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EGR2_CERTH
ID   EGR2_CERTH              Reviewed;          62 AA.
AC   P26634;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=E3 SUMO-protein ligase EGR2;
DE            EC=2.3.2.- {ECO:0000250|UniProtKB:P11161};
DE   AltName: Full=E3 SUMO-protein transferase ERG2 {ECO:0000305};
DE   AltName: Full=Early growth response protein 2;
DE            Short=EGR-2;
DE   AltName: Full=Zinc finger protein Krox-20;
DE   Flags: Fragment;
GN   Name=EGR2; Synonyms=KROX20;
OS   Cerdocyon thous (Crab-eating fox) (Dusicyon thous).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Cerdocyon.
OX   NCBI_TaxID=9620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1930167; DOI=10.1016/0006-291x(91)91702-e;
RA   Lanfear J., Jowett T., Holland P.W.;
RT   "Cloning of fish zinc-finger genes related to Krox-20 and Krox-24.";
RL   Biochem. Biophys. Res. Commun. 179:1220-1224(1991).
CC   -!- FUNCTION: Sequence-specific DNA-binding transcription factor (By
CC       similarity). Plays a role in hindbrain segmentation by regulating the
CC       expression of a subset of homeobox containing genes and in Schwann cell
CC       myelination by regulating the expression of genes involved in the
CC       formation and maintenance of myelin (By similarity). Binds to two EGR2-
CC       consensus sites EGR2A (5'-CTGTAGGAG-3') and EGR2B (5'-ATGTAGGTG-3') in
CC       the HOXB3 enhancer and promotes HOXB3 transcriptional activation (By
CC       similarity). Binds to specific DNA sites located in the promoter region
CC       of HOXA4, HOXB2 and ERBB2 (By similarity). Regulates hindbrain
CC       segmentation by controlling the expression of Hox genes, such as HOXA4,
CC       HOXB3 and HOXB2, and thereby specifying odd and even rhombomeres (By
CC       similarity). Promotes the expression of HOXB3 in the rhombomere r5 in
CC       the hindbrain (By similarity). Regulates myelination in the peripheral
CC       nervous system after birth, possibly by regulating the expression of
CC       myelin proteins, such as MPZ, and by promoting the differentiation of
CC       Schwann cells (By similarity). Involved in the development of the jaw
CC       openener musculature, probably by playing a role in its innervation
CC       through trigeminal motor neurons (By similarity). May play a role in
CC       adipogenesis, possibly by regulating the expression of CEBPB (By
CC       similarity). {ECO:0000250|UniProtKB:P08152}.
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:0000250|UniProtKB:P11161}.
CC   -!- PATHWAY: Protein modification; protein sumoylation.
CC   -!- SUBUNIT: Interacts with HCFC1 (By similarity). Interacts with WWP2 (By
CC       similarity). Interacts with UBC9 (By similarity). Interacts with CITED1
CC       (By similarity). Interacts (via phosphorylated form) with SFN (By
CC       similarity). {ECO:0000250|UniProtKB:P08152,
CC       ECO:0000250|UniProtKB:P11161}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P08152}.
CC   -!- PTM: Ubiquitinated by WWP2 leading to proteasomal degradation.
CC       {ECO:0000250|UniProtKB:P08152}.
CC   -!- PTM: Acetylated. May be deacetylated by HDAC6, HDAC10 or SIRT1.
CC       {ECO:0000250|UniProtKB:P08152}.
CC   -!- SIMILARITY: Belongs to the EGR C2H2-type zinc-finger protein family.
CC       {ECO:0000305}.
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DR   EMBL; M81106; AAA30905.1; -; Genomic_DNA.
DR   PIR; PQ0235; PQ0235.
DR   AlphaFoldDB; P26634; -.
DR   SMR; P26634; -.
DR   UniPathway; UPA00886; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0021612; P:facial nerve structural organization; ISS:UniProtKB.
DR   GO; GO:0031643; P:positive regulation of myelination; ISS:UniProtKB.
DR   GO; GO:0014040; P:positive regulation of Schwann cell differentiation; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0006611; P:protein export from nucleus; ISS:UniProtKB.
DR   GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
DR   GO; GO:0021659; P:rhombomere 3 structural organization; ISS:UniProtKB.
DR   GO; GO:0021665; P:rhombomere 5 structural organization; ISS:UniProtKB.
DR   GO; GO:0014037; P:Schwann cell differentiation; ISS:UniProtKB.
DR   GO; GO:0035914; P:skeletal muscle cell differentiation; ISS:UniProtKB.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   3: Inferred from homology;
KW   Acetylation; Activator; DNA-binding; Metal-binding; Nucleus; Repeat;
KW   Transcription; Transcription regulation; Transferase; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           <1..>62
FT                   /note="E3 SUMO-protein ligase EGR2"
FT                   /id="PRO_0000047118"
FT   ZN_FING         <1..21
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         27..49
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         55..>62
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   NON_TER         1
FT   NON_TER         62
SQ   SEQUENCE   62 AA;  7176 MW;  D14B288F9706641F CRC64;
     AEGCDRRFSA SDELTRHIRI HTGHKPFQCA ICMRNFSRSD HLTTHIRTHT GEKPFACDYC
     GR
 
 
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