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RSMB_YEAST
ID   RSMB_YEAST              Reviewed;         196 AA.
AC   P40018; D3DLS8;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 186.
DE   RecName: Full=Small nuclear ribonucleoprotein-associated protein B;
DE            Short=snRNP-B;
DE   AltName: Full=Sm protein B;
DE            Short=Sm-B;
DE            Short=SmB;
GN   Name=SMB1; OrderedLocusNames=YER029C;
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], AND INTERACTION WITH SMD3.
RX   PubMed=9528767; DOI=10.1128/mcb.18.4.1956;
RA   Camasses A., Bragado-Nilsson E., Martin R., Seraphin B., Bordonne R.;
RT   "Interactions within the yeast Sm core complex: from proteins to amino
RT   acids.";
RL   Mol. Cell. Biol. 18:1956-1966(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND RNA-BINDING.
RX   PubMed=10369684; DOI=10.1093/emboj/18.12.3451;
RA   Salgado-Garrido J., Bragado-Nilsson E., Kandels-Lewis S., Seraphin B.;
RT   "Sm and Sm-like proteins assemble in two related complexes of deep
RT   evolutionary origin.";
RL   EMBO J. 18:3451-3462(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA   Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA   Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA   Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(1997).
RN   [4]
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   [5]
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   [6]
RP   PROTEIN SEQUENCE OF 12-19 AND 81-88.
RX   PubMed=9630245;
RA   Gottschalk A., Tang J., Puig O., Salgado J., Neubauer G., Colot H.V.,
RA   Mann M., Seraphin B., Rosbash M., Luehrmann R., Fabrizio P.;
RT   "A comprehensive biochemical and genetic analysis of the yeast U1 snRNP
RT   reveals five novel proteins.";
RL   RNA 4:374-393(1998).
RN   [7]
RP   SUBUNIT, IDENTIFICATION IN THE U4/U5/U6 TRI-SNRNP COMPLEX, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=10449419; DOI=10.1093/emboj/18.16.4535;
RA   Gottschalk A., Neubauer G., Banroques J., Mann M., Luehrmann R.,
RA   Fabrizio P.;
RT   "Identification by mass spectrometry and functional analysis of novel
RT   proteins of the yeast [U4/U6.U5] tri-snRNP.";
RL   EMBO J. 18:4535-4548(1999).
RN   [8]
RP   NUCLEAR LOCALIZATION SIGNAL.
RX   PubMed=11027265; DOI=10.1128/mcb.20.21.7943-7954.2000;
RA   Bordonne R.;
RT   "Functional characterization of nuclear localization signals in yeast Sm
RT   proteins.";
RL   Mol. Cell. Biol. 20:7943-7954(2000).
RN   [9]
RP   SUBUNIT.
RX   PubMed=11302706; DOI=10.1006/jmbi.2001.4549;
RA   Walke S., Bragado-Nilsson E., Seraphin B., Nagai K.;
RT   "Stoichiometry of the Sm proteins in yeast spliceosomal snRNPs supports the
RT   heptamer ring model of the core domain.";
RL   J. Mol. Biol. 308:49-58(2001).
RN   [10]
RP   CHARACTERIZATION OF THE SPLICEOSOME.
RX   PubMed=11804584; DOI=10.1016/s1097-2765(02)00436-7;
RA   Stevens S.W., Ryan D.E., Ge H.Y., Moore R.E., Young M.K., Lee T.D.,
RA   Abelson J.;
RT   "Composition and functional characterization of the yeast spliceosomal
RT   penta-snRNP.";
RL   Mol. Cell 9:31-44(2002).
RN   [11]
RP   INTERACTION WITH TGS1.
RX   PubMed=11983179; DOI=10.1016/s1097-2765(02)00484-7;
RA   Mouaikel J., Verheggen C., Bertrand E., Tazi J., Bordonne R.;
RT   "Hypermethylation of the cap structure of both yeast snRNAs and snoRNAs
RT   requires a conserved methyltransferase that is localized to the
RT   nucleolus.";
RL   Mol. Cell 9:891-901(2002).
RN   [12]
RP   IDENTIFICATION IN THE CWC COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=11884590; DOI=10.1128/mcb.22.7.2011-2024.2002;
RA   Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.;
RT   "Proteomics analysis reveals stable multiprotein complexes in both fission
RT   and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA
RT   splicing factors, and snRNAs.";
RL   Mol. Cell. Biol. 22:2011-2024(2002).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA   Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA   Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA   Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT   "Assigning function to yeast proteins by integration of technologies.";
RL   Mol. Cell 12:1353-1365(2003).
RN   [14]
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   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [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: Plays a role in pre-mRNA splicing as a core component of the
CC       spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins
CC       (snRNPs), the building blocks of the spliceosome (By similarity).
CC       {ECO:0000250|UniProtKB:P14678}.
CC   -!- SUBUNIT: Component of the Sm core complex, present in spliceosomal
CC       snRNP U1, U2, U4/U6 and U5. The core complex contains SMB1, SMD1, SMD2,
CC       SMD3, SME1, SMX3 and SMX2 (Sm proteins B, D1, D2, D3, E, F and G,
CC       respectively), and is probably a heptameric ring structure. SMB1
CC       specifically interacts with SMD3. Belongs to the CWC complex (or CEF1-
CC       associated complex), a spliceosome sub-complex reminiscent of a late-
CC       stage spliceosome composed of the U2, U5 and U6 snRNAs and at least
CC       BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22,
CC       CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1,
CC       NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7,
CC       SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2,
CC       RSE1 and YJU2. Component of the U4/U6-U5 tri-snRNP complex composed of
CC       the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18,
CC       PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3,
CC       SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1.
CC       Interacts with the trimethylguanosine synthase TGS1.
CC       {ECO:0000269|PubMed:10449419, ECO:0000269|PubMed:11302706,
CC       ECO:0000269|PubMed:11884590, ECO:0000269|PubMed:11983179,
CC       ECO:0000269|PubMed:9528767}.
CC   -!- INTERACTION:
CC       P40018; P43321: SMD3; NbExp=3; IntAct=EBI-432, EBI-529;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q10163}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q10163}.
CC   -!- DOMAIN: C-terminal extension may function as a nuclear localization
CC       signal (NLS).
CC   -!- MISCELLANEOUS: Present with 861 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the snRNP SmB/SmN family. {ECO:0000305}.
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DR   EMBL; U18778; AAB64562.1; -; Genomic_DNA.
DR   EMBL; AY558450; AAS56776.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07682.1; -; Genomic_DNA.
DR   PIR; S50487; S50487.
DR   RefSeq; NP_010946.3; NM_001178920.3.
DR   PDB; 3JCM; EM; 3.80 A; O/S=1-196.
DR   PDB; 5GAM; EM; 3.70 A; b=1-196.
DR   PDB; 5GAN; EM; 3.60 A; b/k=1-196.
DR   PDB; 5GAO; EM; 3.60 A; k=1-196.
DR   PDB; 5GM6; EM; 3.50 A; k=1-196.
DR   PDB; 5GMK; EM; 3.40 A; k/s=1-196.
DR   PDB; 5LJ3; EM; 3.80 A; b/k=1-196.
DR   PDB; 5LJ5; EM; 3.80 A; b/k=1-196.
DR   PDB; 5LQW; EM; 5.80 A; b=1-196.
DR   PDB; 5MPS; EM; 3.85 A; b=1-196.
DR   PDB; 5MQ0; EM; 4.17 A; b/k=1-196.
DR   PDB; 5NRL; EM; 7.20 A; b/k/s=1-196.
DR   PDB; 5WSG; EM; 4.00 A; F/k=1-196.
DR   PDB; 5Y88; EM; 3.70 A; a/h=1-196.
DR   PDB; 5YLZ; EM; 3.60 A; a/h=1-196.
DR   PDB; 5ZWM; EM; 3.40 A; P/a/h=1-196.
DR   PDB; 5ZWN; EM; 3.30 A; a=1-196.
DR   PDB; 5ZWO; EM; 3.90 A; P/a/h=1-196.
DR   PDB; 6BK8; EM; 3.30 A; f/k=1-196.
DR   PDB; 6EXN; EM; 3.70 A; b/k=1-196.
DR   PDB; 6G90; EM; 4.00 A; b/s=1-196.
DR   PDB; 6J6G; EM; 3.20 A; k/s=1-196.
DR   PDB; 6J6H; EM; 3.60 A; k/s=1-196.
DR   PDB; 6J6N; EM; 3.86 A; k/s=1-196.
DR   PDB; 6J6Q; EM; 3.70 A; k/s=1-196.
DR   PDB; 6N7P; EM; 3.60 A; K=1-196.
DR   PDB; 6N7R; EM; 3.20 A; K=1-196.
DR   PDB; 6N7X; EM; 3.60 A; K=1-196.
DR   PDB; 7B9V; EM; 2.80 A; b/k=1-196.
DR   PDB; 7OQB; EM; 9.00 A; s=1-196.
DR   PDB; 7OQC; EM; 4.10 A; b=1-196.
DR   PDB; 7OQE; EM; 5.90 A; b/s=1-196.
DR   PDBsum; 3JCM; -.
DR   PDBsum; 5GAM; -.
DR   PDBsum; 5GAN; -.
DR   PDBsum; 5GAO; -.
DR   PDBsum; 5GM6; -.
DR   PDBsum; 5GMK; -.
DR   PDBsum; 5LJ3; -.
DR   PDBsum; 5LJ5; -.
DR   PDBsum; 5LQW; -.
DR   PDBsum; 5MPS; -.
DR   PDBsum; 5MQ0; -.
DR   PDBsum; 5NRL; -.
DR   PDBsum; 5WSG; -.
DR   PDBsum; 5Y88; -.
DR   PDBsum; 5YLZ; -.
DR   PDBsum; 5ZWM; -.
DR   PDBsum; 5ZWN; -.
DR   PDBsum; 5ZWO; -.
DR   PDBsum; 6BK8; -.
DR   PDBsum; 6EXN; -.
DR   PDBsum; 6G90; -.
DR   PDBsum; 6J6G; -.
DR   PDBsum; 6J6H; -.
DR   PDBsum; 6J6N; -.
DR   PDBsum; 6J6Q; -.
DR   PDBsum; 6N7P; -.
DR   PDBsum; 6N7R; -.
DR   PDBsum; 6N7X; -.
DR   PDBsum; 7B9V; -.
DR   PDBsum; 7OQB; -.
DR   PDBsum; 7OQC; -.
DR   PDBsum; 7OQE; -.
DR   AlphaFoldDB; P40018; -.
DR   SMR; P40018; -.
DR   BioGRID; 36764; 122.
DR   ComplexPortal; CPX-1651; PRP19-associated complex.
DR   ComplexPortal; CPX-23; U1 small nuclear ribonucleoprotein complex.
DR   ComplexPortal; CPX-25; U4/U6.U5 tri-small nuclear ribonucleoprotein complex.
DR   ComplexPortal; CPX-26; U2 small nuclear ribonucleoprotein complex.
DR   ComplexPortal; CPX-29; U5 small nuclear ribonucleoprotein complex.
DR   ComplexPortal; CPX-30; U5 small nuclear ribonucleoprotein complex, AAR2 variant.
DR   ComplexPortal; CPX-31; U4 small nuclear ribonucleoprotein complex.
DR   ComplexPortal; CPX-32; U4/U6 small nuclear ribonucleoprotein complex.
DR   ComplexPortal; CPX-43; Sm complex.
DR   DIP; DIP-843N; -.
DR   IntAct; P40018; 67.
DR   MINT; P40018; -.
DR   STRING; 4932.YER029C; -.
DR   MaxQB; P40018; -.
DR   PaxDb; P40018; -.
DR   PRIDE; P40018; -.
DR   EnsemblFungi; YER029C_mRNA; YER029C; YER029C.
DR   GeneID; 856751; -.
DR   KEGG; sce:YER029C; -.
DR   SGD; S000000831; SMB1.
DR   VEuPathDB; FungiDB:YER029C; -.
DR   eggNOG; KOG3168; Eukaryota.
DR   GeneTree; ENSGT00940000170258; -.
DR   HOGENOM; CLU_076902_1_2_1; -.
DR   InParanoid; P40018; -.
DR   OMA; VRKFQPP; -.
DR   BioCyc; YEAST:G3O-30210-MON; -.
DR   PRO; PR:P40018; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P40018; protein.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR   GO; GO:0000243; C:commitment complex; IC:ComplexPortal.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR   GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR   GO; GO:0005685; C:U1 snRNP; IDA:SGD.
DR   GO; GO:0005686; C:U2 snRNP; IBA:GO_Central.
DR   GO; GO:0071004; C:U2-type prespliceosome; IDA:SGD.
DR   GO; GO:0005687; C:U4 snRNP; IPI:ComplexPortal.
DR   GO; GO:0071001; C:U4/U6 snRNP; IC:ComplexPortal.
DR   GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:SGD.
DR   GO; GO:0005682; C:U5 snRNP; IDA:SGD.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0036261; P:7-methylguanosine cap hypermethylation; IMP:ComplexPortal.
DR   GO; GO:0000395; P:mRNA 5'-splice site recognition; IC:ComplexPortal.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IPI:ComplexPortal.
DR   GO; GO:0000245; P:spliceosomal complex assembly; IC:ComplexPortal.
DR   GO; GO:0000387; P:spliceosomal snRNP assembly; IC:ComplexPortal.
DR   GO; GO:1903241; P:U2-type prespliceosome assembly; IC:ComplexPortal.
DR   InterPro; IPR001163; LSM_dom_euk/arc.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   Pfam; PF01423; LSM; 1.
DR   SMART; SM00651; Sm; 1.
DR   SUPFAM; SSF50182; SSF50182; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; mRNA processing;
KW   mRNA splicing; Nucleus; Reference proteome; Ribonucleoprotein; RNA-binding.
FT   CHAIN           1..196
FT                   /note="Small nuclear ribonucleoprotein-associated protein
FT                   B"
FT                   /id="PRO_0000125527"
FT   REGION          108..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           105..132
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        108..136
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..183
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   TURN            12..14
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   STRAND          19..24
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   STRAND          29..34
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   STRAND          44..52
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   HELIX           55..58
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   TURN            59..61
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   STRAND          78..87
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   TURN            89..91
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   STRAND          92..97
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   HELIX           105..108
FT                   /evidence="ECO:0007829|PDB:6J6G"
SQ   SEQUENCE   196 AA;  22379 MW;  0A1078D5AA241430 CRC64;
     MSKIQVAHSS RLANLIDYKL RVLTQDGRVY IGQLMAFDKH MNLVLNECIE ERVPKTQLDK
     LRPRKDSKDG TTLNIKVEKR VLGLTILRGE QILSTVVEDK PLLSKKERLV RDKKEKKQAQ
     KQTKLRKEKE KKPGKIAKPN TANAKHTSSN SREIAQPSSS RYNGGNDNIG ANRSRFNNEA
     PPQTRKFQPP PGFKRK
 
 
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