ID   BRL1_SCHPO              Reviewed;         692 AA.
AC   Q1MTQ0;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=E3 ubiquitin-protein ligase brl1;
DE            EC=2.3.2.27 {ECO:0000305};
DE   AltName: Full=BRE1-like protein 1;
DE   AltName: Full=RING finger protein 2;
DE   AltName: Full=RING-type E3 ubiquitin transferase brl1 {ECO:0000305};
GN   Name=brl1; Synonyms=rfp2; ORFNames=SPCC1919.15, SPCC790.01;
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; CAA22646.1; -; Genomic_DNA.
DR   RefSeq; NP_588497.1; NM_001023487.2.
DR   AlphaFoldDB; Q1MTQ0; -.
DR   SMR; Q1MTQ0; -.
DR   BioGRID; 275674; 10.
DR   IntAct; Q1MTQ0; 2.
DR   STRING; 4896.SPCC1919.15.1; -.
DR   iPTMnet; Q1MTQ0; -.
DR   MaxQB; Q1MTQ0; -.
DR   PaxDb; Q1MTQ0; -.
DR   PRIDE; Q1MTQ0; -.
DR   EnsemblFungi; SPCC1919.15.1; SPCC1919.15.1:pep; SPCC1919.15.
DR   GeneID; 2539102; -.
DR   KEGG; spo:SPCC1919.15; -.
DR   PomBase; SPCC1919.15; brl1.
DR   VEuPathDB; FungiDB:SPCC1919.15; -.
DR   eggNOG; KOG0978; Eukaryota.
DR   HOGENOM; CLU_407184_0_0_1; -.
DR   InParanoid; Q1MTQ0; -.
DR   OMA; QNASICK; -.
DR   PhylomeDB; Q1MTQ0; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q1MTQ0; -.
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; IDA: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; 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; 2.
DR   Pfam; PF00097; zf-C3HC4; 1.
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..692
FT                   /note="E3 ubiquitin-protein ligase brl1"
FT                   /id="PRO_0000352846"
FT   ZN_FING         639..679
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   COILED          302..370
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   692 AA;  80723 MW;  371F827BD0CA2A33 CRC64;
     MSVVNESRKR RRLIHSEKET RRLDLGEEDD LELFQKEAAW RRSREYEHLT VLEKKLYEYW
     ESLVLKLDHY VAAALENHEQ SFEELEKITA SLYQPDDNLQ TLDLSLAEFS LIKDAQNYLN
     KYASYFQAHE PTLQKLAKFG SFKLKETPNV HEWIDQRQVH FTSMINYRTS QLKLALLKRK
     LSFFREALNS AELEWKRVQQ DQLTSASERS IENIADDIPA SEPKAILENG EGCLNDNDNI
     SKLKNNFQSQ ADLMQANINS KLDELSQKST RAAQLYVDIM GITDERVSRE PHYLELKGVL
     SSNEEKIESI NRDLSSLFED IQFFISQRTK RQKDIIDLKL ACVKEKQQLI KTLESSLTQI
     RNERDSLVAK QQMQYTNNLF FDDMMLLLSN LSNARVAILE GYSNRLCIWD RIERSKTGEM
     NNVLDEKEEI SASSALEKLI KNNSCLEAEL PSMYAAFDQS QSRLLKKYEE LETKEKKALE
     MHYEKARATQ KYFAAMKARD ILMTEKKTLK LAENKEHDYI GKLQEREHAL TKYESSLKAE
     LEVYKQIKEI YGKHSVEVLT EDKHLQVKQT KLTQKLEDLI ESVQKSGEKL MIMHQKLFHL
     QEEHTILSIK ASYNKKESHL INQAYETQEA QVYKGMLKCS VCNFSNWKSK LIPNCGHAFC
     SNCMEPFYEH KTSTCPQCET PFSVSDILTI HL