FKH2_SCHPO
ID FKH2_SCHPO Reviewed; 642 AA.
AC O60129;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Fork head protein homolog 2;
GN Name=fkh2; ORFNames=SPBC16G5.15c;
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 PHOSPHORYLATION.
RX PubMed=15509866; DOI=10.1242/jcs.01473;
RA Buck V., Ng S.S., Ruiz-Garcia A.B., Papadopoulou K., Bhatti S.,
RA Samuel J.M., Anderson M., Millar J.B.A., McInerny C.J.;
RT "Fkh2p and Sep1p regulate mitotic gene transcription in fission yeast.";
RL J. Cell Sci. 117:5623-5632(2004).
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, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=15302827; DOI=10.1128/ec.3.4.944-954.2004;
RA Bulmer R., Pic-Taylor A., Whitehall S.K., Martin K.A., Millar J.B.A.,
RA Quinn J., Morgan B.A.;
RT "The forkhead transcription factor Fkh2 regulates the cell division cycle
RT of Schizosaccharomyces pombe.";
RL Eukaryot. Cell 3:944-954(2004).
RN [4]
RP FUNCTION.
RX PubMed=15777722; DOI=10.1016/j.gene.2004.12.043;
RA Szilagyi Z., Batta G., Enczi K., Sipiczki M.;
RT "Characterisation of two novel fork-head gene homologues of
RT Schizosaccharomyces pombe: their involvement in cell cycle and sexual
RT differentiation.";
RL Gene 348:101-109(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319; SER-321; SER-322;
RP SER-334; SER-336; SER-375; SER-535 AND SER-626, AND IDENTIFICATION BY MASS
RP 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: Required for promoter sequence element PCB-driven, M-phase-
CC specific transcription. Acts as a transcriptional activator with a role
CC in the regulation of mitosis. Binds, cooperatively with mcm1, the CLB
CC cluster regulatory elements throughout the cell cycle. Regulates the
CC periodic transcription of cdc15 and spo12. Required for the correct
CC timing, positioning and contraction of the division septum.
CC {ECO:0000269|PubMed:15302827, ECO:0000269|PubMed:15509866,
CC ECO:0000269|PubMed:15777722}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089,
CC ECO:0000269|PubMed:15302827}.
CC -!- PTM: Phosphorylated. Occurs periodically during mitosis.
CC {ECO:0000269|PubMed:15302827, ECO:0000269|PubMed:15509866,
CC ECO:0000269|PubMed:18257517}.
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DR EMBL; CU329671; CAA19034.1; -; Genomic_DNA.
DR PIR; T39607; T39607.
DR RefSeq; NP_596764.1; NM_001023784.2.
DR AlphaFoldDB; O60129; -.
DR SMR; O60129; -.
DR BioGRID; 276256; 24.
DR STRING; 4896.SPBC16G5.15c.1; -.
DR iPTMnet; O60129; -.
DR MaxQB; O60129; -.
DR PaxDb; O60129; -.
DR PRIDE; O60129; -.
DR EnsemblFungi; SPBC16G5.15c.1; SPBC16G5.15c.1:pep; SPBC16G5.15c.
DR GeneID; 2539703; -.
DR KEGG; spo:SPBC16G5.15c; -.
DR PomBase; SPBC16G5.15c; fkh2.
DR VEuPathDB; FungiDB:SPBC16G5.15c; -.
DR eggNOG; KOG2294; Eukaryota.
DR HOGENOM; CLU_435571_0_0_1; -.
DR InParanoid; O60129; -.
DR OMA; YSVMIAQ; -.
DR PhylomeDB; O60129; -.
DR PRO; PR:O60129; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0097221; C:M/G1 phase-specific MADS box-forkhead transcription factor complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:PomBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:PomBase.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IMP:PomBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:PomBase.
DR GO; GO:0006325; P:chromatin organization; IMP:PomBase.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0110045; P:negative regulation of cell cycle switching, mitotic to meiotic cell cycle; IMP:PomBase.
DR GO; GO:1900237; P:positive regulation of induction of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:PomBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:PomBase.
DR CDD; cd00059; FH; 1.
DR CDD; cd00060; FHA; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR001766; Fork_head_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR018122; TF_fork_head_CS_1.
DR InterPro; IPR030456; TF_fork_head_CS_2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00250; Forkhead; 1.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00339; FH; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00657; FORK_HEAD_1; 1.
DR PROSITE; PS00658; FORK_HEAD_2; 1.
DR PROSITE; PS50039; FORK_HEAD_3; 1.
PE 1: Evidence at protein level;
KW Activator; Cell cycle; Cell division; DNA-binding; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome; Septation; Transcription;
KW Transcription regulation.
FT CHAIN 1..642
FT /note="Fork head protein homolog 2"
FT /id="PRO_0000091905"
FT DOMAIN 96..160
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT DNA_BIND 223..318
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 642 AA; 71174 MW; DBEC705EF3C595B9 CRC64;
MTVRRLESKS EHISDDEERK EQLDYKKQMD VDTDRNIVLN GRLESQIAKL SVPPHEMRVV
DDYSNSKNAE RHSGEIQAYA KFAGSTWTYY VKKIRIILGR EPANPSPKGK NEDLEVIDMN
FGPSKVVSRK HAVVEYDLDD QTWNCSVYGR NGIKVDGKLF KNGETVKLTS GSILEVAGLQ
MMFVLPNAAE QKQTDESTIK EDAIKSEISA AVNDAAEYGD NKKPPYSYSV MIAQAILSSS
ECMMTLSNIY SWISTHYPYY RTTKSGWQNS IRHNLSLNKA FRKVPRKSGE QGKGMKWSIV
PEFREEFIAK TRKTPRKRSP SSPVPLLAKK REGSPSLPIP ILPKMKDTSI PAAEPASSTT
SARDQTPSTP KDVGSPSTAE TSAEEKQMET YKTPTHAALS DIISTHDYAL DANSASQTKK
AAFGSPIGSS TYPTSSPAPF WKYVAVPNPH DWPQVGSYDT ISPYRNPVNS HLIYSQIQQS
SPKKIDEQLH DLQGVDLVNG FEGISSWRES MVNKLRSSVS DSPTMNLANS NSKSSPVAVQ
RVSTLPQASA NKQAKEMESK MSNSPTQKSK TEENNQAVRA ILDASATMEK QYDLHRLPTP
TSQTESASVP QIANPPNSQN LVKEKSPQQY IQVPQSNVKS SA
