GenomeNet

Database: UniProt
Entry: T1EDE7_HELRO
LinkDB: T1EDE7_HELRO
Original site: T1EDE7_HELRO 
ID   T1EDE7_HELRO            Unreviewed;      1032 AA.
AC   T1EDE7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Enhancer of polycomb-like protein {ECO:0000256|RuleBase:RU361124};
GN   Name=20194599 {ECO:0000313|EnsemblMetazoa:HelroP103167};
GN   ORFNames=HELRODRAFT_103167 {ECO:0000313|EMBL:ESN93811.1};
OS   Helobdella robusta (Californian leech).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Hirudinea; Rhynchobdellida; Glossiphoniidae; Helobdella.
OX   NCBI_TaxID=6412 {ECO:0000313|EnsemblMetazoa:HelroP103167, ECO:0000313|Proteomes:UP000015101};
RN   [1] {ECO:0000313|Proteomes:UP000015101}
RP   NUCLEOTIDE SEQUENCE.
RA   Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA   Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA   Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA   Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA   Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ESN93811.1, ECO:0000313|Proteomes:UP000015101}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA   Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA   Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(2013).
RN   [3] {ECO:0000313|EnsemblMetazoa:HelroP103167}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- FUNCTION: Component of the NuA4 histone acetyltransferase complex which
CC       is involved in transcriptional activation of selected genes principally
CC       by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is
CC       also involved in DNA repair. Involved in gene silencing by neighboring
CC       heterochromatin, blockage of the silencing spreading along the
CC       chromosome, and required for cell cycle progression through G2/M.
CC       {ECO:0000256|ARBA:ARBA00025513}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU361124}.
CC   -!- SIMILARITY: Belongs to the enhancer of polycomb family.
CC       {ECO:0000256|ARBA:ARBA00008035, ECO:0000256|RuleBase:RU361124}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AMQM01007209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KB097587; ESN93811.1; -; Genomic_DNA.
DR   RefSeq; XP_009028025.1; XM_009029777.1.
DR   AlphaFoldDB; T1EDE7; -.
DR   STRING; 6412.T1EDE7; -.
DR   EnsemblMetazoa; HelroT103167; HelroP103167; HelroG103167.
DR   GeneID; 20194599; -.
DR   KEGG; hro:HELRODRAFT_103167; -.
DR   CTD; 20194599; -.
DR   eggNOG; KOG2261; Eukaryota.
DR   HOGENOM; CLU_294104_0_0_1; -.
DR   InParanoid; T1EDE7; -.
DR   OrthoDB; 5398022at2759; -.
DR   Proteomes; UP000015101; Unassembled WGS sequence.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0032777; C:piccolo histone acetyltransferase complex; IBA:GO_Central.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR024943; Enhancer_polycomb.
DR   InterPro; IPR019542; Enhancer_polycomb-like_N.
DR   PANTHER; PTHR14898; ENHANCER OF POLYCOMB; 1.
DR   PANTHER; PTHR14898:SF0; ENHANCER OF POLYCOMB-LIKE PROTEIN; 1.
DR   Pfam; PF10513; EPL1; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU361124};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015101};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU361124};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|RuleBase:RU361124}.
FT   DOMAIN          14..158
FT                   /note="Enhancer of polycomb-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10513"
FT   REGION          378..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          503..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          609..664
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          764..826
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..413
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..438
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..468
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..487
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..527
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        617..640
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        649..664
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1032 AA;  116845 MW;  EF3C94C0F485083A CRC64;
     MEGVFRMNKL TFRAKALDSN KPLQVFVGDD IPDSTDFVTA NRTVPEMPTG MEKEEETQHH
     LQKALISQQS FGLVNRLIIP VPDVKVIDER YKQTYSSRSK FQLPKKFIHV QPSSTDQDVP
     DYDMDEEDEE WLMSHPLTNQ KLLNDPIRFE CVMDKLEKSS SHTVISLPEA KALIKEKDDV
     IIAIYDYWLT KRLKQQTKLQ HLIKLERKEL AATAAASSST SAATTSTTLL SSSCIGGGGS
     SGSSISNVHS INPYVAFRKR AERMQTRKNR KNDEQSYLKM LKVKDGLLKT MSLLKMLRQR
     EILKKAQVQI KSDLFIKRYE QSDWSGSQLE EAIQKFKSTR PVSRPITIQS TNSYTSSNNR
     CHNNNNLIYN ETYGPNIYHN DVNNSNNNNF HKNNSNNNNV QSHRPQKNQK SQKNYLKSTH
     KKHYHTHHHG HYHHHLHRHT FARNTTDNDI HLSDNDSKND DDDDYVCDRN NNNNNNNNNN
     NNSTADKGDV ITLTKSLTLF PTSVMDSRQD DDDDDDVNVD DDFTGDDNDE ASMDGRFAFR
     RKKGCLYYDV IPFLSFHFSA NDHSSTDNTV FSRCPRQQRN QNFSLVSIDE SHRRIGQLRQ
     RIGRGGRVIW DRSPYEPNEW QSHQPPHRHQ PQNQQQQPHR PHVYTRHKQV RSTGNDDVSG
     HHNSLKREGF LNSDVMDSNF CFSTFLDDYT SDDCNVKVED VEVDVVSDDK TFFSNFEDGS
     ISTSDDNCSN MSSLNVITSS SSSSRTARGQ QSCSSFLKRK CTSRTGSADS GISSPSLPAS
     SVSPSLSTYL PQSSSLSSSS STSSSSTLSS SSSSSSSSSS SLSNKSSSSS LVTRVAICSD
     NKCKTNNNNI ICNHLPRHHH DDNNNNNNYN NNNNNNISGD INNTNNDNKF CDITNHTNVD
     SSYESLNRPQ FTESKYLKVN NHKRLKIEEE VSSSGGTKNI RTTSMATGRQ IATLSFKNEK
     INKVHSNNNS NNINSNNINS NNINSNNINS NNSNHNNKYL LVNDSRYNFI AVVTNEDFLK
     KNNETISALD LI
//
DBGET integrated database retrieval system