ASH2_SCHPO
ID ASH2_SCHPO Reviewed; 652 AA.
AC O60070;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Set1 complex component ash2;
DE Short=Set1C component ash2;
DE AltName: Full=COMPASS component ash2;
DE AltName: Full=Complex proteins associated with set1 protein ash2;
DE AltName: Full=Lid2 complex component ash2;
DE Short=Lid2C component ash2;
GN Name=ash2; ORFNames=SPBC13G1.08c;
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] {ECO:0000312|EMBL:CAA18661.1}
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] {ECO:0000305}
RP FUNCTION OF THE SET1 COMPLEX, AND COMPOSITION OF THE SET1 AND LID2
RP COMPLEXES.
RX PubMed=12488447; DOI=10.1074/jbc.m209562200;
RA Roguev A., Schaft D., Shevchenko A., Aasland R., Shevchenko A.,
RA Stewart A.F.;
RT "High conservation of the Set1/Rad6 axis of histone 3 lysine 4 methylation
RT in budding and fission yeasts.";
RL J. Biol. Chem. 278:8487-8493(2003).
RN [3] {ECO:0000305}
RP COMPOSITION OF THE SET1 AND LID2 COMPLEXES.
RX PubMed=14617822; DOI=10.1074/mcp.m300081-mcp200;
RA Roguev A., Shevchenko A., Schaft D., Thomas H., Stewart A.F.,
RA Shevchenko A.;
RT "A comparative analysis of an orthologous proteomic environment in the
RT yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe.";
RL Mol. Cell. Proteomics 3:125-132(2004).
CC -!- FUNCTION: The Set1 complex specifically methylates 'Lys-4' of histone
CC H3. {ECO:0000269|PubMed:12488447}.
CC -!- SUBUNIT: Component of the Set1 complex composed of ash2, sdc1, set1,
CC shg1, spp1, swd1, swd2 and swd3. Component of the Lid2 complex composed
CC of ash2, jmj3, lid2, sdc1 and snt2. {ECO:0000269|PubMed:12488447,
CC ECO:0000269|PubMed:14617822}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR EMBL; CU329671; CAA18661.1; -; Genomic_DNA.
DR PIR; T39409; T39409.
DR RefSeq; NP_596557.1; NM_001022478.2.
DR AlphaFoldDB; O60070; -.
DR SMR; O60070; -.
DR BioGRID; 276222; 246.
DR STRING; 4896.SPBC13G1.08c.1; -.
DR iPTMnet; O60070; -.
DR MaxQB; O60070; -.
DR PaxDb; O60070; -.
DR PRIDE; O60070; -.
DR EnsemblFungi; SPBC13G1.08c.1; SPBC13G1.08c.1:pep; SPBC13G1.08c.
DR GeneID; 2539667; -.
DR KEGG; spo:SPBC13G1.08c; -.
DR PomBase; SPBC13G1.08c; ash2.
DR VEuPathDB; FungiDB:SPBC13G1.08c; -.
DR eggNOG; KOG2626; Eukaryota.
DR HOGENOM; CLU_380890_0_0_1; -.
DR InParanoid; O60070; -.
DR OMA; SWYSTVQ; -.
DR PhylomeDB; O60070; -.
DR PRO; PR:O60070; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IC:PomBase.
DR GO; GO:0048189; C:Lid2 complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0031507; P:heterochromatin assembly; IC:PomBase.
DR GO; GO:0051568; P:histone H3-K4 methylation; IBA:GO_Central.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IMP:PomBase.
DR Gene3D; 2.60.120.920; -; 1.
DR InterPro; IPR037353; ASH2.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR PANTHER; PTHR10598; PTHR10598; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
PE 4: Predicted;
KW Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..652
FT /note="Set1 complex component ash2"
FT /id="PRO_0000059320"
FT DOMAIN 330..519
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 40..94
FT /note="PHD-type"
FT /evidence="ECO:0000255"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 652 AA; 74253 MW; 998E783EC8BD0360 CRC64;
MLAHGSNDYG VSLKGNKTGS SPSKASSLNW NEPHTLNEQN TYCYCGKDRN LRFPDLQCSV
CLNMFHLSCL SPPCTSMMGF STNYQFVCKH CTEDGFERFE RGVSAWKAIT ATAMANLVVK
RYVETNPDVP VDSFNAEKMR NFQANTYFFK KKEDLIPFIE EHWQLLCPDR EKVQTWQATL
GSCLVANRDT YRAKDETMRN QNSEYALNNP NLFDFRSGYI FPFQRVGATV PKKRLVETET
PPPSSSKLKE DYKDSKREMK RSNTPWSNAS IKKNEVPTVP IRYKPPPWRD SDFETVPKLP
IFYPNSSSPN FFSLSEIPFN RRGFRYSPCE AAKDLPNVMY REIELPPFTS RINWHDISTP
VFIDHSALCA TVEKGFRMAR SNVFMTSGEW YFEIKIEKGG GDDGAHVRIG VSRREAPLDA
PVGYDAYSYG LRDLGGQKVH MSRPRNFMDS FGTGDIIGLH ISLPKPSFAQ HTTLPSCHDR
IPIRYKGQLY FEQPDYVPSK MMDELMIPSK HNRYIDLPYI PGSFIKVYKN GSYMGTAFEN
LLDFNPPNSI NSNHYSFDDG SLGYYPSISM YGGGIARFQF GPQFSHRPLV LGSNVRPVSE
RYNEQIAEDV LCDILDEIDY AEDPNTSSVT IDVPQEPNAG ITIIPEIKDI TE
