GenomeNet

Database: UniProt
Entry: E9Q8T2
LinkDB: E9Q8T2
Original site: E9Q8T2 
ID   PRD15_MOUSE             Reviewed;        1174 AA.
AC   E9Q8T2; E9Q6A1; Q3UML7;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   16-JAN-2019, entry version 66.
DE   RecName: Full=PR domain zinc finger protein 15 {ECO:0000305};
DE            EC=2.1.1.- {ECO:0000305};
DE   AltName: Full=PR domain-containing protein 15 {ECO:0000305};
GN   Name=Prdm15 {ECO:0000312|MGI:MGI:1930121};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Lung;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=28740264; DOI=10.1038/ng.3922;
RA   Mzoughi S., Zhang J., Hequet D., Teo S.X., Fang H., Xing Q.R.,
RA   Bezzi M., Seah M.K.Y., Ong S.L.M., Shin E.M., Wollmann H.,
RA   Wong E.S.M., Al-Haddawi M., Stewart C.L., Tergaonkar V., Loh Y.H.,
RA   Dunn N.R., Messerschmidt D.M., Guccione E.;
RT   "PRDM15 safeguards naive pluripotency by transcriptionally regulating
RT   WNT and MAPK-ERK signaling.";
RL   Nat. Genet. 49:1354-1363(2017).
CC   -!- FUNCTION: Sequence-specific DNA-binding transcriptional regulator.
CC       Plays a role as a molecular node in a transcriptional network
CC       regulating embryonic development and cell fate decision.
CC       Stimulates the expression of upstream key transcriptional
CC       activators and repressors of the Wnt/beta-catenin and MAPK/ERK
CC       pathways, respectively, that are essential for naive pluripotency
CC       and self-renewal maintenance of embryonic stem cells (ESCs).
CC       Specifically promotes SPRY1 and RSPO1 transcription activation
CC       through recognition and direct binding of a specific DNA sequence
CC       in their promoter regions. Plays also a role in induced
CC       pluripotent stem cells (iPSCs) reprogramming. Involved in early
CC       embryo development. {ECO:0000269|PubMed:28740264}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28740264}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=E9Q8T2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=E9Q8T2-2; Sequence=VSP_059647;
CC   -!- TISSUE SPECIFICITY: Expressed in embryonic stem cells (ESCs) (at
CC       protein level). {ECO:0000269|PubMed:28740264}.
CC   -!- DISRUPTION PHENOTYPE: Mice die before birth and show early
CC       postimplantation developmental defect. Display reduced embryonic
CC       stem cells (ESCs) proliferation and self-renewal capacity. Show
CC       altered transcription of naive pluripotency and self-renewal
CC       modulator genes. {ECO:0000269|PubMed:28740264}.
DR   EMBL; AK144820; BAE26081.1; -; mRNA.
DR   EMBL; AC121560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS49926.1; -. [E9Q8T2-1]
DR   RefSeq; NP_659038.2; NM_144789.2. [E9Q8T2-1]
DR   RefSeq; XP_006522932.1; XM_006522869.3. [E9Q8T2-2]
DR   UniGene; Mm.328741; -.
DR   SMR; E9Q8T2; -.
DR   STRING; 10090.ENSMUSP00000093533; -.
DR   MaxQB; E9Q8T2; -.
DR   PaxDb; E9Q8T2; -.
DR   PRIDE; E9Q8T2; -.
DR   Ensembl; ENSMUST00000095849; ENSMUSP00000093533; ENSMUSG00000014039. [E9Q8T2-1]
DR   Ensembl; ENSMUST00000121584; ENSMUSP00000113791; ENSMUSG00000014039. [E9Q8T2-2]
DR   GeneID; 114604; -.
DR   KEGG; mmu:114604; -.
DR   UCSC; uc012ajc.1; mouse. [E9Q8T2-1]
DR   CTD; 63977; -.
DR   MGI; MGI:1930121; Prdm15.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00940000157890; -.
DR   HOGENOM; HOG000115685; -.
DR   HOVERGEN; HBG053669; -.
DR   InParanoid; E9Q8T2; -.
DR   OrthoDB; 1318335at2759; -.
DR   TreeFam; TF331419; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   Bgee; ENSMUSG00000014039; Expressed in 248 organ(s), highest expression level in pituitary gland.
DR   ExpressionAtlas; E9Q8T2; baseline and differential.
DR   Genevisible; E9Q8T2; MM.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
DR   GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:UniProtKB.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:2000035; P:regulation of stem cell division; IMP:UniProtKB.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 6.
DR   SMART; SM00355; ZnF_C2H2; 17.
DR   SUPFAM; SSF57667; SSF57667; 7.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 16.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 15.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Complete proteome;
KW   Developmental protein; DNA-binding; Isopeptide bond; Metal-binding;
KW   Methyltransferase; Nucleus; Reference proteome; Repeat; Repressor;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1   1174       PR domain zinc finger protein 15.
FT                                /FTId=PRO_0000444718.
FT   DOMAIN       75    185       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING     402    424       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     434    457       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     468    486       C2H2-type 3; degenerate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     495    517       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     522    544       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     571    593       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     598    620       C2H2-type 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     661    684       C2H2-type 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     689    711       C2H2-type 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     725    747       C2H2-type 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     753    775       C2H2-type 11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     781    803       C2H2-type 12. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     809    831       C2H2-type 13. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     837    859       C2H2-type 14. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     865    888       C2H2-type 15. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   CROSSLNK    552    552       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P57071}.
FT   VAR_SEQ       1     26       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_059647.
FT   CONFLICT    298    298       R -> I (in Ref. 1; BAE26081).
FT                                {ECO:0000305}.
FT   CONFLICT    609    609       R -> L (in Ref. 1; BAE26081).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1174 AA;  132870 MW;  2C12468F8E056D76 CRC64;
     MCPPTIWEKG GQVGARWSLR APEVSAMAED GSEEIMFIWC EDCSQYHDSE CPELGPVVMV
     KDSFVLSRAR SSLPSNLEIR RLDDGAEGVF AVTQLVKRTQ FGPFESRRVA KWEKESAFPL
     KVFQKDGHPV CFDTSNEDDC NWMMLVRPAL EPGHQNLTAY QHGSDVYFTT SKDIPAGTEL
     RVWYAAFYAK KMDKPMLKQA CSSVQAAGTP EPSVSVEPER GQWVCKVCSN TFLELQLLNE
     HLLGHLEQAK SLPAGGQQHE AASEKEPDAP RMEPPTAAES KSIQSVMVTK EPKKKPRRGR
     KPKASKVEQP LVIIKDKEPS EHVAEIITEI PPDEPVSATP DERIMELVLG KLAAPTNEAS
     SVPKFPHHPS STIALKRGLV LSSRHGVRRK LVRQLGEHKR IHQCGTCSKV FQNSSNLSRH
     VRSHGECAHG DKLFKCEECS KLFSRKESLK QHVSYKHSRN EVDGEYRYRC GSCGKTFRME
     SALEFHNCRT DDKTFQCEMC FRFFSTNSNL SKHKKKHGDK KFACEVCSKM FYRKDVMLDH
     QRRHLDGVRR VKREDLEASG ESLVRYKKEP SGCPVCGKVF SCRSNMNKHL LTHGDKKYTC
     EICGRKFFRV DVLRDHIHVH FKDIALMDDH QREEFIGKIG ISSEENDDNS DESADSEPHK
     YSCKRCQLTF GRGKEYLKHI MEVHKEKGHG CSICHRRFAL KATYHAHMVI HRENLPDPNV
     QKYIHPCEIC GRIFNSIGNL ERHKLIHTGV KSHACEQCGK SFARKDMLKE HMRVHDNIRE
     YLCAECGKGM KTKHALRHHM KLHKGIKEYE CKECHRKFAQ KVNMLKHYKR HTGIKDFMCE
     LCGKTFSERN TMETHKLIHT VGKQWTCSVC DKKYVTEYML QKHVQLTHDK VEAQSCQLCG
     TKVSTRASMS RHMRRKHPEV LAVRIDDLDH LPETTTIDAS SIGIVQPALG LEQEELAEGK
     HGKAAKRSHK RKQKPEEEAG APVPEDTTFS EYPEKEPEFT GSVGDETNSA VQSIQQVVVT
     LGDPNVTAPS SSVGLTNITV TPITTAAGTQ FTNLQPVAVG HLTNPDRQLQ LDNSILTVTF
     DTVSGSAMLH NRQNDVQIHP QPEATNPQSV AHFINLTTLV NSITPLGNQL SEQHPLTWRA
     VPQTDVLQPP QAPAAPQQAV QPQVQNEQQQ MYSY
//
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