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LSM12_YEAST
ID   LSM12_YEAST             Reviewed;         187 AA.
AC   P38828; D3DL71;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=Protein LSM12;
DE   AltName: Full=Sm-like protein 12;
GN   Name=LSM12; OrderedLocusNames=YHR121W;
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=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
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   IDENTIFICATION.
RX   PubMed=15225602; DOI=10.1016/j.febslet.2004.03.126;
RA   Albrecht M., Lengauer T.;
RT   "Novel Sm-like proteins with long C-terminal tails and associated
RT   methyltransferases.";
RL   FEBS Lett. 569:18-26(2004).
RN   [7]
RP   INTERACTION WITH PBP1 AND PBP4, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16702403; DOI=10.1101/gad.1422006;
RA   Fleischer T.C., Weaver C.M., McAfee K.J., Jennings J.L., Link A.J.;
RT   "Systematic identification and functional screens of uncharacterized
RT   proteins associated with eukaryotic ribosomal complexes.";
RL   Genes Dev. 20:1294-1307(2006).
RN   [8]
RP   INTERACTION WITH IGO1.
RX   PubMed=20471941; DOI=10.1016/j.molcel.2010.02.039;
RA   Talarek N., Cameroni E., Jaquenoud M., Luo X., Bontron S., Lippman S.,
RA   Devgan G., Snyder M., Broach J.R., De Virgilio C.;
RT   "Initiation of the TORC1-regulated G0 program requires Igo1/2, which
RT   license specific mRNAs to evade degradation via the 5'-3' mRNA decay
RT   pathway.";
RL   Mol. Cell 38:345-355(2010).
RN   [9]
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   -!- SUBUNIT: Interacts with IGO1, PBP1 and PBP4.
CC       {ECO:0000269|PubMed:16702403, ECO:0000269|PubMed:20471941}.
CC   -!- INTERACTION:
CC       P38828; P53297: PBP1; NbExp=4; IntAct=EBI-24700, EBI-12961;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 8320 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the LSM12 family. {ECO:0000305}.
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DR   EMBL; U00059; AAB68870.1; -; Genomic_DNA.
DR   EMBL; AY557853; AAS56179.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06815.1; -; Genomic_DNA.
DR   PIR; S48963; S48963.
DR   RefSeq; NP_011989.1; NM_001179251.1.
DR   AlphaFoldDB; P38828; -.
DR   BioGRID; 36554; 205.
DR   DIP; DIP-5545N; -.
DR   IntAct; P38828; 24.
DR   MINT; P38828; -.
DR   STRING; 4932.YHR121W; -.
DR   iPTMnet; P38828; -.
DR   MaxQB; P38828; -.
DR   PaxDb; P38828; -.
DR   PRIDE; P38828; -.
DR   EnsemblFungi; YHR121W_mRNA; YHR121W; YHR121W.
DR   GeneID; 856521; -.
DR   KEGG; sce:YHR121W; -.
DR   SGD; S000001163; LSM12.
DR   VEuPathDB; FungiDB:YHR121W; -.
DR   eggNOG; KOG4401; Eukaryota.
DR   GeneTree; ENSGT00390000006956; -.
DR   HOGENOM; CLU_073383_1_1_1; -.
DR   InParanoid; P38828; -.
DR   OMA; FWLEVDN; -.
DR   BioCyc; YEAST:G3O-31163-MON; -.
DR   PRO; PR:P38828; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P38828; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0003723; F:RNA binding; ISS:SGD.
DR   GO; GO:0016070; P:RNA metabolic process; IPI:SGD.
DR   InterPro; IPR019181; Anticodon-binding_dom.
DR   InterPro; IPR039683; Lsm12-like.
DR   InterPro; IPR016521; RNA-processing_Lsm12.
DR   PANTHER; PTHR13542; PTHR13542; 1.
DR   Pfam; PF09793; AD; 1.
DR   PIRSF; PIRSF007783; UCP007783_YHR121w; 1.
DR   SMART; SM00995; AD; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Nucleus; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..187
FT                   /note="Protein LSM12"
FT                   /id="PRO_0000202913"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
SQ   SEQUENCE   187 AA;  21314 MW;  0594E464F662CF49 CRC64;
     MSVSLEQTLG FRIKVTNVLD VVTEGRLYSF NSSNNTLTIQ TTKKNQSPQN FKVIKCTFIK
     HLEVIGDKPS FNSFKKQQIK PSYVNVERVE KLLKESVIAS KKKELLRGKG VSAEGQFIFD
     QIFKTIGDTK WVAKDIIILD DVKVQPPYKV EDIKVLHEGS NQSITLIQRI VERSWEQLEQ
     DDGRKGG
 
 
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