(data stored in ACNUC14376 zone)

HOGENOM: HS17_PE1870

ID   HS17_PE1870                          STANDARD;      PRT;   484 AA.
AC   HS17_PE1870; P43268; A8K314; Q96AW9;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=ETS translocation variant 4;AltName: Full=Adenovirus E1A
DE   enhancer-binding protein;AltName: Full=E1A-F;AltName: Full=Polyomavirus
DE   enhancer activator 3 homolog; Short=Protein PEA3; (HS17.PE1870).
GN   Name=ETV4; Synonyms=E1AF, PEA3;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS17.PE1870.
CC       Homo sapiens chromosome 17 GRCh37  sequence 1..81195210 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:ETV4_HUMAN
CC   -!- FUNCTION: Transcriptional activator that binds to the enhancer of
CC       the adenovirus E1A gene; the core-binding sequence is
CC       5'[AC]GGA[AT]GT-3'.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- PTM: Sumoylated; enhanced upon ERK/MAP kinase pathway activation,
CC       it positively regulates the transcriptional activator capacity.
CC       Sumoylation at Lys-96 probably requires phosphorylation at Ser-
CC       101. Transiently polysumoylated and desumoylated by SENP1.
CC       Sumoylation is a prerequisite to polyubiquitination which in turn
CC       increases proteasomal-mediated degradation. Probably
CC       polyubiquitinated by RNF4 and deubiquitinated by USP2.
CC   -!- SIMILARITY: Belongs to the ETS family.
CC   -!- SIMILARITY: Contains 1 ETS DNA-binding domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA95991.1; Type=Erroneous initiation;
CC   -!- GENE_FAMILY: HOG000230986 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000175832;ENST00000393664;ENSP00000377273.
DR   EMBL; AF095887; - ;
DR   EMBL; AF095888; - ;
DR   EMBL; AF095889; - ;
DR   EMBL; AF095890; - ;
DR   EMBL; AK290429; - ;
DR   EMBL; AK299019; - ;
DR   EMBL; AK315961; - ;
DR   EMBL; BC016623; - ;
DR   EMBL; CH471178; - ;
DR   EMBL; D12765; - ;
DR   EMBL; U18018; - ;
DR   UniProtKB/Swiss-Prot; P43268; A8K314; Q96AW9; -.
DR   EMBL; U18018; AAA95991.1; ALT_INIT; mRNA.
DR   EMBL; AF095890; AAD09186.1; -; Genomic_DNA.
DR   EMBL; AF095887; AAD09186.1; JOINED; Genomic_DNA.
DR   EMBL; AF095888; AAD09186.1; JOINED; Genomic_DNA.
DR   EMBL; AF095889; AAD09186.1; JOINED; Genomic_DNA.
DR   EMBL; AK290429; BAF83118.1; -; mRNA.
DR   EMBL; BC016623; AAH16623.1; -; mRNA.
DR   EMBL; D12765; BAA02234.1; -; mRNA.
DR   IPI; IPI00017382; -.
DR   PIR; S35534; S35534.
DR   RefSeq; NP_001073143.1; NM_001079675.1.
DR   RefSeq; NP_001977.1; NM_001986.2.
DR   UniGene; Hs.434059; -.
DR   ProteinModelPortal; P43268; -.
DR   SMR; P43268; 354-427.
DR   DIP; DIP-748N; -.
DR   STRING; P43268; -.
DR   PhosphoSite; P43268; -.
DR   PRIDE; P43268; -.
DR   Ensembl; ENST00000319349; ENSP00000321835; ENSG00000175832.
DR   Ensembl; ENST00000393664; ENSP00000377273; ENSG00000175832.
DR   GeneID; 2118; -.
DR   KEGG; hsa:2118; -.
DR   UCSC; uc002idw.1; human.
DR   CTD; 2118; -.
DR   GeneCards; GC17M037370; -.
DR   H-InvDB; HIX0019239; -.
DR   HGNC; HGNC:3493; ETV4.
DR   HPA; HPA005768; -.
DR   MIM; 600711; gene.
DR   neXtProt; NX_P43268; -.
DR   Orphanet; 319; Ewing sarcoma.
DR   PharmGKB; PA27907; -.
DR   eggNOG; prNOG09615; -.
DR   GeneTree; ENSGT00600000083997; -.
DR   InParanoid; P43268; -.
DR   OMA; PFPRAEQ; -.
DR   OrthoDB; EOG4W0XCT; -.
DR   NextBio; 8559; -.
DR   ArrayExpress; P43268; -.
DR   Bgee; P43268; -.
DR   CleanEx; HS_ETV4; -.
DR   Genevestigator; P43268; -.
DR   GermOnline; ENSG00000175832; Homo sapiens.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; NAS:UniProtKB.
DR   InterPro; IPR000418; Ets.
DR   InterPro; IPR006715; ETS_PEA3_N.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF00178; Ets; 1.
DR   Pfam; PF04621; ETS_PEA3_N; 1.
DR   PRINTS; PR00454; ETSDOMAIN.
DR   SMART; SM00413; ETS; 1.
DR   PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR   PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR   PROSITE; PS50061; ETS_DOMAIN_3; 1.
DR   HOGENOMDNA; HS17.PE1870; -.
KW   ENSG000001758321755old_1320000031; ENSP000003772737901old_1320000031;
KW   B7Z5J3_HUMAN; B7Z9J6_HUMAN; D3DX44_HUMAN; AF095887; AF095888; AF095889;
KW   AK290429; AK299019; AK315961; BC016623; CH471178; D12765; U18018;
KW   Activator; Complete proteome; DNA-binding; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Polymorphism; Reference proteome; Transcription;
KW   Transcription regulation; Ubl conjugation.
SQ   SEQUENCE   484 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MERRMKAGYL DQQVPYTFSS KSPGNGSLRE ALIGPLGKLM DPGSLPPLDS EDLFQDLSHF
     QETWLAEAQV PDSDEQFVPD FHSENLAFHS PTTRIKKEPQ SPRTDPALSC SRKPPLPYHH
     GEQCLYSSAY DPPRQIAIKS PAPGALGQSP LQPFPRAEQR NFLRSSGTSQ PHPGHGYLGE
     HSSVFQQPLD ICHSFTSQGG GREPLPAPYQ HQLSEPCPPY PQQSFKQEYH DPLYEQAGQP
     AVDQGGVNGH RYPGAGVVIK QEQTDFAYDS DVTGCASMYL HTEGFSGPSP GDGAMGYGYE
     KPLRPFPDDV CVVPEKFEGD IKQEGVGAFR EGPPYQRRGA LQLWQFLVAL LDDPTNAHFI
     AWTGRGMEFK LIEPEEVARL WGIQKNRPAM NYDKLSRSLR YYYEKGIMQK VAGERYVYKF
     VCEPEALFSL AFPDNQRPAL KAEFDRPVSE EDTVPLSHLD ESPAYLPELA GPAQPFGPKG
     GYSY
//

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