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Protein

Small nuclear ribonucleoprotein-associated protein B

Gene

Snrpb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. As part of the U7 snRNP it is involved in histone 3'-end processing.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-109688. Cleavage of Growing Transcript in the Termination Region.
R-MMU-111367. SLBP independent Processing of Histone Pre-mRNAs.
R-MMU-191859. snRNP Assembly.
R-MMU-72163. mRNA Splicing - Major Pathway.
R-MMU-72165. mRNA Splicing - Minor Pathway.
R-MMU-77588. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.

Names & Taxonomyi

Protein namesi
Recommended name:
Small nuclear ribonucleoprotein-associated protein B
Short name:
snRNP-B
Short name:
snRPB
Alternative name(s):
Sm protein B
Short name:
Sm-B
Short name:
SmB
Gene namesi
Name:Snrpb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:98342. Snrpb.

Subcellular locationi

  • Cytoplasmcytosol By similarity
  • Nucleus By similarity

  • Note: SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes.By similarity

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: MGI
  • cytoplasm Source: MGI
  • cytosol Source: UniProtKB
  • extracellular exosome Source: MGI
  • histone pre-mRNA 3'end processing complex Source: UniProtKB
  • methylosome Source: UniProtKB
  • nucleus Source: MGI
  • SMN-Sm protein complex Source: UniProtKB
  • telomerase holoenzyme complex Source: Ensembl
  • U12-type spliceosomal complex Source: MGI
  • U1 snRNP Source: UniProtKB
  • U4 snRNP Source: UniProtKB
  • U7 snRNP Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 231231Small nuclear ribonucleoprotein-associated protein BPRO_0000125519Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei108 – 1081Dimethylated arginine; alternateBy similarity
Modified residuei108 – 1081Omega-N-methylated arginine; alternateBy similarity
Modified residuei112 – 1121Dimethylated arginine; alternateBy similarity
Modified residuei112 – 1121Omega-N-methylated arginine; alternateBy similarity
Modified residuei147 – 1471Omega-N-methylarginineBy similarity

Post-translational modificationi

Methylated. Arg-108 and Arg-112 are dimethylated, probably to asymmetric dimethylarginine (By similarity).By similarity

Keywords - PTMi

Methylation

Proteomic databases

EPDiP27048.
MaxQBiP27048.
PaxDbiP27048.
PRIDEiP27048.

PTM databases

iPTMnetiP27048.
PhosphoSiteiP27048.

Miscellaneous databases

PMAP-CutDBP27048.

Expressioni

Gene expression databases

BgeeiP27048.
CleanExiMM_SNRPB.
ExpressionAtlasiP27048. baseline and differential.
GenevisibleiP27048. MM.

Interactioni

Subunit structurei

U1 snRNP is for instance composed of the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP, and at least three U1 snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C. Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Component of the heptameric ring U7 snRNP complex, or U7 Sm protein core complex, at least composed of LSM10, LSM11, SNRPB, SNRPD3, SNRPE, SNRPF, SNRPG and U7 snRNA. Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG; catalyzes core snRNPs assembly. Forms a 6S pICln-Sm complex composed of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like structure where CLNS1A/pICln mimics additional Sm proteins and which is unable to assemble into the core snRNP. Identified in a histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1. Interacts with TDRD3 and SNUPN.1 Publication

Protein-protein interaction databases

BioGridi203377. 3 interactions.
IntActiP27048. 4 interactions.
MINTiMINT-1851409.
STRINGi10090.ENSMUSP00000099488.

Structurei

3D structure databases

ProteinModelPortaliP27048.
SMRiP27048. Positions 2-128.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati175 – 1817
Repeati191 – 1966
Repeati216 – 2216
Repeati222 – 2287

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni175 – 22854Repeat-rich regionAdd
BLAST

Sequence similaritiesi

Belongs to the snRNP SmB/SmN family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3168. Eukaryota.
COG1958. LUCA.
GeneTreeiENSGT00670000098029.
HOGENOMiHOG000188899.
HOVERGENiHBG001019.
InParanoidiP27048.
KOiK11086.
OMAiSSGPRYH.
OrthoDBiEOG7J70HT.
PhylomeDBiP27048.
TreeFamiTF314232.

Family and domain databases

InterProiIPR010920. LSM_dom.
IPR001163. LSM_dom_euk/arc.
IPR017131. snRNP-assoc_SmB/SmN.
[Graphical view]
PfamiPF01423. LSM. 1 hit.
[Graphical view]
PIRSFiPIRSF037187. snRNP_SmB/SmN. 1 hit.
SMARTiSM00651. Sm. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 1 hit.

Sequencei

Sequence statusi: Complete.

P27048-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVGKSSKML QHIDYRMRCI LQDGRIFIGT FKAFDKHMNL ILCDCDEFRK
60 70 80 90 100
IKPKNSKQAE REEKRVLGLV LLRGENLVSM TVEGPPPKDT GIARVPLAGA
110 120 130 140 150
AGGPGIGRAA GRGIPAGVPM PQAPAGLAGP VRGVGGPSQQ VMTPQGRGTV
160 170 180 190 200
AAAAAAATAS IAGAPTQYPP GRGGPPPPMG RGAPPPGMMG PPPGMRPPMG
210 220 230
PPMGLPPGRG TPMGMPPPGM RPPPPGMRGL L
Length:231
Mass (Da):23,656
Last modified:August 1, 1992 - v1
Checksum:i5CB0BE7E20B93D4A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58761 mRNA. Translation: AAA40119.1.
AK146319 mRNA. Translation: BAE27074.1.
CCDSiCCDS16735.1.
PIRiI53659.
RefSeqiNP_033251.1. NM_009225.2.
UniGeneiMm.88216.

Genome annotation databases

EnsembliENSMUST00000103199; ENSMUSP00000099488; ENSMUSG00000027404.
GeneIDi20638.
KEGGimmu:20638.
UCSCiuc008mij.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58761 mRNA. Translation: AAA40119.1.
AK146319 mRNA. Translation: BAE27074.1.
CCDSiCCDS16735.1.
PIRiI53659.
RefSeqiNP_033251.1. NM_009225.2.
UniGeneiMm.88216.

3D structure databases

ProteinModelPortaliP27048.
SMRiP27048. Positions 2-128.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203377. 3 interactions.
IntActiP27048. 4 interactions.
MINTiMINT-1851409.
STRINGi10090.ENSMUSP00000099488.

PTM databases

iPTMnetiP27048.
PhosphoSiteiP27048.

Proteomic databases

EPDiP27048.
MaxQBiP27048.
PaxDbiP27048.
PRIDEiP27048.

Protocols and materials databases

DNASUi20638.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000103199; ENSMUSP00000099488; ENSMUSG00000027404.
GeneIDi20638.
KEGGimmu:20638.
UCSCiuc008mij.1. mouse.

Organism-specific databases

CTDi6628.
MGIiMGI:98342. Snrpb.

Phylogenomic databases

eggNOGiKOG3168. Eukaryota.
COG1958. LUCA.
GeneTreeiENSGT00670000098029.
HOGENOMiHOG000188899.
HOVERGENiHBG001019.
InParanoidiP27048.
KOiK11086.
OMAiSSGPRYH.
OrthoDBiEOG7J70HT.
PhylomeDBiP27048.
TreeFamiTF314232.

Enzyme and pathway databases

ReactomeiR-MMU-109688. Cleavage of Growing Transcript in the Termination Region.
R-MMU-111367. SLBP independent Processing of Histone Pre-mRNAs.
R-MMU-191859. snRNP Assembly.
R-MMU-72163. mRNA Splicing - Major Pathway.
R-MMU-72165. mRNA Splicing - Minor Pathway.
R-MMU-77588. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.

Miscellaneous databases

ChiTaRSiSnrpb. mouse.
NextBioi299039.
PMAP-CutDBP27048.
PROiP27048.
SOURCEiSearch...

Gene expression databases

BgeeiP27048.
CleanExiMM_SNRPB.
ExpressionAtlasiP27048. baseline and differential.
GenevisibleiP27048. MM.

Family and domain databases

InterProiIPR010920. LSM_dom.
IPR001163. LSM_dom_euk/arc.
IPR017131. snRNP-assoc_SmB/SmN.
[Graphical view]
PfamiPF01423. LSM. 1 hit.
[Graphical view]
PIRSFiPIRSF037187. snRNP_SmB/SmN. 1 hit.
SMARTiSM00651. Sm. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The murine gene encoding the highly conserved Sm B protein contains a nonfunctional alternative 3' splice site."
    Griffith A., deJonge E., Huang S., Ohosone Y., Craft J.E.
    Gene 114:195-201(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BALB/cJ.
  3. "Three proteins of the U7-specific Sm ring function as the molecular ruler to determine the site of 3'-end processing in mammalian histone pre-mRNA."
    Yang X.-C., Torres M.P., Marzluff W.F., Dominski Z.
    Mol. Cell. Biol. 29:4045-4056(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A HISTONE PRE-MRNA COMPLEX, RNA-BINDING, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiRSMB_MOUSE
AccessioniPrimary (citable) accession number: P27048
Secondary accession number(s): Q3UJT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: May 11, 2016
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.