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P14678 (RSMB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 167. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SNRPB
Synonyms:COD, SNRPB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length240 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 an 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. Ref.19

Subunit structure

U1 snRNP is for instance composed of the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in an 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. Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19

Subcellular location

Cytoplasmcytosol. Nucleus. Note: SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes. Ref.19

Post-translational modification

Methylated. Arg-108 and Arg-112 are dimethylated, probably to asymmetric dimethylarginine. Ref.10 Ref.18

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.

Sequence similarities

Belongs to the snRNP SmB/SmN family.

Sequence caution

The sequence AAD54488.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentCytoplasm
Nucleus
Spliceosome
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandRNA-binding
   Molecular functionRibonucleoprotein
   PTMMethylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

RNA splicing

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

histone mRNA metabolic process

Traceable author statement. Source: Reactome

mRNA 3'-end processing

Traceable author statement. Source: Reactome

mRNA splicing, via spliceosome

Inferred by curator Ref.14. Source: UniProtKB

ncRNA metabolic process

Traceable author statement. Source: Reactome

spliceosomal snRNP assembly

Inferred from direct assay Ref.19. Source: UniProtKB

termination of RNA polymerase II transcription

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

   Cellular_componentSMN-Sm protein complex

Inferred from direct assay Ref.19. Source: UniProtKB

U1 snRNP

Inferred from direct assay PubMed 21113136. Source: UniProtKB

U12-type spliceosomal complex

Inferred from direct assay Ref.16. Source: UniProtKB

U4 snRNP

Inferred from direct assay Ref.23. Source: UniProtKB

U7 snRNP

Inferred from direct assay Ref.12. Source: UniProtKB

catalytic step 2 spliceosome

Inferred from direct assay Ref.14. Source: UniProtKB

cytosol

Inferred from direct assay Ref.19. Source: UniProtKB

histone pre-mRNA 3'end processing complex

Inferred from electronic annotation. Source: Ensembl

methylosome

Inferred from direct assay Ref.19. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

small nuclear ribonucleoprotein complex

Traceable author statement Ref.1. Source: ProtInc

spliceosomal complex

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionhistone pre-mRNA DCP binding

Inferred from electronic annotation. Source: Ensembl

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 15494309. Source: IntAct

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform SM-B' (identifier: P14678-1)

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.
Isoform SM-B (identifier: P14678-2)

The sequence of this isoform differs from the canonical sequence as follows:
     230-240: PPPPGMRPPRP → LL
Isoform SM-B1 (identifier: P14678-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 240240Small nuclear ribonucleoprotein-associated proteins B and B'
PRO_0000125517

Regions

Repeat175 – 1817
Repeat191 – 1966
Repeat216 – 2216
Repeat222 – 2287
Repeat230 – 2367
Region175 – 23662Repeat-rich region

Amino acid modifications

Modified residue1081Omega-N-methylated arginine Ref.10
Modified residue1121Dimethylated arginine; in A2780 ovarian carcinoma cell line Ref.10
Modified residue1121Omega-N-methylated arginine Ref.10
Modified residue1471Omega-N-methylarginine Ref.10

Natural variations

Alternative sequence227 – 2282MR → GCEAFFDPWPQSMEVAPQRR GLDSSGPRYHRPVCFLCCCS WSLMGLSGFLT in isoform SM-B1.
VSP_012221
Alternative sequence230 – 24011PPPPGMRPPRP → LL in isoform SM-B.
VSP_005914
Natural variant791S → P.
Corresponds to variant rs11545672 [ dbSNP | Ensembl ].
VAR_052274

Experimental info

Sequence conflict172 – 1732RG → L Ref.4
Sequence conflict2011Missing Ref.4
Sequence conflict217 – 2182PP → S Ref.4

Secondary structure

.............. 240
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform SM-B' [UniParc].

Last modified November 1, 1991. Version 2.
Checksum: F2E1D5E11A601170

FASTA24024,610
        10         20         30         40         50         60 
MTVGKSSKML QHIDYRMRCI LQDGRIFIGT FKAFDKHMNL ILCDCDEFRK IKPKNSKQAE 

        70         80         90        100        110        120 
REEKRVLGLV LLRGENLVSM TVEGPPPKDT GIARVPLAGA AGGPGIGRAA GRGIPAGVPM 

       130        140        150        160        170        180 
PQAPAGLAGP VRGVGGPSQQ VMTPQGRGTV AAAAAAATAS IAGAPTQYPP GRGGPPPPMG 

       190        200        210        220        230        240 
RGAPPPGMMG PPPGMRPPMG PPMGIPPGRG TPMGMPPPGM RPPPPGMRGP PPPGMRPPRP 

« Hide

Isoform SM-B [UniParc].

Checksum: 5CB0BB2E75B93D4A
Show »

FASTA23123,656
Isoform SM-B1 [UniParc].

Checksum: 573E8A21414E2C22
Show »

FASTA28930,032

References

« Hide 'large scale' references
[1]"Cloned human snRNP proteins B and B' differ only in their carboxy-terminal part."
van Dam A., Winkel I., Zijlstra-Baalbergen J., Smeenk R., Cuypers H.T.
EMBO J. 8:3853-3860(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SM-B AND SM-B').
[2]"A comparison of snRNP-associated Sm-autoantigens: human N, rat N and human B/B'."
Schmauss C., McAllister G., Ohosone Y., Hardin J.A., Lerner M.R.
Nucleic Acids Res. 17:1733-1743(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SM-B).
Tissue: Thyroid carcinoma.
[3]Erratum
Schmauss C., McAllister G., Ohosone Y., Hardin J.A., Lerner M.R.
Nucleic Acids Res. 17:6777-6777(1989)
[4]"Molecular cloning of cDNA encoding Sm autoantigen: derivation of a cDNA for a B polypeptide of the U series of small nuclear ribonucleoprotein particles."
Ohosone Y., Mimori T., Griffith A., Akizuki M., Homma M., Craft J., Hardin J.A.
Proc. Natl. Acad. Sci. U.S.A. 86:4249-4253(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SM-B1).
Tissue: Fibroblast.
[5]"Concerted regulation and molecular evolution of the duplicated SNRPB'/B and SNRPN loci."
Gray T.A., Smithwick M.J., Schaldach M.A., Martone D.L., Graves J.A., McCarrey J.R., Nicholls R.D.
Nucleic Acids Res. 27:4577-4584(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SM-B').
[7]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"Epitope mapping of recombinant HeLa SmB and B' peptides obtained by the polymerase chain reaction."
Elkon K.B., Hines J.J., Chu J.-L., Parnassa A.
J. Immunol. 145:636-643(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-240 (ISOFORMS SM-B AND SM-B').
[10]Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 9-16; 19-32 AND 66-147, METHYLATION AT ARG-108; ARG-112 AND ARG-147, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[11]"The small nuclear ribonucleoproteins, SmB and B', are products of a single gene."
Chu J.-L., Elkon K.B.
Gene 97:311-312(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 209-240.
[12]"Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new 14 kDa Sm D1-like protein."
Pillai R.S., Will C.L., Luehrmann R., Schuemperli D., Mueller B.
EMBO J. 20:5470-5479(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE U7 SNRNP COMPLEX.
[13]"SMN, the spinal muscular atrophy protein, forms a pre-import snRNP complex with snurportin1 and importin beta."
Narayanan U., Ospina J.K., Frey M.R., Hebert M.D., Matera A.G.
Hum. Mol. Genet. 11:1785-1795(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DDX20; SNUPN AND SMN1.
[14]"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[15]"Unique Sm core structure of U7 snRNPs: assembly by a specialized SMN complex and the role of a new component, Lsm11, in histone RNA processing."
Pillai R.S., Grimmler M., Meister G., Will C.L., Luehrmann R., Fischer U., Schuemperli D.
Genes Dev. 17:2321-2333(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LSM11.
Tissue: Cervix carcinoma.
[16]"The human 18S U11/U12 snRNP contains a set of novel proteins not found in the U2-dependent spliceosome."
Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R., Elbashir S., Tuschl T., Luehrmann R.
RNA 10:929-941(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH THE U11/U12 SPLICEOSOME, IDENTIFICATION BY MASS SPECTROMETRY.
[17]"Tudor domains bind symmetrical dimethylated arginines."
Cote J., Richard S.
J. Biol. Chem. 280:28476-28483(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TDRD3.
[18]"Toward an assembly line for U7 snRNPs: interactions of U7-specific Lsm proteins with PRMT5 and SMN complexes."
Azzouz T.N., Pillai R.S., Dapp C., Chari A., Meister G., Kambach C., Fischer U., Schuemperli D.
J. Biol. Chem. 280:34435-34440(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CLNS1A AND SMN, METHYLATION.
[19]"An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs."
Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B., Englbrecht C., Sickmann A., Stark H., Fischer U.
Cell 135:497-509(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN SNRNP BIOGENESIS, IDENTIFICATION IN 6S PICLN-SM COMPLEX, IDENTIFICATION IN SMN-SM COMPLEX, SUBCELLULAR LOCATION.
[20]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs."
Kambach C., Walke S., Young R., Avis J.M., de la Fortelle E., Raker V.A., Luehrmann R., Li J., Nagai K.
Cell 96:375-387(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[22]"Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution."
Pomeranz Krummel D.A., Oubridge C., Leung A.K., Li J., Nagai K.
Nature 458:475-480(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (5.49 ANGSTROMS) OF 1-174 IN SPLICEOSOMAL U1 SNRNP.
[23]"Structure of the spliceosomal U4 snRNP core domain and its implication for snRNP biogenesis."
Leung A.K., Nagai K., Li J.
Nature 473:536-539(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 1-95 IN SPLICEOSOMAL CORE U4 SNRNP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X17567 mRNA. Translation: CAB57867.1.
X17568 mRNA. Translation: CAB57868.1.
X15893 mRNA. Translation: CAA33902.1.
AF134825 expand/collapse EMBL AC list , 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.
CCDSCCDS13026.1. [P14678-1]
CCDS13027.1. [P14678-2]
PIRS09377.
RefSeqNP_003082.1. NM_003091.3. [P14678-2]
NP_937859.1. NM_198216.1. [P14678-1]
UniGeneHs.83753.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D3BX-ray2.00B/D/F/H/J/L1-91[»]
2Y9AX-ray3.60A/H/O1-95[»]
2Y9BX-ray3.60A/H/O1-95[»]
2Y9CX-ray3.60A/H/O1-95[»]
2Y9DX-ray3.60A/H/O1-95[»]
3CW1X-ray5.49A/H/I/J1-174[»]
3PGWX-ray4.40B/Q1-229[»]
ProteinModelPortalP14678.
SMRP14678. Positions 1-95.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112512. 80 interactions.
DIPDIP-31239N.
IntActP14678. 43 interactions.
MINTMINT-124876.
STRING9606.ENSP00000412566.

PTM databases

PhosphoSiteP14678.

Polymorphism databases

DMDM134037.

Proteomic databases

MaxQBP14678.
PaxDbP14678.
PRIDEP14678.

Protocols and materials databases

DNASU6628.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000381342; ENSP00000370746; ENSG00000125835. [P14678-2]
ENST00000438552; ENSP00000412566; ENSG00000125835. [P14678-1]
GeneID6628.
KEGGhsa:6628.
UCSCuc002wfz.1. human. [P14678-1]

Organism-specific databases

CTD6628.
GeneCardsGC20M002442.
HGNCHGNC:11153. SNRPB.
HPACAB009610.
HPA003482.
MIM182282. gene.
neXtProtNX_P14678.
PharmGKBPA35995.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1958.
HOGENOMHOG000188899.
HOVERGENHBG001019.
KOK11086.
OMAKNNKMIQ.
OrthoDBEOG7J70HT.
PhylomeDBP14678.
TreeFamTF314232.

Enzyme and pathway databases

ReactomeREACT_1788. Transcription.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpressP14678.
BgeeP14678.
CleanExHS_SNRPB.
GenevestigatorP14678.

Family and domain databases

InterProIPR010920. LSM_dom.
IPR001163. Ribonucl_LSM.
IPR006649. Ribonucl_LSM_euk/arc.
IPR017131. snRNP-assoc_SmB/SmN.
[Graphical view]
PfamPF01423. LSM. 1 hit.
[Graphical view]
PIRSFPIRSF037187. snRNP_SmB/SmN. 1 hit.
SMARTSM00651. Sm. 1 hit.
[Graphical view]
SUPFAMSSF50182. SSF50182. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSNRPB. human.
EvolutionaryTraceP14678.
GeneWikiSNRPB.
GenomeRNAi6628.
NextBio25817.
PROP14678.
SOURCESearch...

Entry information

Entry nameRSMB_HUMAN
AccessionPrimary (citable) accession number: P14678
Secondary accession number(s): Q15490, Q6IB35, Q9UIS5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1991
Last modified: July 9, 2014
This is version 167 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM