Ref.8

Induction

Expression is decreased in Caco-2 cells upon PPARD activation. Ref.9

Post-translational modification

Highly glycosylated By similarity.

Polymorphism

Variations in NPC1L1 gene could be associated with non-response to ezetimibe treatment.

Sequence similarities

Belongs to the patched family.

Contains 1 SSD (sterol-sensing) domain.

Ontologies

Keywords
   Biological processCholesterol metabolism
Lipid metabolism
Steroid metabolism
Sterol metabolism
   Cellular componentCell membrane
Cytoplasmic vesicle
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
Transmembrane
Transmembrane helix
   PTMGlycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcholesterol biosynthetic process

Inferred from mutant phenotype PubMed 17140581. Source: HGNC

cholesterol transport

Inferred from mutant phenotype PubMed 17140581. Source: HGNC

intestinal cholesterol absorption

Inferred from mutant phenotype PubMed 17140581. Source: HGNC

lipoprotein metabolic process

Inferred from mutant phenotype PubMed 17140581. Source: HGNC

response to drug

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

sterol transport

Traceable author statement. Source: Reactome

   Cellular_componentapical plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

brush border membrane

Inferred from electronic annotation. Source: Ensembl

cytoplasmic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from direct assay Ref.3. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionRab GTPase binding

Inferred from physical interaction Ref.11. Source: UniProtKB

drug binding

Inferred from electronic annotation. Source: Ensembl

hedgehog receptor activity

Inferred from electronic annotation. Source: InterPro

myosin V binding

Inferred from physical interaction Ref.11. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UHC9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9UHC9-2)

Also known as: NPC1L1DELTAE15;

The sequence of this isoform differs from the canonical sequence as follows:
     1046-1072: Missing.
Isoform 3 (identifier: Q9UHC9-3)

Also known as: NPCL1T;

The sequence of this isoform differs from the canonical sequence as follows:
     723-724: RL → GP
     725-1359: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 13591338Niemann-Pick C1-like protein 1
PRO_0000023266

Regions

Topological domain22 – 284263Extracellular Potential
Transmembrane285 – 30521Helical; Name=1; Potential
Topological domain306 – 35146Cytoplasmic Potential
Transmembrane352 – 37221Helical; Name=2; Potential
Topological domain373 – 632260Extracellular Potential
Transmembrane633 – 65321Helical; Name=3; Potential
Topological domain654 – 66613Cytoplasmic Potential
Transmembrane667 – 68721Helical; Name=4; Potential
Topological domain688 – 6969Extracellular Potential
Transmembrane697 – 71721Helical; Name=5; Potential
Topological domain718 – 74225Cytoplasmic Potential
Transmembrane743 – 76321Helical; Name=6; Potential
Topological domain764 – 77613Extracellular Potential
Transmembrane777 – 79721Helical; Name=7; Potential
Topological domain798 – 84649Cytoplasmic Potential
Transmembrane847 – 86721Helical; Name=8; Potential
Topological domain868 – 88215Extracellular Potential
Transmembrane883 – 90321Helical; Name=9; Potential
Topological domain904 – 1139236Cytoplasmic Potential
Transmembrane1140 – 116021Helical; Name=10; Potential
Topological domain1161 – 11688Extracellular Potential
Transmembrane1169 – 118921Helical; Name=11; Potential
Topological domain1190 – 11912Cytoplasmic Potential
Transmembrane1192 – 121221Helical; Name=12; Potential
Topological domain1213 – 123624Extracellular Potential
Transmembrane1237 – 125721Helical; Name=13; Potential
Topological domain1258 – 1359102Cytoplasmic Potential
Domain632 – 797166SSD
Compositional bias500 – 5034Poly-Leu

Amino acid modifications

Glycosylation541N-linked (GlcNAc...) Potential
Glycosylation1321N-linked (GlcNAc...) Potential
Glycosylation1381N-linked (GlcNAc...) Potential
Glycosylation2441N-linked (GlcNAc...) Potential
Glycosylation4161N-linked (GlcNAc...) Potential
Glycosylation4311N-linked (GlcNAc...) Potential
Glycosylation4641N-linked (GlcNAc...) Potential
Glycosylation4791N-linked (GlcNAc...) Potential
Glycosylation4971N-linked (GlcNAc...) Potential
Glycosylation5061N-linked (GlcNAc...) Potential
Glycosylation6261N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence723 – 7242RL → GP in isoform 3.
VSP_015312
Alternative sequence725 – 1359635Missing in isoform 3.
VSP_015313
Alternative sequence1046 – 107227Missing in isoform 2.
VSP_015314
Natural variant551V → L Non-response to ezetimibe treatment. Ref.13
VAR_023369
Natural variant5101M → I.
Corresponds to variant rs1468384 [ dbSNP | Ensembl ].
VAR_056659
Natural variant12331I → N. Ref.13
Corresponds to variant rs52815063 [ dbSNP | Ensembl ].
VAR_023370
Natural variant13081E → K.
Corresponds to variant rs217435 [ dbSNP | Ensembl ].
VAR_056660

Experimental info

Sequence conflict10731T → A in AAF20396. Ref.1

Secondary structure

............................................... 1359
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 28, 2012. Version 2.
Checksum: 594F698B48D66DE7

FASTA1,359148,728
        10         20         30         40         50         60 
MAEAGLRGWL LWALLLRLAQ SEPYTTIHQP GYCAFYDECG KNPELSGSLM TLSNVSCLSN 

        70         80         90        100        110        120 
TPARKITGDH LILLQKICPR LYTGPNTQAC CSAKQLVSLE ASLSITKALL TRCPACSDNF 

       130        140        150        160        170        180 
VNLHCHNTCS PNQSLFINVT RVAQLGAGQL PAVVAYEAFY QHSFAEQSYD SCSRVRVPAA 

       190        200        210        220        230        240 
ATLAVGTMCG VYGSALCNAQ RWLNFQGDTG NGLAPLDITF HLLEPGQAVG SGIQPLNEGV 

       250        260        270        280        290        300 
ARCNESQGDD VATCSCQDCA ASCPAIARPQ ALDSTFYLGQ MPGSLVLIII LCSVFAVVTI 

       310        320        330        340        350        360 
LLVGFRVAPA RDKSKMVDPK KGTSLSDKLS FSTHTLLGQF FQGWGTWVAS WPLTILVLSV 

       370        380        390        400        410        420 
IPVVALAAGL VFTELTTDPV ELWSAPNSQA RSEKAFHDQH FGPFFRTNQV ILTAPNRSSY 

       430        440        450        460        470        480 
RYDSLLLGPK NFSGILDLDL LLELLELQER LRHLQVWSPE AQRNISLQDI CYAPLNPDNT 

       490        500        510        520        530        540 
SLYDCCINSL LQYFQNNRTL LLLTANQTLM GQTSQVDWKD HFLYCANAPL TFKDGTALAL 

       550        560        570        580        590        600 
SCMADYGAPV FPFLAIGGYK GKDYSEAEAL IMTFSLNNYP AGDPRLAQAK LWEEAFLEEM 

       610        620        630        640        650        660 
RAFQRRMAGM FQVTFMAERS LEDEINRTTA EDLPIFATSY IVIFLYISLA LGSYSSWSRV 

       670        680        690        700        710        720 
MVDSKATLGL GGVAVVLGAV MAAMGFFSYL GIRSSLVILQ VVPFLVLSVG ADNIFIFVLE 

       730        740        750        760        770        780 
YQRLPRRPGE PREVHIGRAL GRVAPSMLLC SLSEAICFFL GALTPMPAVR TFALTSGLAV 

       790        800        810        820        830        840 
ILDFLLQMSA FVALLSLDSK RQEASRLDVC CCVKPQELPP PGQGEGLLLG FFQKAYAPFL 

       850        860        870        880        890        900 
LHWITRGVVL LLFLALFGVS LYSMCHISVG LDQELALPKD SYLLDYFLFL NRYFEVGAPV 

       910        920        930        940        950        960 
YFVTTLGYNF SSEAGMNAIC SSAGCNNFSF TQKIQYATEF PEQSYLAIPA SSWVDDFIDW 

       970        980        990       1000       1010       1020 
LTPSSCCRLY ISGPNKDKFC PSTVNSLNCL KNCMSITMGS VRPSVEQFHK YLPWFLNDRP 

      1030       1040       1050       1060       1070       1080 
NIKCPKGGLA AYSTSVNLTS DGQVLDTVAI LSPRLEYSGT ISAHCNLYLL DSTSRFMAYH 

      1090       1100       1110       1120       1130       1140 
KPLKNSQDYT EALRAARELA ANITADLRKV PGTDPAFEVF PYTITNVFYE QYLTILPEGL 

      1150       1160       1170       1180       1190       1200 
FMLSLCLVPT FAVSCLLLGL DLRSGLLNLL SIVMILVDTV GFMALWGISY NAVSLINLVS 

      1210       1220       1230       1240       1250       1260 
AVGMSVEFVS HITRSFAIST KPTWLERAKE ATISMGSAVF AGVAMTNLPG ILVLGLAKAQ 

      1270       1280       1290       1300       1310       1320 
LIQIFFFRLN LLITLLGLLH GLVFLPVILS YVGPDVNPAL ALEQKRAEEA VAAVMVASCP 

      1330       1340       1350 
NHPSRVSTAD NIYVNHSFEG SIKGAGAISN FLPNNGRQF 

« Hide

Isoform 2 (NPC1L1DELTAE15) [UniParc].

Checksum: 8483F336EBFD3EA3
Show »

FASTA1,332145,794
Isoform 3 (NPCL1T) [UniParc].

Checksum: 15564FF42565270F
Show »

FASTA72479,138

References

« Hide 'large scale' references
[1]"Evidence for a Niemann-Pick C (NPC) gene family: identification and characterization of NPC1L1."
Davies J.P., Levy B., Ioannou Y.A.
Genomics 65:137-145(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY.
[2]"Niemann-Pick C1 like 1 protein is critical for intestinal cholesterol absorption."
Altmann S.W., Davis H.R. Jr., Zhu L.-J., Yao X., Hoos L.M., Tetzloff G., Iyer S.P.N., Maguire M., Golovko A., Zeng M., Wang L., Murgolo N., Graziano M.P.
Science 303:1201-1204(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
[3]"Membrane topology of human NPC1L1, a key protein in enterohepatic cholesterol absorption."
Wang J., Chu B.-B., Ge L., Li B.-L., Yan Y., Song B.L.
J. Lipid Res. 50:1653-1662(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TOPOLOGY.
[4]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Liver.
[8]"Inactivation of NPC1L1 causes multiple lipid transport defects and protects against diet-induced hypercholesterolemia."
Davies J.P., Scott C., Oishi K., Liapis A., Ioannou Y.A.
J. Biol. Chem. 280:12710-12720(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[9]"Reduced cholesterol absorption upon PPARdelta activation coincides with decreased intestinal expression of NPC1L1."
van der Veen J.N., Kruit J.K., Havinga R., Baller J.F.W., Chimini G., Lestavel S., Staels B., Groot P.H.E., Groen A.K., Kuipers F.
J. Lipid Res. 46:526-534(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[10]"The target of ezetimibe is Niemann-Pick C1-like 1 (NPC1L1)."
Garcia-Calvo M., Lisnock J., Bull H.G., Hawes B.E., Burnett D.A., Braun M.P., Crona J.H., Davis H.R. Jr., Dean D.C., Detmers P.A., Graziano M.P., Hughes M., MacIntyre D.E., Ogawa A., O'neill K.A., Iyer S.P.N., Shevell D.E., Smith M.M. expand/collapse author list , Tang Y.S., Makarewicz A.M., Ujjainwalla F., Altmann S.W., Chapman K.T., Thornberry N.A.
Proc. Natl. Acad. Sci. U.S.A. 102:8132-8137(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Requirement of myosin Vb.Rab11a.Rab11-FIP2 complex in cholesterol-regulated translocation of NPC1L1 to the cell surface."
Chu B.-B., Ge L., Xie C., Zhao Y., Miao H.-H., Wang J., Li B.-L., Song B.-L.
J. Biol. Chem. 284:22481-22490(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB11A; MYO5B AND RAB11FIP2.
[12]"Novel function of Niemann-Pick C1-like 1 as a negative regulator of Niemann-Pick C2 protein."
Yamanashi Y., Takada T., Shoda J., Suzuki H.
Hepatology 55:953-964(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NPC2.
[13]"Compound heterozygosity for two non-synonymous polymorphisms in NPC1L1 in a non-responder to ezetimibe."
Wang J., Williams C.M., Hegele R.A.
Clin. Genet. 67:175-177(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LEU-55 AND ASN-1233.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF192522 mRNA. Translation: AAF20396.1.
AF192523 mRNA. Translation: AAF20397.1.
AY515256 mRNA. Translation: AAS56939.1.
AY437865 mRNA. Translation: AAR97886.1.
FJ481111 mRNA. Translation: ACL18055.1.
AC004938 Genomic DNA. No translation available.
CH236960 Genomic DNA. Translation: EAL23753.1.
CH471128 Genomic DNA. Translation: EAW61096.1.
CH471128 Genomic DNA. Translation: EAW61097.1.
CH471128 Genomic DNA. Translation: EAW61098.1.
BC117178 mRNA. Translation: AAI17179.1.
RefSeqNP_001095118.1. NM_001101648.1.
NP_037521.2. NM_013389.2.
UniGeneHs.567486.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3QNTX-ray2.83A22-284[»]
ProteinModelPortalQ9UHC9.
SMRQ9UHC9. Positions 22-265.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9UHC9. 1 interaction.
STRING9606.ENSP00000289547.

Chemistry

BindingDBQ9UHC9.
ChEMBLCHEMBL2027.
DrugBankDB00973. Ezetimibe.
GuidetoPHARMACOLOGY2629.

Protein family/group databases

TCDB2.A.6.6.6. the resistance-nodulation-cell division (rnd) superfamily.

PTM databases

PhosphoSiteQ9UHC9.

Polymorphism databases

DMDM425906049.

Proteomic databases

PaxDbQ9UHC9.
PRIDEQ9UHC9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000289547; ENSP00000289547; ENSG00000015520. [Q9UHC9-1]
ENST00000381160; ENSP00000370552; ENSG00000015520.
ENST00000423141; ENSP00000404670; ENSG00000015520. [Q9UHC9-3]
GeneID29881.
KEGGhsa:29881.
UCSCuc003tlb.3. human. [Q9UHC9-1]
uc003tlc.3. human. [Q9UHC9-2]
uc003tld.3. human. [Q9UHC9-3]

Organism-specific databases

CTD29881.
GeneCardsGC07M044552.
H-InvDBHIX0201184.
HGNCHGNC:7898. NPC1L1.
HPAHPA018105.
MIM608010. gene+phenotype.
neXtProtNX_Q9UHC9.
PharmGKBPA31699.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG149152.
HOGENOMHOG000036674.
HOVERGENHBG003913.
InParanoidQ9UHC9.
KOK14461.
OMALQMTAFV.
OrthoDBEOG7QRQT0.
PhylomeDBQ9UHC9.
TreeFamTF300416.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ9UHC9.
BgeeQ9UHC9.
CleanExHS_NPC1L1.
GenevestigatorQ9UHC9.

Family and domain databases

InterProIPR003392. Patched.
IPR000731. SSD.
[Graphical view]
PfamPF02460. Patched. 1 hit.
[Graphical view]
PROSITEPS50156. SSD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi29881.
NextBio52405.
PROQ9UHC9.
SOURCESearch...

Entry information

Entry nameNPCL1_HUMAN
AccessionPrimary (citable) accession number: Q9UHC9
Secondary accession number(s): A4D2J7 expand/collapse secondary AC list , D3DVK9, Q17RV5, Q6R3Q4, Q9UHC8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: November 28, 2012
Last modified: April 16, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM