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BRE1B_ORYSI
ID   BRE1B_ORYSI             Reviewed;         844 AA.
AC   A2ZAC2; B8BIA7;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=E3 ubiquitin-protein ligase BRE1-like 2;
DE            EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9C895};
DE   AltName: Full=RING-type E3 ubiquitin transferase BRE1-like 2 {ECO:0000305};
GN   Name=BRE1B; ORFNames=OsI_34687;
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that monoubiquitinates H2B to
CC       form H2BK143ub1. H2BK143ub1 gives a specific tag for epigenetic
CC       transcriptional activation and is also prerequisite for H3K4me and
CC       maybe H3K79me. It thereby plays a central role in histone code and gene
CC       regulation. Forms a ubiquitin ligase complex in cooperation with the E2
CC       enzyme UBC2/RAD6. {ECO:0000250|UniProtKB:Q9C895}.
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:Q9C895};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9C895}.
CC   -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC       ubiquitin-conjugating enzyme. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000305}.
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DR   EMBL; CM000135; EEC67460.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2ZAC2; -.
DR   SMR; A2ZAC2; -.
DR   STRING; 39946.A2ZAC2; -.
DR   PRIDE; A2ZAC2; -.
DR   EnsemblPlants; BGIOSGA033459-TA; BGIOSGA033459-PA; BGIOSGA033459.
DR   Gramene; BGIOSGA033459-TA; BGIOSGA033459-PA; BGIOSGA033459.
DR   HOGENOM; CLU_002640_1_0_1; -.
DR   OMA; DENTSCT; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000007015; Chromosome 10.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblPlants.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0044260; P:cellular macromolecule metabolic process; IEA:UniProt.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0033523; P:histone H2B ubiquitination; IEA:EnsemblPlants.
DR   GO; GO:0010390; P:histone monoubiquitination; IEA:EnsemblPlants.
DR   GO; GO:0045087; P:innate immune response; IEA:EnsemblPlants.
DR   GO; GO:0009965; P:leaf morphogenesis; IEA:EnsemblPlants.
DR   GO; GO:0010162; P:seed dormancy process; IEA:EnsemblPlants.
DR   GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IEA:EnsemblPlants.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR23163; PTHR23163; 1.
DR   SMART; SM00184; RING; 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;
KW   Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..844
FT                   /note="E3 ubiquitin-protein ligase BRE1-like 2"
FT                   /id="PRO_0000293113"
FT   ZN_FING         792..831
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          244..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1..38
FT                   /evidence="ECO:0000255"
FT   COILED          160..240
FT                   /evidence="ECO:0000255"
FT   COILED          290..604
FT                   /evidence="ECO:0000255"
FT   COILED          640..670
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        244..264
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   844 AA;  96498 MW;  2A57EDD94FDE5E94 CRC64;
     MDAAALQYEN QKLVQQLEAQ KSKMRALEGK FKELRDEQCS YDNTLICLNK MWNQLIDDLV
     LLGVRAGGDL NGLQALDHEE MSEESLESCP SEEIFLFRLL NSRNFRNNDD SSLSKLVEEA
     LALRYSTTVT LMKSLQEAFA VQQARSESLS LALNGQNSSE DVIVALENHN DYLKEVVDNL
     RQAVSIINRK HEKYLDEIEA FKNNQSRELH EVKCLSGELE ESMAELEESR RKLAVLQLQT
     GGGSLMNTSA PNGVNGSVST DKSSDKGMGW RDLKDAVEEA KTLAANRLFE LHETQEDNLI
     LSKQLEDIQD QLKDENYIVT SKPYTILSDQ LHHLNAEIER YRGLVEVLQN EKDQLMQKEE
     EMLAKAESVD AVQQSITTYK AKIEDLEHEI QKLMAEKNDL EIKAEEALQD SGKKDFKDEI
     HVMAASLSKE MELLDNQMNR SKDAASEALA LREEADYLRT LLAKKIDEQK EISDRYNTQV
     TEIKSLKALI ETLDQEKQEL QFIVDMLGKE CSESRAISEI EESENRARKQ AEYLRKCLEE
     HNLELRVKAA NEAETACQQR LSIAEAELED LRAKVDASER DVMKLKESIR IKEAEVDGHI
     SEIETIGQAY EDMQTQNQHL LQQVADRDDF NIKLVSDSVK MKQAYGSLLA EKNMLQKQLQ
     HVNSSLESSK LKITSGEEQM KTYVAQAMKS SSENRHLAIS LERTMLEVSD AEKELKWLRS
     ATGSAEKEYE INQKKIAELK MELERERNER IKLEEEYEEV KNEVSELTSE TEETTIQKLQ
     DEIKECKAIL KCGVCFDRPK EVVITKCFHL FCSPCIQRNL EIRHRKCPGC GTPFGQSDVR
     EVKI
 
 
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