Q8WTV0 (SCRB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Scavenger receptor class B member 1
Short name=SRB1

Alternative name(s):
CD36 and LIMPII analogous 1
Short name=CLA-1
CD36 antigen-like 1
Collagen type I receptor, thrombospondin receptor-like 1
SR-BI
CD_antigen=CD36

Gene names

Name:	SCARB1
Synonyms:	CD36L1, CLA1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	552 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Receptor for different ligands such as phospholipids, cholesterol ester, lipoproteins, phosphatidylserine and apoptotic cells. Probable receptor for HDL, located in particular region of the plasma membrane, called caveolae. Facilitates the flux of free and esterified cholesterol between the cell surface and extracellular donors and acceptors, such as HDL and to a lesser extent, apoB-containing lipoproteins and modified lipoproteins. Probably involved in the phagocytosis of apoptotic cells, via its phosphatidylserine binding activity. Receptor for hepatitis C virus glycoprotein E2. Binding between SCARB1 and E2 was found to be independent of the genotype of the viral isolate. Plays an important role in the uptake of HDL cholesteryl ester By similarity. Ref.5
Subunit structure	Plays a critical role in HCV attachment and/or cell entry by interacting with HCV E1/E2 glycoproteins heterodimer. The C-terminal region binds to PDZK1 By similarity.
Subcellular location	Cell membrane; Multi-pass membrane protein. Membrane › caveola; Multi-pass membrane protein. Note: Predominantly localized to cholesterol and sphingomyelin-enriched domains within the plasma membrane, called caveolae.
Tissue specificity	Widely expressed.
Post-translational modification	N-glycosylated. Ref.6 The six cysteines of the extracellular domain are all involved in intramolecular disulfide bonds By similarity.
Polymorphism	Genetic variations in SCARB1 define the high density lipoprotein cholesterol level quantitative trait locus 6 (HDLCQ16) [MIM:610762].
Sequence similarities	Belongs to the CD36 family.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adhesion to symbiont Inferred from mutant phenotype PubMed 19087225. Source: BHF-UCL androgen biosynthetic process Inferred from electronic annotation. Source: Compara blood vessel endothelial cell migration Inferred from electronic annotation. Source: Compara cell adhesion Inferred from electronic annotation. Source: InterPro cholesterol catabolic process Inferred from electronic annotation. Source: Compara cholesterol efflux Inferred from sequence or structural similarity PubMed 14718538. Source: BHF-UCL cholesterol homeostasis Inferred from sequence or structural similarity. Source: BHF-UCL cholesterol import Inferred from sequence or structural similarity PubMed 14718538. Source: BHF-UCL detection of lipopolysaccharide Inferred from direct assay PubMed 12651854. Source: BHF-UCL endothelial cell proliferation Inferred from electronic annotation. Source: Compara high-density lipoprotein particle clearance Inferred from direct assay PubMed 9211901. Source: BHF-UCL high-density lipoprotein particle remodeling Inferred from sequence or structural similarity. Source: BHF-UCL lipid metabolic process Traceable author statement. Source: Reactome lipopolysaccharide transport Inferred from direct assay PubMed 12651854. Source: BHF-UCL lipoprotein metabolic process Traceable author statement. Source: Reactome low-density lipoprotein particle clearance Inferred from sequence or structural similarity. Source: BHF-UCL phospholipid transport Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of cholesterol storage Inferred from direct assay PubMed 9211901. Source: BHF-UCL positive regulation of endothelial cell migration Traceable author statement PubMed 17574123. Source: BHF-UCL positive regulation of nitric-oxide synthase activity Inferred from direct assay PubMed 11792700. Source: BHF-UCL positive regulation of triglyceride biosynthetic process Inferred from sequence or structural similarity. Source: BHF-UCL recognition of apoptotic cell Inferred from direct assay PubMed 9211901. Source: BHF-UCL regulation of phagocytosis Inferred by curator PubMed 9211901. Source: BHF-UCL regulation of phosphatidylcholine catabolic process Inferred from sequence or structural similarity. Source: BHF-UCL reverse cholesterol transport Inferred from expression pattern PubMed 9211901. Source: BHF-UCL small molecule metabolic process Traceable author statement. Source: Reactome triglyceride homeostasis Inferred from sequence or structural similarity. Source: BHF-UCL virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW wound healing Traceable author statement PubMed 17574123. Source: BHF-UCL
Cellular_component	caveola Traceable author statement PubMed 12651854. Source: BHF-UCL cell surface Inferred from electronic annotation. Source: Compara cytoplasm Inferred from electronic annotation. Source: Compara integral to plasma membrane Inferred from electronic annotation. Source: Compara microvillus membrane Inferred from electronic annotation. Source: Compara
Molecular_function	1-phosphatidylinositol binding Traceable author statement PubMed 9211901. Source: BHF-UCL high-density lipoprotein particle binding Inferred from electronic annotation. Source: Compara high-density lipoprotein particle receptor activity Inferred from direct assay PubMed 9211901. Source: BHF-UCL lipopolysaccharide binding Inferred from direct assay PubMed 12651854. Source: BHF-UCL lipopolysaccharide receptor activity Inferred from direct assay PubMed 12651854. Source: BHF-UCL low-density lipoprotein particle binding Inferred from direct assay PubMed 9211901. Source: BHF-UCL phosphatidylserine binding Inferred from sequence or structural similarity. Source: BHF-UCL transporter activity Traceable author statement PubMed 9211901. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PRMT2	P55345	1	EBI-78657,EBI-78458

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 3 (identifier: Q8WTV0-1)

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.

Note: May be due to a competing donor splice site. No experimental confirmation available.

Isoform 1 (identifier: Q8WTV0-2)

Also known as: SR-BI;

The sequence of this isoform differs from the canonical sequence as follows:
     468-552: VGAGQRAARA...GPSLGGGTGS → EKCYLFWSSS...KGSVLQEAKL

Isoform 2 (identifier: Q8WTV0-3)

Also known as: SR-BII;

The sequence of this isoform differs from the canonical sequence as follows:
     43-142: Missing.
     468-552: VGAGQRAARA...GPSLGGGTGS → EKCYLFWSSS...KGSVLQEAKL

Isoform 4 (identifier: Q8WTV0-4)

Also known as: SR-BIII;

The sequence of this isoform differs from the canonical sequence as follows:
     1-42: MGCSAKARWAAGALGVAGLLCAVLGAVMIVMVPSLIKQQVLK → MALQPSW
     468-552: VGAGQRAARA...GPSLGGGTGS → EKCYLFWSSS...KGSVLQEAKL

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 552	552	Scavenger receptor class B member 1		PRO_0000144160
Regions
	Topological domain	1 – 11	11	Cytoplasmic Potential
	Transmembrane	12 – 32	21	Helical; Potential
	Topological domain	33 – 443	411	Extracellular Potential
	Transmembrane	444 – 464	21	Helical; Potential
	Topological domain	465 – 552	88	Cytoplasmic Potential
Amino acid modifications
	Glycosylation	102	1	N-linked (GlcNAc...) Ref.8
	Glycosylation	108	1	N-linked (GlcNAc...) Potential
	Glycosylation	173	1	N-linked (GlcNAc...) Potential
	Glycosylation	212	1	N-linked (GlcNAc...) Potential
	Glycosylation	227	1	N-linked (GlcNAc...) Potential
	Glycosylation	255	1	N-linked (GlcNAc...) Potential
	Glycosylation	310	1	N-linked (GlcNAc...) Potential
	Glycosylation	330	1	N-linked (GlcNAc...) Ref.8
	Glycosylation	383	1	N-linked (GlcNAc...) Potential
	Disulfide bond	251 ↔ 384		By similarity
Natural variations
	Alternative sequence	1 – 42	42	MGCSA…QQVLK → MALQPSW in isoform 4.		VSP_011037
	Alternative sequence	43 – 142	100	Missing in isoform 2.		VSP_008553
	Alternative sequence	468 – 552	85	VGAGQ…GGTGS → EKCYLFWSSSKKGSKDKEAI QAYSESLMTSAPKGSVLQEA KL in isoform 1, isoform 2 and isoform 4.		VSP_008554
	Natural variant	2	1	G → S Associated with higher plasma triglyceride concentration in subjects with hypercholesterolemia. Ref.11 Ref.12 Corresponds to variant rs4238001 [ dbSNP | Ensembl ].		VAR_017098
	Natural variant	135	1	V → I. Ref.12 Corresponds to variant rs5891 [ dbSNP | Ensembl ].		VAR_017099
	Natural variant	167	1	G → S. Ref.12		VAR_017100
	Natural variant	229	1	S → G. Corresponds to variant rs10396213 [ dbSNP | Ensembl ].		VAR_019507
	Natural variant	297	1	P → S Mutation carriers have increased HDL cholesterol levels and a reduction in cholesterol efflux from macrophages. Ref.13		VAR_064909
	Natural variant	511	1	C → R. Corresponds to variant rs2293440 [ dbSNP | Ensembl ].		VAR_017101
Experimental info
	Sequence conflict	70	1	F → L in AAQ08185. Ref.2
	Sequence conflict	97	1	F → S in CAA80277. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 3 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 06B0BD771FEA284F	FASTA	552	60,878
	10 20 30 40 50 60 MGCSAKARWA AGALGVAGLL CAVLGAVMIV MVPSLIKQQV LKNVRIDPSS LSFNMWKEIP 70 80 90 100 110 120 IPFYLSVYFF DVMNPSEILK GEKPQVRERG PYVYREFRHK SNITFNNNDT VSFLEYRTFQ 130 140 150 160 170 180 FQPSKSHGSE SDYIVMPNIL VLGAAVMMEN KPMTLKLIMT LAFTTLGERA FMNRTVGEIM 190 200 210 220 230 240 WGYKDPLVNL INKYFPGMFP FKDKFGLFAE LNNSDSGLFT VFTGVQNISR IHLVDKWNGL 250 260 270 280 290 300 SKVDFWHSDQ CNMINGTSGQ MWPPFMTPES SLEFYSPEAC RSMKLMYKES GVFEGIPTYR 310 320 330 340 350 360 FVAPKTLFAN GSIYPPNEGF CPCLESGIQN VSTCRFSAPL FLSHPHFLNA DPVLAEAVTG 370 380 390 400 410 420 LHPNQEAHSL FLDIHPVTGI PMNCSVKLQL SLYMKSVAGI GQTGKIEPVV LPLLWFAESG 430 440 450 460 470 480 AMEGETLHTF YTQLVLMPKV MHYAQYVLLA LGCVLLLVPV ICQIRSQVGA GQRAARADSH 490 500 510 520 530 540 SLACWGKGAS DRTLWPTAAW SPPPAAVLRL CRSGSGHCWG LRSTLASFAC RVATTLPVLE 550 GLGPSLGGGT GS
	Isoform 1 (SR-BI) [UniParc]. Checksum: 0184AE9CEC595374	FASTA	509	56,973
	10 20 30 40 50 60 MGCSAKARWA AGALGVAGLL CAVLGAVMIV MVPSLIKQQV LKNVRIDPSS LSFNMWKEIP 70 80 90 100 110 120 IPFYLSVYFF DVMNPSEILK GEKPQVRERG PYVYREFRHK SNITFNNNDT VSFLEYRTFQ 130 140 150 160 170 180 FQPSKSHGSE SDYIVMPNIL VLGAAVMMEN KPMTLKLIMT LAFTTLGERA FMNRTVGEIM 190 200 210 220 230 240 WGYKDPLVNL INKYFPGMFP FKDKFGLFAE LNNSDSGLFT VFTGVQNISR IHLVDKWNGL 250 260 270 280 290 300 SKVDFWHSDQ CNMINGTSGQ MWPPFMTPES SLEFYSPEAC RSMKLMYKES GVFEGIPTYR 310 320 330 340 350 360 FVAPKTLFAN GSIYPPNEGF CPCLESGIQN VSTCRFSAPL FLSHPHFLNA DPVLAEAVTG 370 380 390 400 410 420 LHPNQEAHSL FLDIHPVTGI PMNCSVKLQL SLYMKSVAGI GQTGKIEPVV LPLLWFAESG 430 440 450 460 470 480 AMEGETLHTF YTQLVLMPKV MHYAQYVLLA LGCVLLLVPV ICQIRSQEKC YLFWSSSKKG 490 500 SKDKEAIQAY SESLMTSAPK GSVLQEAKL
	Isoform 2 (SR-BII) [UniParc]. Checksum: 88B30340CD403541	FASTA	409	45,103
	10 20 30 40 50 60 MGCSAKARWA AGALGVAGLL CAVLGAVMIV MVPSLIKQQV LKGAAVMMEN KPMTLKLIMT 70 80 90 100 110 120 LAFTTLGERA FMNRTVGEIM WGYKDPLVNL INKYFPGMFP FKDKFGLFAE LNNSDSGLFT 130 140 150 160 170 180 VFTGVQNISR IHLVDKWNGL SKVDFWHSDQ CNMINGTSGQ MWPPFMTPES SLEFYSPEAC 190 200 210 220 230 240 RSMKLMYKES GVFEGIPTYR FVAPKTLFAN GSIYPPNEGF CPCLESGIQN VSTCRFSAPL 250 260 270 280 290 300 FLSHPHFLNA DPVLAEAVTG LHPNQEAHSL FLDIHPVTGI PMNCSVKLQL SLYMKSVAGI 310 320 330 340 350 360 GQTGKIEPVV LPLLWFAESG AMEGETLHTF YTQLVLMPKV MHYAQYVLLA LGCVLLLVPV 370 380 390 400 ICQIRSQEKC YLFWSSSKKG SKDKEAIQAY SESLMTSAPK GSVLQEAKL
	Isoform 4 (SR-BIII) [UniParc]. Checksum: 1CF55DEB32EF3D3B	FASTA	474	53,579
	10 20 30 40 50 60 MALQPSWNVR IDPSSLSFNM WKEIPIPFYL SVYFFDVMNP SEILKGEKPQ VRERGPYVYR 70 80 90 100 110 120 EFRHKSNITF NNNDTVSFLE YRTFQFQPSK SHGSESDYIV MPNILVLGAA VMMENKPMTL 130 140 150 160 170 180 KLIMTLAFTT LGERAFMNRT VGEIMWGYKD PLVNLINKYF PGMFPFKDKF GLFAELNNSD 190 200 210 220 230 240 SGLFTVFTGV QNISRIHLVD KWNGLSKVDF WHSDQCNMIN GTSGQMWPPF MTPESSLEFY 250 260 270 280 290 300 SPEACRSMKL MYKESGVFEG IPTYRFVAPK TLFANGSIYP PNEGFCPCLE SGIQNVSTCR 310 320 330 340 350 360 FSAPLFLSHP HFLNADPVLA EAVTGLHPNQ EAHSLFLDIH PVTGIPMNCS VKLQLSLYMK 370 380 390 400 410 420 SVAGIGQTGK IEPVVLPLLW FAESGAMEGE TLHTFYTQLV LMPKVMHYAQ YVLLALGCVL 430 440 450 460 470 LLVPVICQIR SQEKCYLFWS SSKKGSKDKE AIQAYSESLM TSAPKGSVLQ EAKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification, primary structure and distribution of CLA-1, a novel member of the CD36/LIMPII gene family." Calvo D., Vega M. J. Biol. Chem. 268:18929-18935(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). Tissue: Promyelocyte.
[2]	Hirano K., Yamashita S., Matsuzawa Y. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[3]	Mural R.J., Istrail S., Sutton G.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. , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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] (ISOFORMS 1 AND 3). Tissue: Liver, Prostate and Rhabdomyosarcoma.
[5]	"The human scavenger receptor class B type I is a novel candidate receptor for the hepatitis C virus." Scarselli E., Ansuini H., Cerino R., Roccasecca R.M., Acali S., Filocamo G., Traboni C., Nicosia A., Cortese R., Vitelli A. EMBO J. 21:5017-5025(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"Phosphatidylserine binding of class B scavenger receptor type I, a phagocytosis receptor of testicular Sertoli cells." Kawasaki Y., Nakagawa A., Nagaosa K., Shiratsuchi A., Nakanishi Y. J. Biol. Chem. 277:27559-27566(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION.
[7]	"Cell entry of hepatitis C virus requires a set of co-receptors that include the CD81 tetraspanin and the SR-B1 scavenger receptor." Bartosch B., Vitelli A., Granier C., Goujon C., Dubuisson J., Pascale S., Scarselli E., Cortese R., Nicosia A., Cosset F.-L. J. Biol. Chem. 278:41624-41630(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HCV E1/E2 ENVELOPE HETERODIMER.
[8]	"Glycoproteomics analysis of human liver tissue by combination of multiple 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) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-102 AND ASN-330, MASS SPECTROMETRY. Tissue: Liver.
[9]	"Biological, clinical and population relevance of 95 loci for blood lipids." Teslovich T.M., Musunuru K., Smith A.V., Edmondson A.C., Stylianou I.M., Koseki M., Pirruccello J.P., Ripatti S., Chasman D.I., Willer C.J., Johansen C.T., Fouchier S.W., Isaacs A., Peloso G.M., Barbalic M., Ricketts S.L., Bis J.C., Aulchenko Y.S. , Thorleifsson G., Feitosa M.F., Chambers J., Orho-Melander M., Melander O., Johnson T., Li X., Guo X., Li M., Shin Cho Y., Jin Go M., Jin Kim Y., Lee J.Y., Park T., Kim K., Sim X., Twee-Hee Ong R., Croteau-Chonka D.C., Lange L.A., Smith J.D., Song K., Hua Zhao J., Yuan X., Luan J., Lamina C., Ziegler A., Zhang W., Zee R.Y., Wright A.F., Witteman J.C., Wilson J.F., Willemsen G., Wichmann H.E., Whitfield J.B., Waterworth D.M., Wareham N.J., Waeber G., Vollenweider P., Voight B.F., Vitart V., Uitterlinden A.G., Uda M., Tuomilehto J., Thompson J.R., Tanaka T., Surakka I., Stringham H.M., Spector T.D., Soranzo N., Smit J.H., Sinisalo J., Silander K., Sijbrands E.J., Scuteri A., Scott J., Schlessinger D., Sanna S., Salomaa V., Saharinen J., Sabatti C., Ruokonen A., Rudan I., Rose L.M., Roberts R., Rieder M., Psaty B.M., Pramstaller P.P., Pichler I., Perola M., Penninx B.W., Pedersen N.L., Pattaro C., Parker A.N., Pare G., Oostra B.A., O'Donnell C.J., Nieminen M.S., Nickerson D.A., Montgomery G.W., Meitinger T., McPherson R., McCarthy M.I., McArdle W., Masson D., Martin N.G., Marroni F., Mangino M., Magnusson P.K., Lucas G., Luben R., Loos R.J., Lokki M.L., Lettre G., Langenberg C., Launer L.J., Lakatta E.G., Laaksonen R., Kyvik K.O., Kronenberg F., Konig I.R., Khaw K.T., Kaprio J., Kaplan L.M., Johansson A., Jarvelin M.R., Janssens A.C., Ingelsson E., Igl W., Kees Hovingh G., Hottenga J.J., Hofman A., Hicks A.A., Hengstenberg C., Heid I.M., Hayward C., Havulinna A.S., Hastie N.D., Harris T.B., Haritunians T., Hall A.S., Gyllensten U., Guiducci C., Groop L.C., Gonzalez E., Gieger C., Freimer N.B., Ferrucci L., Erdmann J., Elliott P., Ejebe K.G., Doring A., Dominiczak A.F., Demissie S., Deloukas P., de Geus E.J., de Faire U., Crawford G., Collins F.S., Chen Y.D., Caulfield M.J., Campbell H., Burtt N.P., Bonnycastle L.L., Boomsma D.I., Boekholdt S.M., Bergman R.N., Barroso I., Bandinelli S., Ballantyne C.M., Assimes T.L., Quertermous T., Altshuler D., Seielstad M., Wong T.Y., Tai E.S., Feranil A.B., Kuzawa C.W., Adair L.S., Taylor H.A. Jr., Borecki I.B., Gabriel S.B., Wilson J.G., Holm H., Thorsteinsdottir U., Gudnason V., Krauss R.M., Mohlke K.L., Ordovas J.M., Munroe P.B., Kooner J.S., Tall A.R., Hegele R.A., Kastelein J.J., Schadt E.E., Rotter J.I., Boerwinkle E., Strachan D.P., Mooser V., Stefansson K., Reilly M.P., Samani N.J., Schunkert H., Cupples L.A., Sandhu M.S., Ridker P.M., Rader D.J., van Duijn C.M., Peltonen L., Abecasis G.R., Boehnke M., Kathiresan S. Nature 466:707-713(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN HDLCQ16.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"Polymorphisms at the SRBI locus are associated with lipoprotein levels in subjects with heterozygous familial hypercholesterolemia." Tai E.S., Adiconis X., Ordovas J.M., Carmena-Ramon R., Real J., Corella D., Ascaso J., Carmena R. Clin. Genet. 63:53-58(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SER-2.
[12]	"Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors." Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S., Alvin G.B., Das K., Gilliam T.C. Hum. Mol. Genet. 12:2733-2743(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS SER-2; ILE-135 AND SER-167.
[13]	"Genetic variant of the scavenger receptor BI in humans." Vergeer M., Korporaal S.J., Franssen R., Meurs I., Out R., Hovingh G.K., Hoekstra M., Sierts J.A., Dallinga-Thie G.M., Motazacker M.M., Holleboom A.G., Van Berkel T.J., Kastelein J.J., Van Eck M., Kuivenhoven J.A. N. Engl. J. Med. 364:136-145(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SER-297, INVOLVEMENT IN HDLCQ16.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z22555 mRNA. Translation: CAA80277.1. AF515445 mRNA. Translation: AAQ08185.1. BC022087 mRNA. No translation available. CH471054 Genomic DNA. Translation: EAW98459.1. BC080647 mRNA. Translation: AAH80647.1. BC093732 mRNA. Translation: AAH93732.1. BC112037 mRNA. Translation: AAI12038.1.
IPI	IPI00177968. IPI00291007. IPI00375570. IPI00447020.
PIR	A48528. S36656.
RefSeq	NP_005496.4. NM_005505.4.
UniGene	Hs.731377.
3D structure databases
ProteinModelPortal	Q8WTV0.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8WTV0. 3 interactions.
MINT	MINT-5001419.
STRING	9606.ENSP00000261693.
PTM databases
PhosphoSite	Q8WTV0.
Polymorphism databases
DMDM	37999904.
Proteomic databases
PaxDb	Q8WTV0.
PRIDE	Q8WTV0.
Protocols and materials databases
DNASU	949.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000261693; ENSP00000261693; ENSG00000073060. ENST00000376788; ENSP00000365984; ENSG00000073060. ENST00000415380; ENSP00000414979; ENSG00000073060.
GeneID	949.
KEGG	hsa:949.
UCSC	uc001ugm.4. human. uc001ugo.4. human.
Organism-specific databases
CTD	949.
GeneCards	GC12M125262.
HGNC	HGNC:1664. SCARB1.
MIM	601040. gene. 610762. phenotype.
neXtProt	NX_Q8WTV0.
PharmGKB	PA97.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG257244.
HOVERGEN	HBG106577.
InParanoid	Q8WTV0.
KO	K13885.
OMA	PYVYREF.
OrthoDB	EOG4J3WGW.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	Q8WTV0.
Bgee	Q8WTV0.
CleanEx	HS_SCARB1.
Genevestigator	Q8WTV0.
GermOnline	ENSG00000073060. Homo sapiens.
Family and domain databases
InterPro	IPR002159. CD36. IPR005428. CD36_antigen. [Graphical view]
PANTHER	PTHR11923. PTHR11923. 1 hit.
Pfam	PF01130. CD36. 1 hit. [Graphical view]
PRINTS	PR01610. CD36ANTIGEN. PR01609. CD36FAMILY.
ProtoNet	Search...
Other
BindingDB	Q8WTV0.
ChEMBL	CHEMBL1914272.
ChiTaRS	SCARB1. human.
DrugBank	DB00144. Phosphatidylserine.
GenomeRNAi	949.
NextBio	3946.
SOURCE	Search...

Entry information

Entry name

SCRB1_HUMAN

Accession

Primary (citable) accession number: Q8WTV0
Secondary accession number(s): Q14016, Q52LZ5, Q6KFX4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2003
Last sequence update:	March 1, 2002
Last modified:	May 29, 2013
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.