ILF2_PONAB
ID ILF2_PONAB Reviewed; 390 AA.
AC Q5RFJ1; Q5RB97;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Interleukin enhancer-binding factor 2;
GN Name=ILF2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Chromatin-interacting protein that forms a stable heterodimer
CC with interleukin enhancer-binding factor 3/ILF3 and plays a role in
CC several biological processes including transcription, innate immunity
CC or cell growth. Essential for the efficient reshuttling of ILF3
CC (isoform 1 and isoform 2) into the nucleus. Together with ILF3, forms
CC an RNA-binding complex that is required for mitotic progression and
CC cytokinesis by regulating the expression of a cluster of mitotic genes.
CC Mechanistically, competes with STAU1/STAU2-mediated mRNA decay. Plays
CC also a role in the inhibition of various viruses including Japanese
CC encephalitis virus or enterovirus 71. {ECO:0000250|UniProtKB:Q12905}.
CC -!- SUBUNIT: Forms heterodimers with ILF3. ILF2-ILF3 heterodimers may also
CC bind to PRKDC/XRCC7: this may stabilize the interaction of PRKDC/XRCC7
CC and the heterodimeric complex of G22P1/KU70 and XRCC5/KU80. Forms a
CC complex with ILF3, YLPM1, KHDRBS1, RBMX, NCOA5 and PPP1CA. Identified
CC in a IGF2BP1-dependent mRNP granule complex containing untranslated
CC mRNAs. Interacts with IGF2BP1. Interacts with CRBN; this interaction
CC promotes ubiquitination and subsequent degradation of ILF2.
CC {ECO:0000250|UniProtKB:Q12905}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q12905}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q12905}. Nucleus {ECO:0000250|UniProtKB:Q12905}.
CC Note=Localized in cytoplasmic mRNP granules containing untranslated
CC mRNAs. {ECO:0000250|UniProtKB:Q12905}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5RFJ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5RFJ1-2; Sequence=VSP_013410;
CC -!- PTM: Ubiquitinated at Lys-45 by CRBN with polyubiquitin chains by the
CC CUL4-RING E3 ligase (CRL4-CRBN) and then degraded by the proteasome.
CC {ECO:0000250|UniProtKB:Q12905}.
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DR EMBL; CR857165; CAH89466.1; -; mRNA.
DR EMBL; CR858754; CAH90963.1; -; mRNA.
DR RefSeq; NP_001125555.1; NM_001132083.1. [Q5RFJ1-2]
DR RefSeq; NP_001128737.1; NM_001135265.1. [Q5RFJ1-1]
DR RefSeq; XP_009242123.1; XM_009243848.1. [Q5RFJ1-1]
DR AlphaFoldDB; Q5RFJ1; -.
DR SMR; Q5RFJ1; -.
DR STRING; 9601.ENSPPYP00000000934; -.
DR Ensembl; ENSPPYT00000000967; ENSPPYP00000000934; ENSPPYG00000000800. [Q5RFJ1-1]
DR GeneID; 100172468; -.
DR GeneID; 100189627; -.
DR KEGG; pon:100172468; -.
DR CTD; 3608; -.
DR eggNOG; KOG3793; Eukaryota.
DR GeneTree; ENSGT00940000154879; -.
DR HOGENOM; CLU_064863_1_0_1; -.
DR InParanoid; Q5RFJ1; -.
DR TreeFam; TF320194; -.
DR Proteomes; UP000001595; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR006561; DZF_dom.
DR InterPro; IPR043519; NT_sf.
DR Pfam; PF07528; DZF; 1.
DR SMART; SM00572; DZF; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS51703; DZF; 1.
PE 2: Evidence at transcript level;
KW Activator; Alternative splicing; Cytoplasm; DNA-binding; Isopeptide bond;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..390
FT /note="Interleukin enhancer-binding factor 2"
FT /id="PRO_0000126065"
FT DOMAIN 24..371
FT /note="DZF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01040"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..390
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CXY6"
FT MOD_RES 16
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q12905"
FT MOD_RES 24
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q12905"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12905"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12905"
FT MOD_RES 388
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12905"
FT CROSSLNK 45
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q12905"
FT CROSSLNK 186
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q12905"
FT CROSSLNK 364
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q12905"
FT VAR_SEQ 1..38
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_013410"
SQ SEQUENCE 390 AA; 43062 MW; 75BAD022DCD4EE01 CRC64;
MRGDRGRGRG GRFGSRGGPG GGFRPFVPHI PFDFYLCEMA FPRVKPAPDE TSFSEALLKR
NQDLAPNSAE QASILSLVTK INNVIDNLIV APGTFEVQIE EVRQVGSYKK GTMTTGHNVA
DLVVILKILP TLEAVAALGN KVVESLRAQD PSEVLTMLTN ETGFEISSSD ATVKILITTV
PPNLRKLDPE LHLDIKVLQS ALAAIRHARW FEENASQSTV KVLIRLLKDL RIRFPGFEPL
TPWILDLLGH YAVMNNPTRQ PLALNVAYRR CLQILAAGLF LPGSVGITDP CESGNFRVHT
VMTLEQQDMV CYTAQTLVRI LSHGGFRKIL GQEGDASYLA SEISTWDGVI VTPSEKAYEK
PPEKKEGEEE EENTEEPPQG EEEESMETQE
