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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.
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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
 
 
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