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UTP5_YEAST
ID   UTP5_YEAST              Reviewed;         643 AA.
AC   Q04177; D6VT31;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 166.
DE   RecName: Full=U3 small nucleolar RNA-associated protein 5;
DE            Short=U3 snoRNA-associated protein 5;
DE   AltName: Full=U three protein 5;
DE   AltName: Full=U3 protein 5 required for transcription;
DE   AltName: Full=t-UTP5;
GN   Name=UTP5; OrderedLocusNames=YDR398W; ORFNames=D9509.17;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [2]
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   [3]
RP   FUNCTION, INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU
RP   PROCESSOME BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=12068309; DOI=10.1038/nature00769;
RA   Dragon F., Gallagher J.E.G., Compagnone-Post P.A., Mitchell B.M.,
RA   Porwancher K.A., Wehner K.A., Wormsley S., Settlage R.E., Shabanowitz J.,
RA   Osheim Y., Beyer A.L., Hunt D.F., Baserga S.J.;
RT   "A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA
RT   biogenesis.";
RL   Nature 417:967-970(2002).
RN   [4]
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   [5]
RP   FUNCTION, IDENTIFICATION IN COMPLEX WITH OTHER T-UTPS, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=15489292; DOI=10.1101/gad.1226604;
RA   Gallagher J.E.G., Dunbar D.A., Granneman S., Mitchell B.M., Osheim Y.,
RA   Beyer A.L., Baserga S.J.;
RT   "RNA polymerase I transcription and pre-rRNA processing are linked by
RT   specific SSU processome components.";
RL   Genes Dev. 18:2506-2517(2004).
CC   -!- FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA.
CC       Required for optimal pre-ribosomal RNA transcription by RNA polymerase
CC       I together with a subset of U3 proteins required for transcription (t-
CC       UTPs). {ECO:0000269|PubMed:12068309, ECO:0000269|PubMed:15489292}.
CC   -!- SUBUNIT: Interacts with snoRNA U3. Interacts with MPP10. Component of
CC       the ribosomal small subunit (SSU) processome composed of at least 40
CC       protein subunits and snoRNA U3. In the absence of snoRNA3, forms a
CC       complex with other t-UTPs. This complex can associate with pre-18S
CC       ribosomal RNAs. {ECO:0000269|PubMed:12068309,
CC       ECO:0000269|PubMed:15489292}.
CC   -!- INTERACTION:
CC       Q04177; P32899: IMP3; NbExp=2; IntAct=EBI-35844, EBI-9237;
CC       Q04177; Q04305: UTP15; NbExp=10; IntAct=EBI-35844, EBI-28183;
CC       Q04177; P53254: UTP22; NbExp=2; IntAct=EBI-35844, EBI-1878;
CC       Q04177; Q06679: UTP4; NbExp=6; IntAct=EBI-35844, EBI-35712;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12068309,
CC       ECO:0000269|PubMed:15489292}. Note=Associated with ribosomal chromatin,
CC       even in the absence of transcription.
CC   -!- MISCELLANEOUS: Present with 33100 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the UTP5 family. {ECO:0000305}.
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DR   EMBL; U32274; AAB64839.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12241.1; -; Genomic_DNA.
DR   PIR; S69681; S69681.
DR   RefSeq; NP_010686.1; NM_001180706.1.
DR   PDB; 5WLC; EM; 3.80 A; LL=1-643.
DR   PDB; 6KE6; EM; 3.40 A; A5=1-643.
DR   PDB; 6LQP; EM; 3.20 A; A5=1-643.
DR   PDB; 6LQQ; EM; 4.10 A; A5=1-643.
DR   PDB; 6LQR; EM; 8.60 A; A5=1-643.
DR   PDB; 6LQS; EM; 3.80 A; A5=1-643.
DR   PDB; 6LQT; EM; 4.90 A; A5=1-643.
DR   PDB; 6LQU; EM; 3.70 A; A5=1-643.
DR   PDB; 6LQV; EM; 4.80 A; A5=1-643.
DR   PDB; 6ND4; EM; 4.30 A; L=1-643.
DR   PDB; 6ZQA; EM; 4.40 A; UE=1-643.
DR   PDB; 6ZQB; EM; 3.90 A; UE=1-643.
DR   PDB; 6ZQC; EM; 3.80 A; UE=1-643.
DR   PDB; 6ZQD; EM; 3.80 A; UE=1-643.
DR   PDB; 6ZQE; EM; 7.10 A; UI=1-643.
DR   PDB; 7AJT; EM; 4.60 A; UE=1-643.
DR   PDB; 7AJU; EM; 3.80 A; UE=1-643.
DR   PDB; 7D4I; EM; 4.00 A; A5=1-643.
DR   PDB; 7D5S; EM; 4.60 A; A5=1-643.
DR   PDB; 7D5T; EM; 6.00 A; A5=1-643.
DR   PDB; 7D63; EM; 12.30 A; A5=1-643.
DR   PDBsum; 5WLC; -.
DR   PDBsum; 6KE6; -.
DR   PDBsum; 6LQP; -.
DR   PDBsum; 6LQQ; -.
DR   PDBsum; 6LQR; -.
DR   PDBsum; 6LQS; -.
DR   PDBsum; 6LQT; -.
DR   PDBsum; 6LQU; -.
DR   PDBsum; 6LQV; -.
DR   PDBsum; 6ND4; -.
DR   PDBsum; 6ZQA; -.
DR   PDBsum; 6ZQB; -.
DR   PDBsum; 6ZQC; -.
DR   PDBsum; 6ZQD; -.
DR   PDBsum; 6ZQE; -.
DR   PDBsum; 7AJT; -.
DR   PDBsum; 7AJU; -.
DR   PDBsum; 7D4I; -.
DR   PDBsum; 7D5S; -.
DR   PDBsum; 7D5T; -.
DR   PDBsum; 7D63; -.
DR   AlphaFoldDB; Q04177; -.
DR   SMR; Q04177; -.
DR   BioGRID; 32459; 307.
DR   ComplexPortal; CPX-1409; UTP-A complex.
DR   DIP; DIP-1317N; -.
DR   IntAct; Q04177; 51.
DR   MINT; Q04177; -.
DR   STRING; 4932.YDR398W; -.
DR   iPTMnet; Q04177; -.
DR   MaxQB; Q04177; -.
DR   PaxDb; Q04177; -.
DR   PRIDE; Q04177; -.
DR   EnsemblFungi; YDR398W_mRNA; YDR398W; YDR398W.
DR   GeneID; 852007; -.
DR   KEGG; sce:YDR398W; -.
DR   SGD; S000002806; UTP5.
DR   VEuPathDB; FungiDB:YDR398W; -.
DR   eggNOG; KOG4547; Eukaryota.
DR   HOGENOM; CLU_023936_0_0_1; -.
DR   InParanoid; Q04177; -.
DR   OMA; WVKWCLI; -.
DR   BioCyc; YEAST:G3O-29945-MON; -.
DR   Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   PRO; PR:Q04177; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q04177; protein.
DR   GO; GO:0005730; C:nucleolus; IDA:SGD.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0033553; C:rDNA heterochromatin; IDA:SGD.
DR   GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR   GO; GO:0034455; C:t-UTP complex; IDA:SGD.
DR   GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR   GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR   GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IMP:SGD.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR007148; SSU_processome_Utp12.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF04003; Utp12; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Nucleus; Reference proteome; Repeat; Ribonucleoprotein;
KW   Ribosome biogenesis; rRNA processing; Transcription; WD repeat.
FT   CHAIN           1..643
FT                   /note="U3 small nucleolar RNA-associated protein 5"
FT                   /id="PRO_0000051318"
FT   REPEAT          14..54
FT                   /note="WD 1"
FT   REPEAT          55..98
FT                   /note="WD 2"
FT   REPEAT          186..225
FT                   /note="WD 3"
FT   REPEAT          227..266
FT                   /note="WD 4"
FT   REPEAT          340..389
FT                   /note="WD 5"
FT   REPEAT          471..511
FT                   /note="WD 6"
FT   REGION          565..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        569..609
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..630
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   643 AA;  72002 MW;  7A6F60C7C6F46C2A CRC64;
     MDSPVLQSAY DPSGQYLCYV TVALDKQRVG VQPTQRATSS GVDTVWNENF LYLEDSKLKV
     TCLKWVNLAS SDTVAIILGM NNGEIWLYSV LANEVTYKFT TGNSYEIKDI DLMGNQLWCI
     DSSDAFYQFD LLQFKLLQHF RINNCVQLNK LTIVPAGDSV AQLLVASHSI SLIDIEEKKV
     VMTFPGHVSP VSTLQVITNE FFISGAEGDR FLNVYDIHSG MTKCVLVAES DIKELSHSGQ
     ADSIAVTTED GSLEIFVDPL VSSSTKKRGN KSKKSSKKIQ IVSKDGRKVP IYNAFINKDL
     LNVSWLQNAT MPYFKNLQWR EIPNEYTVEI SLNWNNKNKS ADRDLHGKDL ASATNYVEGN
     ARVTSGDNFK HVDDAIKSWE RELTSLEQEQ AKPPQANELL TETFGDKLES STVARISGKK
     TNLKGSNLKT ATTTGTVTVI LSQALQSNDH SLLETVLNNR DERVIRDTIF RLKPALAVIL
     LERLAERIAR QTHRQGPLNV WVKWCLIIHG GYLVSIPNLM STLSSLHSTL KRRSDLLPRL
     LALDARLDCT INKFKTLNYE AGDIHSSEPV VEEDEDDVEY NEELDDAGLI EDGEESYGSE
     EEEEGDSDNE EEQKHTSSKQ DGRLETEQSD GEEEAGYSDV EME
 
 
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