PHF2_SCHPO
ID PHF2_SCHPO Reviewed; 538 AA.
AC Q09908;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=SWM histone demethylase complex subunit phf2;
DE AltName: Full=PHD finger domain-containing protein phf2;
GN Name=phf2; Synonyms=saf60, swp2; ORFNames=SPAC30D11.08c;
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]
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 IDENTIFICATION IN THE SWM HISTONE DEMETHYLASE COMPLEX.
RX PubMed=16990277; DOI=10.1074/jbc.m606349200;
RA Nicolas E., Lee M.G., Hakimi M.-A., Cam H.P., Grewal S.I.S.,
RA Shiekhattar R.;
RT "Fission yeast homologs of human histone H3 lysine 4 demethylase regulate a
RT common set of genes with diverse functions.";
RL J. Biol. Chem. 281:35983-35988(2006).
RN [3]
RP IDENTIFICATION IN THE SWM HISTONE DEMETHYLASE COMPLEX, AND FUNCTION OF THE
RP SWM COMPLEX.
RX PubMed=17434129; DOI=10.1016/j.molcel.2007.02.023;
RA Lan F., Zaratiegui M., Villen J., Vaughn M.W., Verdel A., Huarte M.,
RA Shi Y., Gygi S.P., Moazed D., Martienssen R.A., Shi Y.;
RT "S. pombe LSD1 homologs regulate heterochromatin propagation and
RT euchromatic gene transcription.";
RL Mol. Cell 26:89-101(2007).
RN [4]
RP IDENTIFICATION IN THE SWM HISTONE DEMETHYLASE COMPLEX, AND FUNCTION OF THE
RP SWM COMPLEX.
RX PubMed=17440621; DOI=10.1371/journal.pone.0000386;
RA Opel M., Lando D., Bonilla C., Trewick S.C., Boukaba A., Walfridsson J.,
RA Cauwood J., Werler P.J., Carr A.M., Kouzarides T., Murzina N.V.,
RA Allshire R.C., Ekwall K., Laue E.D.;
RT "Genome-wide studies of histone demethylation catalysed by the fission
RT yeast homologues of mammalian LSD1.";
RL PLoS ONE 2:E386-E386(2007).
CC -!- FUNCTION: Component of the SWM histone demethylase complex that
CC specifically demethylates H3K9me2, a specific tag for epigenetic
CC transcriptional activation, thereby acting as a corepressor. Has a role
CC in regulating heterochromatin propagation and euchromatic
CC transcription. {ECO:0000269|PubMed:17434129,
CC ECO:0000269|PubMed:17440621}.
CC -!- SUBUNIT: Component of the SWM histone demethylase complex composed of
CC at least lsd1, lsd2, phf1 and phf2. {ECO:0000269|PubMed:16990277,
CC ECO:0000269|PubMed:17434129, ECO:0000269|PubMed:17440621}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR EMBL; CU329670; CAA91894.1; -; Genomic_DNA.
DR PIR; T38591; S62566.
DR RefSeq; NP_593209.1; NM_001018605.2.
DR AlphaFoldDB; Q09908; -.
DR SMR; Q09908; -.
DR BioGRID; 278708; 14.
DR STRING; 4896.SPAC30D11.08c.1; -.
DR iPTMnet; Q09908; -.
DR MaxQB; Q09908; -.
DR PaxDb; Q09908; -.
DR EnsemblFungi; SPAC30D11.08c.1; SPAC30D11.08c.1:pep; SPAC30D11.08c.
DR GeneID; 2542236; -.
DR KEGG; spo:SPAC30D11.08c; -.
DR PomBase; SPAC30D11.08c; phf2.
DR VEuPathDB; FungiDB:SPAC30D11.08c; -.
DR eggNOG; KOG4323; Eukaryota.
DR HOGENOM; CLU_506376_0_0_1; -.
DR InParanoid; Q09908; -.
DR OMA; FHQLCHE; -.
DR PRO; PR:Q09908; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0033193; C:Lsd1/2 complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IPI:PomBase.
DR GO; GO:0033696; P:heterochromatin boundary formation; IPI:PomBase.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..538
FT /note="SWM histone demethylase complex subunit phf2"
FT /id="PRO_0000116437"
FT ZN_FING 232..288
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 28..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 538 AA; 60696 MW; 2FD754D50145982C CRC64;
MPNSSYYDDD GGSFEAASYP FQFDGSRRFP NDLHPTMFEG EESNQNGGSV LIDQAFQDIQ
NPNVNSNMHL ENQFQHFHEP NKESGAFGSY KNDDVAKEIE SSKNQETDAK SEQAPFTEDA
SSSNYAHHRS ADSQTKSALP PNVPASSSPL PPMSIAMNIA RKRSWPASLA IERDNTADAL
FSTEDGREEQ FNLEGVKTKS GRKVHRPNHF DPLVKLPTRR RGPGRRPVVA LAMKCSVCQR
LQSPPKNRIV FCDGCNTPFH QLCHEPYISD ELLDSPNGEW FCDDCIRRKK QAPLVTGTTA
RELNLSSEEK KSYLLSLPIS QLVDILLFCE QLHPDIPFYS PKTSTIVQEL QSKRSAFTAT
MNEPVTGDQY LSLNNGTESQ SKTTKHSTSL PSTEPVEVDK QYMESEKIPT IDEYLQEYSN
EDEIVLQVLE SFPAAVSFST ITNTIQAKYS NRKIKNSNIT RSLNRLVRKN RVLRDARGSS
YELNRTFDAD RPSVRPDISI TGPIPIDWML YTPHTEDLTE NFCTYYMFDE TPIVLSSI
