UniProtKB - P14678 (RSMB_HUMAN)
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Protein
Small nuclear ribonucleoprotein-associated proteins B and B'
Gene
SNRPB
Organism
Homo sapiens (Human)
Status
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: BHF-UCL
- telomerase RNA binding Source: BHF-UCL
- U2 snRNA binding Source: BHF-UCL
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
Keywordsi
Molecular function | Ribonucleoprotein, RNA-binding |
Biological process | mRNA processing, mRNA splicing |
Enzyme and pathway databases
Reactomei | R-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 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
EuPathDBi | HostDB:ENSG00000125835.17. |
HGNCi | HGNC:11153. SNRPB. |
MIMi | 182282. gene. |
neXtProti | NX_P14678. |
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:117650Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_073380 | 55 | N → S in CCMS; expression of the protein is reduced. 2 Publications | 1 | |
Natural variantiVAR_073381 | 55 | N → T in CCMS. 1 Publication | 1 | |
Natural variantiVAR_073382 | 56 | S → R in CCMS. 2 Publications | 1 | |
Natural variantiVAR_073383 | 56 | S → W in CCMS. 1 Publication | 1 |
Keywords - Diseasei
Disease mutation, Mental retardationOrganism-specific databases
DisGeNETi | 6628. |
MalaCardsi | SNRPB. |
MIMi | 117650. phenotype. |
OpenTargetsi | ENSG00000125835. |
Orphaneti | 1393. Cerebro-costo-mandibular syndrome. |
PharmGKBi | PA35995. |
Polymorphism and mutation databases
BioMutai | SNRPB. |
DMDMi | 134037. |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000125517 | 1 – 240 | Small nuclear ribonucleoprotein-associated proteins B and B'Add BLAST | 240 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 108 | Asymmetric dimethylarginine; alternateCombined sources | 1 | |
Modified residuei | 108 | Dimethylated arginine; in A2780 ovarian carcinoma cell line1 Publication | 1 | |
Modified residuei | 108 | Omega-N-methylarginine; alternateCombined sources | 1 | |
Modified residuei | 112 | Asymmetric dimethylarginine; alternateCombined sources | 1 | |
Modified residuei | 112 | Dimethylated arginine; in A2780 ovarian carcinoma cell line1 Publication | 1 | |
Modified residuei | 112 | Omega-N-methylarginine; alternateCombined sources | 1 | |
Modified residuei | 147 | Omega-N-methylarginine1 Publication | 1 | |
Modified residuei | 172 | Omega-N-methylarginineBy similarity | 1 |
Post-translational modificationi
Methylated. Arg-108 and Arg-112 are dimethylated, probably to asymmetric dimethylarginine.2 Publications
Keywords - PTMi
MethylationProteomic databases
EPDi | P14678. |
MaxQBi | P14678. |
PaxDbi | P14678. |
PeptideAtlasi | P14678. |
PRIDEi | P14678. |
TopDownProteomicsi | P14678-2. [P14678-2] |
PTM databases
iPTMneti | P14678. |
PhosphoSitePlusi | P14678. |
SwissPalmi | P14678. |
Expressioni
Gene expression databases
Bgeei | ENSG00000125835. |
CleanExi | HS_SNRPB. |
ExpressionAtlasi | P14678. baseline and differential. |
Genevisiblei | P14678. HS. |
Organism-specific databases
HPAi | CAB009610. 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
Protein-protein interaction databases
BioGridi | 112512. 154 interactors. |
CORUMi | P14678. |
DIPi | DIP-31239N. |
IntActi | P14678. 114 interactors. |
MINTi | P14678. |
STRINGi | 9606.ENSP00000412566. |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Helixi | 10 – 12 | Combined sources | 3 | |
Beta strandi | 15 – 21 | Combined sources | 7 | |
Beta strandi | 26 – 33 | Combined sources | 8 | |
Beta strandi | 40 – 51 | Combined sources | 12 | |
Beta strandi | 54 – 58 | Combined sources | 5 | |
Beta strandi | 61 – 72 | Combined sources | 12 | |
Helixi | 74 – 76 | Combined sources | 3 | |
Beta strandi | 77 – 84 | Combined sources | 8 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1D3B | X-ray | 2.00 | B/D/F/H/J/L | 1-91 | [»] | |
3CW1 | X-ray | 5.49 | A/H/I/J | 1-174 | [»] | |
3JCR | electron microscopy | 7.00 | O/o | 1-240 | [»] | |
3PGW | X-ray | 4.40 | B/Q | 1-229 | [»] | |
4PJO | X-ray | 3.30 | B/P/b/p | 1-95 | [»] | |
4WZJ | X-ray | 3.60 | AA/AH/AO/BA/BH/BO/CA/CH/CO/DA/DH/DO | 1-95 | [»] | |
5MQF | electron microscopy | 5.90 | f/m | 1-240 | [»] | |
5O9Z | electron microscopy | 4.50 | X/f/m | 1-240 | [»] | |
5XJC | electron microscopy | 3.60 | b/i | 1-229 | [»] | |
ProteinModelPortali | P14678. | |||||
SMRi | P14678. | |||||
ModBasei | Search... | |||||
MobiDBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P14678. |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 175 – 181 | 7 | ||
Repeati | 191 – 196 | 6 | ||
Repeati | 216 – 221 | 6 | ||
Repeati | 222 – 228 | 7 | ||
Repeati | 230 – 236 | 7 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 175 – 236 | Repeat-rich regionAdd BLAST | 62 |
Sequence similaritiesi
Belongs to the snRNP SmB/SmN family.Curated
Keywords - Domaini
RepeatPhylogenomic databases
eggNOGi | KOG3168. Eukaryota. COG1958. LUCA. |
GeneTreei | ENSGT00670000098029. |
HOGENOMi | HOG000188899. |
HOVERGENi | HBG001019. |
KOi | K11086. |
OMAi | RGMGMMP. |
PhylomeDBi | P14678. |
TreeFami | TF314232. |
Family and domain databases
InterProi | View protein in InterPro IPR001163. LSM_dom_euk/arc. IPR010920. LSM_dom_sf. IPR017131. snRNP-assoc_SmB/SmN. |
Pfami | View protein in Pfam PF01423. LSM. 1 hit. |
PIRSFi | PIRSF037187. snRNP_SmB/SmN. 1 hit. |
SMARTi | View protein in SMART SM00651. Sm. 1 hit. |
SUPFAMi | SSF50182. SSF50182. 1 hit. |
s (3)i Sequence
Sequence statusi: Complete.
This entry describes 3 produced by isoformsialternative 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.
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
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
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
Sequence cautioni
The sequence AAD54488 differs from that shown. Reason: Erroneous gene model prediction.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 172 – 173 | RG → L no nucleotide entry (PubMed:2524838).Curated | 2 | |
Sequence conflicti | 201 | Missing no nucleotide entry (PubMed:2524838).Curated | 1 | |
Sequence conflicti | 217 – 218 | PP → S no nucleotide entry (PubMed:2524838).Curated | 2 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_073380 | 55 | N → S in CCMS; expression of the protein is reduced. 2 Publications | 1 | |
Natural variantiVAR_073381 | 55 | N → T in CCMS. 1 Publication | 1 | |
Natural variantiVAR_073382 | 56 | S → R in CCMS. 2 Publications | 1 | |
Natural variantiVAR_073383 | 56 | S → W in CCMS. 1 Publication | 1 | |
Natural variantiVAR_052274 | 79 | S → P. Corresponds to variant dbSNP:rs11545672Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_012221 | 227 – 228 | MR → GCEAFFDPWPQSMEVAPQRR GLDSSGPRYHRPVCFLCCCS WSLMGLSGFLT in isoform SM-B1. 1 Publication | 2 | |
Alternative sequenceiVSP_005914 | 230 – 240 | PPPPGMRPPRP → LL in isoform SM-B. 3 PublicationsAdd BLAST | 11 |
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 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. |
CCDSi | CCDS13026.1. [P14678-1] CCDS13027.1. [P14678-2] |
PIRi | S09377. |
RefSeqi | NP_003082.1. NM_003091.3. [P14678-2] NP_937859.1. NM_198216.1. [P14678-1] |
UniGenei | Hs.83753. |
Genome annotation databases
Ensembli | ENST00000381342; ENSP00000370746; ENSG00000125835. [P14678-2] ENST00000438552; ENSP00000412566; ENSG00000125835. [P14678-1] |
GeneIDi | 6628. |
KEGGi | hsa:6628. |
UCSCi | uc002wfz.2. human. [P14678-1] |
Keywords - Coding sequence diversityi
Alternative splicing, PolymorphismSimilar proteinsi
Entry informationi
Entry namei | RSMB_HUMAN | |
Accessioni | P14678Primary (citable) accession number: P14678 Secondary accession number(s): Q15490, Q6IB35, Q9UIS5 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1990 |
Last sequence update: | November 1, 1991 | |
Last modified: | March 28, 2018 | |
This is version 204 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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. |