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P51142

- DVL2_XENLA

UniProt

P51142 - DVL2_XENLA

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Protein
Segment polarity protein dishevelled homolog DVL-2
Gene
dvl2, dsh
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in at least 2 independent signaling cascades, controlling cell fate via canonical Wnt signaling and cell polarity via a planar cell polarity (PCP) cascade. Acts synergistically with dal/dapple-like to activate Wnt signaling, stabilizing ctnnb1/beta-catenin and leading to dorsal axis formation. Also prevents degradation of ctnnb1/beta-catenin by displacing gsk3 from a complex with ARP/Axin-related protein. Has an additional role in anterior-posterior (A/P) axis formation, specifying different neuroectodermal cell fates along the A/P axis in a dose-dependent manner by activating several early patterning genes. In the PCP pathway, required at the cell membrane for PCP-mediated neural and mesodermal convergent extension during gastrulation and subsequent neural tube closure, acting to activate jnk. Also involved in blastopore closure and archenteron elongation during early, but not late, gastrulation. Associates with ephrin receptors and ligands and acts as part of a downstream PCP pathway to mediate ephrin-mediated cell repulsion via activation of rhoa. Required for efnb1/ephrin-B1-driven movement of non-retinal progenitor cells into the retina during eye field formation. Patterns the hindbrain. Required for ciliogenesis. Controls the docking of basal bodies to the apical plasma membrane; mediates the activation, but not localization of rhoa at the apical surface of ciliated cells during basal body docking. Furthermore, required for the association of basal bodies with membrane-bound vesicles and the vesicle-trafficking protein exoc4/sec8, and this association is in turn required for basal body docking. Once basal bodies are docked, required for the planar polarization of basal bodies that underlies ciliary beating and the directional fluid flow across ciliated epithelia.17 Publications

GO - Molecular functioni

  1. ephrin receptor binding Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. signal transducer activity Source: InterPro
  4. syndecan binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. Wnt signaling pathway Source: UniProtKB
  2. activation of Rho GTPase activity Source: UniProtKB
  3. anterior/posterior axis specification Source: UniProtKB
  4. canonical Wnt signaling pathway Source: BHF-UCL
  5. ciliary basal body organization Source: UniProtKB
  6. cilium assembly Source: UniProtKB
  7. convergent extension Source: UniProtKB
  8. convergent extension involved in gastrulation Source: UniProtKB
  9. dorsal/ventral axis specification Source: UniProtKB
  10. ephrin receptor signaling pathway Source: UniProtKB
  11. establishment of planar polarity Source: UniProtKB
  12. establishment or maintenance of cell polarity Source: UniProtKB
  13. gastrulation with mouth forming second Source: UniProtKB
  14. intracellular signal transduction Source: InterPro
  15. neural tube closure Source: UniProtKB
  16. neurogenesis Source: UniProtKB
  17. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  18. protein homooligomerization Source: UniProtKB
  19. protein stabilization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cilium biogenesis/degradation, Gastrulation, Wnt signaling pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Segment polarity protein dishevelled homolog DVL-2
Short name:
Dishevelled-2
Alternative name(s):
DSH homolog 2
Xdsh
Gene namesi
Name:dvl2
Synonyms:dsh
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-1017467. dvl2.

Subcellular locationi

Cytoplasm. Cytoplasmic vesicle. Cell projectioncilium. Nucleus. Cell membrane; Peripheral membrane protein
Note: Phosphorylated and recruited from the cytoplasm to the cell membrane by frizzled proteins. Also relocated to the cell membrane by sdc4 and ephb1/ephrin-B1. Concentrated at cell membrane in both ciliated and non-ciliated cells. Enriched at the apical surface of ciliated cells. Localized to the cilium rootlet.10 Publications

GO - Cellular componenti

  1. cell cortex Source: MGI
  2. cell surface Source: UniProtKB
  3. ciliary rootlet Source: UniProtKB
  4. cytoplasm Source: UniProtKB
  5. cytoplasmic membrane-bounded vesicle Source: UniProtKB
  6. cytoplasmic vesicle Source: UniProtKB
  7. nucleus Source: UniProtKB
  8. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cilium, Cytoplasm, Cytoplasmic vesicle, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi272 – 2754QSNE → AANA: No effect on interaction with dact1-B/dpr. 1 Publication
Mutagenesisi317 – 3171N → T: Abolishes interaction with dact1-B/dpr. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 736736Segment polarity protein dishevelled homolog DVL-2
PRO_0000145748Add
BLAST

Post-translational modificationi

Phosphorylated. Phosphorylation is controlled by frizzled proteins, correlates with the onset of embryo dorsalizing events and is higher in the dorsal half of early cleavage embryos. Phosphorylated on tyrosine residues in response to association with efnb1/ephrin-B1.2 Publications

Keywords - PTMi

Phosphoprotein

Expressioni

Tissue specificityi

Expressed equally in both animal-vegetal and dorsal-ventral directions of the early blastula. Becomes enriched on the dorsal side of the embryo after cortical rotation. Expressed along the anterior margin of eye field of neurulae (stage 16 embryos) and in the anterolateral crescent that borders the eye field. Continues to be expressed in the optic cup at stage 26. Expressed in the central nervous system throughout the early tailbud stage including the entire hindbrain.4 Publications

Developmental stagei

Expressed maternally. Most abundant in eggs and expressed at a low level in blastulae, gastrulae, neurulae and tailbud embryonic stages.1 Publication

Interactioni

Subunit structurei

Can form homomultimers. Interacts with prickle1. Interacts (via PDZ domain) with ccdc88c/dal and dact1-B/dpr. Interacts (via DIX domain) with ARP/Axin-related protein and dact1-A/frodo. Interacts with sdc4, possibly via fz7. Interacts directly (via DEP domain) with efnb1/ephrin-B1 and indirectly with the phosphorylated ephrin receptors ephb1 and ephb2, via association with SH domain-containing adapters. May interact with lrrc6.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
A5J0904EBI-6257503,EBI-7401819
ctnnd1Q8AXM92EBI-6257503,EBI-6260685
dact1-bQ8QG922EBI-6257503,EBI-6257549

Protein-protein interaction databases

BioGridi100626. 2 interactions.
IntActiP51142. 5 interactions.
MINTiMINT-100832.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi252 – 2576
Helixi259 – 2624
Beta strandi267 – 2704
Beta strandi281 – 2877
Helixi291 – 2955
Beta strandi303 – 3075
Helixi317 – 32913
Beta strandi330 – 3323
Beta strandi334 – 3396

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L6OX-ray2.20A/B/C252-340[»]
2F0AX-ray1.80A/B/C/D252-340[»]
3FY5X-ray2.40A/B254-343[»]
ProteinModelPortaliP51142.
SMRiP51142. Positions 252-340, 412-502.

Miscellaneous databases

EvolutionaryTraceiP51142.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8282DIX
Add
BLAST
Domaini254 – 32673PDZ
Add
BLAST
Domaini428 – 50275DEP
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi99 – 11315Poly-Pro
Add
BLAST
Compositional biasi222 – 2276Poly-Arg
Compositional biasi680 – 6878Poly-Pro

Domaini

The C-terminal region containing the DEP domain is required for membrane accumulation and phosphorylation. Wnt signaling and axis induction requires the DIX domain. The C-terminus contributes to the localization at the cilia base.3 Publications

Sequence similaritiesi

Belongs to the DSH family.
Contains 1 DEP domain.
Contains 1 DIX domain.
Contains 1 PDZ (DHR) domain.

Phylogenomic databases

HOVERGENiHBG005542.
KOiK02353.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.30.42.10. 1 hit.
InterProiIPR000591. DEP_dom.
IPR008341. Dishevelled_2.
IPR024580. Dishevelled_C-dom.
IPR008339. Dishevelled_fam.
IPR003351. Dishevelled_protein_dom.
IPR001158. DIX.
IPR015506. Dsh/Dvl-rel.
IPR001478. PDZ.
IPR029071. Ubiquitin-rel_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10878. PTHR10878. 1 hit.
PTHR10878:SF8. PTHR10878:SF8. 1 hit.
PfamiPF00610. DEP. 1 hit.
PF02377. Dishevelled. 1 hit.
PF00778. DIX. 1 hit.
PF12316. Dsh_C. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]
PRINTSiPR01760. DISHEVELLED.
PR01762. DISHEVELLED2.
SMARTiSM00021. DAX. 1 hit.
SM00049. DEP. 1 hit.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50186. DEP. 1 hit.
PS50841. DIX. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P51142-1 [UniParc]FASTAAdd to Basket

« Hide

MAETKVIYHL DEEETPYLVK VPVPATDIRL RDFKAALGRG HAKYFFKAMD    50
QDFGVVKEEI SDDNAKLPCF NDRVVSWLAS SEGSQPDSAP PAPATEVRPE 100
PPPPVPPPIP PPPAERTSGI GDSRPPSFHP NVSGSTEQLD QDNESVISMR 150
RDRVRRRESS EQAGVGRGVN GRTERHLSGY ESSSTLLTSE IETSICDSEE 200
DDTMSRFSSS TEQSSASRLL KRHRRRRKQR PPRLERTSSF SSVTDSTMSL 250
NIITVTLNME KYNFLGISIV GQSNERGDGG IYIGSIMKGG AVAADGRIEP 300
GDMLLQVNDI NFENMSNDDA VRVLRDIVHK PGPIVLTVAK CWDPSPQGYF 350
TLPRNEPIHP IDPAAWVSHS AALSGSFPVY PGSASMSSMT SSTSVTETEL 400
SHALPPVSLF SLSVHTDLAS VVKVMASPES GLEVRDRMWL KITIPNAFLG 450
SDVVDWLYHH VEGFQDRREA RKFASNLLKA GFIRHTVNKI TFSEQCYYIF 500
GDLTGCENYM TNLSLNDNDG SSGASDQDTL APLPLPGASP WPLLPTFSYQ 550
YQAPHPYSTQ PPAYHELSSY SYGMGSAGSQ HSEGSRSSGS NRSDGGRGMQ 600
KDDRSGVAGV GGGDSKSGSG SESEYSTRSS IRRVGGGEAG PPSERSTSSR 650
LPPHHPPSVH SYAAPGVPLS YNPMMLMMMP PPPLPPPGVC PPNSSVPPGA 700
PPLVRDLASV PPELTATRQS FHMAMGNPSE FFVDVM 736
Length:736
Mass (Da):79,787
Last modified:October 1, 1996 - v1
Checksum:iAF6C9A1662DD7CEB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U31552 mRNA. Translation: AAB00688.1.
PIRiI51691.
RefSeqiNP_001084096.1. NM_001090627.1.
UniGeneiXl.7670.

Genome annotation databases

GeneIDi399301.
KEGGixla:399301.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U31552 mRNA. Translation: AAB00688.1 .
PIRi I51691.
RefSeqi NP_001084096.1. NM_001090627.1.
UniGenei Xl.7670.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1L6O X-ray 2.20 A/B/C 252-340 [» ]
2F0A X-ray 1.80 A/B/C/D 252-340 [» ]
3FY5 X-ray 2.40 A/B 254-343 [» ]
ProteinModelPortali P51142.
SMRi P51142. Positions 252-340, 412-502.
ModBasei Search...

Protein-protein interaction databases

BioGridi 100626. 2 interactions.
IntActi P51142. 5 interactions.
MINTi MINT-100832.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 399301.
KEGGi xla:399301.

Organism-specific databases

CTDi 1856.
Xenbasei XB-GENE-1017467. dvl2.

Phylogenomic databases

HOVERGENi HBG005542.
KOi K02353.

Miscellaneous databases

EvolutionaryTracei P51142.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
2.30.42.10. 1 hit.
InterProi IPR000591. DEP_dom.
IPR008341. Dishevelled_2.
IPR024580. Dishevelled_C-dom.
IPR008339. Dishevelled_fam.
IPR003351. Dishevelled_protein_dom.
IPR001158. DIX.
IPR015506. Dsh/Dvl-rel.
IPR001478. PDZ.
IPR029071. Ubiquitin-rel_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
PANTHERi PTHR10878. PTHR10878. 1 hit.
PTHR10878:SF8. PTHR10878:SF8. 1 hit.
Pfami PF00610. DEP. 1 hit.
PF02377. Dishevelled. 1 hit.
PF00778. DIX. 1 hit.
PF12316. Dsh_C. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view ]
PRINTSi PR01760. DISHEVELLED.
PR01762. DISHEVELLED2.
SMARTi SM00021. DAX. 1 hit.
SM00049. DEP. 1 hit.
SM00228. PDZ. 1 hit.
[Graphical view ]
SUPFAMi SSF50156. SSF50156. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEi PS50186. DEP. 1 hit.
PS50841. DIX. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Dorsalizing and neuralizing properties of Xdsh, a maternally expressed Xenopus homolog of dishevelled."
    Sokol S.Y., Klingensmith J., Perrimon N., Itoh K.
    Development 121:1637-1647(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: Oocyte.
  2. Erratum
    Sokol S.Y., Klingensmith J., Perrimon N., Itoh K.
    Development 121:3487-3487(1995) [PubMed] [Europe PMC] [Abstract]
  3. "Analysis of Dishevelled signalling pathways during Xenopus development."
    Sokol S.Y.
    Curr. Biol. 6:1456-1467(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "Graded amounts of Xenopus dishevelled specify discrete anteroposterior cell fates in prospective ectoderm."
    Itoh K., Sokol S.Y.
    Mech. Dev. 61:113-125(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Establishment of the dorsal-ventral axis in Xenopus embryos coincides with the dorsal enrichment of dishevelled that is dependent on cortical rotation."
    Miller J.R., Rowning B.A., Larabell C.A., Yang-Snyder J.A., Bates R.L., Moon R.T.
    J. Cell Biol. 146:427-437(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. "Interaction of Frizzled 7 and Dishevelled in Xenopus."
    Medina A., Steinbeisser H.
    Dev. Dyn. 218:671-680(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "Dishevelled phosphorylation, subcellular localization and multimerization regulate its role in early embryogenesis."
    Rothbaecher U., Laurent M.N., Deardorff M.A., Klein P.S., Cho K.W.Y., Fraser S.E.
    EMBO J. 19:1010-1022(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION, PHOSPHORYLATION, DOMAIN.
  8. "Interaction of dishevelled and Xenopus axin-related protein is required for wnt signal transduction."
    Itoh K., Antipova A., Ratcliffe M.J., Sokol S.Y.
    Mol. Cell. Biol. 20:2228-2238(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ARP, SUBCELLULAR LOCATION, DOMAIN.
  9. "Dishevelled controls cell polarity during Xenopus gastrulation."
    Wallingford J.B., Rowning B.A., Vogeli K.M., Rothbaecher U., Fraser S.E., Harland R.M.
    Nature 405:81-85(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. "Xenopus Dishevelled signaling regulates both neural and mesodermal convergent extension: parallel forces elongating the body axis."
    Wallingford J.B., Harland R.M.
    Development 128:2581-2592(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Neural tube closure requires Dishevelled-dependent convergent extension of the midline."
    Wallingford J.B., Harland R.M.
    Development 129:5815-5825(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Frodo interacts with Dishevelled to transduce Wnt signals."
    Gloy J., Hikasa H., Sokol S.Y.
    Nat. Cell Biol. 4:351-357(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DACT1-A.
  13. "The prickle-related gene in vertebrates is essential for gastrulation cell movements."
    Takeuchi M., Nakabayashi J., Sakaguchi T., Yamamoto T.S., Takahashi H., Takeda H., Ueno N.
    Curr. Biol. 13:674-679(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRICKLE1.
  14. "Association of Dishevelled with Eph tyrosine kinase receptor and ephrin mediates cell repulsion."
    Tanaka M., Kamo T., Ota S., Sugimura H.
    EMBO J. 22:847-858(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EFNB1; EPHB1 AND EPHB2, TISSUE SPECIFICITY, TYROSINE PHOSPHORYLATION.
  15. "Regional requirements for Dishevelled signaling during Xenopus gastrulation: separable effects on blastopore closure, mesendoderm internalization and archenteron formation."
    Ewald A.J., Peyrot S.M., Tyszka J.M., Fraser S.E., Wallingford J.B.
    Development 131:6195-6209(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "Subcellular localization and signaling properties of dishevelled in developing vertebrate embryos."
    Park T.J., Gray R.S., Sato A., Habas R., Wallingford J.B.
    Curr. Biol. 15:1039-1044(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  17. "Novel Daple-like protein positively regulates both the Wnt/beta-catenin pathway and the Wnt/JNK pathway in Xenopus."
    Kobayashi H., Michiue T., Yukita A., Danno H., Sakurai K., Fukui A., Kikuchi A., Asashima M.
    Mech. Dev. 122:1138-1153(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CCDC88C.
  18. "Identification of the Wnt signaling activator leucine-rich repeat in Flightless interaction protein 2 by a genome-wide functional analysis."
    Liu J., Bang A.G., Kintner C., Orth A.P., Chanda S.K., Ding S., Schultz P.G.
    Proc. Natl. Acad. Sci. U.S.A. 102:1927-1932(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. "Dishevelled mediates ephrinB1 signalling in the eye field through the planar cell polarity pathway."
    Lee H.-S., Bong Y.-S., Moore K.B., Soria K., Moody S.A., Daar I.O.
    Nat. Cell Biol. 8:55-63(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EFNB1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  20. "Syndecan-4 regulates non-canonical Wnt signalling and is essential for convergent and extension movements in Xenopus embryos."
    Munoz R., Moreno M., Oliva C., Orbenes C., Larrain J.
    Nat. Cell Biol. 8:492-500(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SDC4, SUBCELLULAR LOCATION.
  21. "Cystic kidney gene seahorse regulates cilia-mediated processes and Wnt pathways."
    Kishimoto N., Cao Y., Park A., Sun Z.
    Dev. Cell 14:954-961(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LRRC6.
  22. "Dishevelled controls apical docking and planar polarization of basal bodies in ciliated epithelial cells."
    Park T.J., Mitchell B.J., Abitua P.B., Kintner C., Wallingford J.B.
    Nat. Genet. 40:871-879(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN.
  23. "Dapper, a Dishevelled-associated antagonist of beta-catenin and JNK signaling, is required for notochord formation."
    Cheyette B.N.R., Waxman J.S., Miller J.R., Takemaru K., Sheldahl L.C., Khlebtsova N., Fox E.P., Earnest T.N., Moon R.T.
    Dev. Cell 2:449-461(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 252-340 IN COMPLEX WITH DACT1-B, FUNCTION, INTERACTION WITH DACT1-B, SUBCELLULAR LOCATION, MUTAGENESIS OF 272-GLN--GLU-275 AND ASN-317.
  24. "Conformational flexibility in the PDZ domain of Dishevelled induced by target binding."
    Friedland N., Hung L.-W., Cheyette B.N.R., Miller J.R., Moon R.T., Earnest T.N.
    Submitted (NOV-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 252-340.

Entry informationi

Entry nameiDVL2_XENLA
AccessioniPrimary (citable) accession number: P51142
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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