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URB1_YEAST
ID   URB1_YEAST              Reviewed;        1764 AA.
AC   P34241; D6VXS2; P34242;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Nucleolar pre-ribosomal-associated protein 1;
DE   AltName: Full=Unhealthy ribosome biogenesis protein 1;
GN   Name=URB1; Synonyms=NPA1; OrderedLocusNames=YKL014C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8154185; DOI=10.1002/yea.320091208;
RA   Wiemann S., Voss H., Schwager C., Rupp T., Stegemann J., Zimmermann J.,
RA   Grothues D., Sensen C., Erfle H., Hewitt N., Banrevi A., Ansorge W.;
RT   "Sequencing and analysis of 51.6 kilobases on the left arm of chromosome XI
RT   from Saccharomyces cerevisiae reveals 23 open reading frames including the
RT   FAS1 gene.";
RL   Yeast 9:1343-1348(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH URB2.
RX   PubMed=15242642; DOI=10.1016/j.cell.2004.06.013;
RA   Mnaimneh S., Davierwala A.P., Haynes J., Moffat J., Peng W.-T., Zhang W.,
RA   Yang X., Pootoolal J., Chua G., Lopez A., Trochesset M., Morse D.,
RA   Krogan N.J., Hiley S.L., Li Z., Morris Q., Grigull J., Mitsakakis N.,
RA   Roberts C.J., Greenblatt J.F., Boone C., Kaiser C.A., Andrews B.J.,
RA   Hughes T.R.;
RT   "Exploration of essential gene functions via titratable promoter alleles.";
RL   Cell 118:31-44(2004).
RN   [7]
RP   FUNCTION, SUBUNIT, INTERACTION WITH URB2, AND SUBCELLULAR LOCATION.
RX   PubMed=15226434; DOI=10.1128/mcb.24.14.6324-6337.2004;
RA   Dez C., Froment C., Noaillac-Depeyre J., Monsarrat B.,
RA   Caizergues-Ferrer M., Henry Y.;
RT   "Npa1p, a component of very early pre-60S ribosomal particles, associates
RT   with a subset of small nucleolar RNPs required for peptidyl transferase
RT   center modification.";
RL   Mol. Cell. Biol. 24:6324-6337(2004).
RN   [8]
RP   FUNCTION, ASSOCIATION WITH PRE-RIBOSOMAL PARTICLES, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=15208443; DOI=10.1261/rna.7340404;
RA   Rosado I.V., de la Cruz J.;
RT   "Npa1p is an essential trans-acting factor required for an early step in
RT   the assembly of 60S ribosomal subunits in Saccharomyces cerevisiae.";
RL   RNA 10:1073-1083(2004).
RN   [9]
RP   IDENTIFICATION IN A COMPLEX WITH DBP6; NOP8; URB2 AND RSA3.
RX   PubMed=17145778; DOI=10.1128/mcb.01523-06;
RA   Rosado I.V., Dez C., Lebaron S., Caizergues-Ferrer M., Henry Y.,
RA   de la Cruz J.;
RT   "Characterization of Saccharomyces cerevisiae Npa2p (Urb2p) reveals a Low-
RT   molecular-mass complex containing Dbp6p, Npa1p (Urb1p), Nop8p, and Rsa3p
RT   involved in early steps of 60S ribosomal subunit biogenesis.";
RL   Mol. Cell. Biol. 27:1207-1221(2007).
CC   -!- FUNCTION: Required for 60S ribosomal subunit formation and pre-rRNA
CC       processing. Required for normal accumulation of 25S and 5.8S rRNAs.
CC       {ECO:0000269|PubMed:15208443, ECO:0000269|PubMed:15226434,
CC       ECO:0000269|PubMed:15242642}.
CC   -!- SUBUNIT: Associates with pre-60S ribosomal particles. Predominantly
CC       associated with the 27SA2 pre-rRNA. Can associate with a subset of box
CC       H/ACA and box C/D small nucleolar RNPs (snoRNPs) required for peptidyl
CC       transferase center modification and with small RNAs snR37 and snR42.
CC       Interacts with URB2. Together with DBP6, NOP8, URB2 and RSA3, forms an
CC       RNA-independent complex, which is required during early maturation of
CC       nascent 60S ribosomal subunits. {ECO:0000269|PubMed:15226434,
CC       ECO:0000269|PubMed:15242642, ECO:0000269|PubMed:17145778}.
CC   -!- INTERACTION:
CC       P34241; P53734: DBP6; NbExp=4; IntAct=EBI-26595, EBI-5625;
CC       P34241; Q04660: ERB1; NbExp=3; IntAct=EBI-26595, EBI-28098;
CC       P34241; P10962: MAK16; NbExp=3; IntAct=EBI-26595, EBI-10937;
CC       P34241; Q08287: NOP8; NbExp=3; IntAct=EBI-26595, EBI-12135;
CC       P34241; Q05942: RSA3; NbExp=4; IntAct=EBI-26595, EBI-33602;
CC       P34241; P47108: URB2; NbExp=5; IntAct=EBI-26595, EBI-25492;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:15208443, ECO:0000269|PubMed:15226434}.
CC       Note=Accumulates in the immediate vicinity of the dense fibrillar
CC       component of the nucleolus.
CC   -!- MISCELLANEOUS: Present with 5890 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; X74152; CAA52264.1; -; Genomic_DNA.
DR   EMBL; Z28014; CAA81849.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09142.1; -; Genomic_DNA.
DR   PIR; S37827; S37827.
DR   RefSeq; NP_012911.3; NM_001179580.3.
DR   AlphaFoldDB; P34241; -.
DR   BioGRID; 34118; 128.
DR   ComplexPortal; CPX-1421; NOP8 60s ribosome pre-assembly complex.
DR   DIP; DIP-2701N; -.
DR   IntAct; P34241; 26.
DR   MINT; P34241; -.
DR   STRING; 4932.YKL014C; -.
DR   iPTMnet; P34241; -.
DR   MaxQB; P34241; -.
DR   PaxDb; P34241; -.
DR   PRIDE; P34241; -.
DR   EnsemblFungi; YKL014C_mRNA; YKL014C; YKL014C.
DR   GeneID; 853855; -.
DR   KEGG; sce:YKL014C; -.
DR   SGD; S000001497; URB1.
DR   VEuPathDB; FungiDB:YKL014C; -.
DR   eggNOG; KOG1791; Eukaryota.
DR   GeneTree; ENSGT00390000014210; -.
DR   HOGENOM; CLU_003174_0_0_1; -.
DR   InParanoid; P34241; -.
DR   OMA; MTSYWFG; -.
DR   BioCyc; YEAST:G3O-31823-MON; -.
DR   PRO; PR:P34241; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P34241; protein.
DR   GO; GO:0005730; C:nucleolus; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR   GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR   GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR   GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR   GO; GO:0042273; P:ribosomal large subunit biogenesis; IC:ComplexPortal.
DR   InterPro; IPR032436; NopRA1_C.
DR   InterPro; IPR021714; Npa1_N.
DR   InterPro; IPR039844; URB1.
DR   PANTHER; PTHR13500; PTHR13500; 1.
DR   Pfam; PF16201; NopRA1; 1.
DR   Pfam; PF11707; Npa1; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Reference proteome; Ribosome biogenesis; rRNA processing.
FT   CHAIN           1..1764
FT                   /note="Nucleolar pre-ribosomal-associated protein 1"
FT                   /id="PRO_0000203190"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1764 AA;  203287 MW;  D4EC1FA19E051367 CRC64;
     MSNHSEAYGS RDQRREKYTQ GKEFEDGTLE TLESIISAVE DETLSKDYQP LIVFFQRGFG
     AQLVQTWSYY AQVNNHGKFS KTTSLLTKTL RVLSSDTSTV TIGSGLIRLI LTDYTKVLYR
     GLNNMRAQLT NPILRLLKQI VNFNNGQHIE ELVSYFDFSL PILPRLLVPS KSELANGNSS
     ADSSKHDSLR FTFIKFWLTL ISNASPFVRK ELLTENFKIM SNLFKFMNKA DSDKLSEHIL
     SVFINDILKE KSFKRTTKTK ILNELAASKI HHFYYSSNKN LVKKANEFFL TFGASRDFSV
     AFPDNCVWFK NSVADGASHG APITVNQVEF QIHNKLLFNT LRLFKPWEDT LQLGTLIKIL
     ENVPELVAPY SIFLTTNGNY DPKMTSYWFG ITLLINKIIN LKIPQFMEKV DSNIPPATSL
     VIENILPSLL TKSSLVKSLQ FETPIIRQLA CQSIVLALKK LEKVSTFYDQ KGWRNEKTIL
     LNEFHTRIPD LPIFVSTLSN SLASNKDNRI LPLSISIIFN YYSKMFPNLF SINLPSSNIY
     TDIMQKSKIS GIEFAILDNY LQFQEFNSTQ TRWWNPSSGG NSLFTLLLKL ASSKNASNVI
     TTRISNLLDE LTRTNVIFNI SLISPVMALV NSLQGLSLQV SEIDNMEQVW KWFDETISRV
     VKTPYKYVDM AKEYNYISPF IMCLSEQWKY VDKSGNPEFL IKWLILFLRN MIFIGEDHIG
     IDKLVKNVFP EVSDHDVNIY LKLDSFEENI KKTNSSNSLI SSMKSSSFFQ YISALPSKNL
     MNISRLPVNK LDAAGILFRV QLLVEDDSVV YDNWFEATAC ELTGKIASYM VTDTEFPIIK
     VLERYINFAL PKLAIEKRNA LLMKKSRFMC NLIGAVCFET GHQLVEFREI IQKVVFSGEN
     VEEYANYNEL YQKEDVNAFL TSVSEYLSTS ALTSLLMCST KLESTRNILQ KLFNEGKTIK
     ISLVKNILNK AANEDPASIK EVNISLAKFF EENKVCVDAS SDPMGKLSLS ETTSLINSFV
     SSDLNYLVLK AFYRWEHFSF PSFIPSIWRI KDSPLLSIVT TAALFKHMQD KDFSAFAHET
     ISKYGNEIAK STYTTSKSEI FDEILNMITT YIDFYDETKR NEILKCVLSQ SDHKYHAATV
     RYIAAHNNFT YPGVETWLHK TLLYLTKYLS ERKVISNSFF ELLRAMAELL KLEEVPNKLN
     VKIINSQLEA ILGSEWIKQI KVLEYVIVLI FCVSKKSIQS QRMVQLLLSN DSYSSIMIKD
     NDEDSSYRKF LSTMILFSLF SIDPVVNSTP IVQEKLLTFY SGTISSNDKL ILKILETIES
     HTATSWTNMI FSWEFIKDEE EEILEAIGDT RLITKEREGL ILTLQKNMIK KSIDRYVLER
     PQVPELYTDS NTNNYDATTR CDLVKKYYDD TERSGVDMYD PLFLLLLIIH NKELVKMVKD
     DEGNVTYRYE FENFLDCKIF QFIICSLSDC HTVANISYEH LSNLASSLEK KTAQMNLEKQ
     ITSKDNERKE SDSDLIKYNS IYQVLIKRIL YQRQQNQDPI NPLIWFSISR IVDLLGSPTA
     PLHEKAYRWV LSNSTIRSWD IPMVSDVMMS YNKRQQDDNK KEIDMEIYYG ELSWVLTTIC
     KGIKTDEDYK MLEKKGVFEW LLNLINMPYL KERLRELIYF IFYKVQRVAD DGGLNLISRN
     GIVSFFEVLN NNIKSRLPQD DILNNIGTLR NENRGTLNTT LRLAQEQNGI EKLLLGYNEL
     VKSQKRLILW TEGDSDNVVK RLRK
 
 
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