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BRE1_CRYNB
ID   BRE1_CRYNB              Reviewed;         820 AA.
AC   P0CQ63; Q55N50; Q5KBI0;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=E3 ubiquitin-protein ligase BRE1;
DE            EC=2.3.2.27 {ECO:0000250|UniProtKB:Q07457};
DE   AltName: Full=RING-type E3 ubiquitin transferase BRE1 {ECO:0000305};
GN   Name=BRE1; OrderedLocusNames=CNBH2340;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that mediates monoubiquitination
CC       of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for
CC       epigenetic transcriptional activation and is also a prerequisite for
CC       H3K4me and H3K79me formation. {ECO:0000250|UniProtKB:Q07457}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q07457};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q07457}.
CC   -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000305}.
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DR   EMBL; AAEY01000042; EAL19135.1; -; Genomic_DNA.
DR   RefSeq; XP_773782.1; XM_768689.1.
DR   AlphaFoldDB; P0CQ63; -.
DR   SMR; P0CQ63; -.
DR   EnsemblFungi; EAL19135; EAL19135; CNBH2340.
DR   GeneID; 4937757; -.
DR   KEGG; cnb:CNBH2340; -.
DR   VEuPathDB; FungiDB:CNBH2340; -.
DR   HOGENOM; CLU_019713_0_0_1; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001435; Chromosome 8.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0010390; P:histone monoubiquitination; IEA:InterPro.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR23163; PTHR23163; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator; Coiled coil; Metal-binding; Nucleus; Transferase;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..820
FT                   /note="E3 ubiquitin-protein ligase BRE1"
FT                   /id="PRO_0000410242"
FT   ZN_FING         767..806
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          213..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          68..92
FT                   /evidence="ECO:0000255"
FT   COILED          164..226
FT                   /evidence="ECO:0000255"
FT   COILED          287..738
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..235
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..251
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   820 AA;  92867 MW;  C9B7A566354DEE4D CRC64;
     MNADLKRVRE NTLDDSPSPS AKRRLNSNAS SPIQPSDDEG MAEWMKIVEV KRKEAIYRQM
     LEYRRISEHE TKRANDLEAQ RRVLEASFHA VELCWTQIVA AVRDLAGAEN LQLKEEEVLE
     PLLDPSTPVP ELEKALRSRL PTTRQLVTRF VDLVAHNATR PASEADLQAR CLKLEAEASA
     LRSNSKLLES EISALKGSRD EAQRDLQRIR KALDRERMEH GKAQEEWKEE RTRGGQATPN
     LRANGSGHST PNGKVEADKK FYSGAGPSMA GVLQDTSELE QLAASRLKQL EQLRFEQTQL
     QQEVDRLKIL ANHPSETALR ESPFFQVYLH QLSTSINRAE SLQTRFTATE SKLDQLRDSN
     GEFREAVLAE ARGQTETLRA QMAKKDSDIA RLRGQRDELN SEIMERRAKE VEKCKYTEQI
     ENLANSRQER ISFLTSEVRR LKGKLAAAHS SDGYLSFLKE SGIDGDYVKD LEAKVVTSQD
     QINALTSQLE RVSSDTAAAK SETEVRTELE SAKRLLARYE RILGPNPEAA EDVRYLSQQL
     EKKEKERASL EMKLEEAEAA TNALYSEVEG LSKLWEALDQ TVKSKVLELR DGEQKITRLA
     TEKAKADNKY FAAMRAKEAV DMEAKAAQRS VEKQLRLLER AQEVETSLRS QITANEKGLT
     ALKNNALDLQ NQLATVVAEK TQLELRLQQS QNALVEAQQI MHQRVAEAIA EKEARAKLQD
     EADGQMKIIK KLKERQDAVA AASQTGMSDH EWAITQERDK LLKLLKCSCC EQNFKQQVIV
     KCMHTFCKQC LEQRIASRQR KCPACGLAFA KEDIQTLYWQ
 
 
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