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   27-MAR-2024, entry version 178.
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   PDB; 8HIB; X-ray; 2.45 A; D=59-84.
DR   PDBsum; 2XB1; -.
DR   PDBsum; 4UP0; -.
DR   PDBsum; 4UP5; -.
DR   PDBsum; 8HIB; -.
DR   AlphaFoldDB; Q9BRQ0; -.
DR   SMR; Q9BRQ0; -.
DR   BioGRID; 124760; 48.
DR   IntAct; Q9BRQ0; 31.
DR   MINT; Q9BRQ0; -.
DR   STRING; 9606.ENSP00000357442; -.
DR   GlyGen; Q9BRQ0; 1 site, 1 O-linked glycan (1 site).
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; 9606-ENSP00000357442; -.
DR   PeptideAtlas; Q9BRQ0; -.
DR   ProteomicsDB; 78801; -.
DR   Pumba; Q9BRQ0; -.
DR   Antibodypedia; 20404; 186 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   AGR; HGNC:30257; -.
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; GGMVFPC; -.
DR   OrthoDB; 5403712at2759; -.
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   SIGNOR; Q9BRQ0; -.
DR   BioGRID-ORCS; 90780; 23 hits in 1165 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 177 other cell types or tissues.
DR   ExpressionAtlas; Q9BRQ0; baseline and differential.
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: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   CDD; cd15636; PHD_PYGO2; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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   PANTHER; PTHR23194; PYGOPUS; 1.
DR   PANTHER; PTHR23194:SF7; PYGOPUS HOMOLOG 2; 1.
DR   Pfam; PF00628; PHD; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
DR   Genevisible; Q9BRQ0; HS.
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
//