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DescriptionSubName: Full=PHD finger protein 20, b {ECO:0000313|Ensembl:ENSDARP00000056569}; SubName: Full=Zgc:91986 {ECO:0000313|EMBL:AAH80250.1};
MyHits logo
MyHits synonymsQ68EI2_DANRE , Q68EI2 , 8C33AFB443445232
match map segment
iprf:ZINC_FINGER_C2H2_2 ismart:PHD ipat:ZF_PHD_1 ipfam:MBT ismart:TUDOR ipat:ZINC_FINGER_C2H2_1  
Legends: 1, C2H2-type. {ECO:0000259|PROSITE:PS50157}; 2, iprf:ZINC_FINGER_C2H2_2 [T]; 3, ismart:PHD [T]; 4, ipat:ZF_PHD_1 [T]; 5, ipfam:MBT [T]; 6, ismart:TUDOR [T]; 7, ipat:ZINC_FINGER_C2H2_1 [T].
ID   Q68EI2_DANRE            Unreviewed;       986 AA.
AC   Q68EI2;
DT   11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2004, sequence version 1.
DT   10-MAY-2017, entry version 111.
DE   SubName: Full=PHD finger protein 20, b {ECO:0000313|Ensembl:ENSDARP00000056569};
DE   SubName: Full=Zgc:91986 {ECO:0000313|EMBL:AAH80250.1};
GN   Name=phf20b {ECO:0000313|Ensembl:ENSDARP00000056569,
GN   ECO:0000313|ZFIN:ZDB-GENE-040822-33};
GN   Synonyms=zgc:91986 {ECO:0000313|EMBL:AAH80250.1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|EMBL:AAH80250.1};
RN   [1] {ECO:0000313|EMBL:AAH80250.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Whole {ECO:0000313|EMBL:AAH80250.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSDARP00000056569}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000056569};
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSDARP00000056569, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000056569,
RC   ECO:0000313|Proteomes:UP000000437};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
RA   Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
RA   McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
RA   Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
RA   Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
RA   Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
RA   Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
RA   Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J.,
RA   Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P.,
RA   Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G.,
RA   Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D.,
RA   Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K.,
RA   Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C.,
RA   Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J.,
RA   Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S.,
RA   Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A.,
RA   Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D.,
RA   Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z.,
RA   Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J.,
RA   Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C.,
RA   Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C.,
RA   Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J.,
RA   Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
RA   Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
RA   Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
RA   Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the
RT   human genome.";
RL   Nature 496:498-503(2013).
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DR   EMBL; CR352242; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC080250; AAH80250.1; -; mRNA.
DR   RefSeq; NP_001004114.1; NM_001004114.1.
DR   UniGene; Dr.2818; -.
DR   STRING; 7955.ENSDARP00000112091; -.
DR   Ensembl; ENSDART00000056570; ENSDARP00000056569; ENSDARG00000038737.
DR   GeneID; 445482; -.
DR   KEGG; dre:445482; -.
DR   CTD; 445482; -.
DR   ZFIN; ZDB-GENE-040822-33; phf20b.
DR   eggNOG; KOG1844; Eukaryota.
DR   eggNOG; ENOG410XX7Z; LUCA.
DR   GeneTree; ENSGT00390000006451; -.
DR   HOGENOM; HOG000231997; -.
DR   HOVERGEN; HBG053586; -.
DR   KO; K18402; -.
DR   TreeFam; TF106475; -.
DR   Reactome; R-DRE-3214847; HATs acetylate histones.
DR   Reactome; R-DRE-6804759; Regulation of TP53 Activity through Association with Co-factors.
DR   Proteomes; UP000000437; Chromosome 23.
DR   Bgee; ENSDARG00000038737; -.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR004092; Mbt.
DR   InterPro; IPR002999; Tudor.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF02820; MBT; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00333; TUDOR; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000437};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00592111};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Zinc {ECO:0000256|SAAS:SAAS00592111};
KW   Zinc-finger {ECO:0000256|SAAS:SAAS00592111}.
FT   DOMAIN      421    451       C2H2-type. {ECO:0000259|PROSITE:PS50157}.
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CC   The following FT lines are automated annotations from the MyHits database.
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FT   MYHIT       421    451       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       618    662       ismart:PHD [T]
FT   MYHIT       619    661       ipat:ZF_PHD_1 [T]
FT   MYHIT        19     68       ipfam:MBT [T]
FT   MYHIT        85    141       ismart:TUDOR [T]
FT   MYHIT       423    446       ipat:ZINC_FINGER_C2H2_1 [T]
SQ   SEQUENCE   986 AA;  112865 MW;  8C33AFB443445232 CRC64;
     MTKSPPNRRG IVFEVGAQLE ARDTLKNWYA ANIEKIDYED EKVLIHYRQW SHRYDEWFDW
     SSPYLRPVER IQLRKQGLNE RQCASGFQVN QKVLASWSDC RYYPAKILSR DKDDFYTVKF
     FDGIIKTVKG IKVKPFRKQS SDGRSNQQAR KRADQNEKEL KPKENGNSRH NSSRHSVSDH
     DGESESEADE DTTVMDESTD LQNGGEKEST ETKMVNDSEV SSAEHQPSED QNQPSEDKTE
     NLENGNVEIK IEEEEEEEMD GGQEEAKVLH NGIDKNDEHK GEASDESPSL PKRTRSRTAD
     GKEAEMVNGP ELRKRRASTG QTSPAKRSRA NSSTDRNTQT PIKPVKSDSV PDTLDIKDEK
     TSPAGKPAPA EEAGSTPELA AALKRQVHLP TTNKYSREPL YRVIKNQPPP ILSIELDHNP
     FKCKMAGCLK SFRKASLLHY HMKYYHAQSD PSPPRCVQTR SSDKQSPSQE TPRRRRTVSA
     SHHTPSPLSD SKSGHSLSPP AVGIKHRQRS ATLGAERSKE NQVFNRSLHD DRDWVAKETA
     LKERERLREK RQREFFRIKL KKKKKKKRKS KSGEDSSSDL SSDSPVWSED ESDTELDLNV
     PLSEQGVETV THSSEIVRCI CEVQEENDFM IQCDECLCWQ HGTCMGLYED SVPDSYSCYI
     CRDPPAQRQS QRYWYDKDWL SSGHMYGLSF LEENYSHQNS KKVTAAHQLL GDVHRVFEVL
     NGLQLKMSIL QTQAHPDLKL WRQPWKHADG LRRRMAGDSG IATPLPPSPP EMGENEFETL
     KSEAPSPMET HCSFQDSYIS SEHCYQKPRT YYPAVERRLV VETRGGSELE DSLRSTEDLL
     EMAEQRYGTQ LDHDQHKLAD RSFSKELESR MKRLVSAEQE KSCGVEIKEE EPDPVTPDPK
     PDPDLVLHQQ WQLNLLEHIE AVQDEVTHRM DLIERELDVL ESWLDYTGEL EPPDPLARLP
     QLKHRIRQLL TDLGTVQQIA LCSSSS
//