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Protein

Frizzled-4

Gene

FZD4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin (CTNNB1) canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin (CTNNB1) and activation of Wnt target genes. Plays a critical role in retinal vascularization by acting as a receptor for Wnt proteins and norrin (NDP). In retina, it can be both activated by Wnt protein-binding, but also by a Wnt-independent signaling via binding of norrin (NDP), promoting in both cases beta-catenin (CTNNB1) accumulation and stimulation of LEF/TCF-mediated transcriptional programs. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues.

GO - Molecular functioni

  • cytokine binding Source: BHF-UCL
  • G-protein coupled receptor activity Source: GO_Central
  • PDZ domain binding Source: UniProtKB
  • protein heterodimerization activity Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL
  • ubiquitin protein ligase binding Source: UniProtKB
  • Wnt-activated receptor activity Source: BHF-UCL
  • Wnt-protein binding Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Wnt signaling pathway

Enzyme and pathway databases

BioCyciZFISH:ENSG00000174804-MONOMER.
ReactomeiR-HSA-373080. Class B/2 (Secretin family receptors).
R-HSA-4086398. Ca2+ pathway.
R-HSA-4608870. Asymmetric localization of PCP proteins.
R-HSA-4641263. Regulation of FZD by ubiquitination.
R-HSA-5099900. WNT5A-dependent internalization of FZD4.
R-HSA-5340588. RNF mutants show enhanced WNT signaling and proliferation.
R-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-HSA-8856828. Clathrin-mediated endocytosis.
SignaLinkiQ9ULV1.
SIGNORiQ9ULV1.

Names & Taxonomyi

Protein namesi
Recommended name:
Frizzled-4
Short name:
Fz-4
Short name:
hFz4
Alternative name(s):
FzE4
CD_antigen: CD344
Gene namesi
Name:FZD4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:4042. FZD4.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini37 – 222ExtracellularSequence analysisAdd BLAST186
Transmembranei223 – 243Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini244 – 254CytoplasmicSequence analysisAdd BLAST11
Transmembranei255 – 275Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini276 – 302ExtracellularSequence analysisAdd BLAST27
Transmembranei303 – 323Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini324 – 344CytoplasmicSequence analysisAdd BLAST21
Transmembranei345 – 365Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini366 – 389ExtracellularSequence analysisAdd BLAST24
Transmembranei390 – 410Helical; Name=5Sequence analysisAdd BLAST21
Topological domaini411 – 436CytoplasmicSequence analysisAdd BLAST26
Transmembranei437 – 457Helical; Name=6Sequence analysisAdd BLAST21
Topological domaini458 – 477ExtracellularSequence analysisAdd BLAST20
Transmembranei478 – 498Helical; Name=7Sequence analysisAdd BLAST21
Topological domaini499 – 537CytoplasmicSequence analysisAdd BLAST39

GO - Cellular componenti

  • cell-cell junction Source: Ensembl
  • cell surface Source: BHF-UCL
  • clathrin-coated endocytic vesicle membrane Source: Reactome
  • extracellular exosome Source: UniProtKB
  • integral component of membrane Source: GO_Central
  • integral component of plasma membrane Source: BHF-UCL
  • plasma membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Vitreoretinopathy, exudative 1 (EVR1)12 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder of the retinal vasculature characterized by an abrupt cessation of growth of peripheral capillaries, leading to an avascular peripheral retina. This may lead to compensatory retinal neovascularization, which is thought to be induced by hypoxia from the initial avascular insult. New vessels are prone to leakage and rupture causing exudates and bleeding, followed by scarring, retinal detachment and blindness. Clinical features can be highly variable, even within the same family. Patients with mild forms of the disease are asymptomatic, and their only disease related abnormality is an arc of avascular retina in the extreme temporal periphery. In many ways the disease resembles retinopathy of prematurity but there is no evidence of prematurity or small birth weight in the patient history.
See also OMIM:133780
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06392033P → S in EVR1. 3 PublicationsCorresponds to variant rs61735304dbSNPEnsembl.1
Natural variantiVAR_06392136G → D in EVR1. 1 PublicationCorresponds to variant rs80358281dbSNPEnsembl.1
Natural variantiVAR_06392240E → Q in EVR1. 1 PublicationCorresponds to variant rs139401671dbSNPEnsembl.1
Natural variantiVAR_06392369H → Y in EVR1; minor reduction of its wild-type activity. 4 PublicationsCorresponds to variant rs80358282dbSNPEnsembl.1
Natural variantiVAR_063924105M → T in EVR1. 1 PublicationCorresponds to variant rs80358285dbSNPEnsembl.1
Natural variantiVAR_038947105M → V in EVR1; loss of function. 4 PublicationsCorresponds to variant rs80358284dbSNPEnsembl.1
Natural variantiVAR_063925114I → T in EVR1. 1 Publication1
Natural variantiVAR_038948157M → V in EVR1; loss of function. 2 PublicationsCorresponds to variant rs80358286dbSNPEnsembl.1
Natural variantiVAR_063927181C → R in EVR1. 1 PublicationCorresponds to variant rs80358287dbSNPEnsembl.1
Natural variantiVAR_063929204C → R in EVR1. 1 PublicationCorresponds to variant rs80358288dbSNPEnsembl.1
Natural variantiVAR_063930204C → Y in EVR1. 1 Publication1
Natural variantiVAR_063931223M → K in EVR1. 1 Publication1
Natural variantiVAR_063932256I → V in EVR1. 1 PublicationCorresponds to variant rs104894223dbSNPEnsembl.1
Natural variantiVAR_063933335W → C in EVR1. 1 PublicationCorresponds to variant rs80358292dbSNPEnsembl.1
Natural variantiVAR_063934342M → V in EVR1. 2 PublicationsCorresponds to variant rs80358293dbSNPEnsembl.1
Natural variantiVAR_063936417R → Q in EVR1; 48% loss of its wild-type activity; associated in a EVR4 patient with mutation CYS-444 in LPR5. 3 PublicationsCorresponds to variant rs80358294dbSNPEnsembl.1
Natural variantiVAR_063937445T → P in EVR1. 1 PublicationCorresponds to variant rs80358297dbSNPEnsembl.1
Natural variantiVAR_063938488G → D in EVR1. 2 PublicationsCorresponds to variant rs80358298dbSNPEnsembl.1
Natural variantiVAR_017777493 – 494Missing in EVR1; loss of function. 3 Publications2
Natural variantiVAR_063939497S → F in EVR1. 1 PublicationCorresponds to variant rs80358300dbSNPEnsembl.1
Natural variantiVAR_063940525G → R in EVR1. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi8322.
MalaCardsiFZD4.
MIMi133780. phenotype.
OpenTargetsiENSG00000174804.
Orphaneti891. Familial exudative vitreoretinopathy.
91495. Persistent hyperplastic primary vitreous.
90050. Retinopathy of prematurity.
PharmGKBiPA28459.

Polymorphism and mutation databases

BioMutaiFZD4.
DMDMi62298045.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 36Sequence analysisAdd BLAST36
ChainiPRO_000001298537 – 537Frizzled-4Add BLAST501

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi45 ↔ 106PROSITE-ProRule annotation
Disulfide bondi53 ↔ 99PROSITE-ProRule annotation
Glycosylationi59N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi90 ↔ 128PROSITE-ProRule annotation
Disulfide bondi117 ↔ 158PROSITE-ProRule annotation
Disulfide bondi121 ↔ 145PROSITE-ProRule annotation
Glycosylationi144N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

Ubiquitinated by ZNRF3, leading to its degradation by the proteasome.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9ULV1.
PaxDbiQ9ULV1.
PeptideAtlasiQ9ULV1.
PRIDEiQ9ULV1.

PTM databases

iPTMnetiQ9ULV1.
PhosphoSitePlusiQ9ULV1.

Expressioni

Tissue specificityi

Almost ubiquitous. Largely expressed in adult heart, skeletal muscle, ovary, and fetal kidney. Moderate amounts in adult liver, kidney, pancreas, spleen, and fetal lung, and small amounts in placenta, adult lung, prostate, testis, colon, fetal brain and liver.

Gene expression databases

BgeeiENSG00000174804.
CleanExiHS_FZD4.
GenevisibleiQ9ULV1. HS.

Organism-specific databases

HPAiHPA042328.

Interactioni

Subunit structurei

Interacts with MAGI3 and norrin (NDP). Component of a complex, at least composed of TSPAN12, FZD4 and norrin (NDP) (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
I79_000956G3GTH22EBI-2466380,EBI-3504975From a different organism.
NDPQ006044EBI-2466380,EBI-2466352

GO - Molecular functioni

  • cytokine binding Source: BHF-UCL
  • PDZ domain binding Source: UniProtKB
  • protein heterodimerization activity Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL
  • ubiquitin protein ligase binding Source: UniProtKB
  • Wnt-protein binding Source: GO_Central

Protein-protein interaction databases

BioGridi113918. 4 interactors.
IntActiQ9ULV1. 8 interactors.
MINTiMINT-2822299.
STRINGi9606.ENSP00000434034.

Structurei

Secondary structure

1537
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi45 – 47Combined sources3
Helixi51 – 53Combined sources3
Beta strandi55 – 57Combined sources3
Beta strandi59 – 61Combined sources3
Helixi72 – 79Combined sources8
Helixi80 – 82Combined sources3
Helixi83 – 88Combined sources6
Helixi94 – 102Combined sources9
Beta strandi105 – 107Combined sources3
Beta strandi110 – 114Combined sources5
Helixi118 – 134Combined sources17
Helixi141 – 143Combined sources3
Helixi145 – 147Combined sources3
Beta strandi153 – 155Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5BPBX-ray2.20A/B/C/D42-179[»]
5BPQX-ray2.40A/B/C/D42-179[»]
5BQCX-ray3.00B42-179[»]
5BQEX-ray2.30C42-179[»]
5CL1X-ray3.80C/D38-160[»]
5CM4X-ray2.40A/B40-164[»]
ProteinModelPortaliQ9ULV1.
SMRiQ9ULV1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini40 – 161FZPROSITE-ProRule annotationAdd BLAST122

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi499 – 504Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family membersBy similarity6
Motifi535 – 537PDZ-binding3

Domaini

Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl (Disheveled) family members and is involved in the activation of the Wnt/beta-catenin signaling pathway.By similarity
The FZ domain is involved in binding with Wnt ligands.By similarity

Sequence similaritiesi

Contains 1 FZ (frizzled) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3577. Eukaryota.
ENOG410XRC8. LUCA.
GeneTreeiENSGT00760000118864.
HOGENOMiHOG000233236.
HOVERGENiHBG006977.
InParanoidiQ9ULV1.
KOiK02354.
OMAiSMCLSVK.
OrthoDBiEOG091G0N5M.
PhylomeDBiQ9ULV1.
TreeFamiTF317907.

Family and domain databases

Gene3Di1.10.2000.10. 1 hit.
InterProiIPR000539. Frizzled.
IPR015526. Frizzled/SFRP.
IPR020067. Frizzled_dom.
IPR026551. FZD4.
IPR017981. GPCR_2-like.
[Graphical view]
PANTHERiPTHR11309. PTHR11309. 1 hit.
PTHR11309:SF23. PTHR11309:SF23. 1 hit.
PfamiPF01534. Frizzled. 1 hit.
PF01392. Fz. 1 hit.
[Graphical view]
PRINTSiPR00489. FRIZZLED.
SMARTiSM00063. FRI. 1 hit.
SM01330. Frizzled. 1 hit.
[Graphical view]
SUPFAMiSSF63501. SSF63501. 1 hit.
PROSITEiPS50038. FZ. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9ULV1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAWRGAGPSV PGAPGGVGLS LGLLLQLLLL LGPARGFGDE EERRCDPIRI
60 70 80 90 100
SMCQNLGYNV TKMPNLVGHE LQTDAELQLT TFTPLIQYGC SSQLQFFLCS
110 120 130 140 150
VYVPMCTEKI NIPIGPCGGM CLSVKRRCEP VLKEFGFAWP ESLNCSKFPP
160 170 180 190 200
QNDHNHMCME GPGDEEVPLP HKTPIQPGEE CHSVGTNSDQ YIWVKRSLNC
210 220 230 240 250
VLKCGYDAGL YSRSAKEFTD IWMAVWASLC FISTAFTVLT FLIDSSRFSY
260 270 280 290 300
PERPIIFLSM CYNIYSIAYI VRLTVGRERI SCDFEEAAEP VLIQEGLKNT
310 320 330 340 350
GCAIIFLLMY FFGMASSIWW VILTLTWFLA AGLKWGHEAI EMHSSYFHIA
360 370 380 390 400
AWAIPAVKTI VILIMRLVDA DELTGLCYVG NQNLDALTGF VVAPLFTYLV
410 420 430 440 450
IGTLFIAAGL VALFKIRSNL QKDGTKTDKL ERLMVKIGVF SVLYTVPATC
460 470 480 490 500
VIACYFYEIS NWALFRYSAD DSNMAVEMLK IFMSLLVGIT SGMWIWSAKT
510 520 530
LHTWQKCSNR LVNSGKVKRE KRGNGWVKPG KGSETVV
Length:537
Mass (Da):59,881
Last modified:March 29, 2005 - v2
Checksum:iE0A83ECEC560A381
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti481I → T in BAA86286 (PubMed:10544037).Curated1
Sequence conflicti500T → S in BAA86286 (PubMed:10544037).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06392033P → S in EVR1. 3 PublicationsCorresponds to variant rs61735304dbSNPEnsembl.1
Natural variantiVAR_06392136G → D in EVR1. 1 PublicationCorresponds to variant rs80358281dbSNPEnsembl.1
Natural variantiVAR_06392240E → Q in EVR1. 1 PublicationCorresponds to variant rs139401671dbSNPEnsembl.1
Natural variantiVAR_06392369H → Y in EVR1; minor reduction of its wild-type activity. 4 PublicationsCorresponds to variant rs80358282dbSNPEnsembl.1
Natural variantiVAR_063924105M → T in EVR1. 1 PublicationCorresponds to variant rs80358285dbSNPEnsembl.1
Natural variantiVAR_038947105M → V in EVR1; loss of function. 4 PublicationsCorresponds to variant rs80358284dbSNPEnsembl.1
Natural variantiVAR_063925114I → T in EVR1. 1 Publication1
Natural variantiVAR_038948157M → V in EVR1; loss of function. 2 PublicationsCorresponds to variant rs80358286dbSNPEnsembl.1
Natural variantiVAR_063926168P → S.3 PublicationsCorresponds to variant rs61735303dbSNPEnsembl.1
Natural variantiVAR_063927181C → R in EVR1. 1 PublicationCorresponds to variant rs80358287dbSNPEnsembl.1
Natural variantiVAR_063928203K → N in retinopathy of prematurity. 1 Publication1
Natural variantiVAR_063929204C → R in EVR1. 1 PublicationCorresponds to variant rs80358288dbSNPEnsembl.1
Natural variantiVAR_063930204C → Y in EVR1. 1 Publication1
Natural variantiVAR_063931223M → K in EVR1. 1 Publication1
Natural variantiVAR_063932256I → V in EVR1. 1 PublicationCorresponds to variant rs104894223dbSNPEnsembl.1
Natural variantiVAR_063933335W → C in EVR1. 1 PublicationCorresponds to variant rs80358292dbSNPEnsembl.1
Natural variantiVAR_063934342M → V in EVR1. 2 PublicationsCorresponds to variant rs80358293dbSNPEnsembl.1
Natural variantiVAR_063935370A → G in retinopathy of prematurity. 1 Publication1
Natural variantiVAR_063936417R → Q in EVR1; 48% loss of its wild-type activity; associated in a EVR4 patient with mutation CYS-444 in LPR5. 3 PublicationsCorresponds to variant rs80358294dbSNPEnsembl.1
Natural variantiVAR_036413436K → T in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_063937445T → P in EVR1. 1 PublicationCorresponds to variant rs80358297dbSNPEnsembl.1
Natural variantiVAR_063938488G → D in EVR1. 2 PublicationsCorresponds to variant rs80358298dbSNPEnsembl.1
Natural variantiVAR_017777493 – 494Missing in EVR1; loss of function. 3 Publications2
Natural variantiVAR_063939497S → F in EVR1. 1 PublicationCorresponds to variant rs80358300dbSNPEnsembl.1
Natural variantiVAR_063940525G → R in EVR1. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB032417 mRNA. Translation: BAA86286.1.
AY462097 mRNA. Translation: AAR23924.1.
AK292768 mRNA. Translation: BAF85457.1.
AP001528 Genomic DNA. No translation available.
BC114527 mRNA. Translation: AAI14528.1.
BC114622 mRNA. Translation: AAI14623.1.
CCDSiCCDS8279.1.
PIRiJC7127.
RefSeqiNP_036325.2. NM_012193.3.
UniGeneiHs.591968.

Genome annotation databases

EnsembliENST00000531380; ENSP00000434034; ENSG00000174804.
GeneIDi8322.
KEGGihsa:8322.
UCSCiuc001pce.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB032417 mRNA. Translation: BAA86286.1.
AY462097 mRNA. Translation: AAR23924.1.
AK292768 mRNA. Translation: BAF85457.1.
AP001528 Genomic DNA. No translation available.
BC114527 mRNA. Translation: AAI14528.1.
BC114622 mRNA. Translation: AAI14623.1.
CCDSiCCDS8279.1.
PIRiJC7127.
RefSeqiNP_036325.2. NM_012193.3.
UniGeneiHs.591968.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5BPBX-ray2.20A/B/C/D42-179[»]
5BPQX-ray2.40A/B/C/D42-179[»]
5BQCX-ray3.00B42-179[»]
5BQEX-ray2.30C42-179[»]
5CL1X-ray3.80C/D38-160[»]
5CM4X-ray2.40A/B40-164[»]
ProteinModelPortaliQ9ULV1.
SMRiQ9ULV1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113918. 4 interactors.
IntActiQ9ULV1. 8 interactors.
MINTiMINT-2822299.
STRINGi9606.ENSP00000434034.

Protein family/group databases

GPCRDBiSearch...

PTM databases

iPTMnetiQ9ULV1.
PhosphoSitePlusiQ9ULV1.

Polymorphism and mutation databases

BioMutaiFZD4.
DMDMi62298045.

Proteomic databases

MaxQBiQ9ULV1.
PaxDbiQ9ULV1.
PeptideAtlasiQ9ULV1.
PRIDEiQ9ULV1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000531380; ENSP00000434034; ENSG00000174804.
GeneIDi8322.
KEGGihsa:8322.
UCSCiuc001pce.4. human.

Organism-specific databases

CTDi8322.
DisGeNETi8322.
GeneCardsiFZD4.
GeneReviewsiFZD4.
HGNCiHGNC:4042. FZD4.
HPAiHPA042328.
MalaCardsiFZD4.
MIMi133780. phenotype.
604579. gene.
neXtProtiNX_Q9ULV1.
OpenTargetsiENSG00000174804.
Orphaneti891. Familial exudative vitreoretinopathy.
91495. Persistent hyperplastic primary vitreous.
90050. Retinopathy of prematurity.
PharmGKBiPA28459.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3577. Eukaryota.
ENOG410XRC8. LUCA.
GeneTreeiENSGT00760000118864.
HOGENOMiHOG000233236.
HOVERGENiHBG006977.
InParanoidiQ9ULV1.
KOiK02354.
OMAiSMCLSVK.
OrthoDBiEOG091G0N5M.
PhylomeDBiQ9ULV1.
TreeFamiTF317907.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000174804-MONOMER.
ReactomeiR-HSA-373080. Class B/2 (Secretin family receptors).
R-HSA-4086398. Ca2+ pathway.
R-HSA-4608870. Asymmetric localization of PCP proteins.
R-HSA-4641263. Regulation of FZD by ubiquitination.
R-HSA-5099900. WNT5A-dependent internalization of FZD4.
R-HSA-5340588. RNF mutants show enhanced WNT signaling and proliferation.
R-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-HSA-8856828. Clathrin-mediated endocytosis.
SignaLinkiQ9ULV1.
SIGNORiQ9ULV1.

Miscellaneous databases

GeneWikiiFZD4.
GenomeRNAii8322.
PROiQ9ULV1.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000174804.
CleanExiHS_FZD4.
GenevisibleiQ9ULV1. HS.

Family and domain databases

Gene3Di1.10.2000.10. 1 hit.
InterProiIPR000539. Frizzled.
IPR015526. Frizzled/SFRP.
IPR020067. Frizzled_dom.
IPR026551. FZD4.
IPR017981. GPCR_2-like.
[Graphical view]
PANTHERiPTHR11309. PTHR11309. 1 hit.
PTHR11309:SF23. PTHR11309:SF23. 1 hit.
PfamiPF01534. Frizzled. 1 hit.
PF01392. Fz. 1 hit.
[Graphical view]
PRINTSiPR00489. FRIZZLED.
SMARTiSM00063. FRI. 1 hit.
SM01330. Frizzled. 1 hit.
[Graphical view]
SUPFAMiSSF63501. SSF63501. 1 hit.
PROSITEiPS50038. FZ. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFZD4_HUMAN
AccessioniPrimary (citable) accession number: Q9ULV1
Secondary accession number(s): A8K9Q3, Q14C97, Q6S9E4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: March 29, 2005
Last modified: November 30, 2016
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  3. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  8. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.