SLM9_SCHPO
ID SLM9_SCHPO Reviewed; 807 AA.
AC O74309;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Histone transcription regulator slm9;
GN Name=slm9; ORFNames=SPBC15D4.03;
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 [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10835386; DOI=10.1093/genetics/155.2.623;
RA Kanoh J., Russell P.;
RT "Slm9, a novel nuclear protein involved in mitotic control in fission
RT yeast.";
RL Genetics 155:623-631(2000).
RN [2]
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 [3]
RP FUNCTION, AND INTERACTION WITH HIP1.
RX PubMed=15121850; DOI=10.1128/mcb.24.10.4309-4320.2004;
RA Blackwell C., Martin K.A., Greenall A., Pidoux A., Allshire R.C.,
RA Whitehall S.K.;
RT "The Schizosaccharomyces pombe HIRA-like protein Hip1 is required for the
RT periodic expression of histone genes and contributes to the function of
RT complex centromeres.";
RL Mol. Cell. Biol. 24:4309-4320(2004).
RN [4]
RP FUNCTION, AND INTERACTION WITH HIP3.
RX PubMed=16428807; DOI=10.1074/jbc.m512170200;
RA Greenall A., Williams E.S., Martin K.A., Palmer J.M., Gray J., Liu C.,
RA Whitehall S.K.;
RT "Hip3 interacts with the HIRA proteins Hip1 and Slm9 and is required for
RT transcriptional silencing and accurate chromosome segregation.";
RL J. Biol. Chem. 281:8732-8739(2006).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406; SER-421 AND SER-422, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Probably required for replication-independent chromatin
CC assembly (By similarity). Required for transcriptional silencing in the
CC outer repeat (otr) centromeric repeats and the Tf2 long terminal repeat
CC retrotransposons. May play an indirect role in the regulation of cdc2
CC and/or wee1 at the G2/M stage of mitosis. {ECO:0000250,
CC ECO:0000269|PubMed:10835386, ECO:0000269|PubMed:15121850,
CC ECO:0000269|PubMed:16428807}.
CC -!- SUBUNIT: Interacts with hip1 and hip3. {ECO:0000269|PubMed:15121850,
CC ECO:0000269|PubMed:16428807}.
CC -!- INTERACTION:
CC O74309; P87314: hip1; NbExp=4; IntAct=EBI-1556117, EBI-1556094;
CC O74309; P87315: hip3; NbExp=3; IntAct=EBI-1556117, EBI-1556159;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- SIMILARITY: Belongs to the WD repeat HIR1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA20478.1; -; Genomic_DNA.
DR PIR; T39479; T39479.
DR RefSeq; NP_596243.1; NM_001022162.2.
DR AlphaFoldDB; O74309; -.
DR SMR; O74309; -.
DR BioGRID; 276665; 76.
DR IntAct; O74309; 2.
DR STRING; 4896.SPBC15D4.03.1; -.
DR iPTMnet; O74309; -.
DR MaxQB; O74309; -.
DR PaxDb; O74309; -.
DR PRIDE; O74309; -.
DR EnsemblFungi; SPBC15D4.03.1; SPBC15D4.03.1:pep; SPBC15D4.03.
DR GeneID; 2540128; -.
DR KEGG; spo:SPBC15D4.03; -.
DR PomBase; SPBC15D4.03; slm9.
DR VEuPathDB; FungiDB:SPBC15D4.03; -.
DR eggNOG; KOG0973; Eukaryota.
DR HOGENOM; CLU_350606_0_0_1; -.
DR InParanoid; O74309; -.
DR OMA; SEGWWMI; -.
DR PhylomeDB; O74309; -.
DR PRO; PR:O74309; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IC:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000417; C:HIR complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR031120; HIR1.
DR InterPro; IPR011494; Hira.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13831; PTHR13831; 2.
DR Pfam; PF07569; Hira; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; WD repeat.
FT CHAIN 1..807
FT /note="Histone transcription regulator slm9"
FT /id="PRO_0000051219"
FT REPEAT 62..100
FT /note="WD 1"
FT REPEAT 102..140
FT /note="WD 2"
FT REPEAT 182..221
FT /note="WD 3"
FT REPEAT 230..273
FT /note="WD 4"
FT REPEAT 276..322
FT /note="WD 5"
FT REPEAT 326..367
FT /note="WD 6"
FT REPEAT 492..526
FT /note="WD 7"
FT REPEAT 528..574
FT /note="WD 8"
FT REGION 144..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 807 AA; 90433 MW; B8BFB73852EB7B45 CRC64;
MHIFVPKLLE NHQFSSISSS KDFVAVSAET NVYILSKDFF YPKSSEKRII QSLNGHKTTH
LSFDSPISCI RFTYDGSCLA VATEAGTFLY HSEKWDKAFQ VLSGPAYEVC WSQQGHILAT
SWKQISIYVK DEGLRTETIV KKTEHADSNH QPAVSIEESK EAVESTSQSS EISFKLIKVI
EGHHTFVGGL AFDPMGQFLA SQSFDHTLKV WKLSTFGVEK SIAKPFEQMP TGNRFLRLSW
SPDGAHIASV NAVNEGAYVI AIVQRDTWTY DINLVGHQGP LECATFNPYL YEDPFQKSII
ASAAHDGCVS IWNTACARPM AVIHELSCSS FVDLQWSTSG FELYGVSLDG NLMLLQFEES
EFGEKMDTIH YPDDLSYFNS SRSKAHVNKN AAADRTTSPT QGQPESPSKS ILLRPPPSIA
SSPESKRRKC PKKFVARPPV PHPTSLYSQI RIGCPYLKPK LVISKSFGTL IVKNHNQLSL
LKCTFSNLDG NDCSWFSYLP NAIVLANGTS VFWAVATEDS SIYIYSPAGR LLLPPVVVAA
TPCFLECCGD FLCCIVSTGL LYIWNIKNFE AIHSPVSTLP LFHSNFSVSK IARGPSIEQF
FVTKQGHPVA IMSDGNAFAF IRDSSSWLRV SEGWWMIGSQ YWGPLASESN EESPLGFLER
CTDEEIIKAG RGRFLQRLVK ALMLRQGYDN YEMLVSIRHL ENRLMSSAKL DLEYDFRENL
ILYAKKIAEE GMKDKMDELC KELLGPLRIP HNGIDTVKVG NRLWSPTIAG NNKRNLLKDI
IIHTAKYRDM QRITSQYSDL LRRSALL
