PYGO1_MOUSE
ID PYGO1_MOUSE Reviewed; 417 AA.
AC Q9D0P5;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Pygopus homolog 1;
GN Name=Pygo1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- FUNCTION: Involved in signal transduction through the Wnt pathway.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with BCL9 via The PHD-type zinc finger motiv, and
CC thereby becomes part of the nuclear beta-catenin/TCF complex. Found in
CC a complex with BCL9L, CDC73, CTNNB1 and PYGO1. Interacts with histone
CC H3 mono-, di- or tri-methylated at 'Lys4' (H3K4me1, H3K4me2, H3K4me3);
CC the interaction is enhanced by the interaction with BCL9 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9D0P5; Q9W0N9: ebd1; Xeno; NbExp=3; IntAct=EBI-8607760, EBI-141287;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR EMBL; AK011208; BAB27468.1; -; mRNA.
DR CCDS; CCDS23332.1; -.
DR RefSeq; NP_082392.1; NM_028116.2.
DR PDB; 2DX8; X-ray; 2.70 A; A/B=330-396.
DR PDB; 2YYR; X-ray; 2.50 A; A/B=330-396.
DR PDBsum; 2DX8; -.
DR PDBsum; 2YYR; -.
DR AlphaFoldDB; Q9D0P5; -.
DR SMR; Q9D0P5; -.
DR BioGRID; 215174; 6.
DR IntAct; Q9D0P5; 9.
DR MINT; Q9D0P5; -.
DR STRING; 10090.ENSMUSP00000044368; -.
DR iPTMnet; Q9D0P5; -.
DR PhosphoSitePlus; Q9D0P5; -.
DR PaxDb; Q9D0P5; -.
DR PRIDE; Q9D0P5; -.
DR ProteomicsDB; 301984; -.
DR Antibodypedia; 25101; 164 antibodies from 23 providers.
DR Ensembl; ENSMUST00000038489; ENSMUSP00000044368; ENSMUSG00000034910.
DR GeneID; 72135; -.
DR KEGG; mmu:72135; -.
DR UCSC; uc009qqi.1; mouse.
DR CTD; 26108; -.
DR MGI; MGI:1919385; Pygo1.
DR VEuPathDB; HostDB:ENSMUSG00000034910; -.
DR eggNOG; ENOG502QTIZ; Eukaryota.
DR GeneTree; ENSGT00530000063948; -.
DR HOGENOM; CLU_686883_0_0_1; -.
DR InParanoid; Q9D0P5; -.
DR OMA; YNTFRMP; -.
DR OrthoDB; 919773at2759; -.
DR PhylomeDB; Q9D0P5; -.
DR TreeFam; TF333020; -.
DR Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex.
DR BioGRID-ORCS; 72135; 2 hits in 75 CRISPR screens.
DR EvolutionaryTrace; Q9D0P5; -.
DR PRO; PR:Q9D0P5; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9D0P5; protein.
DR Bgee; ENSMUSG00000034910; Expressed in cortical plate and 116 other tissues.
DR ExpressionAtlas; Q9D0P5; baseline and differential.
DR Genevisible; Q9D0P5; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; ISO:MGI.
DR GO; GO:0048856; P:anatomical structure development; IGI:MGI.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IGI:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IGI:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0034504; P:protein localization to nucleus; IDA:MGI.
DR GO; GO:0007286; P:spermatid development; IGI:MGI.
DR GO; GO:0007289; P:spermatid nucleus differentiation; IGI:MGI.
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; Metal-binding; Nucleus; Reference proteome;
KW Wnt signaling pathway; Zinc; Zinc-finger.
FT CHAIN 1..417
FT /note="Pygopus homolog 1"
FT /id="PRO_0000097122"
FT ZN_FING 338..396
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..386
FT /note="Interaction with H3K4me2"
FT /evidence="ECO:0000250"
FT REGION 371..389
FT /note="Interaction with BCL9"
FT /evidence="ECO:0000250"
FT MOTIF 35..41
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 175..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:2YYR"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:2YYR"
FT TURN 358..361
FT /evidence="ECO:0007829|PDB:2YYR"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:2YYR"
FT HELIX 367..370
FT /evidence="ECO:0007829|PDB:2YYR"
FT HELIX 374..382
FT /evidence="ECO:0007829|PDB:2YYR"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:2YYR"
FT HELIX 391..394
FT /evidence="ECO:0007829|PDB:2YYR"
SQ SEQUENCE 417 AA; 45090 MW; 614023BD83221F86 CRC64;
MSAEQDKEPI ALKRVRGGDS GLDGLGGPNI QLGSPDKKKR KANTQGSSFP PLSEYAPPPN
PNSDHLVAAN PFDDSYNTIS YKPLPSSNPY LGPGYPGFGG YSTFRMPPHV PPRMSSPYCG
PYSLRNQPHP FPQNPLGMGF NRPHAFNFGP HDNSNFGNPP YNNVLTQDIN MPGQHFRQGS
AENFSQIPPQ NVGQVSNPDL ASNFAPGNNS NFTSPLETNH SFIPPPNAFG QAKAPLPKQD
FTQGATKTPN QNSSTHPPHL NMEDPVNQSN VELKNVNRNN VVQENSRSGS AEATNNHANG
TQNKPRQPRG AADLCTPDKS RKFSLLPSRH GHSSSDPVYP CGICTNEVND DQDAILCEAS
CQKWFHRICT GMTETAYGLL TAEASAVWGC DTCMADKDVQ LMRTREAFGP PAVGGDA
