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Q92673 (SORL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 145. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sortilin-related receptor
Alternative name(s):
Low-density lipoprotein receptor relative with 11 ligand-binding repeats
Short name=LDLR relative with 11 ligand-binding repeats
Short name=LR11
SorLA-1
Sorting protein-related receptor containing LDLR class A repeats
Short name=SorLA
Gene names
Name:SORL1
Synonyms:C11orf32
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2214 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Likely to be a multifunctional endocytic receptor, that may be implicated in the uptake of lipoproteins and of proteases. Binds LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. Binds the receptor-associated protein (RAP). Could play a role in cell-cell interaction. Involved in APP trafficking to and from the Golgi apparatus. It probably acts as a sorting receptor that protects APP from trafficking to late endosome and from processing into amyloid beta, thereby reducing the burden of amyloidogenic peptide formation. Involved in the regulation of smooth muscle cells migration, probably through PLAUR binding and decreased internalization. Ref.6 Ref.7

Subunit structure

Interacts with GGA1 and ROCK2. Interacts with PLAUR. Interacts with APP. Ref.6 Ref.7 Ref.12 Ref.15

Subcellular location

Membrane; Single-pass type I membrane protein Potential. Golgi apparatus. Endosome. Secreted Ref.6 Ref.7.

Tissue specificity

Expressed mainly in brain, where it is most abundant in the cerebellum, cerebral cortex and the occipital pole; low expression in the putamen and the thalamus. Expression is significantly reduced in the frontal cortex of patients suffering from Alzheimer disease. According to Ref.1, found in spinal cord, testis, liver, kidney and pancreas with detectable levels in placenta, lung and heart. According to Ref.2, expressed in the prostate, ovary, thyroid and spleen, but not found in kidney, liver, lung, skeletal muscle, bone marrow and adrenals. Ref.7

Post-translational modification

The propeptide removed in the N-terminus may be cleaved by furin or homologous proteases.

Involvement in disease

Alzheimer disease (AD) [MIM:104300]: Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death.
Note: The gene represented in this entry is involved in disease pathogenesis. Ref.8 Ref.11 Ref.13 Ref.17 Ref.18

Sequence similarities

Belongs to the VPS10-related sortilin family. SORL1 subfamily.

Contains 5 BNR repeats.

Contains 1 EGF-like domain.

Contains 6 fibronectin type-III domains.

Contains 11 LDL-receptor class A domains.

Contains 5 LDL-receptor class B repeats.

Ontologies

Keywords
   Biological processCholesterol metabolism
Endocytosis
Lipid metabolism
Lipid transport
Steroid metabolism
Sterol metabolism
Transport
   Cellular componentEndosome
Golgi apparatus
LDL
Membrane
Secreted
   Coding sequence diversityPolymorphism
   DiseaseAlzheimer disease
Amyloidosis
Disease mutation
Neurodegeneration
   DomainEGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell death

Inferred from electronic annotation. Source: UniProtKB-KW

cell migration

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Inferred from electronic annotation. Source: Ensembl

cholesterol metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

lipid transport

Inferred from electronic annotation. Source: UniProtKB-KW

protein targeting

Inferred from mutant phenotype Ref.7. Source: UniProtKB

receptor-mediated endocytosis

Traceable author statement Ref.1. Source: ProtInc

regulation of smooth muscle cell migration

Inferred from direct assay Ref.6. Source: UniProtKB

signal transduction

Traceable author statement Ref.1. Source: GOC

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.7. Source: UniProtKB

endosome

Inferred from direct assay Ref.7. Source: UniProtKB

extracellular space

Inferred from direct assay Ref.6. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

low-density lipoprotein particle

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Inferred from direct assay Ref.6. Source: UniProtKB

multivesicular body

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionlow-density lipoprotein particle binding

Inferred from physical interaction PubMed 17326667. Source: BHF-UCL

transmembrane signaling receptor activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Propeptide29 – 8153Removed in mature form
PRO_0000033164
Chain82 – 22142133Sortilin-related receptor
PRO_0000033165

Regions

Topological domain82 – 21372056Extracellular Potential
Transmembrane2138 – 215821Helical; Potential
Topological domain2159 – 221456Cytoplasmic Potential
Repeat136 – 14712BNR 1
Repeat232 – 24312BNR 2
Repeat441 – 45212BNR 3
Repeat521 – 53212BNR 4
Repeat562 – 57312BNR 5
Repeat800 – 84344LDL-receptor class B 1
Repeat844 – 88744LDL-receptor class B 2
Repeat888 – 93245LDL-receptor class B 3
Repeat933 – 97038LDL-receptor class B 4
Repeat971 – 101343LDL-receptor class B 5
Domain1026 – 107247EGF-like
Domain1076 – 111439LDL-receptor class A 1
Domain1115 – 115541LDL-receptor class A 2
Domain1156 – 119439LDL-receptor class A 3
Domain1198 – 123639LDL-receptor class A 4
Domain1238 – 127235LDL-receptor class A 5
Domain1273 – 131745LDL-receptor class A 6
Domain1323 – 136139LDL-receptor class A 7
Domain1366 – 140540LDL-receptor class A 8
Domain1417 – 145539LDL-receptor class A 9
Domain1469 – 150840LDL-receptor class A 10
Domain1512 – 155140LDL-receptor class A 11
Domain1557 – 164993Fibronectin type-III 1
Domain1653 – 174593Fibronectin type-III 2
Domain1749 – 184496Fibronectin type-III 3
Domain1843 – 192785Fibronectin type-III 4
Domain1934 – 202996Fibronectin type-III 5
Domain2030 – 211889Fibronectin type-III 6
Motif63 – 653Cell attachment site Potential
Motif2172 – 21776Endocytosis signal Potential

Amino acid modifications

Modified residue1141Phosphoserine Ref.10
Modified residue22061Phosphoserine; by ROCK2 Ref.12
Glycosylation991N-linked (GlcNAc...) Ref.9
Glycosylation1581N-linked (GlcNAc...) Potential
Glycosylation3681N-linked (GlcNAc...) Potential
Glycosylation4301N-linked (GlcNAc...) Potential
Glycosylation6161N-linked (GlcNAc...) Potential
Glycosylation6741N-linked (GlcNAc...) Potential
Glycosylation8181N-linked (GlcNAc...) Potential
Glycosylation8711N-linked (GlcNAc...) Potential
Glycosylation10351N-linked (GlcNAc...) Potential
Glycosylation10681N-linked (GlcNAc...) Potential
Glycosylation11641N-linked (GlcNAc...) Potential
Glycosylation11911N-linked (GlcNAc...) Potential
Glycosylation12461N-linked (GlcNAc...) Potential
Glycosylation13671N-linked (GlcNAc...) Potential
Glycosylation14581N-linked (GlcNAc...) Potential
Glycosylation16081N-linked (GlcNAc...) Potential
Glycosylation17061N-linked (GlcNAc...) Potential
Glycosylation17331N-linked (GlcNAc...) Ref.9
Glycosylation18091N-linked (GlcNAc...) Potential
Glycosylation18541N-linked (GlcNAc...) Potential
Glycosylation18941N-linked (GlcNAc...) Potential
Glycosylation19861N-linked (GlcNAc...) Potential
Glycosylation20101N-linked (GlcNAc...) Ref.9
Glycosylation20541N-linked (GlcNAc...) Potential
Glycosylation20691N-linked (GlcNAc...) Potential
Glycosylation20761N-linked (GlcNAc...) Ref.9
Glycosylation20921N-linked (GlcNAc...) Ref.9
Disulfide bond1078 ↔ 1090 By similarity
Disulfide bond1085 ↔ 1103 By similarity
Disulfide bond1097 ↔ 1112 By similarity
Disulfide bond1117 ↔ 1131 By similarity
Disulfide bond1125 ↔ 1144 By similarity
Disulfide bond1138 ↔ 1153 By similarity
Disulfide bond1158 ↔ 1170 By similarity
Disulfide bond1165 ↔ 1183 By similarity
Disulfide bond1177 ↔ 1192 By similarity
Disulfide bond1199 ↔ 1211 By similarity
Disulfide bond1206 ↔ 1224 By similarity
Disulfide bond1218 ↔ 1235 By similarity
Disulfide bond1239 ↔ 1249 By similarity
Disulfide bond1244 ↔ 1262 By similarity
Disulfide bond1256 ↔ 1271 By similarity
Disulfide bond1275 ↔ 1289 By similarity
Disulfide bond1283 ↔ 1302 By similarity
Disulfide bond1296 ↔ 1315 By similarity
Disulfide bond1325 ↔ 1337 By similarity
Disulfide bond1332 ↔ 1350 By similarity
Disulfide bond1344 ↔ 1359 By similarity
Disulfide bond1368 ↔ 1381 By similarity
Disulfide bond1376 ↔ 1394 By similarity
Disulfide bond1388 ↔ 1403 By similarity
Disulfide bond1419 ↔ 1431 By similarity
Disulfide bond1426 ↔ 1444 By similarity
Disulfide bond1438 ↔ 1453 By similarity
Disulfide bond1471 ↔ 1484 By similarity
Disulfide bond1478 ↔ 1497 By similarity
Disulfide bond1491 ↔ 1506 By similarity
Disulfide bond1514 ↔ 1527 By similarity
Disulfide bond1521 ↔ 1540 By similarity
Disulfide bond1534 ↔ 1549 By similarity

Natural variations

Natural variant1201L → S in a breast cancer sample; somatic mutation. Ref.16
VAR_036371
Natural variant1411Y → C in AD; unknown pathological significance. Ref.18
VAR_070012
Natural variant5111G → R in AD; unknown pathological significance. Ref.18
VAR_070013
Natural variant5281A → T. Ref.17
Corresponds to variant rs2298813 [ dbSNP | Ensembl ].
VAR_020360
Natural variant9241N → S in AD; unknown pathological significance. Ref.18
Corresponds to variant rs377498269 [ dbSNP | Ensembl ].
VAR_070014
Natural variant10741Q → E. Ref.1 Ref.2 Ref.4 Ref.5
Corresponds to variant rs1699107 [ dbSNP | Ensembl ].
VAR_034508
Natural variant13581N → S in AD; unknown pathological significance. Ref.18
VAR_070015
Natural variant15811M → L in a breast cancer sample; somatic mutation. Ref.16
VAR_036372
Natural variant16811G → D in AD; unknown pathological significance. Ref.18
VAR_070016
Natural variant19671V → I. Ref.1 Ref.2 Ref.4 Ref.5
Corresponds to variant rs1792120 [ dbSNP | Ensembl ].
VAR_034509
Natural variant19721L → V in a colorectal cancer sample; somatic mutation. Ref.16
VAR_036373

Secondary structure

............... 2214
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q92673 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: 4C215BB33E65C0B2

FASTA2,214248,426
        10         20         30         40         50         60 
MATRSSRRES RLPFLFTLVA LLPPGALCEV WTQRLHGGSA PLPQDRGFLV VQGDPRELRL 

        70         80         90        100        110        120 
WARGDARGAS RADEKPLRRK RSAALQPEPI KVYGQVSLND SHNQMVVHWA GEKSNVIVAL 

       130        140        150        160        170        180 
ARDSLALARP KSSDVYVSYD YGKSFKKISD KLNFGLGNRS EAVIAQFYHS PADNKRYIFA 

       190        200        210        220        230        240 
DAYAQYLWIT FDFCNTLQGF SIPFRAADLL LHSKASNLLL GFDRSHPNKQ LWKSDDFGQT 

       250        260        270        280        290        300 
WIMIQEHVKS FSWGIDPYDK PNTIYIERHE PSGYSTVFRS TDFFQSRENQ EVILEEVRDF 

       310        320        330        340        350        360 
QLRDKYMFAT KVVHLLGSEQ QSSVQLWVSF GRKPMRAAQF VTRHPINEYY IADASEDQVF 

       370        380        390        400        410        420 
VCVSHSNNRT NLYISEAEGL KFSLSLENVL YYSPGGAGSD TLVRYFANEP FADFHRVEGL 

       430        440        450        460        470        480 
QGVYIATLIN GSMNEENMRS VITFDKGGTW EFLQAPAFTG YGEKINCELS QGCSLHLAQR 

       490        500        510        520        530        540 
LSQLLNLQLR RMPILSKESA PGLIIATGSV GKNLASKTNV YISSSAGARW REALPGPHYY 

       550        560        570        580        590        600 
TWGDHGGIIT AIAQGMETNE LKYSTNEGET WKTFIFSEKP VFVYGLLTEP GEKSTVFTIF 

       610        620        630        640        650        660 
GSNKENVHSW LILQVNATDA LGVPCTENDY KLWSPSDERG NECLLGHKTV FKRRTPHATC 

       670        680        690        700        710        720 
FNGEDFDRPV VVSNCSCTRE DYECDFGFKM SEDLSLEVCV PDPEFSGKSY SPPVPCPVGS 

       730        740        750        760        770        780 
TYRRTRGYRK ISGDTCSGGD VEARLEGELV PCPLAEENEF ILYAVRKSIY RYDLASGATE 

       790        800        810        820        830        840 
QLPLTGLRAA VALDFDYEHN CLYWSDLALD VIQRLCLNGS TGQEVIINSG LETVEALAFE 

       850        860        870        880        890        900 
PLSQLLYWVD AGFKKIEVAN PDGDFRLTIV NSSVLDRPRA LVLVPQEGVM FWTDWGDLKP 

       910        920        930        940        950        960 
GIYRSNMDGS AAYHLVSEDV KWPNGISVDD QWIYWTDAYL ECIERITFSG QQRSVILDNL 

       970        980        990       1000       1010       1020 
PHPYAIAVFK NEIYWDDWSQ LSIFRASKYS GSQMEILANQ LTGLMDMKIF YKGKNTGSNA 

      1030       1040       1050       1060       1070       1080 
CVPRPCSLLC LPKANNSRSC RCPEDVSSSV LPSGDLMCDC PQGYQLKNNT CVKQENTCLR 

      1090       1100       1110       1120       1130       1140 
NQYRCSNGNC INSIWWCDFD NDCGDMSDER NCPTTICDLD TQFRCQESGT CIPLSYKCDL 

      1150       1160       1170       1180       1190       1200 
EDDCGDNSDE SHCEMHQCRS DEYNCSSGMC IRSSWVCDGD NDCRDWSDEA NCTAIYHTCE 

      1210       1220       1230       1240       1250       1260 
ASNFQCRNGH CIPQRWACDG DTDCQDGSDE DPVNCEKKCN GFRCPNGTCI PSSKHCDGLR 

      1270       1280       1290       1300       1310       1320 
DCSDGSDEQH CEPLCTHFMD FVCKNRQQCL FHSMVCDGII QCRDGSDEDA AFAGCSQDPE 

      1330       1340       1350       1360       1370       1380 
FHKVCDEFGF QCQNGVCISL IWKCDGMDDC GDYSDEANCE NPTEAPNCSR YFQFRCENGH 

      1390       1400       1410       1420       1430       1440 
CIPNRWKCDR ENDCGDWSDE KDCGDSHILP FSTPGPSTCL PNYYRCSSGT CVMDTWVCDG 

      1450       1460       1470       1480       1490       1500 
YRDCADGSDE EACPLLANVT AASTPTQLGR CDRFEFECHQ PKTCIPNWKR CDGHQDCQDG 

      1510       1520       1530       1540       1550       1560 
RDEANCPTHS TLTCMSREFQ CEDGEACIVL SERCDGFLDC SDESDEKACS DELTVYKVQN 

      1570       1580       1590       1600       1610       1620 
LQWTADFSGD VTLTWMRPKK MPSASCVYNV YYRVVGESIW KTLETHSNKT NTVLKVLKPD 

      1630       1640       1650       1660       1670       1680 
TTYQVKVQVQ CLSKAHNTND FVTLRTPEGL PDAPRNLQLS LPREAEGVIV GHWAPPIHTH 

      1690       1700       1710       1720       1730       1740 
GLIREYIVEY SRSGSKMWAS QRAASNFTEI KNLLVNTLYT VRVAAVTSRG IGNWSDSKSI 

      1750       1760       1770       1780       1790       1800 
TTIKGKVIPP PDIHIDSYGE NYLSFTLTME SDIKVNGYVV NLFWAFDTHK QERRTLNFRG 

      1810       1820       1830       1840       1850       1860 
SILSHKVGNL TAHTSYEISA WAKTDLGDSP LAFEHVMTRG VRPPAPSLKA KAINQTAVEC 

      1870       1880       1890       1900       1910       1920 
TWTGPRNVVY GIFYATSFLD LYRNPKSLTT SLHNKTVIVS KDEQYLFLVR VVVPYQGPSS 

      1930       1940       1950       1960       1970       1980 
DYVVVKMIPD SRLPPRHLHV VHTGKTSVVI KWESPYDSPD QDLLYAVAVK DLIRKTDRSY 

      1990       2000       2010       2020       2030       2040 
KVKSRNSTVE YTLNKLEPGG KYHIIVQLGN MSKDSSIKIT TVSLSAPDAL KIITENDHVL 

      2050       2060       2070       2080       2090       2100 
LFWKSLALKE KHFNESRGYE IHMFDSAMNI TAYLGNTTDN FFKISNLKMG HNYTFTVQAR 

      2110       2120       2130       2140       2150       2160 
CLFGNQICGE PAILLYDELG SGADASATQA ARSTDVAAVV VPILFLILLS LGVGFAILYT 

      2170       2180       2190       2200       2210 
KHRRLQSSFT AFANSHYSSR LGSAIFSSGD DLGEDDEDAP MITGFSDDVP MVIA 

« Hide

References

« Hide 'large scale' references
[1]"A novel mosaic protein containing LDL receptor elements is highly conserved in humans and chickens."
Morwald S., Yamazaki H., Bujo H., Kusunoki J., Kanaki T., Seimiya K., Morisaki N., Nimpf J., Schneider W.J., Saito Y.
Arterioscler. Thromb. Vasc. Biol. 17:996-1002(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS GLU-1074 AND ILE-1967.
Tissue: Brain.
[2]"Molecular characterization of a novel human hybrid-type receptor that binds the alpha2-macroglobulin receptor-associated protein."
Jacobsen L., Madsen P., Moestrup S.K., Lund A.H., Tommerup N., Nykjaer A., Sottrup-Jensen L., Gliemann J., Petersen C.M.
J. Biol. Chem. 271:31379-31383(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, PARTIAL PROTEIN SEQUENCE, VARIANTS GLU-1074 AND ILE-1967.
Tissue: Brain and T-cell.
[3]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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. 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS GLU-1074 AND ILE-1967.
[5]"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], VARIANTS GLU-1074 AND ILE-1967.
Tissue: Brain.
[6]"LR11, an LDL receptor gene family member, is a novel regulator of smooth muscle cell migration."
Zhu Y., Bujo H., Yamazaki H., Ohwaki K., Jiang M., Hirayama S., Kanaki T., Shibasaki M., Takahashi K., Schneider W.J., Saito Y.
Circ. Res. 94:752-758(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PLAUR.
[7]"Neuronal sorting protein-related receptor sorLA/LR11 regulates processing of the amyloid precursor protein."
Andersen O.M., Reiche J., Schmidt V., Gotthardt M., Spoelgen R., Behlke J., von Arnim C.A., Breiderhoff T., Jansen P., Wu X., Bales K.R., Cappai R., Masters C.L., Gliemann J., Mufson E.J., Hyman B.T., Paul S.M., Nykjaer A., Willnow T.E.
Proc. Natl. Acad. Sci. U.S.A. 102:13461-13466(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN APP TRAFFICKING, SUBCELLULAR LOCATION, INTERACTION WITH APP, TISSUE SPECIFICITY.
[8]"No association of SORL1 SNPs with Alzheimer's disease."
Minster R.L., DeKosky S.T., Kamboh M.I.
Neurosci. Lett. 440:190-192(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: LACK OF ASSOCIATION WITH SUSCEPTIBILITY TO LATE-ONSET ALZHEIMER DISEASE.
[9]"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-99; ASN-1733; ASN-2010; ASN-2076 AND ASN-2092.
Tissue: Liver.
[10]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Meta-analysis of the association between variants in SORL1 and Alzheimer disease."
Genetic and Environmental Risk in Alzheimer Disease 1 Consortium
Reitz C., Cheng R., Rogaeva E., Lee J.H., Tokuhiro S., Zou F., Bettens K., Sleegers K., Tan E.K., Kimura R., Shibata N., Arai H., Kamboh M.I., Prince J.A., Maier W., Riemenschneider M., Owen M., Harold D. expand/collapse author list , Hollingworth P., Cellini E., Sorbi S., Nacmias B., Takeda M., Pericak-Vance M.A., Haines J.L., Younkin S., Williams J., van Broeckhoven C., Farrer L.A., St George-Hyslop P.H., Mayeux R.
Arch. Neurol. 68:99-106(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN AD.
[12]"Rho kinase II phosphorylation of the lipoprotein receptor LR11/SORLA alters amyloid-beta production."
Herskowitz J.H., Seyfried N.T., Gearing M., Kahn R.A., Peng J., Levey A.I., Lah J.J.
J. Biol. Chem. 286:6117-6127(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-2206, INTERACTION WITH ROCK2.
[13]"SORL1 is genetically associated with late-onset Alzheimer's disease in Japanese, Koreans and Caucasians."
Alzheimer Disease Genetics Consortium
Miyashita A., Koike A., Jun G., Wang L.S., Takahashi S., Matsubara E., Kawarabayashi T., Shoji M., Tomita N., Arai H., Asada T., Harigaya Y., Ikeda M., Amari M., Hanyu H., Higuchi S., Ikeuchi T., Nishizawa M. expand/collapse author list , Suga M., Kawase Y., Akatsu H., Kosaka K., Yamamoto T., Imagawa M., Hamaguchi T., Yamada M., Moriaha T., Takeda M., Takao T., Nakata K., Fujisawa Y., Sasaki K., Watanabe K., Nakashima K., Urakami K., Ooya T., Takahashi M., Yuzuriha T., Serikawa K., Yoshimoto S., Nakagawa R., Kim J.W., Ki C.S., Won H.H., Na D.L., Seo S.W., Mook-Jung I., St George-Hyslop P., Mayeux R., Haines J.L., Pericak-Vance M.A., Yoshida M., Nishida N., Tokunaga K., Yamamoto K., Tsuji S., Kanazawa I., Ihara Y., Schellenberg G.D., Farrer L.A., Kuwano R.
PLoS ONE 8:E58618-E58618(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN AD.
[14]"Solution structure of the second FN3 domain of human SORLA/LR11."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1651-1745.
[15]"GGA autoinhibition revisited."
Cramer J.F., Gustafsen C., Behrens M.A., Oliveira C.L., Pedersen J.S., Madsen P., Petersen C.M., Thirup S.S.
Traffic 11:259-273(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2202-2214 IN COMPLEX WITH GGA1, INTERACTION WITH GGA1.
[16]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-120; LEU-1581 AND VAL-1972.
[17]"SORL1 is genetically associated with increased risk for late-onset Alzheimer disease in the Belgian population."
Bettens K., Brouwers N., Engelborghs S., De Deyn P.P., Van Broeckhoven C., Sleegers K.
Hum. Mutat. 29:769-770(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE ASSOCIATION WITH SUSCEPTIBILITY TO LATE-ONSET ALZHEIMER DISEASE, VARIANT THR-528.
[18]"High frequency of potentially pathogenic SORL1 mutations in autosomal dominant early-onset Alzheimer disease."
PHRC GMAJ Collaborators
Pottier C., Hannequin D., Coutant S., Rovelet-Lecrux A., Wallon D., Rousseau S., Legallic S., Paquet C., Bombois S., Pariente J., Thomas-Anterion C., Michon A., Croisile B., Etcharry-Bouyx F., Berr C., Dartigues J.F., Amouyel P., Dauchel H. expand/collapse author list , Boutoleau-Bretonniere C., Thauvin C., Frebourg T., Lambert J.C., Campion D.
Mol. Psychiatry 17:875-879(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AD CYS-141; ARG-511; SER-924; SER-1358 AND ASP-1681.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y08110 mRNA. Translation: CAA69325.1.
U60975 mRNA. Translation: AAC50891.2.
AP000664 Genomic DNA. No translation available.
AP000977 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67525.1.
BC137171 mRNA. Translation: AAI37172.1.
RefSeqNP_003096.1. NM_003105.5.
UniGeneHs.368592.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DM4NMR-A1651-1745[»]
3G2SX-ray1.70C/D2202-2214[»]
3G2TX-ray2.00C/D2202-2214[»]
ProteinModelPortalQ92673.
SMRQ92673. Positions 95-1049, 1075-1553, 1555-1745.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112536. 10 interactions.
IntActQ92673. 10 interactions.
MINTMINT-231252.
STRING9606.ENSP00000260197.

PTM databases

PhosphoSiteQ92673.

Polymorphism databases

DMDM296452912.

Proteomic databases

PaxDbQ92673.
PRIDEQ92673.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260197; ENSP00000260197; ENSG00000137642.
GeneID6653.
KEGGhsa:6653.
UCSCuc001pxx.3. human.

Organism-specific databases

CTD6653.
GeneCardsGC11P121356.
HGNCHGNC:11185. SORL1.
HPACAB011500.
HPA031321.
MIM104300. phenotype.
602005. gene.
neXtProtNX_Q92673.
Orphanet1020. Early-onset autosomal dominant Alzheimer disease.
PharmGKBPA36022.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG281049.
HOGENOMHOG000007009.
HOVERGENHBG017830.
InParanoidQ92673.
OMATNVYISS.
OrthoDBEOG7FV3PK.
PhylomeDBQ92673.
TreeFamTF324918.

Gene expression databases

ArrayExpressQ92673.
BgeeQ92673.
CleanExHS_SORL1.
GenevestigatorQ92673.

Family and domain databases

Gene3D2.120.10.30. 1 hit.
2.60.40.10. 4 hits.
4.10.400.10. 10 hits.
InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR000742. EG-like_dom.
IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
IPR006581. VPS10.
[Graphical view]
PfamPF00041. fn3. 3 hits.
PF00057. Ldl_recept_a. 10 hits.
PF00058. Ldl_recept_b. 2 hits.
[Graphical view]
PRINTSPR00261. LDLRECEPTOR.
SMARTSM00181. EGF. 1 hit.
SM00060. FN3. 6 hits.
SM00192. LDLa. 11 hits.
SM00135. LY. 5 hits.
SM00602. VPS10. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 3 hits.
SSF57424. SSF57424. 11 hits.
PROSITEPS01186. EGF_2. 1 hit.
PS50853. FN3. 4 hits.
PS01209. LDLRA_1. 10 hits.
PS50068. LDLRA_2. 11 hits.
PS51120. LDLRB. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSORL1. human.
EvolutionaryTraceQ92673.
GenomeRNAi6653.
NextBio25935.
PROQ92673.
SOURCESearch...

Entry information

Entry nameSORL_HUMAN
AccessionPrimary (citable) accession number: Q92673
Secondary accession number(s): B2RNX7, Q92856
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 145 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 11

Human chromosome 11: entries, gene names and cross-references to MIM