SHF1_SCHPO
ID SHF1_SCHPO Reviewed; 165 AA.
AC Q9UUI2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Small histone ubiquitination factor 1;
GN Name=shf1; ORFNames=SPAC22F8.12c;
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 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: Component of the histone H2B ubiquitin ligase complex (HULC)
CC which plays a role in transcription regulation by catalyzing the
CC monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives
CC a specific tag for epigenetic transcriptional activation and is also a
CC prerequisite for H3K4me and H3K79me formation.
CC {ECO:0000269|PubMed:17363370}.
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}. Cytoplasm
CC {ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, spindle pole body {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329670; CAB52722.1; -; Genomic_DNA.
DR PIR; T38202; T38202.
DR RefSeq; NP_594735.1; NM_001020163.2.
DR AlphaFoldDB; Q9UUI2; -.
DR SMR; Q9UUI2; -.
DR BioGRID; 278171; 41.
DR IntAct; Q9UUI2; 3.
DR STRING; 4896.SPAC22F8.12c.1; -.
DR iPTMnet; Q9UUI2; -.
DR SwissPalm; Q9UUI2; -.
DR MaxQB; Q9UUI2; -.
DR PaxDb; Q9UUI2; -.
DR PRIDE; Q9UUI2; -.
DR EnsemblFungi; SPAC22F8.12c.1; SPAC22F8.12c.1:pep; SPAC22F8.12c.
DR GeneID; 2541675; -.
DR KEGG; spo:SPAC22F8.12c; -.
DR PomBase; SPAC22F8.12c; shf1.
DR VEuPathDB; FungiDB:SPAC22F8.12c; -.
DR HOGENOM; CLU_1611745_0_0_1; -.
DR OMA; YESRFPS; -.
DR PRO; PR:Q9UUI2; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0033503; C:HULC complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005816; C:spindle pole body; IEA:UniProtKB-SubCell.
DR GO; GO:0045815; P:epigenetic maintenance of chromatin in transcription-competent conformation; TAS:PomBase.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:PomBase.
PE 1: Evidence at protein level;
KW Chromatin regulator; Cytoplasm; Cytoskeleton; Nucleus; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..165
FT /note="Small histone ubiquitination factor 1"
FT /id="PRO_0000304068"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 165 AA; 18923 MW; 1721A65EBD472550 CRC64;
MSSRRNDYHY DGNDHQYRSP LKSNVDQNSF YESSYRSRQS YHQRTKTPRS SYDSPSSSTN
SKEHNSPYHY RVPSNNSTRA SFGAASTDTN VELPKINLPD SSLSSKLQSC KSACENSSQS
LLNVEQQYAQ QVHFWEKIRT DIYREGLRSD AAVKSLNDFV NNVSF
