E4F1_DANRE
ID E4F1_DANRE Reviewed; 719 AA.
AC Q4V8R6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Transcription factor E4F1;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q66K89};
DE AltName: Full=Putative E3 ubiquitin-protein ligase E4F1;
DE AltName: Full=RING-type E3 ubiquitin transferase E4F1 {ECO:0000305};
DE AltName: Full=Transcription factor E4F;
GN Name=e4f1; ORFNames=zgc:114190;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May function as a transcriptional repressor. May also
CC function as a ubiquitin ligase. Functions in cell survival and
CC proliferation through control of the cell cycle.
CC {ECO:0000250|UniProtKB:Q66K89}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q66K89};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Cytoplasm
CC {ECO:0000250}. Note=A small fraction is detected in the cytoplasm.
CC {ECO:0000250}.
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DR EMBL; BC097238; AAH97238.1; -; mRNA.
DR RefSeq; NP_001020684.1; NM_001025513.1.
DR AlphaFoldDB; Q4V8R6; -.
DR SMR; Q4V8R6; -.
DR BioGRID; 287308; 2.
DR STRING; 7955.ENSDARP00000055766; -.
DR PaxDb; Q4V8R6; -.
DR GeneID; 561158; -.
DR KEGG; dre:561158; -.
DR CTD; 1877; -.
DR ZFIN; ZDB-GENE-050913-103; e4f1.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q4V8R6; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q4V8R6; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q4V8R6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 5.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cytoplasm; DNA-binding; Growth regulation;
KW Metal-binding; Mitosis; Nucleus; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..719
FT /note="Transcription factor E4F1"
FT /id="PRO_0000324309"
FT ZN_FING 136..158
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 164..186
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 192..216
FT /note="C2H2-type 3; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 365..387
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 393..415
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 421..443
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 449..471
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 477..499
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 505..527
FT /note="C2H2-type 9; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 20..63
FT /note="Required for ubiquitin ligase activity"
FT /evidence="ECO:0000250"
FT REGION 59..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..207
FT /note="Mediates dimerization and DNA-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 62..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 719 AA; 80136 MW; D7D9C7ED001DF922 CRC64;
MTEENNNTAA TVTDQTEHSN IITIQTTLGD EDEDIHKCGK CLAEFSALDA FIQHKLSRSC
KRTQDPQTNV VPNEGVSVEV RSSENECSSD ETATANGEKQ DAKVASGDKK RSRSTSEDES
SSPSKVVWKL NTEGRYVCDI CAKTFKTTNI LRTHMFTHSD QKNFVCEMCE TAFRTKGSLI
RHKRRHTDER PYRCNQCGLA FRESGALTRH LKSLTPCTEK IRYSQCKEIL VSKDGIRKEV
QPSSPEPEKE QIPVVRVVEA GQEIIQIEVV EEVQQVASQP QTATVVEADN LICQAIINSG
IALETEATEA AGQVEAQSPK AVLGAPETET RITEIQVTEE CVETLAEETQ DSSVKEVEPV
QSKLYKCPHC ERMFKTLNYL RVHVKGHVGY KPFKCLTCQK EFLTGYVLKK HMETHVSERR
YKCGECGKQF KAIGHVREHM RAHSDERPYH CSFCDKSYKT KNALQVHHRT HADDKPYVCQ
HCSRGFREKS ALVRHIRHHT GEKPFKCSKC GRGFAEHGTL NRHLRAKGGC FAQLKDCEHV
VNSEEQEVTT ESVSTTIVSD DPHAVLVEFS SVVADTQEYI IGAPAEEAAQ GEEVAIIQDN
QQQMDSHIMK VVQQIVSQSH GGHQIIVRNV TADETPGISD SGDTITIATP ESLTEQVAMT
LANAISDGTI LTTTTEDTDE TSHTTVTMVT AENVETIEQE EQYVIASPEE VEIQTVVVV
