ID H0X820_OTOGA Unreviewed; 473 AA.
AC H0X820;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=E3 SUMO-protein ligase EGR2 {ECO:0000256|ARBA:ARBA00040715};
DE AltName: Full=E3 SUMO-protein transferase ERG2 {ECO:0000256|ARBA:ARBA00042877};
DE AltName: Full=Early growth response protein 2 {ECO:0000256|ARBA:ARBA00042200};
GN Name=EGR2 {ECO:0000313|Ensembl:ENSOGAP00000011595.2};
OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000011595.2, ECO:0000313|Proteomes:UP000005225};
RN [1] {ECO:0000313|Proteomes:UP000005225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSOGAP00000011595.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: E3 SUMO-protein ligase helping SUMO1 conjugation to its
CC coregulators NAB1 and NAB2, whose sumoylation down-regulates EGR2
CC transcriptional activity. {ECO:0000256|ARBA:ARBA00037627}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU363046}.
CC -!- SIMILARITY: Belongs to the EGR C2H2-type zinc-finger protein family.
CC {ECO:0000256|ARBA:ARBA00005682, ECO:0000256|RuleBase:RU363046}.
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DR EMBL; AAQR03019728; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003783676.1; XM_003783628.2.
DR RefSeq; XP_003783677.1; XM_003783629.1.
DR RefSeq; XP_012656775.1; XM_012801321.1.
DR AlphaFoldDB; H0X820; -.
DR STRING; 30611.ENSOGAP00000011595; -.
DR Ensembl; ENSOGAT00000012940.2; ENSOGAP00000011595.2; ENSOGAG00000012939.2.
DR GeneID; 100943294; -.
DR KEGG; oga:100943294; -.
DR CTD; 1959; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158394; -.
DR HOGENOM; CLU_043235_0_0_1; -.
DR InParanoid; H0X820; -.
DR OMA; QCQRELH; -.
DR OrthoDB; 2912670at2759; -.
DR TreeFam; TF318980; -.
DR Proteomes; UP000005225; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0061665; F:SUMO ligase activity; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0035904; P:aorta development; IEA:Ensembl.
DR GO; GO:0035284; P:brain segmentation; IEA:Ensembl.
DR GO; GO:0071310; P:cellular response to organic substance; IEA:Ensembl.
DR GO; GO:0021612; P:facial nerve structural organization; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0008045; P:motor neuron axon guidance; IEA:Ensembl.
DR GO; GO:0042552; P:myelination; IEA:Ensembl.
DR GO; GO:0031643; P:positive regulation of myelination; IEA:Ensembl.
DR GO; GO:0014040; P:positive regulation of Schwann cell differentiation; IEA:Ensembl.
DR GO; GO:0006611; P:protein export from nucleus; IEA:Ensembl.
DR GO; GO:0016925; P:protein sumoylation; IEA:Ensembl.
DR GO; GO:0030278; P:regulation of ossification; IEA:Ensembl.
DR GO; GO:0021660; P:rhombomere 3 formation; IEA:Ensembl.
DR GO; GO:0021659; P:rhombomere 3 structural organization; IEA:Ensembl.
DR GO; GO:0021666; P:rhombomere 5 formation; IEA:Ensembl.
DR GO; GO:0021665; P:rhombomere 5 structural organization; IEA:Ensembl.
DR GO; GO:0007622; P:rhythmic behavior; IEA:Ensembl.
DR GO; GO:0014037; P:Schwann cell differentiation; IEA:Ensembl.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 3.
DR InterPro; IPR021849; EGR_N.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR23235:SF54; E3 SUMO-PROTEIN LIGASE EGR2; 1.
DR PANTHER; PTHR23235; KRUEPPEL-LIKE TRANSCRIPTION FACTOR; 1.
DR Pfam; PF11928; DUF3446; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU363046};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU363046};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU363046};
KW Reference proteome {ECO:0000313|Proteomes:UP000005225};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU363046};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU363046};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU363046};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 337..366
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 367..394
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 395..422
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 147..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 473 AA; 50179 MW; 551025ED8D6F781D CRC64;
MMTAKAVDKI PVTLSGFVHQ LSDNIYPVED LAATSVTIFP NAELGGPFDQ MNGVAGDGMI
NIDMTGEKRS LDLSYPSGFA PVPAPRNQTF TYMGKFSIDP QYPGASCYPE GIINIVSAGI
LQGVTSPAST TASSSVTSAS PNPLATGPLG VCTMSQTQPD LDHHLYSPPP PPPPYSGCAG
DLYQDPTAFL PSTTSTSSSL AYPPPPSYPS PKPATDPGLF PMIPDYPGFF PSQCQRDLHG
TAGPDRKPFP CPLDTLRVPP PLTPLSTIRN FTLGGPSAGV TGPGASGGSE GPRLPGSSSA
AATAAAYNPH HLPLRPILRP RKYPNRPSKT PVHERPYPCP AEGCDRRFSR SDELTRHIRI
HTGHKPFQCR ICMRNFSRSD HLTTHIRTHT GEKPFACDYC GRKFARSDER KRHTKIHLRQ
KERKSSGPST SVPAPATAPC TGGTQAGGAL CSSNSSTIGG GPLAPCSSRT RTP
//
