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UniProtKB/Swiss-Prot entry Q86X29


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LSR_HUMAN
Primary accession number Q86X29
Secondary accession numbers O00112 O00426 Q6ZT80 Q9UQL3
Integrated into Swiss-Prot on July 11, 2006
Sequence was last modified on October 17, 2006 (Sequence version 4)
Annotations were last modified on    June 16, 2009 (Entry version 63)
Name and origin of the protein
Protein name Lipolysis-stimulated lipoprotein receptor
Synonyms None
Gene name
Name: LSR
Synonyms: LISCH
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Teramoto T., Thorgeirsson S.S.;
"Cloning and functional analysis of LISCH.";
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT ASN-363.
TISSUE=Amygdala;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02399; PubMed=15057824 [NCBI, ExPASy, EBI, Israel, Japan]
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-646, AND MASS SPECTROMETRY.
DOI=10.1021/pr050048h; PubMed=16083285 [NCBI, ExPASy, EBI, Israel, Japan]
Kim J.-E., Tannenbaum S.R., White F.M.;
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
J. Proteome Res. 4:1339-1346(2005).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309; TYR-328; TYR-406; TYR-535; TYR-551; TYR-586 AND TYR-615, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-530, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700120-MCP200; PubMed=17693683 [NCBI, ExPASy, EBI, Israel, Japan]
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction.";
Mol. Cell. Proteomics 6:1952-1967(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1002/pmic.200700884; PubMed=18318008 [NCBI, ExPASy, EBI, Israel, Japan]
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.";
Proteomics 8:1346-1361(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF130366; AAD22101.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK126834; BAC86714.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC002128; AAB58317.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AD000684; AAB51178.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC047376; AAH47376.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00328218; -.
IPI00409640; -.
IPI00641640; -.
RefSeq NP_057009.3; -.
NP_991403.1; -.
NP_991404.1; -.
UniGene Hs.466507
3D structure databases
ModBase Q86X29.
Protein-protein interaction databases
IntAct Q86X29; 3.
PTM databases
PhosphoSite Q86X29; -.
Organism-specific databases
GeneCards GC19P040432; -.
HGNC HGNC:29572; LSR.
GenAtlas LSR.
HPA HPA007270; -.
PharmGKB PA142671504; -.
Gene expression databases
ArrayExpress Q86X29; -.
Bgee Q86X29; -.
CleanEx HS_LSR; -.
GermOnline ENSG00000105699; Homo sapiens.
Ontologies
GO
GO:0042627; Cellular component: chylomicron (inferred from electronic annotation from UniProtKB-KW).
GO:0005794; Cellular component: Golgi apparatus (inferred from direct assay from HPA).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0034362; Cellular component: low-density lipoprotein particle (inferred from electronic annotation from UniProtKB-KW).
GO:0005634; Cellular component: nucleus (inferred from direct assay from HPA).
GO:0005886; Cellular component: plasma membrane (inferred from sequence or structural similarity from HGNC).
GO:0034361; Cellular component: very-low-density lipoprotein particle (inferred from electronic annotation from UniProtKB-KW).
GO:0004872; Molecular function: receptor activity (inferred from electronic annotation from UniProtKB-KW).
GO:0009790; Biological process: embryonic development (inferred from sequence or structural similarity from HGNC).
GO:0001889; Biological process: liver development (inferred from sequence or structural similarity from HGNC).
QuickGo view.
Family and domain databases
InterPro IPR007110; Ig-like.
IPR003599; Ig_sub.
IPR008664; LISCH7.
Graphical view of domain structure.
Pfam PF05624; LSR; 1.
Pfam graphical view of domain structure.
SMART SM00409; IG; 1.
SMART graphical view of domain structure.
PROSITE PS50835; IG_LIKE; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q86X29; -.
Genome annotation databases
Ensembl ENSG00000105699; Homo sapiens. [Contig view]
GeneID 51599; -.
KEGG hsa:51599; -.
Phylogenomic databases
HOGENOM Q86X29; -.
HOVERGEN Q86X29; -.
OMA Q86X29; WRSRPSR.
Other
NextBio 55459; -.
ProtoNet Q86X29.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Cell membrane; Chylomicron; Disulfide bond; Immunoglobulin domain; LDL; Membrane; Phosphoprotein; Polymorphism; Receptor; Transmembrane; VLDL.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   649  649     Lipolysis-stimulated lipoprotein receptor. PRO_0000245308
TOPO_DOM   1   259  259     Extracellular (Potential). 
TRANSMEM   260   280  21     Potential. 
TOPO_DOM   281   649  369     Cytoplasmic (Potential). 
DOMAIN   86   234  149     Ig-like V-type. 
COMPBIAS   280   304  25     Cys-rich. 
MOD_RES   185   185        Phosphothreonine (By similarity). 
MOD_RES   309   309        Phosphotyrosine. 
MOD_RES   328   328        Phosphotyrosine. 
MOD_RES   364   364        Phosphoserine (By similarity). 
MOD_RES   406   406        Phosphotyrosine. 
MOD_RES   436   436        Phosphoserine (By similarity). 
MOD_RES   493   493        Phosphoserine. 
MOD_RES   528   528        Phosphoserine. 
MOD_RES   530   530        Phosphoserine. 
MOD_RES   535   535        Phosphotyrosine. 
MOD_RES   551   551        Phosphotyrosine. 
MOD_RES   586   586        Phosphotyrosine. 
MOD_RES   615   615        Phosphotyrosine. 
MOD_RES   646   646        Phosphoserine. 
DISULFID   111   218        By similarity. 
VAR_SEQ   52    88        Missing (in isoform 2). VSP_019691
VAR_SEQ   240   258        Missing (in isoform 3). VSP_019692
VAR_SEQ   366   386        Missing (in isoform 2). VSP_019693
VAR_SEQ   386   386        Missing (in isoform 3). VSP_019694
VARIANT   363   363  1     S -> N (in dbSNP:rs34259399 [NCBI]). VAR_049902 
CONFLICT   259   259        D -> G (in Ref. 3; AAB51178). 
CONFLICT   308   308        L -> R (in Ref. 3; AAB51178). 
CONFLICT   430   430        A -> G (in Ref. 3; AAB51178). 
CONFLICT   518   518        G -> GR (in Ref. 2; BAC86714). 
CONFLICT   639   639        N -> D (in Ref. 3; AAB51178). 
Sequence information
Length: 649 AA [This is the length of the unprocessed precursor] Molecular weight: 71439 Da [This is the MW of the unprocessed precursor] CRC64: 01E8F1CE0197CE9B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MQQDGLGVGT RNGSGKGRSV HPSWPWCAPR PLRYFGRDAR ARRAQTAAMA LLAGGLSRGL 

        70         80         90        100        110        120 
GSHPAAAGRD AVVFVWLLLS TWCTAPARAI QVTVSNPYHV VILFQPVTLP CTYQMTSTPT 

       130        140        150        160        170        180 
QPIVIWKYKS FCRDRIADAF SPASVDNQLN AQLAAGNPGY NPYVECQDSV RTVRVVATKQ 

       190        200        210        220        230        240 
GNAVTLGDYY QGRRITITGN ADLTFDQTAW GDSGVYYCSV VSAQDLQGNN EAYAELIVLG 

       250        260        270        280        290        300 
RTSGVAELLP GFQAGPIEDW LFVVVVCLAA FLIFLLLGIC WCQCCPHTCC CYVRCPCCPD 

       310        320        330        340        350        360 
KCCCPEALYA AGKAATSGVP SIYAPSTYAH LSPAKTPPPP AMIPMGPAYN GYPGGYPGDV 

       370        380        390        400        410        420 
DRSSSAGGQG SYVPLLRDTD SSVASEVRSG YRIQASQQDD SMRVLYYMEK ELANFDPSRP 

       430        440        450        460        470        480 
GPPSGRVERA MSEVTSLHED DWRSRPSRGP ALTPIRDEEW GGHSPRSPRG WDQEPAREQA 

       490        500        510        520        530        540 
GGGWRARRPR ARSVDALDDL TPPSTAESGS RSPTSNGGRS RAYMPPRSRS RDDLYDQDDS 

       550        560        570        580        590        600 
RDFPRSRDPH YDDFRSRERP PADPRSHHHR TRDPRDNGSR SGDLPYDGRL LEEAVRKKGS 

       610        620        630        640 
EERRRPHKEE EEEAYYPPAP PPYSETDSQA SRERRLKKNL ALSRESLVV 

Q86X29 in FASTA format

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