BUN62_SCHPO
ID BUN62_SCHPO Reviewed; 543 AA.
AC Q10437;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=UBP9-binding protein bun62;
DE AltName: Full=Binding ubp9 protein of 62 kDa;
GN Name=bun62; Synonyms=wdr20; ORFNames=SPAC12B10.03;
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 [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 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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, 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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH
RP BUN107 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 bun107. {ECO:0000269|PubMed:20838651}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cell septum. Cell tip.
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DR EMBL; CU329670; CAA94693.1; -; Genomic_DNA.
DR PIR; T37570; T37570.
DR RefSeq; NP_594635.1; NM_001020063.2.
DR AlphaFoldDB; Q10437; -.
DR SMR; Q10437; -.
DR BioGRID; 279390; 44.
DR STRING; 4896.SPAC12B10.03.1; -.
DR iPTMnet; Q10437; -.
DR MaxQB; Q10437; -.
DR PaxDb; Q10437; -.
DR PRIDE; Q10437; -.
DR EnsemblFungi; SPAC12B10.03.1; SPAC12B10.03.1:pep; SPAC12B10.03.
DR GeneID; 2542950; -.
DR KEGG; spo:SPAC12B10.03; -.
DR PomBase; SPAC12B10.03; bun62.
DR VEuPathDB; FungiDB:SPAC12B10.03; -.
DR eggNOG; KOG2394; Eukaryota.
DR HOGENOM; CLU_016971_1_0_1; -.
DR InParanoid; Q10437; -.
DR OMA; LHRPKAA; -.
DR PhylomeDB; Q10437; -.
DR Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR PRO; PR:Q10437; -.
DR Proteomes; UP000002485; Chromosome I.
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:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0032991; C:protein-containing complex; NAS:PomBase.
DR GO; GO:0045013; P:carbon catabolite repression of transcription; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR024977; Apc4_WD40_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12894; ANAPC4_WD40; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..543
FT /note="UBP9-binding protein bun62"
FT /id="PRO_0000051493"
FT REPEAT 239..279
FT /note="WD 1"
FT REPEAT 320..361
FT /note="WD 2"
FT REPEAT 362..401
FT /note="WD 3"
FT REPEAT 404..448
FT /note="WD 4"
FT REPEAT 513..542
FT /note="WD 5"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 543 AA; 61811 MW; 9D6A56F4179DCFAE CRC64;
MQTMSSGIAR PVLFLTAREG EYVLKDEFQL GSSSRSTPQI TGSPLDPNTP VKRLFFMRIN
IAQFSRWDYP YPREYIEELK KIHGVHHVEE NRDVPSILEN YRNSKRKSHN FSSSNTPYLK
LHRPASRAGA PLINAKSFIS SLTFHDNIVR SFQPSIHGKT FVFANHEKSF YWLDVSAANS
HSALLKMEFP RASPVCHDIN SFTKSPKGLD VIIGFDTGDV LWYDPINFKY LRFNKNGQLN
SSSVTAIKWV AGKDSQFLVS FRNGWLVLYD KYRHEQPLHI VVPEKNLKSL YLSSPGTFNI
LISINHRDDR KLNPVACYAF SKSPINGFCF SPDYQYLALV SERGTLKLFD FVKEHVLDVF
HSYFAGLTCV TWSPDGKFIA IGGKDDLVSI YSFPLRKLVA RCQGHKSWVT DVIFDAWRCD
DDNYRIASVG LDRKLLLWDF SVSAIHRPKS AVYYVNHHSN NSKPAISDFD DVGDLTMGSE
IDNSNYVNGD ITIHPTLSRS LIPVISPITI YDVDDSPLSS VFFDPDCMIT CATNGRIRTW
QRP
