BRL2_SCHPO
ID BRL2_SCHPO Reviewed; 680 AA.
AC O74563;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=E3 ubiquitin-protein ligase brl2;
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=BRE1-like protein 2;
DE AltName: Full=RING finger protein 1;
DE AltName: Full=RING-type E3 ubiquitin transferase brl2 {ECO:0000305};
GN Name=brl2; Synonyms=rfp1; ORFNames=SPCC970.10c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP FUNCTION.
RX PubMed=17374714; DOI=10.1101/gad.1516207;
RA Tanny J.C., Erdjument-Bromage H., Tempst P., Allis C.D.;
RT "Ubiquitylation of histone H2B controls RNA polymerase II transcription
RT elongation independently of histone H3 methylation.";
RL Genes Dev. 21:835-847(2007).
RN [4]
RP IDENTIFICATION IN THE HULC COMPLEX, FUNCTION OF THE HULC COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17363370; DOI=10.1074/jbc.m700292200;
RA Zofall M., Grewal S.I.S.;
RT "HULC, a histone H2B ubiquitinating complex, modulates heterochromatin
RT independent of histone methylation in fission yeast.";
RL J. Biol. Chem. 282:14065-14072(2007).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which belongs to the histone H2B
CC ubiquitin ligase complex (HULC) which mediates monoubiquitination of
CC 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:0000269|PubMed:17363370,
CC ECO:0000269|PubMed:17374714}.
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:0000305};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the histone H2B ubiquitin ligase complex (HULC)
CC composed of at least brl1, brl2, rhp6 and shf1.
CC {ECO:0000269|PubMed:17363370}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000305}.
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DR EMBL; CU329672; CAA20703.1; -; Genomic_DNA.
DR PIR; T41670; T41670.
DR RefSeq; NP_587845.1; NM_001022838.2.
DR AlphaFoldDB; O74563; -.
DR SMR; O74563; -.
DR BioGRID; 275874; 7.
DR IntAct; O74563; 2.
DR STRING; 4896.SPCC970.10c.1; -.
DR MaxQB; O74563; -.
DR PaxDb; O74563; -.
DR PRIDE; O74563; -.
DR EnsemblFungi; SPCC970.10c.1; SPCC970.10c.1:pep; SPCC970.10c.
DR GeneID; 2539307; -.
DR KEGG; spo:SPCC970.10c; -.
DR PomBase; SPCC970.10c; brl2.
DR VEuPathDB; FungiDB:SPCC970.10c; -.
DR eggNOG; KOG0978; Eukaryota.
DR HOGENOM; CLU_019713_2_0_1; -.
DR InParanoid; O74563; -.
DR OMA; GAIYRQM; -.
DR PhylomeDB; O74563; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:O74563; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0033503; C:HULC complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; EXP:PomBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR GO; GO:0045815; P:epigenetic maintenance of chromatin in transcription-competent conformation; TAS:PomBase.
DR GO; GO:0071894; P:histone H2B conserved C-terminal lysine ubiquitination; IBA:GO_Central.
DR GO; GO:0010390; P:histone monoubiquitination; IBA:GO_Central.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:PomBase.
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; 2.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Coiled coil; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..680
FT /note="E3 ubiquitin-protein ligase brl2"
FT /id="PRO_0000055855"
FT ZN_FING 627..667
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 206..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 44..72
FT /evidence="ECO:0000255"
FT COILED 261..288
FT /evidence="ECO:0000255"
FT COILED 353..399
FT /evidence="ECO:0000255"
FT COILED 485..609
FT /evidence="ECO:0000255"
FT COMPBIAS 215..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 680 AA; 78053 MW; 61B90DE682436705 CRC64;
MYQNGKPDAP TILGQKRELE DVEIQDDDIQ EVSKEDLLKD VRVRSIQFDE LESKIEGLQN
LAEEKLKVLA TLVSWWPEIL QQFSVVFQGN ELKDFESEGV FSILEKFPEL SYFNDAVKNN
KTKALSIIQK LLSTVDSSTN SVSRDPFSVL SIDDSALTEK LNTINLDIDK ILDELDTTRS
QLHSIIKLPD RSSSFTLQCI NESVRPQSTK VKEEATTSSK GKDEEKKVST VEQRTQLQQL
SRLQDQQNGL MESRSQSLKI LDSNVNEMDK LIMERENALN NVETTNLKKY SSFLALKEAV
SMTSEQLRVL EHLLSECSHE INVLSQQSKN FNGVFESSYQ PLINDLDHQI SVMQNDEKRI
NNAKTELSLS LEKKLEAKKQ KEKVYKDKLD ELANLETMVL EKKKAVATRE AANKIRLVDL
NDLELQKDLS TYLSKELAST EKAFRLVKQQ TVKSSHSHYQ ELITKFSVEK EKAEQKYFLT
MKSTDSLHAE VKLLRQKYQK TNEIISKMLN SQDTAVHRII EFEDQLARLS SVRNNSIKQS
TTFQVKKSSQ KSTIQNLEEK VSYLQQFMDK NNATLTDLEF QCSDLSSSID ILSKQDEEHE
KEKRKLKDTG VSTSAEELKT FRAMCKCSVC NFERWKDRII SLCGHGFCYQ CIQKRIETRQ
RRCPICGRGF GASDVIPIHL
