PYGO2_HUMAN
ID PYGO2_HUMAN Reviewed; 406 AA.
AC Q9BRQ0; Q8WYZ4; Q96CY2;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Pygopus homolog 2;
GN Name=PYGO2; ORFNames=PP7910;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11955446; DOI=10.1016/s0092-8674(02)00679-7;
RA Kramps T., Peter O., Brunner E., Nellen D., Froesch B., Chatterjee S.,
RA Murone M., Zuellig S., Basler K.;
RT "Wnt/wingless signaling requires BCL9/legless-mediated recruitment of
RT pygopus to the nuclear beta-catenin-TCF complex.";
RL Cell 109:47-60(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-406.
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-302, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-302, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40 AND THR-302, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-302, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Involved in signal transduction through the Wnt pathway.
CC -!- SUBUNIT: Binds to BCL9 via the PHD-type zinc finger motif, and thereby
CC becomes part of the nuclear beta-catenin/TCF complex.
CC -!- INTERACTION:
CC Q9BRQ0; O00512: BCL9; NbExp=3; IntAct=EBI-932471, EBI-533127;
CC Q9BRQ0; Q9UPU3: SORCS3; NbExp=3; IntAct=EBI-932471, EBI-7484437;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL55782.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AF457208; AAL91371.1; -; mRNA.
DR EMBL; BC006132; AAH06132.2; -; mRNA.
DR EMBL; BC013725; AAH13725.1; -; mRNA.
DR EMBL; BC032099; AAH32099.1; -; mRNA.
DR EMBL; AF289598; AAL55782.1; ALT_SEQ; mRNA.
DR CCDS; CCDS1075.1; -.
DR RefSeq; NP_612157.1; NM_138300.3.
DR PDB; 2XB1; X-ray; 1.90 A; A/C=325-387.
DR PDB; 4UP0; X-ray; 1.28 A; A=327-387.
DR PDB; 4UP5; X-ray; 1.65 A; A=327-387.
DR PDBsum; 2XB1; -.
DR PDBsum; 4UP0; -.
DR PDBsum; 4UP5; -.
DR AlphaFoldDB; Q9BRQ0; -.
DR SMR; Q9BRQ0; -.
DR BioGRID; 124760; 46.
DR IntAct; Q9BRQ0; 32.
DR MINT; Q9BRQ0; -.
DR STRING; 9606.ENSP00000357442; -.
DR iPTMnet; Q9BRQ0; -.
DR PhosphoSitePlus; Q9BRQ0; -.
DR BioMuta; PYGO2; -.
DR DMDM; 23396825; -.
DR EPD; Q9BRQ0; -.
DR jPOST; Q9BRQ0; -.
DR MassIVE; Q9BRQ0; -.
DR MaxQB; Q9BRQ0; -.
DR PaxDb; Q9BRQ0; -.
DR PeptideAtlas; Q9BRQ0; -.
DR PRIDE; Q9BRQ0; -.
DR ProteomicsDB; 78801; -.
DR Antibodypedia; 20404; 161 antibodies from 33 providers.
DR DNASU; 90780; -.
DR Ensembl; ENST00000368457.3; ENSP00000357442.2; ENSG00000163348.4.
DR GeneID; 90780; -.
DR KEGG; hsa:90780; -.
DR MANE-Select; ENST00000368457.3; ENSP00000357442.2; NM_138300.4; NP_612157.1.
DR UCSC; uc001fft.4; human.
DR CTD; 90780; -.
DR DisGeNET; 90780; -.
DR GeneCards; PYGO2; -.
DR HGNC; HGNC:30257; PYGO2.
DR HPA; ENSG00000163348; Low tissue specificity.
DR MIM; 606903; gene.
DR neXtProt; NX_Q9BRQ0; -.
DR OpenTargets; ENSG00000163348; -.
DR PharmGKB; PA134881185; -.
DR VEuPathDB; HostDB:ENSG00000163348; -.
DR eggNOG; ENOG502QSRS; Eukaryota.
DR GeneTree; ENSGT00530000063948; -.
DR InParanoid; Q9BRQ0; -.
DR OMA; GNFRMQG; -.
DR OrthoDB; 919773at2759; -.
DR PhylomeDB; Q9BRQ0; -.
DR TreeFam; TF333020; -.
DR PathwayCommons; Q9BRQ0; -.
DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
DR SignaLink; Q9BRQ0; -.
DR BioGRID-ORCS; 90780; 21 hits in 1088 CRISPR screens.
DR ChiTaRS; PYGO2; human.
DR GeneWiki; PYGO2; -.
DR GenomeRNAi; 90780; -.
DR Pharos; Q9BRQ0; Tbio.
DR PRO; PR:Q9BRQ0; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BRQ0; protein.
DR Bgee; ENSG00000163348; Expressed in kidney epithelium and 175 other tissues.
DR ExpressionAtlas; Q9BRQ0; baseline and differential.
DR Genevisible; Q9BRQ0; HS.
DR GO; GO:1990907; C:beta-catenin-TCF complex; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0035034; F:histone acetyltransferase regulator activity; IEA:Ensembl.
DR GO; GO:0042393; F:histone binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0048589; P:developmental growth; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IBA:GO_Central.
DR GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl.
DR GO; GO:0030879; P:mammary gland development; IEA:Ensembl.
DR GO; GO:0035563; P:positive regulation of chromatin binding; IEA:Ensembl.
DR GO; GO:0051569; P:regulation of histone H3-K4 methylation; IEA:Ensembl.
DR GO; GO:0033599; P:regulation of mammary gland epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
DR GO; GO:0007289; P:spermatid nucleus differentiation; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Wnt signaling pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..406
FT /note="Pygopus homolog 2"
FT /id="PRO_0000097123"
FT ZN_FING 327..385
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 41..47
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 11..27
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..163
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..252
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 302
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT CONFLICT 157
FT /note="P -> Q (in Ref. 3; AAL55782)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="P -> L (in Ref. 3; AAL55782)"
FT /evidence="ECO:0000305"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:4UP0"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:4UP0"
FT TURN 347..350
FT /evidence="ECO:0007829|PDB:4UP0"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:4UP0"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:4UP0"
FT HELIX 363..371
FT /evidence="ECO:0007829|PDB:4UP0"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:4UP0"
FT HELIX 380..384
FT /evidence="ECO:0007829|PDB:2XB1"
FT TURN 385..387
FT /evidence="ECO:0007829|PDB:2XB1"
SQ SEQUENCE 406 AA; 41244 MW; CA002A5447767CD9 CRC64;
MAASAPPPPD KLEGGGGPAP PPAPPSTGRK QGKAGLQMKS PEKKRRKSNT QGPAYSHLTE
FAPPPTPMVD HLVASNPFED DFGAPKVGVA APPFLGSPVP FGGFRVQGGM AGQVPPGYST
GGGGGPQPLR RQPPPFPPNP MGPAFNMPPQ GPGYPPPGNM NFPSQPFNQP LGQNFSPPSG
QMMPGPVGGF GPMISPTMGQ PPRAELGPPS LSQRFAQPGA PFGPSPLQRP GQGLPSLPPN
TSPFPGPDPG FPGPGGEDGG KPLNPPASTA FPQEPHSGSP AAAVNGNQPS FPPNSSGRGG
GTPDANSLAP PGKAGGGSGP QPPPGLVYPC GACRSEVNDD QDAILCEASC QKWFHRECTG
MTESAYGLLT TEASAVWACD LCLKTKEIQS VYIREGMGQL VAANDG
