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Q9UP38

- FZD1_HUMAN

UniProt

Q9UP38 - FZD1_HUMAN

Protein

Frizzled-1

Gene

FZD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (07 Mar 2006)
      Previous versions | rss
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    Functioni

    Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. 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. Activated by Wnt3A, Wnt3, Wnt1 and to a lesser extent Wnt2, but not by Wnt4, Wnt5A, Wnt5B, Wnt6, Wnt7A or Wnt7B.

    GO - Molecular functioni

    1. frizzled binding Source: UniProtKB
    2. G-protein coupled receptor activity Source: UniProtKB-KW
    3. PDZ domain binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. receptor binding Source: BHF-UCL
    6. Wnt-activated receptor activity Source: BHF-UCL
    7. Wnt-protein binding Source: UniProtKB

    GO - Biological processi

    1. autocrine signaling Source: BHF-UCL
    2. axonogenesis Source: RefGenome
    3. brain development Source: RefGenome
    4. canonical Wnt signaling pathway Source: UniProtKB
    5. canonical Wnt signaling pathway involved in mesenchymal stem cell differentiation Source: BHF-UCL
    6. canonical Wnt signaling pathway involved in osteoblast differentiation Source: BHF-UCL
    7. cell-cell signaling Source: BHF-UCL
    8. epithelial cell differentiation Source: RefGenome
    9. gonad development Source: RefGenome
    10. G-protein coupled receptor signaling pathway coupled to cGMP nucleotide second messenger Source: RefGenome
    11. hard palate development Source: Ensembl
    12. lung alveolus development Source: RefGenome
    13. membranous septum morphogenesis Source: Ensembl
    14. muscular septum morphogenesis Source: Ensembl
    15. negative regulation of BMP signaling pathway Source: RefGenome
    16. negative regulation of canonical Wnt signaling pathway Source: RefGenome
    17. negative regulation of catenin import into nucleus Source: Ensembl
    18. negative regulation of transcription, DNA-templated Source: Ensembl
    19. neuron differentiation Source: UniProtKB
    20. outflow tract morphogenesis Source: Ensembl
    21. planar cell polarity pathway involved in neural tube closure Source: Ensembl
    22. positive regulation of protein phosphorylation Source: Ensembl
    23. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    24. positive regulation of transcription, DNA-templated Source: BHF-UCL
    25. response to drug Source: BHF-UCL
    26. vasculature development Source: RefGenome
    27. Wnt signaling pathway, calcium modulating pathway Source: RefGenome

    Keywords - Molecular functioni

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

    Keywords - Biological processi

    Wnt signaling pathway

    Enzyme and pathway databases

    ReactomeiREACT_172581. PCP/CE pathway.
    REACT_18372. Class B/2 (Secretin family receptors).
    REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_200777. TCF dependent signaling in response to WNT.
    SignaLinkiQ9UP38.

    Protein family/group databases

    MEROPSiI93.001.
    TCDBi9.A.14.16.1. the g-protein-coupled receptor (gpcr) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Frizzled-1
    Short name:
    Fz-1
    Short name:
    hFz1
    Alternative name(s):
    FzE1
    Gene namesi
    Name:FZD1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:4038. FZD1.

    Subcellular locationi

    GO - Cellular componenti

    1. apical part of cell Source: RefGenome
    2. cell surface Source: BHF-UCL
    3. cytoplasm Source: RefGenome
    4. integral component of membrane Source: UniProtKB-KW
    5. neuron projection membrane Source: RefGenome
    6. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28455.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 6969Sequence AnalysisAdd
    BLAST
    Chaini70 – 647578Frizzled-1PRO_0000012973Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi116 ↔ 177PROSITE-ProRule annotation
    Disulfide bondi124 ↔ 170PROSITE-ProRule annotation
    Glycosylationi130 – 1301N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi161 ↔ 198PROSITE-ProRule annotation
    Disulfide bondi187 ↔ 227PROSITE-ProRule annotation
    Disulfide bondi191 ↔ 215PROSITE-ProRule annotation
    Glycosylationi231 – 2311N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Ubiquitinated by ZNRF3, leading to its degradation by the proteasome.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9UP38.
    PaxDbiQ9UP38.
    PRIDEiQ9UP38.

    PTM databases

    PhosphoSiteiQ9UP38.

    Expressioni

    Tissue specificityi

    Expressed in adult heart, placenta, lung, kidney, pancreas, prostate, and ovary and in fetal lung and kidney.

    Gene expression databases

    BgeeiQ9UP38.
    CleanExiHS_FZD1.
    GenevestigatoriQ9UP38.

    Organism-specific databases

    HPAiCAB013008.

    Interactioni

    Subunit structurei

    Interacts with MYOC.1 Publication

    Protein-protein interaction databases

    BioGridi113917. 5 interactions.
    IntActiQ9UP38. 2 interactions.
    STRINGi9606.ENSP00000287934.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UP38.
    SMRiQ9UP38. Positions 116-222, 296-638.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini73 – 322250ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini344 – 35411CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini376 – 40227ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini424 – 44522CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini467 – 48923ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini511 – 53626CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini558 – 60144ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini623 – 64725CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei323 – 34321Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei355 – 37521Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei403 – 42321Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei446 – 46621Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei490 – 51021Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei537 – 55721Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei602 – 62221Helical; Name=7Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini111 – 230120FZPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi625 – 6306Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family membersBy similarity
    Motifi645 – 6473PDZ-binding

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi89 – 935Poly-Pro

    Domaini

    Lys-Thr-X-X-X-Trp motif interacts with the PDZ doman 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

    eggNOGiNOG257258.
    HOGENOMiHOG000233236.
    HOVERGENiHBG006977.
    InParanoidiQ9UP38.
    KOiK02432.
    OMAiHGAGELC.
    OrthoDBiEOG7M3J01.
    PhylomeDBiQ9UP38.
    TreeFamiTF317907.

    Family and domain databases

    Gene3Di1.10.2000.10. 1 hit.
    InterProiIPR000539. Frizzled.
    IPR015526. Frizzled/SFRP.
    IPR020067. Frizzled_dom.
    IPR026548. FZD1.
    IPR017981. GPCR_2-like.
    [Graphical view]
    PANTHERiPTHR11309. PTHR11309. 1 hit.
    PTHR11309:SF81. PTHR11309:SF81. 1 hit.
    PfamiPF01534. Frizzled. 1 hit.
    PF01392. Fz. 1 hit.
    [Graphical view]
    PRINTSiPR00489. FRIZZLED.
    SMARTiSM00063. FRI. 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.

    Q9UP38-1 [UniParc]FASTAAdd to Basket

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    MAEEEAPKKS RAAGGGASWE LCAGALSARL AEEGSGDAGG RRRPPVDPRR    50
    LARQLLLLLW LLEAPLLLGV RAQAAGQGPG QGPGPGQQPP PPPQQQQSGQ 100
    QYNGERGISV PDHGYCQPIS IPLCTDIAYN QTIMPNLLGH TNQEDAGLEV 150
    HQFYPLVKVQ CSAELKFFLC SMYAPVCTVL EQALPPCRSL CERARQGCEA 200
    LMNKFGFQWP DTLKCEKFPV HGAGELCVGQ NTSDKGTPTP SLLPEFWTSN 250
    PQHGGGGHRG GFPGGAGASE RGKFSCPRAL KVPSYLNYHF LGEKDCGAPC 300
    EPTKVYGLMY FGPEELRFSR TWIGIWSVLC CASTLFTVLT YLVDMRRFSY 350
    PERPIIFLSG CYTAVAVAYI AGFLLEDRVV CNDKFAEDGA RTVAQGTKKE 400
    GCTILFMMLY FFSMASSIWW VILSLTWFLA AGMKWGHEAI EANSQYFHLA 450
    AWAVPAIKTI TILALGQVDG DVLSGVCFVG LNNVDALRGF VLAPLFVYLF 500
    IGTSFLLAGF VSLFRIRTIM KHDGTKTEKL EKLMVRIGVF SVLYTVPATI 550
    VIACYFYEQA FRDQWERSWV AQSCKSYAIP CPHLQAGGGA PPHPPMSPDF 600
    TVFMIKYLMT LIVGITSGFW IWSGKTLNSW RKFYTRLTNS KQGETTV 647
    Length:647
    Mass (Da):71,158
    Last modified:March 7, 2006 - v2
    Checksum:i7FC916A736482826
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti93 – 931P → PP in AAD41636. (PubMed:10557084)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti343 – 3431V → M.
    Corresponds to variant rs3750146 [ dbSNP | Ensembl ].
    VAR_049290

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF072872 mRNA. Translation: AAD41636.1.
    AB017363 mRNA. Translation: BAA34666.1.
    AC084381 Genomic DNA. Translation: AAS02008.1.
    CH236949 Genomic DNA. Translation: EAL24161.1.
    CH471091 Genomic DNA. Translation: EAW76871.1.
    BC051271 mRNA. Translation: AAH51271.1.
    CCDSiCCDS5620.1.
    PIRiJE0337.
    RefSeqiNP_003496.1. NM_003505.1.
    UniGeneiHs.94234.

    Genome annotation databases

    EnsembliENST00000287934; ENSP00000287934; ENSG00000157240.
    GeneIDi8321.
    KEGGihsa:8321.
    UCSCiuc003ula.3. human.

    Polymorphism databases

    DMDMi92058705.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF072872 mRNA. Translation: AAD41636.1 .
    AB017363 mRNA. Translation: BAA34666.1 .
    AC084381 Genomic DNA. Translation: AAS02008.1 .
    CH236949 Genomic DNA. Translation: EAL24161.1 .
    CH471091 Genomic DNA. Translation: EAW76871.1 .
    BC051271 mRNA. Translation: AAH51271.1 .
    CCDSi CCDS5620.1.
    PIRi JE0337.
    RefSeqi NP_003496.1. NM_003505.1.
    UniGenei Hs.94234.

    3D structure databases

    ProteinModelPortali Q9UP38.
    SMRi Q9UP38. Positions 116-222, 296-638.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113917. 5 interactions.
    IntActi Q9UP38. 2 interactions.
    STRINGi 9606.ENSP00000287934.

    Chemistry

    ChEMBLi CHEMBL2346493.
    GuidetoPHARMACOLOGYi 229.

    Protein family/group databases

    MEROPSi I93.001.
    TCDBi 9.A.14.16.1. the g-protein-coupled receptor (gpcr) family.
    GPCRDBi Search...

    PTM databases

    PhosphoSitei Q9UP38.

    Polymorphism databases

    DMDMi 92058705.

    Proteomic databases

    MaxQBi Q9UP38.
    PaxDbi Q9UP38.
    PRIDEi Q9UP38.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000287934 ; ENSP00000287934 ; ENSG00000157240 .
    GeneIDi 8321.
    KEGGi hsa:8321.
    UCSCi uc003ula.3. human.

    Organism-specific databases

    CTDi 8321.
    GeneCardsi GC07P090893.
    HGNCi HGNC:4038. FZD1.
    HPAi CAB013008.
    MIMi 603408. gene.
    neXtProti NX_Q9UP38.
    PharmGKBi PA28455.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG257258.
    HOGENOMi HOG000233236.
    HOVERGENi HBG006977.
    InParanoidi Q9UP38.
    KOi K02432.
    OMAi HGAGELC.
    OrthoDBi EOG7M3J01.
    PhylomeDBi Q9UP38.
    TreeFami TF317907.

    Enzyme and pathway databases

    Reactomei REACT_172581. PCP/CE pathway.
    REACT_18372. Class B/2 (Secretin family receptors).
    REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_200777. TCF dependent signaling in response to WNT.
    SignaLinki Q9UP38.

    Miscellaneous databases

    GeneWikii FZD1.
    GenomeRNAii 8321.
    NextBioi 31159.
    PROi Q9UP38.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9UP38.
    CleanExi HS_FZD1.
    Genevestigatori Q9UP38.

    Family and domain databases

    Gene3Di 1.10.2000.10. 1 hit.
    InterProi IPR000539. Frizzled.
    IPR015526. Frizzled/SFRP.
    IPR020067. Frizzled_dom.
    IPR026548. FZD1.
    IPR017981. GPCR_2-like.
    [Graphical view ]
    PANTHERi PTHR11309. PTHR11309. 1 hit.
    PTHR11309:SF81. PTHR11309:SF81. 1 hit.
    Pfami PF01534. Frizzled. 1 hit.
    PF01392. Fz. 1 hit.
    [Graphical view ]
    PRINTSi PR00489. FRIZZLED.
    SMARTi SM00063. FRI. 1 hit.
    [Graphical view ]
    SUPFAMi SSF63501. SSF63501. 1 hit.
    PROSITEi PS50038. FZ. 1 hit.
    PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human frizzled 1 interacts with transforming Wnts to transduce a TCF dependent transcriptional response."
      Gazit A., Yaniv A., Bafico A., Pramila T., Igarashi M., Kitajewski J., Aaronson S.A.
      Oncogene 18:5959-5966(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Prostatic carcinoma.
    2. "Molecular cloning, differential expression, and chromosomal localization of human frizzled-1, frizzled-2, and frizzled-7."
      Sagara N., Toda G., Hirai M., Terada M., Katoh M.
      Biochem. Biophys. Res. Commun. 252:117-122(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fetal lung.
    3. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Eye.
    7. "A novel frizzled gene identified in human esophageal carcinoma mediates APC/beta-catenin signals."
      Tanaka S., Akiyoshi T., Mori M., Wands J.R., Sugimachi K.
      Proc. Natl. Acad. Sci. U.S.A. 95:10164-10169(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 357-418.
      Tissue: Esophageal carcinoma.
    8. Cited for: INTERACTION WITH MYOC.

    Entry informationi

    Entry nameiFZD1_HUMAN
    AccessioniPrimary (citable) accession number: Q9UP38
    Secondary accession number(s): A4D1E8, O94815, Q549T8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 5, 2001
    Last sequence update: March 7, 2006
    Last modified: October 1, 2014
    This is version 131 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

    Complete proteome, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3