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RRP14_YEAST
ID   RRP14_YEAST             Reviewed;         434 AA.
AC   P36080; D6VXK5;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Ribosomal RNA-processing protein 14;
DE   AltName: Full=Ribosome biogenesis protein RRP14;
GN   Name=RRP14; OrderedLocusNames=YKL082C;
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=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   [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.
RX   PubMed=16544271; DOI=10.1002/yea.1353;
RA   Wade C.H., Umbarger M.A., McAlear M.A.;
RT   "The budding yeast rRNA and ribosome biosynthesis (RRB) regulon contains
RT   over 200 genes.";
RL   Yeast 23:293-306(2006).
RN   [4]
RP   FUNCTION, AND IDENTIFICATION IN THE 60S PRE-RIBOSOMAL PARTICLE.
RX   PubMed=17272295; DOI=10.1093/nar/gkl824;
RA   Oeffinger M., Fatica A., Rout M.P., Tollervey D.;
RT   "Yeast Rrp14p is required for ribosomal subunit synthesis and for correct
RT   positioning of the mitotic spindle during mitosis.";
RL   Nucleic Acids Res. 35:1354-1366(2007).
RN   [5]
RP   SUBCELLULAR LOCATION, FUNCTION, AND IDENTIFICATION IN THE 90S PRE-RIBOSOMAL
RP   PARTICLE.
RX   PubMed=17804645; DOI=10.1261/rna.553807;
RA   Yamada H., Horigome C., Okada T., Shirai C., Mizuta K.;
RT   "Yeast Rrp14p is a nucleolar protein involved in both ribosome biogenesis
RT   and cell polarity.";
RL   RNA 13:1977-1987(2007).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Involved in ribosome biogenesis and cell polarity. Required
CC       for the synthesis of both 40S and 60S ribosomal subunits and may also
CC       play some direct role in correct positioning of the mitotic spindle
CC       during mitosis. {ECO:0000269|PubMed:16544271,
CC       ECO:0000269|PubMed:17272295, ECO:0000269|PubMed:17804645}.
CC   -!- SUBUNIT: Component of the 90S and 60S pre-ribosomal particles.
CC       {ECO:0000269|PubMed:17272295, ECO:0000269|PubMed:17804645}.
CC   -!- INTERACTION:
CC       P36080; P43586: LOC1; NbExp=3; IntAct=EBI-26762, EBI-22906;
CC       P36080; P37838: NOP4; NbExp=3; IntAct=EBI-26762, EBI-12122;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:17804645}.
CC   -!- SIMILARITY: Belongs to the SURF6 family. {ECO:0000305}.
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DR   EMBL; Z28082; CAA81921.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09075.1; -; Genomic_DNA.
DR   PIR; S37907; S37907.
DR   RefSeq; NP_012841.1; NM_001179648.1.
DR   PDB; 6C0F; EM; 3.70 A; 8=1-434.
DR   PDBsum; 6C0F; -.
DR   AlphaFoldDB; P36080; -.
DR   SMR; P36080; -.
DR   BioGRID; 34050; 131.
DR   DIP; DIP-2694N; -.
DR   IntAct; P36080; 20.
DR   MINT; P36080; -.
DR   STRING; 4932.YKL082C; -.
DR   iPTMnet; P36080; -.
DR   MaxQB; P36080; -.
DR   PaxDb; P36080; -.
DR   PRIDE; P36080; -.
DR   EnsemblFungi; YKL082C_mRNA; YKL082C; YKL082C.
DR   GeneID; 853780; -.
DR   KEGG; sce:YKL082C; -.
DR   SGD; S000001565; RRP14.
DR   VEuPathDB; FungiDB:YKL082C; -.
DR   eggNOG; KOG2885; Eukaryota.
DR   GeneTree; ENSGT00390000006980; -.
DR   HOGENOM; CLU_018300_0_0_1; -.
DR   InParanoid; P36080; -.
DR   OMA; QKKRTDN; -.
DR   BioCyc; YEAST:G3O-31877-MON; -.
DR   PRO; PR:P36080; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P36080; protein.
DR   GO; GO:0005730; C:nucleolus; IDA:SGD.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:SGD.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:SGD.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   DisProt; DP02355; -.
DR   InterPro; IPR029190; Rrp14/SURF6_C.
DR   InterPro; IPR029188; Rrp14_N.
DR   InterPro; IPR007019; SURF6.
DR   PANTHER; PTHR14369; PTHR14369; 1.
DR   Pfam; PF15459; RRP14; 1.
DR   Pfam; PF04935; SURF6; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Coiled coil; Nucleus; Reference proteome;
KW   Ribosome biogenesis; rRNA processing.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..434
FT                   /note="Ribosomal RNA-processing protein 14"
FT                   /id="PRO_0000203167"
FT   REGION          32..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          375..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          162..230
FT                   /evidence="ECO:0000255"
FT   COILED          293..360
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        32..109
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..135
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..223
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..238
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..257
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..392
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
SQ   SEQUENCE   434 AA;  50482 MW;  BCEDE9F10A466E6E CRC64;
     MSNSLEERLR ANSSAFDGLL ALIPAKYYYD EKSQEQWKAK KKTKEQSKND KLKKLDPEQR
     DDETSSTLEV MKKKEKDAKP VVLPGEKFKH MKMQKQKEAT SKVEGDSDLN VEVNDPMIIA
     PDEDEEEEED IKVIFDDEGN EIPLESKKDT TEPDRSVEKK SITEEEKLQR KKNLEALRSK
     LQAKISDMKS KRKAPGSREA ILAQRKRKEE LKKRKRLESE QEQDQDEIAS DSDMEDIDSD
     LENNSKKRFK KGKKDSEINA DGVMFQNIIF DDGARATSDL QRLRKAGRTK GPAKNDVKSH
     LKLLEAKKNK MEAKDELEQI KQKEKEKWQK AMLQAEGIKI RDDEKLLRKA IKRKEAQKRK
     SAIEWSERKR VVEDTISERQ KRREENLRIR KDNKGKKRNK QEKMKRKYVG SAVPKKRAGF
     EGRLKTGKKK GGPK
 
 
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