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Q9BRQ0

- PYGO2_HUMAN

UniProt

Q9BRQ0 - PYGO2_HUMAN

Protein

Pygopus homolog 2

Gene

PYGO2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (19 Sep 2002)
      Previous versions | rss
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    Functioni

    Involved in signal transduction through the Wnt pathway.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri327 – 38559PHD-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. brain development Source: Ensembl
    2. canonical Wnt signaling pathway Source: Ensembl
    3. developmental growth Source: Ensembl
    4. in utero embryonic development Source: Ensembl
    5. kidney development Source: Ensembl
    6. lens development in camera-type eye Source: Ensembl
    7. mammary gland development Source: Ensembl
    8. palate development Source: Ensembl
    9. post-embryonic development Source: Ensembl
    10. regulation of histone H3-K4 methylation Source: Ensembl
    11. regulation of mammary gland epithelial cell proliferation Source: Ensembl

    Keywords - Biological processi

    Wnt signaling pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_200731. deactivation of the beta-catenin transactivating complex.
    REACT_200753. formation of the beta-catenin:TCF transactivating complex.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pygopus homolog 2
    Gene namesi
    Name:PYGO2
    ORF Names:PP7910
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:30257. PYGO2.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134881185.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 406405Pygopus homolog 2PRO_0000097123Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei40 – 401Phosphoserine1 Publication
    Modified residuei302 – 3021Phosphothreonine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9BRQ0.
    PaxDbiQ9BRQ0.
    PRIDEiQ9BRQ0.

    PTM databases

    PhosphoSiteiQ9BRQ0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9BRQ0.
    BgeeiQ9BRQ0.
    CleanExiHS_PYGO2.
    GenevestigatoriQ9BRQ0.

    Organism-specific databases

    HPAiHPA023689.

    Interactioni

    Subunit structurei

    Binds to BCL9 via the PHD-type zinc finger motif, and thereby becomes part of the nuclear beta-catenin/TCF complex.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BCL9O005122EBI-932471,EBI-533127

    Protein-protein interaction databases

    BioGridi124760. 13 interactions.
    IntActiQ9BRQ0. 3 interactions.
    MINTiMINT-8177751.
    STRINGi9606.ENSP00000357442.

    Structurei

    Secondary structure

    1
    406
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni331 – 3333
    Beta strandi343 – 3453
    Turni347 – 3504
    Beta strandi353 – 3553
    Helixi356 – 3583
    Helixi363 – 3719
    Beta strandi375 – 3773
    Helixi380 – 3845
    Turni385 – 3873

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2XB1X-ray1.90A/C325-387[»]
    ProteinModelPortaliQ9BRQ0.
    SMRiQ9BRQ0. Positions 325-393.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi41 – 477Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi6 – 329324Pro-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri327 – 38559PHD-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG72798.
    HOGENOMiHOG000001580.
    HOVERGENiHBG053774.
    InParanoidiQ9BRQ0.
    OMAiPGLVYPC.
    OrthoDBiEOG79W952.
    PhylomeDBiQ9BRQ0.
    TreeFamiTF333020.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR019786. Zinc_finger_PHD-type_CS.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF00628. PHD. 1 hit.
    [Graphical view]
    SMARTiSM00249. PHD. 1 hit.
    [Graphical view]
    SUPFAMiSSF57903. SSF57903. 1 hit.
    PROSITEiPS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9BRQ0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAASAPPPPD KLEGGGGPAP PPAPPSTGRK QGKAGLQMKS PEKKRRKSNT    50
    QGPAYSHLTE FAPPPTPMVD HLVASNPFED DFGAPKVGVA APPFLGSPVP 100
    FGGFRVQGGM AGQVPPGYST GGGGGPQPLR RQPPPFPPNP MGPAFNMPPQ 150
    GPGYPPPGNM NFPSQPFNQP LGQNFSPPSG QMMPGPVGGF GPMISPTMGQ 200
    PPRAELGPPS LSQRFAQPGA PFGPSPLQRP GQGLPSLPPN TSPFPGPDPG 250
    FPGPGGEDGG KPLNPPASTA FPQEPHSGSP AAAVNGNQPS FPPNSSGRGG 300
    GTPDANSLAP PGKAGGGSGP QPPPGLVYPC GACRSEVNDD QDAILCEASC 350
    QKWFHRECTG MTESAYGLLT TEASAVWACD LCLKTKEIQS VYIREGMGQL 400
    VAANDG 406
    Length:406
    Mass (Da):41,244
    Last modified:September 19, 2002 - v2
    Checksum:iCA002A5447767CD9
    GO

    Sequence cautioni

    The sequence AAL55782.1 differs from that shown. Reason: Sequencing errors.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti157 – 1571P → Q in AAL55782. (PubMed:15498874)Curated
    Sequence conflicti170 – 1701P → L in AAL55782. (PubMed:15498874)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF457208 mRNA. Translation: AAL91371.1.
    BC006132 mRNA. Translation: AAH06132.2.
    BC013725 mRNA. Translation: AAH13725.1.
    BC032099 mRNA. Translation: AAH32099.1.
    AF289598 mRNA. Translation: AAL55782.1. Sequence problems.
    CCDSiCCDS1075.1.
    RefSeqiNP_612157.1. NM_138300.3.
    UniGeneiHs.533597.

    Genome annotation databases

    EnsembliENST00000368457; ENSP00000357442; ENSG00000163348.
    GeneIDi90780.
    KEGGihsa:90780.
    UCSCiuc001fft.3. human.

    Polymorphism databases

    DMDMi23396825.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF457208 mRNA. Translation: AAL91371.1 .
    BC006132 mRNA. Translation: AAH06132.2 .
    BC013725 mRNA. Translation: AAH13725.1 .
    BC032099 mRNA. Translation: AAH32099.1 .
    AF289598 mRNA. Translation: AAL55782.1 . Sequence problems.
    CCDSi CCDS1075.1.
    RefSeqi NP_612157.1. NM_138300.3.
    UniGenei Hs.533597.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2XB1 X-ray 1.90 A/C 325-387 [» ]
    ProteinModelPortali Q9BRQ0.
    SMRi Q9BRQ0. Positions 325-393.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124760. 13 interactions.
    IntActi Q9BRQ0. 3 interactions.
    MINTi MINT-8177751.
    STRINGi 9606.ENSP00000357442.

    PTM databases

    PhosphoSitei Q9BRQ0.

    Polymorphism databases

    DMDMi 23396825.

    Proteomic databases

    MaxQBi Q9BRQ0.
    PaxDbi Q9BRQ0.
    PRIDEi Q9BRQ0.

    Protocols and materials databases

    DNASUi 90780.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368457 ; ENSP00000357442 ; ENSG00000163348 .
    GeneIDi 90780.
    KEGGi hsa:90780.
    UCSCi uc001fft.3. human.

    Organism-specific databases

    CTDi 90780.
    GeneCardsi GC01M154929.
    HGNCi HGNC:30257. PYGO2.
    HPAi HPA023689.
    MIMi 606903. gene.
    neXtProti NX_Q9BRQ0.
    PharmGKBi PA134881185.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG72798.
    HOGENOMi HOG000001580.
    HOVERGENi HBG053774.
    InParanoidi Q9BRQ0.
    OMAi PGLVYPC.
    OrthoDBi EOG79W952.
    PhylomeDBi Q9BRQ0.
    TreeFami TF333020.

    Enzyme and pathway databases

    Reactomei REACT_200731. deactivation of the beta-catenin transactivating complex.
    REACT_200753. formation of the beta-catenin:TCF transactivating complex.

    Miscellaneous databases

    GeneWikii PYGO2.
    GenomeRNAii 90780.
    NextBioi 76956.
    PROi Q9BRQ0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BRQ0.
    Bgeei Q9BRQ0.
    CleanExi HS_PYGO2.
    Genevestigatori Q9BRQ0.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR019786. Zinc_finger_PHD-type_CS.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF00628. PHD. 1 hit.
    [Graphical view ]
    SMARTi SM00249. PHD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57903. SSF57903. 1 hit.
    PROSITEi PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Wnt/wingless signaling requires BCL9/legless-mediated recruitment of pygopus to the nuclear beta-catenin-TCF complex."
      Kramps T., Peter O., Brunner E., Nellen D., Froesch B., Chatterjee S., Murone M., Zuellig S., Basler K.
      Cell 109:47-60(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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: Brain and Ovary.
    3. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
      Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
      , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
      Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-406.
    4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-302, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    5. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    6. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-302, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPYGO2_HUMAN
    AccessioniPrimary (citable) accession number: Q9BRQ0
    Secondary accession number(s): Q8WYZ4, Q96CY2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2002
    Last sequence update: September 19, 2002
    Last modified: October 1, 2014
    This is version 113 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. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3