ID Q9U1I0_DROME Unreviewed; 1406 AA.
AC Q9U1I0;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 22-FEB-2023, entry version 134.
DE SubName: Full=BIP2 protein {ECO:0000313|EMBL:CAB64265.1};
GN Name=Taf3 {ECO:0000313|FlyBase:FBgn0026262};
GN Synonyms=bip2 {ECO:0000313|EMBL:CAB64265.1};
GN ORFNames=CG2009 {ECO:0000313|FlyBase:FBgn0026262};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000313|EMBL:CAB64265.1};
RN [1] {ECO:0000313|EMBL:CAB64265.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11543621; DOI=10.1006/dbio.2001.0358;
RA Pointud J.C., Larsson J., Dastugue B., Couderc J.L.;
RT "The BTB/POZ domain of the regulatory proteins Bric a brac 1 (BAB1) and
RT Bric a brac 2 (BAB2) interacts with the novel Drosophila TAF(II) factor
RT BIP2/dTAF(II)155.";
RL Dev. Biol. 237:368-380(2001).
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DR EMBL; AJ251945; CAB64265.1; -; Genomic_DNA.
DR AGR; FB:FBgn0026262; -.
DR FlyBase; FBgn0026262; Taf3.
DR VEuPathDB; VectorBase:FBgn0026262; -.
DR HOGENOM; CLU_252532_0_0_1; -.
DR ExpressionAtlas; Q9U1I0; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002039; F:p53 binding; IPI:FlyBase.
DR GO; GO:0031208; F:POZ domain binding; IPI:FlyBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR CDD; cd15522; PHD_TAF3; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR006565; BTP.
DR InterPro; IPR009072; Histone-fold.
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; PTHR46452; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 3; 1.
DR PANTHER; PTHR46452:SF1; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 3; 1.
DR Pfam; PF07524; Bromo_TP; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00576; BTP; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 1340..1390
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 674..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1168..1225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1067
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1406 AA; 154485 MW; 6D4FFC30326B4C08 CRC64;
MMADRYASDL ALVVVAQITQ TIGYSCTLSA PLELLQDILQ KFVQEFARDM HRHMEHANRI
EPNLKDARLS IKNLSINVQE LLDYIGNVAP VGFIRDVPQF PIGKSVNMNF LKPGSAETLT
RPVYIFEYLP PMQDPELREI PADVQKEFSE KQEFCSKAEY SSTNAADKLG AKHIDSISPN
TVINFRSNAF ELDVGSSVRE MSSVVMTTGG FISPAIEGKL PEDIIPDIVE KFLGLDAPFS
PTIIVNSLQK SPQLALSDRD KTVNPRKIIP SETKIFKQNA ALLTSGHSES SIIYASNNHT
MLTVTTPKKN RKQKHDLICE PGQSELLTNP FEKAQEKSQR KALKMYKQTS KNQRDSSINQ
IQNMKKLKKK FNRGSFDPNK KHLEKIFKKQ SKLKQNDLQL DIDEKHFLQN SQTTSGLAIK
ANSNENALQA DIPSQPPTVT SQIENNFRNS IYPVQPSVIQ QTQVLLAEKK SGSEPERSKL
DIFKKISKPR TPRPDIGATL VPPGTGVSVF GSTMTPSALI SLPSGTTITP TPSLGLNSEN
KNVPSMKINP CNIFDGTIPL TKAGVEMSII DSPKPKKRGR KPGGKNLIKQ TNVISQPLIN
KVERKKSSQA ITLPLSSSPM IITQSSLNVS PPTEPLNLCN TEQPSNNFLS NLYAKEKKDR
KKYKSLPENV MQLDKSCSPE KASTLHNSIR PTKQNNDVQC SDKFVTISNA LSNASIYPGI
QTGMVPLLPL LQFPPRPGLI PTGPGLFPAV TGLVGFGNHG NRIPISPFID YPGPEESVAD
TVRCPPIKDS PVTDSDQFLS RSSTQTDLQM DRNYCNVAPL VPDSMKFAEC KSVSCASTIL
ENPSAQATSK INTKPLLEAS GNPDDPIEVS DDSDESMHNR QMVQRKTPIS SPTYVKTSFA
ELNPSSFTSA ASNGEEKSKM DLRNIVSLSS NEPLKKFKKL VKQSFPDVKS VPHTPASHSS
FPQFNLPNFM GGDKFSLAGG ADLIPLSRVS DSEYSSKIVP FSSLGGTIPN QIKISEEHNI
FSTFSNYEDI TITPTGLTSL EPKMRKHHKK LKKVKEGKNK KKKEKKDKSK KADQIGLPSF
KSDRKIKAND KRQKKEKKKD KDKQILVHIP DDTEEFDKVP LANNDEPVLK SSSMTINPSL
GAATSGISPN QIPKLTLKLS GKSTLFSSSE KEMTDAGKLK QTTILSSENK KRERDNSPEL
ARFSPLVTGP PKNKQSETLH LGNSSTAVLP VPSPVAVRAV QLPVSQTSSN SAGWLSNPNN
SNTASSTLSA SSVLLPQQLM LAPHTIMNNF VPAMCNSTGT VSKSGLCSSP PNTSEENANA
MQIAESSRPS SYVDAEGNRI WICPACGKVD EGSAMIGCDG CDAWYHWICV GITFAPKDND
DWFCRVCVTK KRIHGSEKKK RRNKKK
//