BU107_SCHPO
ID BU107_SCHPO Reviewed; 962 AA.
AC Q09731; Q9USE0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=UBP9-binding protein bun107;
DE AltName: Full=Binding ubp9 protein of 107 kDa;
GN Name=bun107; Synonyms=wdr48; ORFNames=SPAC31A2.14;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 800-949, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-717, AND IDENTIFICATION BY
RP 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).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BUN62 AND UBP9.
RX PubMed=20838651; DOI=10.1371/journal.pbio.1000471;
RA Kouranti I., McLean J.R., Feoktistova A., Liang P., Johnson A.E.,
RA Roberts-Galbraith R.H., Gould K.L.;
RT "A global census of fission yeast deubiquitinating enzyme localization and
RT interaction networks reveals distinct compartmentalization profiles and
RT overlapping functions in endocytosis and polarity.";
RL PLoS Biol. 8:708-716(2010).
CC -!- FUNCTION: Required for the ubp9 recruitment to septa and cell tips but
CC also for its enzymatic activity at these specific locations.
CC {ECO:0000269|PubMed:20838651}.
CC -!- SUBUNIT: Interacts with ubp9 and bun62. {ECO:0000269|PubMed:20838651}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell septum. Cell tip.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAA90472.1; -; Genomic_DNA.
DR EMBL; AB027832; BAA87136.1; -; Genomic_DNA.
DR PIR; S58107; S58107.
DR RefSeq; NP_592926.1; NM_001018327.2.
DR AlphaFoldDB; Q09731; -.
DR SMR; Q09731; -.
DR BioGRID; 279591; 82.
DR STRING; 4896.SPAC31A2.14.1; -.
DR iPTMnet; Q09731; -.
DR MaxQB; Q09731; -.
DR PaxDb; Q09731; -.
DR PRIDE; Q09731; -.
DR EnsemblFungi; SPAC31A2.14.1; SPAC31A2.14.1:pep; SPAC31A2.14.
DR GeneID; 2543160; -.
DR KEGG; spo:SPAC31A2.14; -.
DR PomBase; SPAC31A2.14; bun107.
DR VEuPathDB; FungiDB:SPAC31A2.14; -.
DR eggNOG; KOG0308; Eukaryota.
DR HOGENOM; CLU_002197_0_0_1; -.
DR InParanoid; Q09731; -.
DR OMA; APMWLGD; -.
DR PhylomeDB; Q09731; -.
DR Reactome; R-SPO-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR PRO; PR:Q09731; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0051285; C:cell cortex of cell tip; HDA:PomBase.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0030428; C:cell septum; IEA:UniProtKB-SubCell.
DR GO; GO:0051286; C:cell tip; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0032991; C:protein-containing complex; NAS:PomBase.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR021772; WDR48/Bun107.
DR Pfam; PF11816; DUF3337; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..962
FT /note="UBP9-binding protein bun107"
FT /id="PRO_0000051487"
FT REPEAT 25..69
FT /note="WD 1"
FT REPEAT 77..116
FT /note="WD 2"
FT REPEAT 121..162
FT /note="WD 3"
FT REPEAT 172..211
FT /note="WD 4"
FT REPEAT 214..253
FT /note="WD 5"
FT REPEAT 302..339
FT /note="WD 6"
FT REGION 568..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..611
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 717
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 822
FT /note="S -> Y (in Ref. 2; BAA87136)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 962 AA; 107276 MW; 44AD1F7F35DDB292 CRC64;
MSVRKRYKVT YVLDSCNDQL GHRLDANCLV LGRYFSEQGS APVTRALYSG GRDGQLFGWD
IGYDYGKASQ PLAKIQAHSA WVNDIALTHD SEGVISCSSD STVKLWKPHV LNASCLSTIG
EHTDYVKRVS IPKYSKSPLV ASGGLDKRII VWDYNVGQEV MRFEQLPDCS LVVGPRSGVY
SLAANNNIIA NGGLQKDIQL WDCVSKKRIT DLVGHTDNVR DILISDDGRT ILTASSDATI
KLWSLRAQKC LFSFIAHSDS VWALYSEHPD LKVFYAGDRS GLITRTDIRN QPNNQSCTAI
CKQDAPVSDI VARQSFIWST SRDGSILRWK DEPLFNQDVG AALSKHTSSH LSVSSDCPSR
HSSDIRNHSC PTLYHDDAED IYYDLHHTES YSNINLTKTP DYVIHGGIGL LKYRMLGDRR
HVLTEDAVGN KCLWDILACK QAGEFDKSED FEKIVQSLDT VQAIPRWASV NCLLGILAVT
LDENHYMDAE IYADECPLLK VDSPSDKRIN LGVWILKNLF REFIDAELHR DLKFRQNLDV
VRSEAKKQIE AQREEARKGN VNMPSALSPL RIRSRPSPLS LPPEPLLSPT IDYSATPFPL
EPPPESPGPS LQIPSNNPVY TNLTDTDSMM GAPDYFSIPA RQNRNRKPHT EVVGSPTVVR
TKEIIPPKVT REGSFMGRLK KLGRSKSSKS LQTDFMKASV ERAASSRVFS TGTSVTSPQA
LSKTNNTVNN AANTENNTLA KDKQQTSEAS SPGTPRELKT TGELIEDLHE QYVHFKDKDT
VLSLMKPPND DTFPMLNLSS QITVIISEES PEAGNSRDIY RSTLENMADD IDLLENIMPF
WLGRLLLLNE FPSKTAPTVN FTLQPFPGSG LPLIVNENTR LSASAMLRAQ KIMDYSYSKL
SQQRKDVSSL QFRCKDVVVT PKMTLATVKA RIWRSGDDVV FHYDVAPRSV SEIVDKTQSL
NI