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Protein Wnt-11b (Protein Wnt-11) (XWnt-11)

 WN11B_XENLA             Reviewed;         353 AA.
P49893; Q5U5D9;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
02-MAR-2010, sequence version 2.
25-OCT-2017, entry version 86.
RecName: Full=Protein Wnt-11b;
AltName: Full=Protein Wnt-11;
Short=XWnt-11;
Flags: Precursor;
Name=wnt11b; Synonyms=wnt-11, wnt11;
Xenopus laevis (African clawed frog).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
Xenopus.
NCBI_TaxID=8355;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
TISSUE=Oocyte;
PubMed=8306880;
Ku M., Melton D.A.;
"Xwnt-11: a maternally expressed Xenopus wnt gene.";
Development 119:1161-1173(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Gastrula;
NIH - Xenopus Gene Collection (XGC) project;
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[3]
TISSUE SPECIFICITY.
PubMed=7539356;
Kloc M., Etkin L.D.;
"Two distinct pathways for the localization of RNAs at the vegetal
cortex in Xenopus oocytes.";
Development 121:287-297(1995).
[4]
FUNCTION.
PubMed=7739543; DOI=10.1128/MCB.15.5.2625;
Du S.J., Purcell S.M., Christian J.L., McGrew L.L., Moon R.T.;
"Identification of distinct classes and functional domains of Wnts
through expression of wild-type and chimeric proteins in Xenopus
embryos.";
Mol. Cell. Biol. 15:2625-2634(1995).
[5]
FUNCTION.
PubMed=8655584; DOI=10.1083/jcb.133.5.1123;
Torres M.A., Yang-Snyder J.A., Purcell S.M., DeMarais A.A.,
McGrew L.L., Moon R.T.;
"Activities of the Wnt-1 class of secreted signaling factors are
antagonized by the Wnt-5A class and by a dominant negative cadherin in
early Xenopus development.";
J. Cell Biol. 133:1123-1137(1996).
[6]
TISSUE SPECIFICITY.
PubMed=10525335; DOI=10.1006/dbio.1999.9426;
Schroeder K.E., Condic M.L., Eisenberg L.M., Yost H.J.;
"Spatially regulated translation in embryos: asymmetric expression of
maternal Wnt-11 along the dorsal-ventral axis in Xenopus.";
Dev. Biol. 214:288-297(1999).
[7]
FUNCTION.
PubMed=10751186;
Sumanas S., Strege P., Heasman J., Ekker S.C.;
"The putative Wnt receptor Xenopus frizzled-7 functions upstream of
beta-catenin in vertebrate dorso-ventral mesoderm patterning.";
Development 127:1981-1990(2000).
[8]
FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=10769246;
Tada M., Smith J.C.;
"Xwnt11 is a target of Xenopus Brachyury: regulation of gastrulation
movements via Dishevelled, but not through the canonical Wnt
pathway.";
Development 127:2227-2238(2000).
[9]
FUNCTION, INTERACTION WITH FZD7, AND SUBCELLULAR LOCATION.
PubMed=10862746;
Djiane A., Riou J.-F., Umbhauer M., Boucaut J.-C., Shi D.-L.;
"Role of frizzled 7 in the regulation of convergent extension
movements during gastrulation in Xenopus laevis.";
Development 127:3091-3100(2000).
[10]
TISSUE SPECIFICITY.
PubMed=10585568; DOI=10.1016/S0925-4773(99)00228-2;
Pannese M., Cagliani R., Pardini C.L., Boncinelli E.;
"Xotx1 maternal transcripts are vegetally localized in Xenopus laevis
oocytes.";
Mech. Dev. 90:111-114(2000).
[11]
INDUCTION.
PubMed=10781937; DOI=10.1016/S0925-4773(00)00260-4;
Saka Y., Tada M., Smith J.C.;
"A screen for targets of the Xenopus T-box gene Xbra.";
Mech. Dev. 93:27-39(2000).
[12]
FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=11128985; DOI=10.1098/rstb.2000.0627;
Smith J.C., Conlon F.L., Saka Y., Tada M.;
"Xwnt11 and the regulation of gastrulation in Xenopus.";
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 355:923-930(2000).
[13]
TISSUE SPECIFICITY.
PubMed=11784070; DOI=10.1006/dbio.2001.0495;
Heasman J., Wessely O., Langland R., Craig E.J., Kessler D.S.;
"Vegetal localization of maternal mRNAs is disrupted by VegT
depletion.";
Dev. Biol. 240:377-386(2001).
[14]
LACK OF FUNCTION IN HEART INDUCTION.
PubMed=11159911; DOI=10.1101/gad.855601;
Schneider V.A., Mercola M.;
"Wnt antagonism initiates cardiogenesis in Xenopus laevis.";
Genes Dev. 15:304-315(2001).
[15]
FUNCTION.
PubMed=12167861; DOI=10.1038/nature00921;
Pandur P., Lasche M., Eisenberg L.M., Kuhl M.;
"Wnt-11 activation of a non-canonical Wnt signalling pathway is
required for cardiogenesis.";
Nature 418:636-641(2002).
[16]
TISSUE SPECIFICITY.
PubMed=12946266; DOI=10.1023/A:1025099320362;
Shatilov D.V., Pshennikova E.S., Voronina A.S.;
"Transition of Xwnt-11 mRNA from inactive form to polyribosomes in
frogs during early embryogenesis.";
Biochemistry (Mosc.) 68:822-825(2003).
[17]
FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=15543138; DOI=10.1038/ncb1191;
Kim S.-W., Park J.-I., Spring C.M., Sater A.K., Ji H., Otchere A.A.,
Daniel J.M., McCrea P.D.;
"Non-canonical Wnt signals are modulated by the Kaiso transcriptional
repressor and p120-catenin.";
Nat. Cell Biol. 6:1212-1220(2004).
[18]
FUNCTION, INTERACTION WITH TDGF1, AND TISSUE SPECIFICITY.
PubMed=15797385; DOI=10.1016/j.cell.2005.01.013;
Tao Q., Yokota C., Puck H., Kofron M., Birsoy B., Yan D., Asashima M.,
Wylie C.C., Lin X., Heasman J.;
"Maternal wnt11 activates the canonical wnt signaling pathway required
for axis formation in Xenopus embryos.";
Cell 120:857-871(2005).
[19]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15857909; DOI=10.1242/dev.01857;
De Calisto J., Araya C., Marchant L., Riaz C.F., Mayor R.;
"Essential role of non-canonical Wnt signalling in neural crest
migration.";
Development 132:2587-2597(2005).
[20]
FUNCTION.
PubMed=16169711; DOI=10.1016/j.mod.2005.06.007;
Carron C., Bourdelas A., Li H.Y., Boucaut J.C., Shi D.L.;
"Antagonistic interaction between IGF and Wnt/JNK signaling in
convergent extension in Xenopus embryo.";
Mech. Dev. 122:1234-1247(2005).
[21]
FUNCTION, INTERACTION WITH FRZB1; FRZB2 AND FZD7, AND TISSUE
SPECIFICITY.
PubMed=16274967; DOI=10.1016/j.mod.2005.06.002;
Shibata M., Itoh M., Hikasa H., Taira S., Taira M.;
"Role of crescent in convergent extension movements by modulating Wnt
signaling in early Xenopus embryogenesis.";
Mech. Dev. 122:1322-1339(2005).
[22]
FUNCTION, AND INTERACTION WITH LRP6.
PubMed=17202189; DOI=10.1242/dev.02739;
Kofron M., Birsoy B., Houston D., Tao Q., Wylie C., Heasman J.;
"Wnt11/beta-catenin signaling in both oocytes and early embryos acts
through LRP6-mediated regulation of axin.";
Development 134:503-513(2007).
[23]
NOMENCLATURE.
PubMed=17436276; DOI=10.1002/dvdy.21156;
Garriock R.J., Warkman A.S., Meadows S.M., D'Agostino S., Krieg P.A.;
"Census of vertebrate Wnt genes: isolation and developmental
expression of Xenopus Wnt2, Wnt3, Wnt9a, Wnt9b, Wnt10a, and Wnt16.";
Dev. Dyn. 236:1249-1258(2007).
[24]
FUNCTION.
PubMed=17663724; DOI=10.1111/j.1365-2443.2007.01106.x;
Yamanaka H., Nishida E.;
"Wnt11 stimulation induces polarized accumulation of Dishevelled at
apical adherens junctions through Frizzled7.";
Genes Cells 12:961-967(2007).
[25]
FUNCTION, AND INDUCTION.
PubMed=18715946; DOI=10.1242/dev.026443;
Afouda B.A., Martin J., Liu F., Ciau-Uitz A., Patient R., Hoppler S.;
"GATA transcription factors integrate Wnt signalling during heart
development.";
Development 135:3185-3190(2008).
[26]
FUNCTION, HOMODIMERIZATION, IDENTIFICATION IN A COMPLEX WITH WNT5, AND
SUBCELLULAR LOCATION.
PubMed=18927149; DOI=10.1242/dev.029025;
Cha S.W., Tadjuidje E., Tao Q., Wylie C., Heasman J.;
"Wnt5a and Wnt11 interact in a maternal Dkk1-regulated fashion to
activate both canonical and non-canonical signaling in Xenopus axis
formation.";
Development 135:3719-3729(2008).
[27]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=18981481; DOI=10.1101/gad.1687308;
Li Y., Rankin S.A., Sinner D., Kenny A.P., Krieg P.A., Zorn A.M.;
"Sfrp5 coordinates foregut specification and morphogenesis by
antagonizing both canonical and noncanonical Wnt11 signaling.";
Genes Dev. 22:3050-3063(2008).
[28]
FUNCTION, AND INTERACTION WITH RYK.
PubMed=18809723; DOI=10.1083/jcb.200710188;
Kim G.H., Her J.H., Han J.K.;
"Ryk cooperates with Frizzled 7 to promote Wnt11-mediated endocytosis
and is essential for Xenopus laevis convergent extension movements.";
J. Cell Biol. 182:1073-1082(2008).
[29]
FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH
WNT5A, GLYCOSYLATION AT ASN-88 AND ASN-299, SULFATION AT TYR-274 AND
TYR-281, AND MUTAGENESIS OF ASN-88; TYR-274; TYR-281 AND ASN-299.
PubMed=19747829; DOI=10.1016/j.cub.2009.07.062;
Cha S.W., Tadjuidje E., White J., Wells J., Mayhew C., Wylie C.,
Heasman J.;
"Wnt11/5a complex formation caused by tyrosine sulfation increases
canonical signaling activity.";
Curr. Biol. 19:1573-1580(2009).
[30]
SUBCELLULAR LOCATION.
PubMed=19906850; DOI=10.1242/dev.032524;
Mii Y., Taira M.;
"Secreted Frizzled-related proteins enhance the diffusion of Wnt
ligands and expand their signalling range.";
Development 136:4083-4088(2009).
[31]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=19582868; DOI=10.1002/dvdy.22012;
Tetelin S., Jones E.A.;
"Xenopus Wnt11b is identified as a potential pronephric inducer.";
Dev. Dyn. 239:148-159(2010).
[32]
REVIEW.
PubMed=12137733; DOI=10.1016/S1084-9521(02)00050-2;
Kuhl M.;
"Non-canonical Wnt signaling in Xenopus: regulation of axis formation
and gastrulation.";
Semin. Cell Dev. Biol. 13:243-249(2002).
[33]
REVIEW.
PubMed=19232955; DOI=10.1016/j.tcm.2008.12.001;
Flaherty M.P., Dawn B.;
"Noncanonical Wnt11 signaling and cardiomyogenic differentiation.";
Trends Cardiovasc. Med. 18:260-268(2008).
-!- FUNCTION: Ligand for the frizzled7 transmembrane receptor.
Primarily acts via non-canonical Wnt pathways mediated by either
Ca(2+) and PKC, or by JNK and dvl2/dsh. Depending on the cellular
context, can also signal via the canonical Wnt pathway mediated by
beta-catenin and dvl2/dsh. May also inhibit canonical Wnt
signaling. Maternally initiates dorsal/ventral axis formation by a
canonical route, which signals via lrp6. In a complex with wnt5a,
activates the canonical and non-canonical processes involved in
axis formation. In the non-canonical pathway, acts through
fzd7/fz7 to induce phosphorylation of dvl2/dsh. Signals through a
non-canonical Wnt pathway to regulate convergent extension
movements during gastrulation. Interactions with the secreted Wnt
antagonist sfrp5 to coordinate foregut development, acting via a
non-canonical Wnt pathway whereby sfrp5 restricts wnt11b activity
to prevent inappropriate foregut formation. Mediates cardiogenesis
via non-canonical Wnt signaling involving JNK-activation and PKC.
Acts redundantly with wnt11/wnt11r during pronephros induction.
{ECO:0000269|PubMed:10751186, ECO:0000269|PubMed:10769246,
ECO:0000269|PubMed:10862746, ECO:0000269|PubMed:11128985,
ECO:0000269|PubMed:12167861, ECO:0000269|PubMed:15543138,
ECO:0000269|PubMed:15797385, ECO:0000269|PubMed:15857909,
ECO:0000269|PubMed:16169711, ECO:0000269|PubMed:16274967,
ECO:0000269|PubMed:17202189, ECO:0000269|PubMed:17663724,
ECO:0000269|PubMed:18715946, ECO:0000269|PubMed:18809723,
ECO:0000269|PubMed:18927149, ECO:0000269|PubMed:18981481,
ECO:0000269|PubMed:19582868, ECO:0000269|PubMed:19747829,
ECO:0000269|PubMed:7739543, ECO:0000269|PubMed:8306880,
ECO:0000269|PubMed:8655584}.
-!- SUBUNIT: Homodimer. Secreted homodimers form a complex with wnt5a
homodimers; tyrosine sulfation of both wnt11 and wnt5a by tpst1 is
required for this interaction. Interacts with the transmembrane
receptor fzd7/fz7. Interacts with lrp6 and ryk. Interacts with
tdgf1/frl1. Interacts weakly with frzb1 and strongly with
frzb2/crescent. Interaction with frzb2/crescent antagonizes wnt11
function in the neuroectoderm, but enhances it in mesodermal
tissue. {ECO:0000269|PubMed:10862746, ECO:0000269|PubMed:15797385,
ECO:0000269|PubMed:16274967, ECO:0000269|PubMed:17202189,
ECO:0000269|PubMed:18809723, ECO:0000269|PubMed:18927149,
ECO:0000269|PubMed:19747829}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000269|PubMed:10862746, ECO:0000269|PubMed:18927149,
ECO:0000269|PubMed:19747829, ECO:0000269|PubMed:19906850}.
-!- TISSUE SPECIFICITY: Transcripts are expressed ubiquitously in
early oocytes but become vegetally localized during mid-oogenesis
then enriched on the dorsal side by the 8 to 16 cell stage. The
protein becomes asymmetrically concentrated on the dorsal side by
the 64-cell stage. During gastrulation, expressed in the lateral
and ventral marginal zone, and during tadpole stages in the
somites and first branchial arch. Weakly expressed in the
pronephros from at least stage 12.5, with kidney expression
increasing until stage 35. Expressed in the prospective posterior
gut between stages 13 and 20, and in the deep foregut endoderm.
Prior to neural crest cell migration, expressed in a domain
flanking the neural crest on the lateral or epidermal side (the
opposite side to wnt11/wnt11-r). {ECO:0000269|PubMed:10525335,
ECO:0000269|PubMed:10585568, ECO:0000269|PubMed:10769246,
ECO:0000269|PubMed:11128985, ECO:0000269|PubMed:11784070,
ECO:0000269|PubMed:12946266, ECO:0000269|PubMed:15543138,
ECO:0000269|PubMed:15797385, ECO:0000269|PubMed:15857909,
ECO:0000269|PubMed:16274967, ECO:0000269|PubMed:18981481,
ECO:0000269|PubMed:19582868, ECO:0000269|PubMed:7539356,
ECO:0000269|PubMed:8306880}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically in
oocytes and embryos through to swimming tadpole stages.
{ECO:0000269|PubMed:8306880}.
-!- INDUCTION: By t/xbra. By gata4 and gata6. Repressed by
zbtb33/kaiso. {ECO:0000269|PubMed:10769246,
ECO:0000269|PubMed:10781937, ECO:0000269|PubMed:11128985,
ECO:0000269|PubMed:15543138, ECO:0000269|PubMed:18715946}.
-!- PTM: Glycosylation is required for protein secretion.
{ECO:0000269|PubMed:19747829}.
-!- PTM: Palmitoleoylation is required for efficient binding to
frizzled receptors. Depalmitoleoylation leads to Wnt signaling
pathway inhibition. {ECO:0000250|UniProtKB:P27467,
ECO:0000250|UniProtKB:P56704}.
-!- MISCELLANEOUS: Xenopus and other lower vertebrates contain
duplicated wnt11 genes resulting from an ancient gene duplication
event, but the second copy has since been lost in mammals. This
gene was originally called wnt-11 (PubMed:8306880) but was renamed
to wnt11b (PubMed:17436276) after the discovery of wnt11r (now
called wnt11). {ECO:0000305|PubMed:17436276,
ECO:0000305|PubMed:8306880}.
-!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
-!- CAUTION: PubMed:11159911 show a lack of role in heart induction
but PubMed:12167861 show a role in heart formation; the
discrepancy may be due to duplication of Xenopus wnt11 genes.
{ECO:0000305}.
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EMBL; L23542; AAA19697.1; -; mRNA.
EMBL; BC084745; AAH84745.1; -; mRNA.
PIR; I51572; I51572.
RefSeq; NP_001084327.1; NM_001090858.1.
UniGene; Xl.24008; -.
ProteinModelPortal; P49893; -.
SMR; P49893; -.
IntAct; P49893; 1.
iPTMnet; P49893; -.
GeneID; 399441; -.
KEGG; xla:399441; -.
CTD; 399441; -.
Xenbase; XB-GENE-6079153; wnt11b.
HOVERGEN; HBG001595; -.
KO; K01384; -.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IPI:UniProtKB.
GO; GO:0043234; C:protein complex; IPI:UniProtKB.
GO; GO:0005578; C:proteinaceous extracellular matrix; IDA:BHF-UCL.
GO; GO:0005109; F:frizzled binding; IPI:UniProtKB.
GO; GO:0019838; F:growth factor binding; IPI:UniProtKB.
GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0030295; F:protein kinase activator activity; ISS:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISS:UniProtKB.
GO; GO:0017147; F:Wnt-protein binding; IPI:UniProtKB.
GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:UniProtKB.
GO; GO:0042074; P:cell migration involved in gastrulation; IMP:UniProtKB.
GO; GO:0060027; P:convergent extension involved in gastrulation; IMP:UniProtKB.
GO; GO:0009950; P:dorsal/ventral axis specification; IMP:UniProtKB.
GO; GO:0006897; P:endocytosis; IMP:UniProtKB.
GO; GO:0007507; P:heart development; IMP:UniProtKB.
GO; GO:0060914; P:heart formation; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
GO; GO:0060548; P:negative regulation of cell death; ISS:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0001755; P:neural crest cell migration; IMP:UniProtKB.
GO; GO:0061101; P:neuroendocrine cell differentiation; ISS:UniProtKB.
GO; GO:0035567; P:non-canonical Wnt signaling pathway; IMP:UniProtKB.
GO; GO:0060021; P:palate development; ISS:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
GO; GO:0046330; P:positive regulation of JNK cascade; IDA:UniProtKB.
GO; GO:0090037; P:positive regulation of protein kinase C signaling; ISS:UniProtKB.
GO; GO:0051496; P:positive regulation of stress fiber assembly; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0048793; P:pronephros development; IMP:UniProtKB.
GO; GO:0034394; P:protein localization to cell surface; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:0016055; P:Wnt signaling pathway; IGI:UniProtKB.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; IGI:UniProtKB.
InterPro; IPR005817; Wnt.
InterPro; IPR018161; Wnt_CS.
PANTHER; PTHR12027; PTHR12027; 1.
Pfam; PF00110; wnt; 1.
PRINTS; PR01349; WNTPROTEIN.
SMART; SM00097; WNT1; 1.
PROSITE; PS00246; WNT1; 1.
1: Evidence at protein level;
Developmental protein; Disulfide bond; Extracellular matrix;
Gastrulation; Glycoprotein; Lipoprotein; Secreted; Signal; Sulfation;
Wnt signaling pathway.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 353 Protein Wnt-11b.
/FTId=PRO_0000041470.
MOD_RES 274 274 Sulfotyrosine.
{ECO:0000269|PubMed:19747829}.
MOD_RES 281 281 Sulfotyrosine.
{ECO:0000269|PubMed:19747829}.
LIPID 214 214 O-palmitoleoyl serine; by PORCN.
{ECO:0000250|UniProtKB:P56704}.
CARBOHYD 31 31 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 38 38 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 88 88 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19747829}.
CARBOHYD 299 299 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19747829}.
DISULFID 78 89 {ECO:0000250|UniProtKB:P28026}.
DISULFID 128 136 {ECO:0000250|UniProtKB:P28026}.
DISULFID 138 155 {ECO:0000250|UniProtKB:P28026}.
DISULFID 208 222 {ECO:0000250|UniProtKB:P28026}.
DISULFID 210 217 {ECO:0000250|UniProtKB:P28026}.
DISULFID 298 313 {ECO:0000250|UniProtKB:P28026}.
DISULFID 328 343 {ECO:0000250|UniProtKB:P28026}.
DISULFID 330 340 {ECO:0000250|UniProtKB:P28026}.
DISULFID 335 336 {ECO:0000250|UniProtKB:P28026}.
MUTAGEN 88 88 N->Q: Loss of glycosylation. Prevents
secretion. No effect on wnt5a-binding.
{ECO:0000269|PubMed:19747829}.
MUTAGEN 274 274 Y->F: Loss of sulfation. No effect on
secretion or homodimerization but
severely reduces interaction with wnt5a
and canonical Wnt signaling activity;
when associated with F-281.
{ECO:0000269|PubMed:19747829}.
MUTAGEN 281 281 Y->F: Loss of sulfation. No effect on
secretion or homodimerization but
severely reduces interaction with wnt5a
and canonical Wnt signaling activity;
when associated with F-274.
{ECO:0000269|PubMed:19747829}.
MUTAGEN 299 299 N->Q: Loss of glycosylation. Prevents
secretion. No effect on wnt5a-binding.
{ECO:0000269|PubMed:19747829}.
CONFLICT 257 257 L -> H (in Ref. 1; AAA19697).
{ECO:0000305}.
SEQUENCE 353 AA; 38785 MW; B59609AB88915554 CRC64;
MAPTRHWVTP LLLLCCSGIC GAIQWLGLTV NGSRVAWNES EHCRLLDGLV PDQSQLCKRN
LELMQSVVNA AKQTKLTCQM TLSDMRWNCS SVENAPSFTP DLSKGTRESA FVYALASATL
SHTIARACAS GELPTCSCGA TPAEVPGTGF RWGGCGDNLH YGLNMGSAFV DAPMKSSKSA
GTQATKIMNL HNNAVGRQVL MDSLETKCKC HGVSGSCSVK TCWKGLQDLP HIANELKSKY
LGATKVIHRQ TGTRRQLVPR ELDIRPVRES ELVYLVSSPD YCTKNPKLGS YGTQDRLCNK
TSVGSDSCNL MCCGRGYNAY TETIVERCQC KYHWCCYVMC KKCERTVERY VCK


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Catalog number Product name Quantity
PAH-G1-2 Protein Arrays containing 234 Human Protein for simultaneous detection of Protein function, including Protein-protein interaction, Protein modification, antibody specificity, auto-antibody and small m 1 glass slide with 2 sub-arrays
29-844 RNF40 contains a RING finger, a motif known to be involved in protein-protein and protein-DNA interactions. This protein was reported to interact with the tumor suppressor protein RB1. Studies of the 0.1 mg
29-850 The protein contains a RING finger, a motif present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions.The protein encoded by this 0.1 mg
EIAAB10617 DCN1-like protein 1,DCUN1 domain-containing protein 1,Dcun1d1,Dcun1l1,Defective in cullin neddylation protein 1-like protein 1,Mouse,Mus musculus,Rp42,Tes3,Testis-specific protein 3
EIAAB44668 Dap12,DNAX-activation protein 12,Karap,KAR-associated protein,Killer-activating receptor-associated protein,Mouse,Mus musculus,TYRO protein tyrosine kinase-binding protein,Tyrobp
EIAAB44667 DAP12,DNAX-activation protein 12,Homo sapiens,Human,KARAP,KAR-associated protein,Killer-activating receptor-associated protein,TYRO protein tyrosine kinase-binding protein,TYROBP
18-003-43520 HSPB1-associated protein 1 - 27 KdA heat shock protein-associated protein 1; Protein associated with small stress protein 1 Polyclonal 0.05 mg Aff Pur
EIAAB25665 AML1T1,CBFA2T1,CDR,Cyclin-D-related protein,Eight twenty one protein,ETO,Homo sapiens,Human,MTG8,Protein CBFA2T1,Protein ETO,Protein MTG8,RUNX1T1,Zinc finger MYND domain-containing protein 2,ZMYND2
EIAAB46018 C6orf55,Dopamine-responsive gene 1 protein,DRG-1,Homo sapiens,HSPC228,Human,LIP5,LYST-interacting protein 5,My012,SBP1,SKD1-binding protein 1,Vacuolar protein sorting-associated protein VTA1 homolog,V
18-003-43690 Guanine nucleotide-binding protein subunit beta-like protein 1 - G protein subunit beta-like protein 1; WD40 repeat-containing protein deleted in VCFS; Protein WDVCF; WD repeat-containing protein 14; 0.1 mg Protein A
EIAAB32247 ADP-ribosylation factor-like protein 6-interacting protein 5,Aip-5,ARL-6-interacting protein 5,ARL6IP5,Cytoskeleton-related vitamin A-responsive protein,Dermal papilla-derived protein 11,DERP11,Glutam
E1773h ELISA kit G-CSF-induced gene 1 protein,GIG1,GIG-1 protein,GMP-17,Granule membrane protein of 17 kDa,Homo sapiens,Human,Natural killer cell protein 7,NKG7,p15-TIA-1,Protein NKG7 96T
U1773h CLIA G-CSF-induced gene 1 protein,GIG1,GIG-1 protein,GMP-17,Granule membrane protein of 17 kDa,Homo sapiens,Human,Natural killer cell protein 7,NKG7,p15-TIA-1,Protein NKG7 96T
E1773h ELISA G-CSF-induced gene 1 protein,GIG1,GIG-1 protein,GMP-17,Granule membrane protein of 17 kDa,Homo sapiens,Human,Natural killer cell protein 7,NKG7,p15-TIA-1,Protein NKG7 96T
EIAAB31034 Androgen receptor-interacting protein 3,ARIP3,DAB2-interacting protein,DIP,E3 SUMO-protein ligase PIAS2,Homo sapiens,Human,Miz1,Msx-interacting zinc finger protein,PIAS2,PIAS-NY protein,PIASX,Protein
EIAAB29586 Mouse,Mus musculus,p53-induced gene 11 protein,Pig11,Tp53i11,Transformation related protein 53 inducible protein 11,Trp53i11,Tumor protein p53-inducible protein 11
EIAAB43486 Mouse,Mus musculus,Protein TAP1,Protein TRUSS,Rabex-5_Rin2-interacting protein,Short transient receptor potential channel 4-associated protein,TNF-receptor ubiquitous scaffolding_signaling protein,Trp
10-663-45493 Heat Shock Protein 22kD (HSP22) Human - HspB8; Alpha crystallin C chain; Small stress protein-like protein HSP22; E2-induced gene 1 protein; Protein kinase H11 N_A 0.002 mg
10-663-45493 Heat Shock Protein 22kD (HSP22) Human - HspB8; Alpha crystallin C chain; Small stress protein-like protein HSP22; E2-induced gene 1 protein; Protein kinase H11 N_A 0.01 mg
10-663-45493 Heat Shock Protein 22kD (HSP22) Human - HspB8; Alpha crystallin C chain; Small stress protein-like protein HSP22; E2-induced gene 1 protein; Protein kinase H11 N_A 0.1 mg
EIAAB43485 C20orf188,Homo sapiens,Human,Protein TAP1,Protein TRUSS,Short transient receptor potential channel 4-associated protein,TNF-receptor ubiquitous scaffolding_signaling protein,Trp4-associated protein,TR
EIAAB33912 E3 ubiquitin-protein ligase RBBP6,Mouse,Mus musculus,P2pr,p53-associated cellular protein of testis,Pact,Proliferation potential-related protein,Protein P2P-R,Rbbp6,Retinoblastoma-binding protein 6
EIAAB38162 Homo sapiens,Human,MAP,Merlin-associated protein,RabGAPLP,RABGAPLP,Rab-GTPase-activating protein-like protein,RUN and TBC1 domain-containing protein 3,RUTBC3,SGSM3,Small G protein signaling modulator
EIAAB29908 Cap1,Contraception-associated protein 1,Fertility protein SP22,Park7,Parkinson disease protein 7 homolog,Protein CAP1,Protein DJ-1,Rat,Rattus norvegicus
EIAAB31031 DDXBP1,DEAD_H box-binding protein 1,E3 SUMO-protein ligase PIAS1,GBP,Gu-binding protein,Homo sapiens,Human,PIAS1,Protein inhibitor of activated STAT protein 1,RNA helicase II-binding protein


 

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