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RSMB_MONDO
ID   RSMB_MONDO              Reviewed;         240 AA.
AC   Q9TU66;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Small nuclear ribonucleoprotein-associated protein B';
DE            Short=snRNP-B';
DE            Short=snRPB';
DE   AltName: Full=Sm protein B';
DE            Short=Sm-B';
DE            Short=SmB';
GN   Name=SNRPB;
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10556313; DOI=10.1093/nar/27.23.4577;
RA   Gray T.A., Smithwick M.J., Schaldach M.A., Martone D.L., Graves J.A.,
RA   McCarrey J.R., Nicholls R.D.;
RT   "Concerted regulation and molecular evolution of the duplicated SNRPB'/B
RT   and SNRPN loci.";
RL   Nucleic Acids Res. 27:4577-4584(1999).
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       Component of both the pre-catalytic spliceosome B complex and activated
CC       spliceosome C complexes (By similarity). Is also a component of the
CC       minor U12 spliceosome (By similarity). As part of the U7 snRNP it is
CC       involved in histone pre-mRNA 3'-end processing (By similarity).
CC       {ECO:0000250|UniProtKB:P14678}.
CC   -!- SUBUNIT: Core component of the spliceosomal U1, U2, U4 and U5 small
CC       nuclear ribonucleoproteins (snRNPs), the building blocks of the
CC       spliceosome (By similarity). Most spliceosomal snRNPs contain a common
CC       set of Sm proteins, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and
CC       SNRPG that assemble in a heptameric protein ring on the Sm site of the
CC       small nuclear RNA to form the core snRNP (By similarity). Component of
CC       the U1 snRNP (By similarity). The U1 snRNP is composed of the U1 snRNA
CC       and the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF
CC       and SNRPG, and at least three U1 snRNP-specific proteins SNRNP70/U1-
CC       70K, SNRPA/U1-A and SNRPC/U1-C (By similarity). Component of the U4/U6-
CC       U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least
CC       PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB,
CC       SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH,
CC       SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7
CC       and LSM8 (By similarity). Component of the U7 snRNP complex, or U7 Sm
CC       protein core complex, that is composed of the U7 snRNA and at least
CC       LSM10, LSM11, SNRPB, SNRPD3, SNRPE, SNRPF and SNRPG; the complex does
CC       not contain SNRPD1 and SNRPD2 (By similarity). Component of the U11/U12
CC       snRNPs that are part of the U12-type spliceosome (By similarity). Part
CC       of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3,
CC       GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins
CC       SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG; catalyzes core
CC       snRNPs assembly (By similarity). Forms a 6S pICln-Sm complex composed
CC       of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like
CC       structure where CLNS1A/pICln mimics additional Sm proteins and which is
CC       unable to assemble into the core snRNP (By similarity). Identified in a
CC       histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP,
CC       SNRPB, SYNCRIP and YBX1 (By similarity). Interacts with TDRD3 and SNUPN
CC       (By similarity). Interacts with PRMT5; interaction leads to its
CC       symmetric arginine dimethylation (By similarity). Interacts with TDRD6;
CC       interaction promotes association with PRMT5 (By similarity). Interacts
CC       with SMN1; the interaction is direct (By similarity).
CC       {ECO:0000250|UniProtKB:P14678, ECO:0000250|UniProtKB:P27048}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P14678}. Nucleus {ECO:0000250|UniProtKB:P14678}.
CC       Note=SMN-mediated assembly into core snRNPs occurs in the cytosol
CC       before SMN-mediated transport to the nucleus to be included in
CC       spliceosomes. {ECO:0000250|UniProtKB:P14678}.
CC   -!- PTM: Methylated by PRMT5 (By similarity). Arg-108 and Arg-112 are
CC       dimethylated, probably to asymmetric dimethylarginine (By similarity).
CC       {ECO:0000250|UniProtKB:P14678, ECO:0000250|UniProtKB:P27048}.
CC   -!- SIMILARITY: Belongs to the snRNP SmB/SmN family. {ECO:0000305}.
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DR   EMBL; AF134827; AAD54482.1; -; mRNA.
DR   RefSeq; NP_001029144.1; NM_001033972.1.
DR   AlphaFoldDB; Q9TU66; -.
DR   SMR; Q9TU66; -.
DR   STRING; 13616.ENSMODP00000017410; -.
DR   GeneID; 554245; -.
DR   KEGG; mdo:554245; -.
DR   CTD; 6628; -.
DR   eggNOG; KOG3168; Eukaryota.
DR   InParanoid; Q9TU66; -.
DR   OrthoDB; 1630470at2759; -.
DR   Proteomes; UP000002280; Unplaced.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0034709; C:methylosome; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0034719; C:SMN-Sm protein complex; ISS:UniProtKB.
DR   GO; GO:0005685; C:U1 snRNP; ISS:UniProtKB.
DR   GO; GO:0005686; C:U2 snRNP; IBA:GO_Central.
DR   GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; ISS:UniProtKB.
DR   GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR   GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
DR   GO; GO:0005687; C:U4 snRNP; ISS:UniProtKB.
DR   GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; ISS:UniProtKB.
DR   GO; GO:0005682; C:U5 snRNP; IBA:GO_Central.
DR   GO; GO:0005683; C:U7 snRNP; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB.
DR   InterPro; IPR001163; LSM_dom_euk/arc.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   InterPro; IPR017131; snRNP-assoc_SmB/SmN.
DR   Pfam; PF01423; LSM; 1.
DR   PIRSF; PIRSF037187; snRNP_SmB/SmN; 1.
DR   SMART; SM00651; Sm; 1.
DR   SUPFAM; SSF50182; SSF50182; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Methylation; mRNA processing; mRNA splicing; Nucleus;
KW   Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; Spliceosome.
FT   CHAIN           1..240
FT                   /note="Small nuclear ribonucleoprotein-associated protein
FT                   B'"
FT                   /id="PRO_0000125518"
FT   REPEAT          175..181
FT   REPEAT          191..196
FT   REPEAT          216..221
FT   REPEAT          222..228
FT   REPEAT          230..236
FT   REGION          163..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          175..236
FT                   /note="Repeat-rich region"
FT   COMPBIAS        170..240
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         108
FT                   /note="Asymmetric dimethylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P14678"
FT   MOD_RES         108
FT                   /note="Dimethylated arginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P14678"
FT   MOD_RES         108
FT                   /note="Omega-N-methylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P14678"
FT   MOD_RES         112
FT                   /note="Asymmetric dimethylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P14678"
FT   MOD_RES         112
FT                   /note="Dimethylated arginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P14678"
FT   MOD_RES         112
FT                   /note="Omega-N-methylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P14678"
FT   MOD_RES         147
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P14678"
FT   MOD_RES         172
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P63162"
SQ   SEQUENCE   240 AA;  24542 MW;  2498CFAEE943C828 CRC64;
     MTVGKSSKML QHIDCRMRCI LQDGRIFIGT FKAFDKHMNL ILCDCDEFRK IKPKNSKQAE
     REEKRVLGLV LLRGENLVSM TVEGPPPKDT GIARVPLAGA AGGPGIGRAA GRGVPAGVPM
     PQAPAGLAGP IRGVGGPSQQ VMTPQGRGTV AAAAAAATAS IAGAPTQYPS GRGGPPPPMG
     RGAPPPGMMA PPPGMRPPMG PPMGMPPGRG APMGMPPPGM RPPPPGMRGP PPPGMRPPRP
 
 
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