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Low-density lipoprotein receptor-related protein 6 (LRP-6)

 LRP6_HUMAN              Reviewed;        1613 AA.
O75581; Q17RZ2;
10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 2.
27-SEP-2017, entry version 157.
RecName: Full=Low-density lipoprotein receptor-related protein 6;
Short=LRP-6;
Flags: Precursor;
Name=LRP6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ILE-1062.
TISSUE=Kidney;
PubMed=9704021; DOI=10.1006/bbrc.1998.9061;
Brown S.D., Twells R.C., Hey P.J., Cox R.D., Levy E.R., Soderman A.R.,
Metzker M.L., Caskey C.T., Todd J.A., Hess J.F.;
"Isolation and characterization of LRP6, a novel member of the low
density lipoprotein receptor gene family.";
Biochem. Biophys. Res. Commun. 248:879-888(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[4]
INTERACTION WITH DKK1, AND FUNCTION.
PubMed=11448771; DOI=10.1016/S0960-9822(01)00290-1;
Semenov M.V., Tamai K., Brott B.K., Kuhl M., Sokol S., He X.;
"Head inducer Dickkopf-1 is a ligand for Wnt coreceptor LRP6.";
Curr. Biol. 11:951-961(2001).
[5]
INTERACTION WITH WNT1, AND FUNCTION.
PubMed=11357136; DOI=10.1038/35077108;
Mao B., Wu W., Li Y., Hoppe D., Stannek P., Glinka A., Niehrs C.;
"LDL-receptor-related protein 6 is a receptor for Dickkopf proteins.";
Nature 411:321-325(2001).
[6]
INTERACTION WITH FZD5; DKK1 AND DKK2.
PubMed=12857724; DOI=10.1074/jbc.M300191200;
Caricasole A., Ferraro T., Iacovelli L., Barletta E., Caruso A.,
Melchiorri D., Terstappen G.C., Nicoletti F.;
"Functional characterization of WNT7A signaling in PC12 cells:
interaction with A FZD5 x LRP6 receptor complex and modulation by
Dickkopf proteins.";
J. Biol. Chem. 278:37024-37031(2003).
[7]
INTERACTION WITH SOST, AND FUNCTION.
PubMed=15778503; DOI=10.1074/jbc.M413274200;
Li X., Zhang Y., Kang H., Liu W., Liu P., Zhang J., Harris S.E.,
Wu D.;
"Sclerostin binds to LRP5/6 and antagonizes canonical Wnt signaling.";
J. Biol. Chem. 280:19883-19887(2005).
[8]
INTERACTION WITH WNT1 IN THE WNT-FZD-LRP5-LRP6 COMPLEX, AND
INTERACTION WITH SOST.
PubMed=15908424; DOI=10.1074/jbc.M504308200;
Semenov M., Tamai K., He X.;
"SOST is a ligand for LRP5/LRP6 and a Wnt signaling inhibitor.";
J. Biol. Chem. 280:26770-26775(2005).
[9]
PHOSPHORYLATION OF PPPSP MOTIFS, PHOSPHORYLATION AT SER-1490 AND
THR-1493, AND FUNCTION.
PubMed=16341017; DOI=10.1038/nature04185;
Zeng X., Tamai K., Doble B., Li S., Huang H., Habas R., Okamura H.,
Woodgett J., He X.;
"A dual-kinase mechanism for Wnt co-receptor phosphorylation and
activation.";
Nature 438:873-877(2005).
[10]
INTERACTION WITH MACF1.
PubMed=16815997; DOI=10.1101/gad.1411206;
Chen H.J., Lin C.M., Lin C.S., Perez-Olle R., Leung C.L., Liem R.K.;
"The role of microtubule actin cross-linking factor 1 (MACF1) in the
Wnt signaling pathway.";
Genes Dev. 20:1933-1945(2006).
[11]
PHOSPHORYLATION AT SER-1420 AND SER-1430, FUNCTION, INTERACTION WITH
CSNKIE AND AXIN1, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS
OF SER-1420 AND SER-1430.
PubMed=16513652; DOI=10.1074/jbc.M510580200;
Swiatek W., Kang H., Garcia B.A., Shabanowitz J., Coombs G.S.,
Hunt D.F., Virshup D.M.;
"Negative regulation of LRP6 function by casein kinase I epsilon
phosphorylation.";
J. Biol. Chem. 281:12233-12241(2006).
[12]
INTERACTION WITH RSPO1, FUNCTION, AND PHOSPHORYLATION.
PubMed=17400545; DOI=10.1074/jbc.M701927200;
Wei Q., Yokota C., Semenov M.V., Doble B., Woodgett J., He X.;
"R-spondin1 is a high affinity ligand for LRP6 and induces LRP6
phosphorylation and beta-catenin signaling.";
J. Biol. Chem. 282:15903-15911(2007).
[13]
PROTEOLYTIC PROCESSING, AND FUNCTION.
PubMed=17326769; DOI=10.1111/j.1471-4159.2007.04447.x;
Mi K., Johnson G.V.;
"Regulated proteolytic processing of LRP6 results in release of its
intracellular domain.";
J. Neurochem. 101:517-529(2007).
[14]
GLYCOSYLATION, PHOSPHORYLATION AT SER-1490, INTERACTION WITH AXIN1,
HOMODIMERIZATION, INDUCTION, AND SUBCELLULAR LOCATION.
PubMed=17698587; DOI=10.1128/MCB.00773-07;
Khan Z., Vijayakumar S., de la Torre T.V., Rotolo S., Bafico A.;
"Analysis of endogenous LRP6 function reveals a novel feedback
mechanism by which Wnt negatively regulates its receptor.";
Mol. Cell. Biol. 27:7291-7301(2007).
[15]
INTERACTION WITH KREM1 AND DKK1.
PubMed=17804805; DOI=10.1073/pnas.0702305104;
Binnerts M.E., Kim K.A., Bright J.M., Patel S.M., Tran K., Zhou M.,
Leung J.M., Liu Y., Lomas W.E. III, Dixon M., Hazell S.A., Wagle M.,
Nie W.S., Tomasevic N., Williams J., Zhan X., Levy M.D., Funk W.D.,
Abo A.;
"R-Spondin1 regulates Wnt signaling by inhibiting internalization of
LRP6.";
Proc. Natl. Acad. Sci. U.S.A. 104:14700-14705(2007).
[16]
PHOSPHORYLATION AT THR-1479, INTERACTION WITH AXIN1, SUBUNIT, AND
SUBCELLULAR LOCATION.
PubMed=17569865; DOI=10.1126/science.1137065;
Bilic J., Huang Y.L., Davidson G., Zimmermann T., Cruciat C.M.,
Bienz M., Niehrs C.;
"Wnt induces LRP6 signalosomes and promotes dishevelled-dependent LRP6
phosphorylation.";
Science 316:1619-1622(2007).
[17]
INTERACTION WITH AXIN1, PHOSPHORYLATION, AND MUTAGENESIS OF LEU-1485;
ASN-1486; PRO-1487; PRO-1488; PRO-1489; SER-1490; PRO-1491; ALA-1492;
THR-1493; GLU-1494; ARG-1495; THR-1529; THR-1530; PRO-1531; THR-1572;
SER-1590 AND SER-1607.
PubMed=18362152; DOI=10.1074/jbc.M800327200;
MacDonald B.T., Yokota C., Tamai K., Zeng X., He X.;
"Wnt signal amplification via activity, cooperativity, and regulation
of multiple intracellular PPPSP motifs in the Wnt co-receptor LRP6.";
J. Biol. Chem. 283:16115-16123(2008).
[18]
INTERACTION WITH CAPRIN2, AND PHOSPHORYLATION AT SER-1490.
PubMed=18762581; DOI=10.1083/jcb.200803147;
Ding Y., Xi Y., Chen T., Wang J.Y., Tao D.L., Wu Z.L., Li Y.P., Li C.,
Zeng R., Li L.;
"Caprin-2 enhances canonical Wnt signaling through regulating LRP5/6
phosphorylation.";
J. Cell Biol. 182:865-872(2008).
[19]
PHOSPHORYLATION ON PPPSP MOTIFS, AND FUNCTION.
PubMed=19107203; DOI=10.1371/journal.pone.0004046;
Piao S., Lee S.H., Kim H., Yum S., Stamos J.L., Xu Y., Lee S.J.,
Lee J., Oh S., Han J.K., Park B.J., Weis W.I., Ha N.C.;
"Direct inhibition of GSK3beta by the phosphorylated cytoplasmic
domain of LRP6 in Wnt/beta-catenin signaling.";
PLoS ONE 3:E4046-E4046(2008).
[20]
PALMITOYLATION AT CYS-1394 AND CYS-1399, UBIQUITINATION AT LYS-1403,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-1394 AND CYS-1399.
PubMed=18378904; DOI=10.1073/pnas.0710389105;
Abrami L., Kunz B., Iacovache I., van der Goot F.G.;
"Palmitoylation and ubiquitination regulate exit of the Wnt signaling
protein LRP6 from the endoplasmic reticulum.";
Proc. Natl. Acad. Sci. U.S.A. 105:5384-5389(2008).
[21]
DOMAIN PPPSP MOTIF, AND PHOSPHORYLATION AT SER-1490.
PubMed=20059949; DOI=10.1016/j.devcel.2009.11.006;
Davidson G., Shen J., Huang Y.L., Su Y., Karaulanov E.,
Bartscherer K., Hassler C., Stannek P., Boutros M., Niehrs C.;
"Cell cycle control of wnt receptor activation.";
Dev. Cell 17:788-799(2009).
[22]
PHOSPHORYLATION OF PPPSP MOTIFS, PHOSPHORYLATION AT SER-1490, AND
FUNCTION.
PubMed=19801552; DOI=10.1074/jbc.M109.047456;
Chen M., Philipp M., Wang J., Premont R.T., Garrison T.R., Caron M.G.,
Lefkowitz R.J., Chen W.;
"G Protein-coupled receptor kinases phosphorylate LRP6 in the Wnt
pathway.";
J. Biol. Chem. 284:35040-35048(2009).
[23]
PHOSPHORYLATION OF PPPSP MOTIFS, AND FUNCTION.
PubMed=19293931; DOI=10.1371/journal.pone.0004926;
Wu G., Huang H., Garcia Abreu J., He X.;
"Inhibition of GSK3 phosphorylation of beta-catenin via phosphorylated
PPPSPXS motifs of Wnt coreceptor LRP6.";
PLoS ONE 4:E4926-E4926(2009).
[24]
INTERACTION WITH WNT3A; WNT9B AND FZD8 IN THE WNT/FZD/LRP6 COMPLEX,
AND INTERACTION WITH DKK1.
PubMed=20093360; DOI=10.1074/jbc.M109.092130;
Bourhis E., Tam C., Franke Y., Bazan J.F., Ernst J., Hwang J.,
Costa M., Cochran A.G., Hannoush R.N.;
"Reconstitution of a frizzled8.Wnt3a.LRP6 signaling complex reveals
multiple Wnt and Dkk1 binding sites on LRP6.";
J. Biol. Chem. 285:9172-9179(2010).
[25]
INTERACTION WITH TMEM198.
PubMed=21536646; DOI=10.1128/MCB.05103-11;
Liang J., Fu Y., Cruciat C.M., Jia S., Wang Y., Tong Z., Tao Q.,
Ingelfinger D., Boutros M., Meng A., Niehrs C., Wu W.;
"Transmembrane protein 198 promotes LRP6 phosphorylation and Wnt
signaling activation.";
Mol. Cell. Biol. 31:2577-2590(2011).
[26]
INTERACTION WITH DAB2.
PubMed=22491013; DOI=10.1038/emboj.2012.83;
Jiang Y., He X., Howe P.H.;
"Disabled-2 (Dab2) inhibits Wnt/beta-catenin signalling by binding
LRP6 and promoting its internalization through clathrin.";
EMBO J. 31:2336-2349(2012).
[27]
UBIQUITINATION BY ZNRF3.
PubMed=22575959; DOI=10.1038/nature11019;
Hao H.X., Xie Y., Zhang Y., Charlat O., Oster E., Avello M., Lei H.,
Mickanin C., Liu D., Ruffner H., Mao X., Ma Q., Zamponi R.,
Bouwmeester T., Finan P.M., Kirschner M.W., Porter J.A., Serluca F.C.,
Cong F.;
"ZNRF3 promotes Wnt receptor turnover in an R-spondin-sensitive
manner.";
Nature 485:195-200(2012).
[28]
INTERACTION WITH LYPD6, AND SUBCELLULAR LOCATION.
PubMed=23987510; DOI=10.1016/j.devcel.2013.07.020;
Oezhan G., Sezgin E., Wehner D., Pfister A.S., Kuehl S.J.,
Kagermeier-Schenk B., Kuehl M., Schwille P., Weidinger G.;
"Lypd6 enhances Wnt/beta-catenin signaling by promoting Lrp6
phosphorylation in raft plasma membrane domains.";
Dev. Cell 26:331-345(2013).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1490, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[30]
INTERACTION WITH CAPRIN2, AND PHOSPHORYLATION AT SER-1490.
PubMed=25331957; DOI=10.1074/jbc.M114.591636;
Miao H., Jia Y., Xie S., Wang X., Zhao J., Chu Y., Zhou Z., Shi Z.,
Song X., Li L.;
"Structural insights into the C1q domain of Caprin-2 in canonical Wnt
signaling.";
J. Biol. Chem. 289:34104-34113(2014).
[31]
IDENTIFICATION IN A COMPLEX WITH CAPRIN2; CCNY AND CDK14, AND
PHOSPHORYLATION AT SER-1490.
PubMed=27821587; DOI=10.1074/jbc.M116.744607;
Wang X., Jia Y., Fei C., Song X., Li L.;
"Caprin-2 positively regulates CDK14/Cyclin Y-mediated LRP5/6
constitutive phosphorylation.";
J. Biol. Chem. 291:26427-26434(2016).
[32]
IDENTIFICATION IN A TERNARY COMPLEX WITH KREM1 AND LRP6.
PubMed=27524201; DOI=10.1016/j.str.2016.06.020;
Zebisch M., Jackson V.A., Zhao Y., Jones E.Y.;
"Structure of the dual-mode wnt regulator Kremen1 and insight into
ternary complex formation with LRP6 and Dickkopf.";
Structure 24:1599-1605(2016).
[33]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 630-1246 IN COMPLEX WITH
DKK1, SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-692; ASN-859;
ASN-865; ASN-926 AND ASN-1039.
PubMed=22000856; DOI=10.1016/j.devcel.2011.09.003;
Ahn V.E., Chu M.L., Choi H.J., Tran D., Abo A., Weis W.I.;
"Structural basis of Wnt signaling inhibition by Dickkopf binding to
LRP5/6.";
Dev. Cell 21:862-873(2011).
[34]
VARIANT ADCAD2 CYS-611, AND CHARACTERIZATION OF VARIANT ADCAD2
CYS-611.
PubMed=17332414; DOI=10.1126/science.1136370;
Mani A., Radhakrishnan J., Wang H., Mani A., Mani M.-A.,
Nelson-Williams C., Carew K.S., Mane S., Najmabadi H., Wu D.,
Lifton R.P.;
"LRP6 mutation in a family with early coronary disease and metabolic
risk factors.";
Science 315:1278-1282(2007).
[35]
VARIANTS ADCAD2 HIS-360; SER-433 AND GLN-473, AND CHARACTERIZATION OF
VARIANT ADCAD2 GLN-473.
PubMed=23703864; DOI=10.1002/humu.22360;
Singh R., Smith E., Fathzadeh M., Liu W., Go G.W., Subrahmanyan L.,
Faramarzi S., McKenna W., Mani A.;
"Rare nonconservative LRP6 mutations are associated with metabolic
syndrome.";
Hum. Mutat. 34:1221-1225(2013).
[36]
INVOLVEMENT IN STHAG7, VARIANT STHAG7 VAL-19, CHARACTERIZATION OF
VARIANT STHAG7 VAL-19, AND SUBCELLULAR LOCATION.
PubMed=26387593; DOI=10.1016/j.ajhg.2015.08.014;
Massink M.P., Creton M.A., Spanevello F., Fennis W.M., Cune M.S.,
Savelberg S.M., Nijman I.J., Maurice M.M., van den Boogaard M.J.,
van Haaften G.;
"Loss-of-Function Mutations in the WNT Co-receptor LRP6 Cause
Autosomal-Dominant Oligodontia.";
Am. J. Hum. Genet. 97:621-626(2015).
-!- FUNCTION: Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers
beta-catenin signaling through inducing aggregation of receptor-
ligand complexes into ribosome-sized signalsomes. Cell-surface
coreceptor of Wnt/beta-catenin signaling, which plays a pivotal
role in bone formation. The Wnt-induced Fzd/LRP6 coreceptor
complex recruits DVL1 polymers to the plasma membrane which, in
turn, recruits the AXIN1/GSK3B-complex to the cell surface
promoting the formation of signalsomes and inhibiting AXIN1/GSK3-
mediated phosphorylation and destruction of beta-catenin. Required
for posterior patterning of the epiblast during gastrulation (By
similarity). {ECO:0000250, ECO:0000269|PubMed:11357136,
ECO:0000269|PubMed:11448771, ECO:0000269|PubMed:15778503,
ECO:0000269|PubMed:16341017, ECO:0000269|PubMed:16513652,
ECO:0000269|PubMed:17326769, ECO:0000269|PubMed:17400545,
ECO:0000269|PubMed:19107203, ECO:0000269|PubMed:19293931,
ECO:0000269|PubMed:19801552}.
-!- SUBUNIT: Homodimer; disulfide-linked. Forms phosphorylated
oligomer aggregates on Wnt-signaling. Forms a WNT-signaling
complex formed of a WNT protein, a FZD protein and LRP5 or LRP6.
Interacts (via the extracellular domain) with WNT1; the
interaction is enhanced by prior formation of the Wnt/Fzd complex.
Interacts (via the beta-propeller regions 3 and 4) with WNT3A.
Interacts (via the beta-propeller regions 1 and 2) with WNT9B.
Interacts with FZD5; the interaction forms a coreceptor complex
for Wnt signaling and is inhibited by DKK1 and DRAXIN. Interacts
(via beta propeller region) with DKK1; the interaction inhibits
FZD5/LRP6 complex formation. Interacts with DKK2. Interacts with
C1orf187/DRAXIN; the interaction inhibits Wnt signaling (By
similarity). Interacts (via the phosphorylated PPPSP motifs) with
AXIN1; the interaction recruits the AXIN1/GSK3B complex to cell
surface LRP6 signalsomes. Interacts with GRB10; the interaction
prevents AXIN1 binding, thus negatively regulating the Wnt
signaling pathway (By similarity). Interacts (via the
extracellular domain) with RSPO1; the interaction activates
Wnt/beta-catenin signaling. Interacts (via the extracellular
domain) with RSPO3 (via the cysteine rich domain); the interaction
activates Wnt/beta-catenin signaling. Interacts (via the beta-
propeller regions 1 and 2) with SOST; the interaction competes
with DKK1 for binding for inhibiting beta-catenin signaling.
Interacts with MESD; the interaction prevents the formation of
LRP6 aggregates and targets LRP6 to the plasma membrane (By
similarity). Interacts (via the cytoplasmic domain) with CSNKIE;
the interaction phosphorylates LRP6, binds AXIN1 and inhibits
AXIN1/GSK3B-mediated phosphorylation of beta-catenin. Interacts
with MACF1. Interacts with DAB2; the interaction involves LRP6
phosphorylation by CK2 and sequesters LRP6 towards clathrin-
mediated endocytosis. Interacts with TMEM198. Interacts with
CAPRIN2; the interaction promotes LRP6 phosphorylation at Ser-1490
(PubMed:18762581, PubMed:25331957). Found in a complex with
CAPRIN2, CCNY and CDK14 during G2/M stage; CAPRIN2 functions as a
scaffold for the complex by binding to CCNY via its N terminus and
to CDK14 via its C terminus (PubMed:27821587). Interacts with
LYPD6 (PubMed:23987510). Forms a ternary complex with DKK1 and
KREM1 (PubMed:27524201). Interacts with KREM1 in a DKK1-dependent
manner (PubMed:17804805). {ECO:0000250|UniProtKB:O88572,
ECO:0000269|PubMed:11357136, ECO:0000269|PubMed:11448771,
ECO:0000269|PubMed:12857724, ECO:0000269|PubMed:15778503,
ECO:0000269|PubMed:15908424, ECO:0000269|PubMed:16513652,
ECO:0000269|PubMed:16815997, ECO:0000269|PubMed:17400545,
ECO:0000269|PubMed:17569865, ECO:0000269|PubMed:17698587,
ECO:0000269|PubMed:17804805, ECO:0000269|PubMed:18362152,
ECO:0000269|PubMed:18762581, ECO:0000269|PubMed:20093360,
ECO:0000269|PubMed:21536646, ECO:0000269|PubMed:22000856,
ECO:0000269|PubMed:22491013, ECO:0000269|PubMed:23987510,
ECO:0000269|PubMed:25331957, ECO:0000269|PubMed:27524201,
ECO:0000269|PubMed:27821587}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-910915, EBI-910915;
Q9Y4X0:AMMECR1; NbExp=5; IntAct=EBI-910915, EBI-8583355;
Q9H6X2:ANTXR1; NbExp=3; IntAct=EBI-910915, EBI-905643;
O35625:Axin1 (xeno); NbExp=2; IntAct=EBI-910915, EBI-2365912;
O70239:Axin1 (xeno); NbExp=12; IntAct=EBI-910915, EBI-6857773;
Q03135:CAV1; NbExp=3; IntAct=EBI-910915, EBI-603614;
P98082:DAB2; NbExp=20; IntAct=EBI-910915, EBI-1171238;
O94907:DKK1; NbExp=3; IntAct=EBI-910915, EBI-742864;
Q61091:Fzd8 (xeno); NbExp=4; IntAct=EBI-910915, EBI-6171689;
P49840:GSK3A; NbExp=2; IntAct=EBI-910915, EBI-1044067;
P49841:GSK3B; NbExp=4; IntAct=EBI-910915, EBI-373586;
Q5S007:LRRK2; NbExp=4; IntAct=EBI-910915, EBI-5323863;
Q9ERE7:Mesdc2 (xeno); NbExp=2; IntAct=EBI-910915, EBI-6662606;
Q9BQB4:SOST; NbExp=2; IntAct=EBI-910915, EBI-5746563;
P04426:Wnt1 (xeno); NbExp=2; IntAct=EBI-910915, EBI-1570911;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26387593};
Single-pass type I membrane protein. Endoplasmic reticulum
{ECO:0000269|PubMed:26387593}. Membrane raft
{ECO:0000269|PubMed:23987510}. Note=On Wnt signaling, undergoes a
cycle of caveolin- or clathrin-mediated endocytosis and plasma
membrane location. Released from the endoplasmic reticulum on
palmitoylation. Mono-ubiquitination retains it in the endoplasmic
reticulum in the absence of palmitoylation. On Wnt signaling,
phosphorylated, aggregates and colocalizes with AXIN1 and GSK3B at
the plasma membrane in LRP6-signalsomes. Chaperoned to the plasma
membrane by MESD (By similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Widely coexpressed with LRP5 during
embryogenesis and in adult tissues.
-!- INDUCTION: Decreased levels on WNT3A stimulation.
{ECO:0000269|PubMed:17698587}.
-!- DOMAIN: The YWTD-EGF-like domains 1 and 2 are required for the
interaction with Wnt-frizzled complex. The YWTD-EGF-like domains 3
and 4 are required for the interaction with DKK1.
{ECO:0000269|PubMed:20059949}.
-!- DOMAIN: The PPPSP motifs play a central role in signal
transduction by being phosphorylated, leading to activate the Wnt
signaling pathway. {ECO:0000269|PubMed:20059949}.
-!- PTM: Dual phosphorylation of cytoplasmic PPPSP motifs sequentially
by GSK3 and CK1 is required for AXIN1-binding, and subsequent
stabilization and activation of beta-catenin via preventing GSK3-
mediated phosphorylation of beta-catenin. Phosphorylated, in
vitro, by GRK5/6 within and outside the PPPSP motifs.
Phosphorylation at Ser-1490 by CDK14 during G2/M phase leads to
regulation of the Wnt signaling pathway during the cell cycle.
Phosphorylation by GSK3B is induced by RPSO1 binding and inhibited
by DKK1. Phosphorylated, in vitro, by casein kinase I on Thr-1479.
{ECO:0000269|PubMed:16341017, ECO:0000269|PubMed:16513652,
ECO:0000269|PubMed:17400545, ECO:0000269|PubMed:17569865,
ECO:0000269|PubMed:17698587, ECO:0000269|PubMed:18362152,
ECO:0000269|PubMed:19107203, ECO:0000269|PubMed:19293931,
ECO:0000269|PubMed:19801552, ECO:0000269|PubMed:20059949}.
-!- PTM: Undergoes gamma-secretase-dependent regulated intramembrane
proteolysis (RIP). The extracellular domain is first released by
shedding, and then, through the action of gamma-secretase, the
intracellular domain (ICD) is released into the cytoplasm where it
is free to bind to GSK3B and to activate canonical Wnt signaling.
-!- PTM: Palmitoylation on the two sites near the transmembrane domain
leads to release of LRP6 from the endoplasmic reticulum.
{ECO:0000269|PubMed:18378904}.
-!- PTM: Mono-ubiquitinated which retains LRP6 in the endoplasmic
reticulum. Ubiquitinated by ZNRF3, leading to its degradation by
the proteasome. {ECO:0000269|PubMed:18378904,
ECO:0000269|PubMed:22575959}.
-!- PTM: N-glycosylation is required for cell surface location.
{ECO:0000269|PubMed:17698587, ECO:0000269|PubMed:22000856}.
-!- DISEASE: Coronary artery disease, autosomal dominant, 2 (ADCAD2)
[MIM:610947]: A common heart disease characterized by reduced or
absent blood flow in one or more of the arteries that encircle and
supply the heart. Its most important complication is acute
myocardial infarction. {ECO:0000269|PubMed:17332414,
ECO:0000269|PubMed:23703864}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Tooth agenesis, selective, 7 (STHAG7) [MIM:616724]: An
autosomal dominant form of selective tooth agenesis, a common
anomaly characterized by the congenital absence of one or more
teeth. Selective tooth agenesis without associated systemic
disorders has sometimes been divided into 2 types: oligodontia,
defined as agenesis of 6 or more permanent teeth, and hypodontia,
defined as agenesis of less than 6 teeth. The number in both cases
does not include absence of third molars (wisdom teeth).
{ECO:0000269|PubMed:26387593}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF074264; AAC33006.1; -; mRNA.
EMBL; AC007537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC007621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC117136; AAI17137.1; -; mRNA.
EMBL; BC126405; AAI26406.1; -; mRNA.
CCDS; CCDS8647.1; -.
PIR; JE0272; JE0272.
RefSeq; NP_002327.2; NM_002336.2.
RefSeq; XP_006719141.1; XM_006719078.3.
UniGene; Hs.584775; -.
UniGene; Hs.658913; -.
PDB; 3S2K; X-ray; 2.80 A; A/B=630-1246.
PDB; 3S8V; X-ray; 3.10 A; A/B=629-1243.
PDB; 3S8Z; X-ray; 2.80 A; A=629-1243.
PDB; 3S94; X-ray; 2.80 A; A/B=20-630.
PDB; 3SOB; X-ray; 1.90 A; B=20-335.
PDB; 3SOQ; X-ray; 1.90 A; A=20-326.
PDB; 3SOV; X-ray; 1.27 A; A=20-326.
PDB; 4A0P; X-ray; 1.90 A; A=629-1244.
PDB; 4DG6; X-ray; 2.90 A; A=20-635.
PDB; 4NM5; X-ray; 2.30 A; C=1568-1575.
PDB; 4NM7; X-ray; 2.30 A; C=1603-1610.
PDB; 5AIR; X-ray; 2.53 A; A/B=1565-1575.
PDB; 5FWW; X-ray; 3.50 A; A=630-1246.
PDB; 5GJE; EM; 21.00 A; A=20-630, B=631-1246.
PDBsum; 3S2K; -.
PDBsum; 3S8V; -.
PDBsum; 3S8Z; -.
PDBsum; 3S94; -.
PDBsum; 3SOB; -.
PDBsum; 3SOQ; -.
PDBsum; 3SOV; -.
PDBsum; 4A0P; -.
PDBsum; 4DG6; -.
PDBsum; 4NM5; -.
PDBsum; 4NM7; -.
PDBsum; 5AIR; -.
PDBsum; 5FWW; -.
PDBsum; 5GJE; -.
ProteinModelPortal; O75581; -.
SMR; O75581; -.
BioGrid; 110219; 51.
DIP; DIP-29884N; -.
IntAct; O75581; 27.
MINT; MINT-3369849; -.
STRING; 9606.ENSP00000261349; -.
ChEMBL; CHEMBL3745588; -.
iPTMnet; O75581; -.
PhosphoSitePlus; O75581; -.
SwissPalm; O75581; -.
BioMuta; LRP6; -.
EPD; O75581; -.
MaxQB; O75581; -.
PaxDb; O75581; -.
PeptideAtlas; O75581; -.
PRIDE; O75581; -.
Ensembl; ENST00000261349; ENSP00000261349; ENSG00000070018.
Ensembl; ENST00000628182; ENSP00000486315; ENSG00000281324.
GeneID; 4040; -.
KEGG; hsa:4040; -.
UCSC; uc001rah.6; human.
CTD; 4040; -.
DisGeNET; 4040; -.
EuPathDB; HostDB:ENSG00000070018.8; -.
GeneCards; LRP6; -.
H-InvDB; HIX0036693; -.
HGNC; HGNC:6698; LRP6.
HPA; CAB004490; -.
HPA; HPA029925; -.
MalaCards; LRP6; -.
MIM; 603507; gene.
MIM; 610947; phenotype.
MIM; 616724; phenotype.
neXtProt; NX_O75581; -.
OpenTargets; ENSG00000070018; -.
Orphanet; 94062; Coronary artery disease - hyperlipidemia - hypertension - diabetes - osteoporosis.
PharmGKB; PA30456; -.
eggNOG; ENOG410IPT4; Eukaryota.
eggNOG; ENOG410XSY5; LUCA.
GeneTree; ENSGT00760000118968; -.
HOGENOM; HOG000230697; -.
HOVERGEN; HBG049167; -.
InParanoid; O75581; -.
KO; K03068; -.
OMA; WQELDQP; -.
OrthoDB; EOG091G0178; -.
PhylomeDB; O75581; -.
TreeFam; TF315253; -.
Reactome; R-HSA-201681; TCF dependent signaling in response to WNT.
Reactome; R-HSA-3772470; Negative regulation of TCF-dependent signaling by WNT ligand antagonists.
Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
Reactome; R-HSA-4641263; Regulation of FZD by ubiquitination.
Reactome; R-HSA-5340588; RNF mutants show enhanced WNT signaling and proliferation.
SignaLink; O75581; -.
SIGNOR; O75581; -.
ChiTaRS; LRP6; human.
EvolutionaryTrace; O75581; -.
GeneWiki; LRP6; -.
GenomeRNAi; 4040; -.
PRO; PR:O75581; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000070018; -.
CleanEx; HS_LRP6; -.
ExpressionAtlas; O75581; baseline and differential.
Genevisible; O75581; HS.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0043235; C:receptor complex; IBA:GO_Central.
GO; GO:0045202; C:synapse; IBA:GO_Central.
GO; GO:1990909; C:Wnt signalosome; IDA:ParkinsonsUK-UCL.
GO; GO:1990851; C:Wnt-Frizzled-LRP5/6 complex; IDA:ParkinsonsUK-UCL.
GO; GO:0034185; F:apolipoprotein binding; IBA:GO_Central.
GO; GO:1904928; F:coreceptor activity involved in canonical Wnt signaling pathway; NAS:ParkinsonsUK-UCL.
GO; GO:0071936; F:coreceptor activity involved in Wnt signaling pathway; IDA:BHF-UCL.
GO; GO:0005109; F:frizzled binding; IPI:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0019210; F:kinase inhibitor activity; IMP:BHF-UCL.
GO; GO:0005041; F:low-density lipoprotein receptor activity; IDA:MGI.
GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
GO; GO:0005102; F:receptor binding; IPI:BHF-UCL.
GO; GO:0019534; F:toxin transporter activity; IMP:BHF-UCL.
GO; GO:0042813; F:Wnt-activated receptor activity; IBA:GO_Central.
GO; GO:0017147; F:Wnt-protein binding; IPI:BHF-UCL.
GO; GO:0090245; P:axis elongation involved in somitogenesis; IBA:GO_Central.
GO; GO:1904886; P:beta-catenin destruction complex disassembly; TAS:Reactome.
GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:UniProtKB.
GO; GO:0044335; P:canonical Wnt signaling pathway involved in neural crest cell differentiation; IC:BHF-UCL.
GO; GO:0044340; P:canonical Wnt signaling pathway involved in regulation of cell proliferation; IC:BHF-UCL.
GO; GO:0071397; P:cellular response to cholesterol; IMP:BHF-UCL.
GO; GO:0021587; P:cerebellum morphogenesis; IBA:GO_Central.
GO; GO:0021987; P:cerebral cortex development; IBA:GO_Central.
GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
GO; GO:0060026; P:convergent extension; IBA:GO_Central.
GO; GO:0071542; P:dopaminergic neuron differentiation; ISS:ParkinsonsUK-UCL.
GO; GO:0009880; P:embryonic pattern specification; IBA:GO_Central.
GO; GO:0060059; P:embryonic retina morphogenesis in camera-type eye; IBA:GO_Central.
GO; GO:0035261; P:external genitalia morphogenesis; IBA:GO_Central.
GO; GO:0060325; P:face morphogenesis; IBA:GO_Central.
GO; GO:1904948; P:midbrain dopaminergic neuron differentiation; TAS:ParkinsonsUK-UCL.
GO; GO:0030917; P:midbrain-hindbrain boundary development; IBA:GO_Central.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:BHF-UCL.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:BHF-UCL.
GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; IDA:BHF-UCL.
GO; GO:0034392; P:negative regulation of smooth muscle cell apoptotic process; IMP:BHF-UCL.
GO; GO:0014033; P:neural crest cell differentiation; IDA:BHF-UCL.
GO; GO:0014029; P:neural crest formation; IDA:BHF-UCL.
GO; GO:0001843; P:neural tube closure; IBA:GO_Central.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IBA:GO_Central.
GO; GO:0060021; P:palate development; IBA:GO_Central.
GO; GO:0003344; P:pericardium morphogenesis; IBA:GO_Central.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IDA:BHF-UCL.
GO; GO:0045787; P:positive regulation of cell cycle; IMP:BHF-UCL.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:BHF-UCL.
GO; GO:2000055; P:positive regulation of Wnt signaling pathway involved in dorsal/ventral axis specification; IDA:BHF-UCL.
GO; GO:0090009; P:primitive streak formation; IBA:GO_Central.
GO; GO:0072659; P:protein localization to plasma membrane; IPI:ParkinsonsUK-UCL.
GO; GO:0090118; P:receptor-mediated endocytosis involved in cholesterol transport; IBA:GO_Central.
GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IGI:ARUK-UCL.
GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
GO; GO:0016337; P:single organismal cell-cell adhesion; IEA:Ensembl.
GO; GO:0021794; P:thalamus development; IBA:GO_Central.
GO; GO:0060535; P:trachea cartilage morphogenesis; IBA:GO_Central.
GO; GO:0016055; P:Wnt signaling pathway; IDA:ParkinsonsUK-UCL.
GO; GO:0044332; P:Wnt signaling pathway involved in dorsal/ventral axis specification; IDA:BHF-UCL.
GO; GO:1904953; P:Wnt signaling pathway involved in midbrain dopaminergic neuron differentiation; TAS:ParkinsonsUK-UCL.
GO; GO:0090244; P:Wnt signaling pathway involved in somitogenesis; IBA:GO_Central.
Gene3D; 2.120.10.30; -; 4.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR023415; LDLR_class-A_CS.
InterPro; IPR000033; LDLR_classB_rpt.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
InterPro; IPR017049; LRP5/6.
Pfam; PF00057; Ldl_recept_a; 3.
Pfam; PF00058; Ldl_recept_b; 11.
PIRSF; PIRSF036314; LDL_recpt-rel_p5/6; 1.
PRINTS; PR00261; LDLRECEPTOR.
SMART; SM00181; EGF; 4.
SMART; SM00192; LDLa; 3.
SMART; SM00135; LY; 20.
SUPFAM; SSF57424; SSF57424; 3.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS01209; LDLRA_1; 3.
PROSITE; PS50068; LDLRA_2; 3.
PROSITE; PS51120; LDLRB; 19.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Developmental protein;
Disease mutation; Disulfide bond; EGF-like domain; Endocytosis;
Endoplasmic reticulum; Glycoprotein; Isopeptide bond; Lipoprotein;
Membrane; Palmitate; Phosphoprotein; Polymorphism; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix; Ubl conjugation; Wnt signaling pathway.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 1613 Low-density lipoprotein receptor-related
protein 6.
/FTId=PRO_0000017330.
TOPO_DOM 20 1370 Extracellular. {ECO:0000255}.
TRANSMEM 1371 1393 Helical. {ECO:0000255}.
TOPO_DOM 1394 1613 Cytoplasmic. {ECO:0000255}.
REPEAT 63 106 LDL-receptor class B 1.
REPEAT 107 149 LDL-receptor class B 2.
REPEAT 150 193 LDL-receptor class B 3.
REPEAT 194 236 LDL-receptor class B 4.
REPEAT 237 276 LDL-receptor class B 5.
DOMAIN 282 324 EGF-like 1.
REPEAT 372 414 LDL-receptor class B 6.
REPEAT 415 457 LDL-receptor class B 7.
REPEAT 458 501 LDL-receptor class B 8.
REPEAT 502 542 LDL-receptor class B 9.
REPEAT 543 584 LDL-receptor class B 10.
DOMAIN 588 628 EGF-like 2.
REPEAT 674 716 LDL-receptor class B 11.
REPEAT 717 759 LDL-receptor class B 12.
REPEAT 760 802 LDL-receptor class B 13.
REPEAT 803 842 LDL-receptor class B 14.
REPEAT 843 885 LDL-receptor class B 15.
DOMAIN 889 930 EGF-like 3.
REPEAT 977 1025 LDL-receptor class B 16.
REPEAT 1026 1068 LDL-receptor class B 17.
REPEAT 1069 1113 LDL-receptor class B 18.
REPEAT 1114 1156 LDL-receptor class B 19.
REPEAT 1157 1198 LDL-receptor class B 20.
DOMAIN 1203 1244 EGF-like 4.
DOMAIN 1248 1286 LDL-receptor class A 1.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1287 1323 LDL-receptor class A 2.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1325 1361 LDL-receptor class A 3.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
REGION 20 275 Beta-propeller 1.
REGION 328 589 Beta-propeller 2.
REGION 631 890 Beta-propeller 3.
REGION 933 1202 Beta-propeller 4.
MOTIF 1487 1493 PPPSP motif A.
MOTIF 1527 1534 PPPSP motif B.
MOTIF 1568 1575 PPPSP motif C.
MOTIF 1588 1593 PPPSP motif D.
MOTIF 1603 1610 PPPSP motif E.
MOD_RES 1420 1420 Phosphoserine; by CK1.
{ECO:0000269|PubMed:16513652}.
MOD_RES 1430 1430 Phosphoserine; by CK1.
{ECO:0000269|PubMed:16513652}.
MOD_RES 1479 1479 Phosphothreonine.
{ECO:0000269|PubMed:17569865}.
MOD_RES 1490 1490 Phosphoserine; by CDK14, GRK5 and GRK6.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:16341017,
ECO:0000269|PubMed:17698587,
ECO:0000269|PubMed:18762581,
ECO:0000269|PubMed:19801552,
ECO:0000269|PubMed:20059949,
ECO:0000269|PubMed:25331957,
ECO:0000269|PubMed:27821587}.
MOD_RES 1493 1493 Phosphothreonine; by CK1.
{ECO:0000269|PubMed:16341017}.
LIPID 1394 1394 S-palmitoyl cysteine.
{ECO:0000269|PubMed:18378904}.
LIPID 1399 1399 S-palmitoyl cysteine.
{ECO:0000269|PubMed:18378904}.
CARBOHYD 42 42 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 81 81 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 281 281 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 433 433 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 486 486 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 692 692 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22000856}.
CARBOHYD 859 859 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22000856}.
CARBOHYD 865 865 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22000856}.
CARBOHYD 926 926 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22000856}.
CARBOHYD 1039 1039 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22000856}.
DISULFID 286 297 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 293 308 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 310 323 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 592 603 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 599 612 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 614 627 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 893 904 {ECO:0000255|PROSITE-ProRule:PRU00124,
ECO:0000269|PubMed:22000856}.
DISULFID 900 914 {ECO:0000255|PROSITE-ProRule:PRU00124,
ECO:0000269|PubMed:22000856}.
DISULFID 916 929 {ECO:0000255|PROSITE-ProRule:PRU00124,
ECO:0000269|PubMed:22000856}.
DISULFID 1207 1218 {ECO:0000255|PROSITE-ProRule:PRU00124,
ECO:0000269|PubMed:22000856}.
DISULFID 1214 1228 {ECO:0000255|PROSITE-ProRule:PRU00124,
ECO:0000269|PubMed:22000856}.
DISULFID 1230 1243 {ECO:0000255|PROSITE-ProRule:PRU00124,
ECO:0000269|PubMed:22000856}.
DISULFID 1249 1263 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1256 1276 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1270 1285 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1288 1300 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1295 1313 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1307 1322 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1326 1338 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1333 1351 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1345 1360 {ECO:0000255|PROSITE-ProRule:PRU00124}.
CROSSLNK 1403 1403 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:18378904}.
VARIANT 19 19 A -> V (in STHAG7; impairs Wnt signaling;
prevents transport to plasma membrane
location; dbSNP:rs864309648).
{ECO:0000269|PubMed:26387593}.
/FTId=VAR_076207.
VARIANT 360 360 R -> H (in ADCAD2; dbSNP:rs141212743).
{ECO:0000269|PubMed:23703864}.
/FTId=VAR_076208.
VARIANT 433 433 N -> S (in ADCAD2; dbSNP:rs397515473).
{ECO:0000269|PubMed:23703864}.
/FTId=VAR_076209.
VARIANT 473 473 R -> Q (in ADCAD2; impairs Wnt signaling;
dbSNP:rs397515474).
{ECO:0000269|PubMed:23703864}.
/FTId=VAR_076210.
VARIANT 483 483 V -> I (in dbSNP:rs7975614).
/FTId=VAR_030349.
VARIANT 611 611 R -> C (in ADCAD2; impairs Wnt signaling
in vitro; dbSNP:rs121918313).
{ECO:0000269|PubMed:17332414}.
/FTId=VAR_034701.
VARIANT 817 817 S -> C (in dbSNP:rs2302686).
/FTId=VAR_030350.
VARIANT 1062 1062 V -> I (in dbSNP:rs2302685).
{ECO:0000269|PubMed:9704021}.
/FTId=VAR_024520.
VARIANT 1401 1401 R -> H (in dbSNP:rs34815107).
/FTId=VAR_034702.
MUTAGEN 1394 1394 C->A: Some reduction of palmitoylation,
little change in plasma membrane location
in the presence of MESD nor in Wnt-
signaling activity. Completely abolishes
palmitoylation, no plasma membrane
location, greatly reduced Wnt-signaling
activity but no effect on ubiquitination;
when associated with A-1399. Exhibits
full Wnt-signaling activity and no change
in plasma membrane location; when
associated with A-1399 and R-1403.
{ECO:0000269|PubMed:18378904}.
MUTAGEN 1399 1399 C->A: Some reduction of palmitoylation,
and little change in plasma membrane
location in the presence of MESD nor in
Wnt-signaling activity. Completely
abolishes palmitoylation, no plasma
membrane location, greatly reduced Wnt-
signaling activity but no effect on
ubiquitination; when associated with A-
1394. Exhibits full Wnt-signaling
activity and no change in plasma membrane
location in the in presence of MESD; when
associated with A-1394 and R-1403.
{ECO:0000269|PubMed:18378904}.
MUTAGEN 1403 1403 K->R: Abolishes ubiquitination, no change
in plasma membrane location in the
presence of MESD but greatly reduced Wnt-
signaling activity. Exhibits full Wnt-
signaling activity and no change in
plasma membrane location; when associated
with A-1394 and A-1399.
MUTAGEN 1420 1420 S->A: Enhanced AXIN1 binding and
increased beta-catenin activity by 2.2-
fold. Further enhanced AXIN1 binding and
increases beta-catenin activity by 3.3-
fold; when associated with A-1430.
{ECO:0000269|PubMed:16513652}.
MUTAGEN 1430 1430 S->A: Enhanced AXIN1 binding. Further
enhanced AXIN1 binding and increases
beta-catenin activity by 3.3-fold; when
associated with A-1420.
{ECO:0000269|PubMed:16513652}.
MUTAGEN 1485 1485 L->A: No change in the phosphorylation
state of PPPSP motif. Some reduction in
Wnt/beta-catenin signaling.
{ECO:0000269|PubMed:18362152}.
MUTAGEN 1486 1486 N->A: No change in the phosphorylation
state of PPPSP motif. Increased Wnt/beta-
catenin signaling.
{ECO:0000269|PubMed:18362152}.
MUTAGEN 1487 1487 P->A: No change in the phosphorylation
state of PPPSP motif A. Greatly reduced
Wnt/beta-catenin signaling.
{ECO:0000269|PubMed:18362152}.
MUTAGEN 1487 1487 P->C: No change in the phosphorylation
state of PPPSP motif A. Greatly reduced
Wnt/beta-catenin signaling.
{ECO:0000269|PubMed:18362152}.
MUTAGEN 1488 1488 P->A: No change in the phosphorylation
state of PPPSP motif A. Greatly reduced
Wnt/beta-catenin signaling.
{ECO:0000269|PubMed:18362152}.
MUTAGEN 1489 1489 P->A: No change in the phosphorylation
state of PPPSP motif A. Greatly reduced
Wnt/beta-catenin signaling.
{ECO:0000269|PubMed:18362152}.
MUTAGEN 1490 1490 S->A: Greatly reduced phosphorylation of
PPPSP motif A. Greatly reduced Wnt/beta-
catenin signaling.
{ECO:0000269|PubMed:18362152}.
MUTAGEN 1490 1490 S->T: Some loss of phosphorylation of
PPPSP motif A. Little reduction in
Wnt/beta-catenin signaling.
{ECO:0000269|PubMed:18362152}.
MUTAGEN 1491 1491 P->A: Greatly reduced phosphorylation of
PPPSP motif A. Greatly reduced Wnt/beta-
catenin signaling.
{ECO:0000269|PubMed:18362152}.
MUTAGEN 1492 1492 A->G: No change in the phosphorylation
state of PPPSP motif A. Greatly reduced
Wnt/beta-catenin signaling.
{ECO:0000269|PubMed:18362152}.
MUTAGEN 1493 1493 T->A: No change in the phosphorylation
state of PPPSP motif A. Greatly reduced
Wnt/beta-catenin signaling.
{ECO:0000269|PubMed:18362152}.
MUTAGEN 1494 1494 E->A: No change in the phosphorylation
state of PPPSP motif A. Little reduction
of Wnt/beta-catenin signaling.
{ECO:0000269|PubMed:18362152}.
MUTAGEN 1495 1495 R->A: No change in the phosphorylation
state of PPPSP motif. No reduction of
Wnt/beta-catenin signaling.
{ECO:0000269|PubMed:18362152}.
MUTAGEN 1529 1529 T->A: No effect on the phosphorylation
state of PPPSP motif B.
{ECO:0000269|PubMed:18362152}.
MUTAGEN 1530 1530 T->A: Abolishes phosphorylation of PPPSP
motif B. Reduced Wnt/beta-catenin
signaling. {ECO:0000269|PubMed:18362152}.
MUTAGEN 1531 1531 P->A: Abolishes phosphorylation of PPPSP
motif B. Reduced Wnt/beta-catenin
signaling. {ECO:0000269|PubMed:18362152}.
MUTAGEN 1572 1572 T->A: Abolishes Wnt/beta-catenin
signaling. {ECO:0000269|PubMed:18362152}.
MUTAGEN 1590 1590 S->A: Abolishes Wnt/beta-catenin
signaling. {ECO:0000269|PubMed:18362152}.
MUTAGEN 1607 1607 S->A: Abolishes Wnt/beta-catenin
signaling. {ECO:0000269|PubMed:18362152}.
STRAND 22 26 {ECO:0000244|PDB:3SOV}.
STRAND 28 35 {ECO:0000244|PDB:3SOV}.
HELIX 36 38 {ECO:0000244|PDB:3SOB}.
STRAND 44 59 {ECO:0000244|PDB:3SOV}.
HELIX 60 62 {ECO:0000244|PDB:3SOV}.
STRAND 64 69 {ECO:0000244|PDB:3SOV}.
TURN 70 73 {ECO:0000244|PDB:3SOV}.
STRAND 74 79 {ECO:0000244|PDB:3SOV}.
STRAND 82 84 {ECO:0000244|PDB:3SOV}.
STRAND 88 92 {ECO:0000244|PDB:3SOV}.
STRAND 99 103 {ECO:0000244|PDB:3SOV}.
TURN 104 107 {ECO:0000244|PDB:3SOV}.
STRAND 108 113 {ECO:0000244|PDB:3SOV}.
TURN 114 117 {ECO:0000244|PDB:3SOV}.
STRAND 118 123 {ECO:0000244|PDB:3SOV}.
STRAND 130 133 {ECO:0000244|PDB:3SOV}.
STRAND 138 146 {ECO:0000244|PDB:3SOV}.
HELIX 147 149 {ECO:0000244|PDB:3SOV}.
STRAND 151 156 {ECO:0000244|PDB:3SOV}.
STRAND 158 160 {ECO:0000244|PDB:3SOV}.
STRAND 162 167 {ECO:0000244|PDB:3SOV}.
STRAND 174 177 {ECO:0000244|PDB:3SOV}.
STRAND 184 190 {ECO:0000244|PDB:3SOV}.
TURN 191 194 {ECO:0000244|PDB:3SOV}.
STRAND 195 200 {ECO:0000244|PDB:3SOV}.
TURN 201 204 {ECO:0000244|PDB:3SOV}.
STRAND 205 210 {ECO:0000244|PDB:3SOV}.
STRAND 217 220 {ECO:0000244|PDB:3SOV}.
STRAND 227 233 {ECO:0000244|PDB:3SOV}.
STRAND 236 241 {ECO:0000244|PDB:3SOV}.
TURN 242 245 {ECO:0000244|PDB:3SOV}.
STRAND 246 251 {ECO:0000244|PDB:3SOV}.
TURN 252 254 {ECO:0000244|PDB:3SOV}.
STRAND 259 262 {ECO:0000244|PDB:3SOV}.
STRAND 271 274 {ECO:0000244|PDB:3SOV}.
HELIX 276 278 {ECO:0000244|PDB:3SOV}.
TURN 285 289 {ECO:0000244|PDB:3SOV}.
HELIX 290 292 {ECO:0000244|PDB:3SOV}.
STRAND 294 299 {ECO:0000244|PDB:3SOV}.
STRAND 305 309 {ECO:0000244|PDB:3SOV}.
STRAND 328 337 {ECO:0000244|PDB:3S94}.
STRAND 339 346 {ECO:0000244|PDB:3S94}.
STRAND 360 368 {ECO:0000244|PDB:3S94}.
TURN 369 372 {ECO:0000244|PDB:3S94}.
STRAND 373 378 {ECO:0000244|PDB:3S94}.
TURN 379 382 {ECO:0000244|PDB:3S94}.
STRAND 383 388 {ECO:0000244|PDB:3S94}.
STRAND 389 391 {ECO:0000244|PDB:4DG6}.
STRAND 395 398 {ECO:0000244|PDB:3S94}.
STRAND 407 411 {ECO:0000244|PDB:3S94}.
TURN 412 415 {ECO:0000244|PDB:3S94}.
STRAND 416 421 {ECO:0000244|PDB:3S94}.
TURN 422 425 {ECO:0000244|PDB:3S94}.
STRAND 426 431 {ECO:0000244|PDB:3S94}.
STRAND 438 441 {ECO:0000244|PDB:3S94}.
STRAND 447 454 {ECO:0000244|PDB:3S94}.
TURN 455 458 {ECO:0000244|PDB:3S94}.
STRAND 459 464 {ECO:0000244|PDB:3S94}.
STRAND 466 468 {ECO:0000244|PDB:3S94}.
STRAND 470 475 {ECO:0000244|PDB:3S94}.
STRAND 482 485 {ECO:0000244|PDB:3S94}.
STRAND 492 498 {ECO:0000244|PDB:3S94}.
TURN 499 502 {ECO:0000244|PDB:3S94}.
STRAND 503 508 {ECO:0000244|PDB:3S94}.
TURN 509 512 {ECO:0000244|PDB:3S94}.
STRAND 513 521 {ECO:0000244|PDB:3S94}.
STRAND 525 529 {ECO:0000244|PDB:3S94}.
STRAND 538 541 {ECO:0000244|PDB:3S94}.
STRAND 544 548 {ECO:0000244|PDB:3S94}.
STRAND 555 562 {ECO:0000244|PDB:3S94}.
STRAND 565 569 {ECO:0000244|PDB:3S94}.
STRAND 575 584 {ECO:0000244|PDB:3S94}.
HELIX 591 593 {ECO:0000244|PDB:3S94}.
HELIX 595 598 {ECO:0000244|PDB:3S94}.
STRAND 600 606 {ECO:0000244|PDB:3S94}.
STRAND 609 613 {ECO:0000244|PDB:3S94}.
STRAND 633 638 {ECO:0000244|PDB:4A0P}.
STRAND 641 648 {ECO:0000244|PDB:4A0P}.
STRAND 653 655 {ECO:0000244|PDB:4A0P}.
STRAND 664 670 {ECO:0000244|PDB:4A0P}.
TURN 671 674 {ECO:0000244|PDB:4A0P}.
STRAND 675 680 {ECO:0000244|PDB:4A0P}.
TURN 681 684 {ECO:0000244|PDB:4A0P}.
STRAND 685 690 {ECO:0000244|PDB:4A0P}.
STRAND 697 700 {ECO:0000244|PDB:4A0P}.
STRAND 709 713 {ECO:0000244|PDB:4A0P}.
TURN 714 717 {ECO:0000244|PDB:4A0P}.
STRAND 718 723 {ECO:0000244|PDB:4A0P}.
TURN 724 727 {ECO:0000244|PDB:4A0P}.
STRAND 728 733 {ECO:0000244|PDB:4A0P}.
STRAND 740 743 {ECO:0000244|PDB:4A0P}.
STRAND 750 756 {ECO:0000244|PDB:4A0P}.
TURN 757 760 {ECO:0000244|PDB:4A0P}.
STRAND 761 766 {ECO:0000244|PDB:4A0P}.
STRAND 768 770 {ECO:0000244|PDB:4A0P}.
STRAND 772 777 {ECO:0000244|PDB:4A0P}.
STRAND 784 787 {ECO:0000244|PDB:4A0P}.
STRAND 791 799 {ECO:0000244|PDB:4A0P}.
TURN 800 803 {ECO:0000244|PDB:4A0P}.
STRAND 804 809 {ECO:0000244|PDB:4A0P}.
TURN 810 813 {ECO:0000244|PDB:4A0P}.
STRAND 814 819 {ECO:0000244|PDB:4A0P}.
STRAND 826 830 {ECO:0000244|PDB:4A0P}.
STRAND 835 841 {ECO:0000244|PDB:4A0P}.
STRAND 844 849 {ECO:0000244|PDB:4A0P}.
TURN 850 853 {ECO:0000244|PDB:4A0P}.
STRAND 854 859 {ECO:0000244|PDB:4A0P}.
TURN 860 862 {ECO:0000244|PDB:4A0P}.
STRAND 867 870 {ECO:0000244|PDB:4A0P}.
STRAND 878 882 {ECO:0000244|PDB:4A0P}.
HELIX 884 886 {ECO:0000244|PDB:4A0P}.
TURN 892 896 {ECO:0000244|PDB:4A0P}.
HELIX 897 899 {ECO:0000244|PDB:4A0P}.
STRAND 901 907 {ECO:0000244|PDB:4A0P}.
TURN 908 910 {ECO:0000244|PDB:4A0P}.
STRAND 911 915 {ECO:0000244|PDB:4A0P}.
STRAND 933 940 {ECO:0000244|PDB:4A0P}.
STRAND 943 947 {ECO:0000244|PDB:4A0P}.
STRAND 967 973 {ECO:0000244|PDB:4A0P}.
TURN 974 977 {ECO:0000244|PDB:4A0P}.
STRAND 978 983 {ECO:0000244|PDB:4A0P}.
TURN 984 987 {ECO:0000244|PDB:4A0P}.
STRAND 988 993 {ECO:0000244|PDB:4A0P}.
STRAND 1000 1003 {ECO:0000244|PDB:4A0P}.
STRAND 1016 1022 {ECO:0000244|PDB:4A0P}.
TURN 1023 1026 {ECO:0000244|PDB:4A0P}.
STRAND 1027 1032 {ECO:0000244|PDB:4A0P}.
TURN 1033 1036 {ECO:0000244|PDB:4A0P}.
STRAND 1037 1042 {ECO:0000244|PDB:4A0P}.
STRAND 1047 1052 {ECO:0000244|PDB:4A0P}.
STRAND 1059 1065 {ECO:0000244|PDB:4A0P}.
TURN 1066 1069 {ECO:0000244|PDB:4A0P}.
STRAND 1070 1077 {ECO:0000244|PDB:4A0P}.
STRAND 1080 1087 {ECO:0000244|PDB:4A0P}.
STRAND 1094 1097 {ECO:0000244|PDB:4A0P}.
STRAND 1104 1110 {ECO:0000244|PDB:4A0P}.
TURN 1111 1114 {ECO:0000244|PDB:4A0P}.
STRAND 1115 1120 {ECO:0000244|PDB:4A0P}.
TURN 1121 1124 {ECO:0000244|PDB:4A0P}.
STRAND 1125 1130 {ECO:0000244|PDB:4A0P}.
STRAND 1137 1140 {ECO:0000244|PDB:4A0P}.
STRAND 1147 1153 {ECO:0000244|PDB:4A0P}.
STRAND 1156 1161 {ECO:0000244|PDB:4A0P}.
TURN 1162 1165 {ECO:0000244|PDB:4A0P}.
STRAND 1166 1171 {ECO:0000244|PDB:4A0P}.
STRAND 1174 1176 {ECO:0000244|PDB:4A0P}.
STRAND 1179 1182 {ECO:0000244|PDB:4A0P}.
STRAND 1188 1194 {ECO:0000244|PDB:4A0P}.
HELIX 1199 1204 {ECO:0000244|PDB:4A0P}.
TURN 1206 1209 {ECO:0000244|PDB:4A0P}.
HELIX 1210 1213 {ECO:0000244|PDB:4A0P}.
STRAND 1215 1220 {ECO:0000244|PDB:4A0P}.
TURN 1222 1224 {ECO:0000244|PDB:3S8Z}.
STRAND 1226 1229 {ECO:0000244|PDB:4A0P}.
STRAND 1234 1236 {ECO:0000244|PDB:4A0P}.
STRAND 1238 1241 {ECO:0000244|PDB:3S8Z}.
SEQUENCE 1613 AA; 180429 MW; 413D2CF70A5D8B5C CRC64;
MGAVLRSLLA CSFCVLLRAA PLLLYANRRD LRLVDATNGK ENATIVVGGL EDAAAVDFVF
SHGLIYWSDV SEEAIKRTEF NKTESVQNVV VSGLLSPDGL ACDWLGEKLY WTDSETNRIE
VSNLDGSLRK VLFWQELDQP RAIALDPSSG FMYWTDWGEV PKIERAGMDG SSRFIIINSE
IYWPNGLTLD YEEQKLYWAD AKLNFIHKSN LDGTNRQAVV KGSLPHPFAL TLFEDILYWT
DWSTHSILAC NKYTGEGLRE IHSDIFSPMD IHAFSQQRQP NATNPCGIDN GGCSHLCLMS
PVKPFYQCAC PTGVKLLENG KTCKDGATEL LLLARRTDLR RISLDTPDFT DIVLQLEDIR
HAIAIDYDPV EGYIYWTDDE VRAIRRSFID GSGSQFVVTA QIAHPDGIAV DWVARNLYWT
DTGTDRIEVT RLNGTMRKIL ISEDLEEPRA IVLDPMVGYM YWTDWGEIPK IERAALDGSD
RVVLVNTSLG WPNGLALDYD EGKIYWGDAK TDKIEVMNTD GTGRRVLVED KIPHIFGFTL
LGDYVYWTDW QRRSIERVHK RSAEREVIID QLPDLMGLKA TNVHRVIGSN PCAEENGGCS
HLCLYRPQGL RCACPIGFEL ISDMKTCIVP EAFLLFSRRA DIRRISLETN NNNVAIPLTG
VKEASALDFD VTDNRIYWTD ISLKTISRAF MNGSALEHVV EFGLDYPEGM AVDWLGKNLY
WADTGTNRIE VSKLDGQHRQ VLVWKDLDSP RALALDPAEG FMYWTEWGGK PKIDRAAMDG
SERTTLVPNV GRANGLTIDY AKRRLYWTDL DTNLIESSNM LGLNREVIAD DLPHPFGLTQ
YQDYIYWTDW SRRSIERANK TSGQNRTIIQ GHLDYVMDIL VFHSSRQSGW NECASSNGHC
SHLCLAVPVG GFVCGCPAHY SLNADNRTCS APTTFLLFSQ KSAINRMVID EQQSPDIILP
IHSLRNVRAI DYDPLDKQLY WIDSRQNMIR KAQEDGSQGF TVVVSSVPSQ NLEIQPYDLS
IDIYSRYIYW TCEATNVINV TRLDGRSVGV VLKGEQDRPR AVVVNPEKGY MYFTNLQERS
PKIERAALDG TEREVLFFSG LSKPIALALD SRLGKLFWAD SDLRRIESSD LSGANRIVLE
DSNILQPVGL TVFENWLYWI DKQQQMIEKI DMTGREGRTK VQARIAQLSD IHAVKELNLQ
EYRQHPCAQD NGGCSHICLV KGDGTTRCSC PMHLVLLQDE LSCGEPPTCS PQQFTCFTGE
IDCIPVAWRC DGFTECEDHS DELNCPVCSE SQFQCASGQC IDGALRCNGD ANCQDKSDEK
NCEVLCLIDQ FRCANGQCIG KHKKCDHNVD CSDKSDELDC YPTEEPAPQA TNTVGSVIGV
IVTIFVSGTV YFICQRMLCP RMKGDGETMT NDYVVHGPAS VPLGYVPHPS SLSGSLPGMS
RGKSMISSLS IMGGSSGPPY DRAHVTGASS SSSSSTKGTY FPAILNPPPS PATERSHYTM
EFGYSSNSPS THRSYSYRPY SYRHFAPPTT PCSTDVCDSD YAPSRRMTSV ATAKGYTSDL
NYDSEPVPPP PTPRSQYLSA EENYESCPPS PYTERSYSHH LYPPPPSPCT DSS


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