GenomeNet

Database: UniProt
Entry: B5DFG8_RAT
LinkDB: B5DFG8_RAT
Original site: B5DFG8_RAT 
ID   B5DFG8_RAT              Unreviewed;       405 AA.
AC   B5DFG8;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   SubName: Full=Pygopus family PHD finger 2 {ECO:0000313|Ensembl:ENSRNOP00000028052.4};
GN   Name=Pygo2 {ECO:0000313|Ensembl:ENSRNOP00000028052.4,
GN   ECO:0000313|RGD:1308535};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000028052.4, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000028052.4, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000028052.4,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0007829|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000028052.4}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000028052.4};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Involved in signal transduction through the Wnt pathway.
CC       {ECO:0000256|ARBA:ARBA00037400}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   RefSeq; NP_001099917.1; NM_001106447.1.
DR   AlphaFoldDB; B5DFG8; -.
DR   SMR; B5DFG8; -.
DR   STRING; 10116.ENSRNOP00000028052; -.
DR   PhosphoSitePlus; B5DFG8; -.
DR   PaxDb; 10116-ENSRNOP00000028052; -.
DR   Ensembl; ENSRNOT00000028052.5; ENSRNOP00000028052.4; ENSRNOG00000020663.5.
DR   GeneID; 295251; -.
DR   KEGG; rno:295251; -.
DR   UCSC; RGD:1308535; rat.
DR   AGR; RGD:1308535; -.
DR   CTD; 90780; -.
DR   RGD; 1308535; Pygo2.
DR   eggNOG; ENOG502QSRS; Eukaryota.
DR   GeneTree; ENSGT00530000063948; -.
DR   HOGENOM; CLU_686883_0_0_1; -.
DR   OMA; GGMVFPC; -.
DR   OrthoDB; 5403712at2759; -.
DR   TreeFam; TF333020; -.
DR   Reactome; R-RNO-201722; Formation of the beta-catenin:TCF transactivating complex.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000020663; Expressed in ovary and 20 other cell types or tissues.
DR   GO; GO:1990907; C:beta-catenin-TCF complex; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR   GO; GO:0035034; F:histone acetyltransferase regulator activity; ISO:RGD.
DR   GO; GO:0042393; F:histone binding; ISO:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048856; P:anatomical structure development; ISO:RGD.
DR   GO; GO:0007420; P:brain development; ISO:RGD.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; ISO:RGD.
DR   GO; GO:0048589; P:developmental growth; ISO:RGD.
DR   GO; GO:0001822; P:kidney development; ISO:RGD.
DR   GO; GO:0002088; P:lens development in camera-type eye; ISO:RGD.
DR   GO; GO:0030879; P:mammary gland development; ISO:RGD.
DR   GO; GO:0033599; P:regulation of mammary gland epithelial cell proliferation; ISO:RGD.
DR   GO; GO:0060021; P:roof of mouth development; ISO:RGD.
DR   GO; GO:0007286; P:spermatid development; ISO:RGD.
DR   GO; GO:0007289; P:spermatid nucleus differentiation; ISO:RGD.
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.
PE   1: Evidence at protein level;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   REGION          1..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          106..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..27
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..162
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..177
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..217
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..251
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..272
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        279..301
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   405 AA;  41084 MW;  BA768F71DDF64444 CRC64;
     MAASAPPPPD KLEGGSGPAP PPAPPSTGRK QGKAGLQMKS PEKKRRKSNT QGPAYSHLTE
     FAPPPTPMVD HLVASNPFED DFGAPKMGGA GPPFLGSPVP FGGFRVQGGM AGQVPPGYGT
     GGGGGPQPLR RQPPPFPPNP MGPAFNMPPQ GPGYPPPGNM NFPSQPFNQS LGQNFSPPGG
     QMIPGPVGGF GPMISPTMGQ PPRGELGPPP LPQRFTQPGA PFGPSLQRPG QGLPSLPPNT
     SPFPGPDPGF PGPGGEDGGK PLNPPAPTAF PQEPHSGSPA AAVNGNQPSF PPSSSGRGGG
     TPDANSLAPP GKAGGGSGPQ PPPGLVYPCG ACRSEVNDDQ DAILCEASCQ KWFHRECTGM
     TESAYGLLTT EASAVWACDL CLKTKEIQSV YIREGMGQLV AANDG
//
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