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UniProtKB - P14678 (RSMB_HUMAN)

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Protein

Small nuclear ribonucleoprotein-associated proteins B and B'

Gene

SNRPB

Organism
Homo sapiens (Human)
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

Miscellaneous

Patients with the autoimmune disease systemic lupus erythematosus (SLE) have autoantibodies directed against some of the individual snRNP polypeptides. The most common autoantigen is called Sm. B/b' bear Sm epitopes.

GO - Molecular functioni

  • histone pre-mRNA DCP binding Source: Ensembl
  • RNA binding Source: UniProtKB
  • telomerase RNA binding Source: BHF-UCL
  • U2 snRNA binding Source: BHF-UCL
Complete GO annotation...

GO - Biological processi

  • histone mRNA metabolic process Source: Reactome
  • mRNA splicing, via spliceosome Source: Reactome
  • nuclear import Source: Reactome
  • protein methylation Source: MGI
  • RNA splicing Source: ProtInc
  • spliceosomal snRNP assembly Source: UniProtKB
  • termination of RNA polymerase II transcription Source: Reactome
Complete GO annotation...

Keywordsi

Molecular functionRibonucleoprotein, RNA-binding
Biological processmRNA processing, mRNA splicing

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Small nuclear ribonucleoprotein-associated proteins B and B'
Short name:
snRNP-B
Alternative name(s):
Sm protein B/B'
Short name:
Sm-B/B'
Short name:
SmB/B'
Gene namesi
Name:SNRPB
Synonyms:COD, SNRPB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:11153. SNRPB.

Subcellular locationi

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: UniProtKB
  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • histone pre-mRNA 3'end processing complex Source: Ensembl
  • methylosome Source: UniProtKB
  • nucleoplasm Source: HPA
  • small nuclear ribonucleoprotein complex Source: ProtInc
  • SMN-Sm protein complex Source: UniProtKB
  • spliceosomal complex Source: ProtInc
  • U12-type spliceosomal complex Source: UniProtKB
  • U1 snRNP Source: UniProtKB
  • U2 snRNP Source: GO_Central
  • U2-type prespliceosome Source: GO_Central
  • U4/U6 x U5 tri-snRNP complex Source: GO_Central
  • U4 snRNP Source: UniProtKB
  • U5 snRNP Source: GO_Central
  • U7 snRNP Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

Pathology & Biotechi

Involvement in diseasei

Cerebrocostomandibular syndrome (CCMS)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA syndrome characterized by severe micrognathia, rib defects ranging from a few dorsal rib segments to complete absence of ossification, and mental retardation.
See also OMIM:117650
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07338055N → S in CCMS; expression of the protein is reduced. 2 Publications1
Natural variantiVAR_07338155N → T in CCMS. 1 Publication1
Natural variantiVAR_07338256S → R in CCMS. 2 Publications1
Natural variantiVAR_07338356S → W in CCMS. 1 Publication1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNETi6628.
MalaCardsiSNRPB.
MIMi117650. phenotype.
OpenTargetsiENSG00000125835.
Orphaneti1393. Cerebro-costo-mandibular syndrome.
PharmGKBiPA35995.

Polymorphism and mutation databases

BioMutaiSNRPB.
DMDMi134037.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001255171 – 240Small nuclear ribonucleoprotein-associated proteins B and B'Add BLAST240

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei108Asymmetric dimethylarginine; alternateCombined sources1
Modified residuei108Dimethylated arginine; in A2780 ovarian carcinoma cell line1 Publication1
Modified residuei108Omega-N-methylarginine; alternateCombined sources1
Modified residuei112Asymmetric dimethylarginine; alternateCombined sources1
Modified residuei112Dimethylated arginine; in A2780 ovarian carcinoma cell line1 Publication1
Modified residuei112Omega-N-methylarginine; alternateCombined sources1
Modified residuei147Omega-N-methylarginine1 Publication1

Post-translational modificationi

Methylated. Arg-108 and Arg-112 are dimethylated, probably to asymmetric dimethylarginine.2 Publications

Keywords - PTMi

Methylation

Proteomic databases

EPDiP14678.
MaxQBiP14678.
PaxDbiP14678.
PeptideAtlasiP14678.
PRIDEiP14678.
TopDownProteomicsiP14678-2. [P14678-2]

PTM databases

iPTMnetiP14678.
PhosphoSitePlusiP14678.
SwissPalmiP14678.

Expressioni

Gene expression databases

BgeeiENSG00000125835.
CleanExiHS_SNRPB.
ExpressionAtlasiP14678. baseline and differential.
GenevisibleiP14678. HS.

Organism-specific databases

HPAiCAB009610.
HPA003482.
HPA067842.

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.8 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi112512. 111 interactors.
DIPiDIP-31239N.
IntActiP14678. 99 interactors.
MINTiMINT-124876.
STRINGi9606.ENSP00000412566.

Structurei

Secondary structure

1240
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 12Combined sources3
Beta strandi15 – 21Combined sources7
Beta strandi26 – 33Combined sources8
Beta strandi40 – 51Combined sources12
Beta strandi54 – 58Combined sources5
Beta strandi61 – 72Combined sources12
Helixi74 – 76Combined sources3
Beta strandi77 – 84Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D3BX-ray2.00B/D/F/H/J/L1-91[»]
3CW1X-ray5.49A/H/I/J1-174[»]
3JCRelectron microscopy7.00O/o1-240[»]
3PGWX-ray4.40B/Q1-229[»]
4PJOX-ray3.30B/P/b/p1-95[»]
4WZJX-ray3.60AA/AH/AO/BA/BH/BO/CA/CH/CO/DA/DH/DO1-95[»]
5MQFelectron microscopy5.90f/m1-240[»]
ProteinModelPortaliP14678.
SMRiP14678.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14678.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati175 – 1817
Repeati191 – 1966
Repeati216 – 2216
Repeati222 – 2287
Repeati230 – 2367

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni175 – 236Repeat-rich regionAdd BLAST62

Sequence similaritiesi

Belongs to the snRNP SmB/SmN family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3168. Eukaryota.
COG1958. LUCA.
GeneTreeiENSGT00670000098029.
HOGENOMiHOG000188899.
HOVERGENiHBG001019.
KOiK11086.
OMAiRGMGMMP.
PhylomeDBiP14678.
TreeFamiTF314232.

Family and domain databases

InterProiView protein in InterPro
IPR010920. LSM_dom.
IPR001163. LSM_dom_euk/arc.
IPR017131. snRNP-assoc_SmB/SmN.
PfamiView protein in Pfam
PF01423. LSM. 1 hit.
PIRSFiPIRSF037187. snRNP_SmB/SmN. 1 hit.
SMARTiView protein in SMART
SM00651. Sm. 1 hit.
SUPFAMiSSF50182. SSF50182. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform SM-B' (identifier: P14678-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« 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        240
PPMGIPPGRG TPMGMPPPGM RPPPPGMRGP PPPGMRPPRP
Length:240
Mass (Da):24,610
Last modified:November 1, 1991 - v2
Checksum:iF2E1D5E11A601170
GO
Isoform SM-B (identifier: P14678-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     230-240: PPPPGMRPPRP → LL

Show »
Length:231
Mass (Da):23,656
Checksum:i5CB0BB2E75B93D4A
GO
Isoform SM-B1 (identifier: P14678-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     227-228: MR → GCEAFFDPWPQSMEVAPQRRGLDSSGPRYHRPVCFLCCCSWSLMGLSGFLT

Show »
Length:289
Mass (Da):30,032
Checksum:i573E8A21414E2C22
GO

Sequence cautioni

The sequence AAD54488 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti172 – 173RG → L no nucleotide entry (PubMed:2524838).Curated2
Sequence conflicti201Missing no nucleotide entry (PubMed:2524838).Curated1
Sequence conflicti217 – 218PP → S no nucleotide entry (PubMed:2524838).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07338055N → S in CCMS; expression of the protein is reduced. 2 Publications1
Natural variantiVAR_07338155N → T in CCMS. 1 Publication1
Natural variantiVAR_07338256S → R in CCMS. 2 Publications1
Natural variantiVAR_07338356S → W in CCMS. 1 Publication1
Natural variantiVAR_05227479S → P. Corresponds to variant dbSNP:rs11545672Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_012221227 – 228MR → GCEAFFDPWPQSMEVAPQRR GLDSSGPRYHRPVCFLCCCS WSLMGLSGFLT in isoform SM-B1. 1 Publication2
Alternative sequenceiVSP_005914230 – 240PPPPGMRPPRP → LL in isoform SM-B. 3 PublicationsAdd BLAST11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17567 mRNA. Translation: CAB57867.1.
X17568 mRNA. Translation: CAB57868.1.
X15893 mRNA. Translation: CAA33902.1.
AF134825
, AF134822, AF134823, AF134824 Genomic DNA. Translation: AAD54488.1. Sequence problems.
AL049650 Genomic DNA. Translation: CAB46715.1.
CH471133 Genomic DNA. Translation: EAX10596.1.
CR456969 mRNA. Translation: CAG33250.1.
AL049650 Genomic DNA. Translation: CAB46714.1.
M34081 mRNA. Translation: AAA36578.1.
M34082 mRNA. Translation: AAA36579.1.
X52979 Genomic DNA. Translation: CAA37170.1.
X52979 Genomic DNA. Translation: CAA37171.1.
CCDSiCCDS13026.1. [P14678-1]
CCDS13027.1. [P14678-2]
PIRiS09377.
RefSeqiNP_003082.1. NM_003091.3. [P14678-2]
NP_937859.1. NM_198216.1. [P14678-1]
UniGeneiHs.83753.

Genome annotation databases

EnsembliENST00000381342; ENSP00000370746; ENSG00000125835. [P14678-2]
ENST00000438552; ENSP00000412566; ENSG00000125835. [P14678-1]
GeneIDi6628.
KEGGihsa:6628.
UCSCiuc002wfz.2. human. [P14678-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17567 mRNA. Translation: CAB57867.1.
X17568 mRNA. Translation: CAB57868.1.
X15893 mRNA. Translation: CAA33902.1.
AF134825
, AF134822, AF134823, AF134824 Genomic DNA. Translation: AAD54488.1. Sequence problems.
AL049650 Genomic DNA. Translation: CAB46715.1.
CH471133 Genomic DNA. Translation: EAX10596.1.
CR456969 mRNA. Translation: CAG33250.1.
AL049650 Genomic DNA. Translation: CAB46714.1.
M34081 mRNA. Translation: AAA36578.1.
M34082 mRNA. Translation: AAA36579.1.
X52979 Genomic DNA. Translation: CAA37170.1.
X52979 Genomic DNA. Translation: CAA37171.1.
CCDSiCCDS13026.1. [P14678-1]
CCDS13027.1. [P14678-2]
PIRiS09377.
RefSeqiNP_003082.1. NM_003091.3. [P14678-2]
NP_937859.1. NM_198216.1. [P14678-1]
UniGeneiHs.83753.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D3BX-ray2.00B/D/F/H/J/L1-91[»]
3CW1X-ray5.49A/H/I/J1-174[»]
3JCRelectron microscopy7.00O/o1-240[»]
3PGWX-ray4.40B/Q1-229[»]
4PJOX-ray3.30B/P/b/p1-95[»]
4WZJX-ray3.60AA/AH/AO/BA/BH/BO/CA/CH/CO/DA/DH/DO1-95[»]
5MQFelectron microscopy5.90f/m1-240[»]
ProteinModelPortaliP14678.
SMRiP14678.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112512. 111 interactors.
DIPiDIP-31239N.
IntActiP14678. 99 interactors.
MINTiMINT-124876.
STRINGi9606.ENSP00000412566.

PTM databases

iPTMnetiP14678.
PhosphoSitePlusiP14678.
SwissPalmiP14678.

Polymorphism and mutation databases

BioMutaiSNRPB.
DMDMi134037.

Proteomic databases

EPDiP14678.
MaxQBiP14678.
PaxDbiP14678.
PeptideAtlasiP14678.
PRIDEiP14678.
TopDownProteomicsiP14678-2. [P14678-2]

Protocols and materials databases

DNASUi6628.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000381342; ENSP00000370746; ENSG00000125835. [P14678-2]
ENST00000438552; ENSP00000412566; ENSG00000125835. [P14678-1]
GeneIDi6628.
KEGGihsa:6628.
UCSCiuc002wfz.2. human. [P14678-1]

Organism-specific databases

CTDi6628.
DisGeNETi6628.
GeneCardsiSNRPB.
HGNCiHGNC:11153. SNRPB.
HPAiCAB009610.
HPA003482.
HPA067842.
MalaCardsiSNRPB.
MIMi117650. phenotype.
182282. gene.
neXtProtiNX_P14678.
OpenTargetsiENSG00000125835.
Orphaneti1393. Cerebro-costo-mandibular syndrome.
PharmGKBiPA35995.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3168. Eukaryota.
COG1958. LUCA.
GeneTreeiENSGT00670000098029.
HOGENOMiHOG000188899.
HOVERGENiHBG001019.
KOiK11086.
OMAiRGMGMMP.
PhylomeDBiP14678.
TreeFamiTF314232.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiSNRPB. human.
EvolutionaryTraceiP14678.
GeneWikiiSNRPB.
GenomeRNAii6628.
PROiPR:P14678.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000125835.
CleanExiHS_SNRPB.
ExpressionAtlasiP14678. baseline and differential.
GenevisibleiP14678. HS.

Family and domain databases

InterProiView protein in InterPro
IPR010920. LSM_dom.
IPR001163. LSM_dom_euk/arc.
IPR017131. snRNP-assoc_SmB/SmN.
PfamiView protein in Pfam
PF01423. LSM. 1 hit.
PIRSFiPIRSF037187. snRNP_SmB/SmN. 1 hit.
SMARTiView protein in SMART
SM00651. Sm. 1 hit.
SUPFAMiSSF50182. SSF50182. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRSMB_HUMAN
AccessioniPrimary (citable) accession number: P14678
Secondary accession number(s): Q15490, Q6IB35, Q9UIS5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1991
Last modified: June 7, 2017
This is version 198 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.