P14678 (RSMB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	SNRPB
Synonyms:	COD, SNRPB1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	240 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › cytosol. 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 process	mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus Spliceosome
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	RNA-binding
Molecular function	Ribonucleoprotein
PTM	Methylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	RNA 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_component	SMN-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_function	histone pre-mRNA DCP binding Inferred from electronic annotation. Source: Ensembl poly(A) RNA binding Inferred from direct assay PubMed 22681889. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CLNS1A	P54105	3	EBI-372458,EBI-724693
SMN2	Q16637-3	3	EBI-372471,EBI-395447
SNRPD3	P62318	2	EBI-372458,EBI-372789

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 240

240

Small nuclear ribonucleoprotein-associated proteins B and B'

PRO_0000125517

Regions

Repeat

175 – 181

7

Repeat

191 – 196

6

Repeat

216 – 221

6

Repeat

222 – 228

7

Repeat

230 – 236

7

Region

175 – 236

62

Repeat-rich region

Amino acid modifications

Modified residue

108

1

Omega-N-methylated arginine Ref.10

Modified residue

112

1

Dimethylated arginine; in A2780 ovarian carcinoma cell line Ref.10

Modified residue

112

1

Omega-N-methylated arginine Ref.10

Modified residue

147

1

Omega-N-methylarginine Ref.10

Natural variations

Alternative sequence

227 – 228

2

MR → GCEAFFDPWPQSMEVAPQRR GLDSSGPRYHRPVCFLCCCS WSLMGLSGFLT in isoform SM-B1.

VSP_012221

Alternative sequence

230 – 240

11

PPPPGMRPPRP → LL in isoform SM-B.

VSP_005914

Natural variant

79

1

S → P.
Corresponds to variant rs11545672 [ dbSNP | Ensembl ].

VAR_052274

Experimental info

Sequence conflict

172 – 173

2

RG → L Ref.4

Sequence conflict

201

1

Missing Ref.4

Sequence conflict

217 – 218

2

PP → S Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

240

Helix Strand Turn

Details...

Helix

10 – 12

3

Beta strand

15 – 21

7

Beta strand

26 – 33

8

Beta strand

40 – 51

12

Beta strand

61 – 72

12

Helix

74 – 76

3

Beta strand

77 – 84

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform SM-B' [UniParc]. Last modified November 1, 1991. Version 2. Checksum: F2E1D5E11A601170	FASTA	240	24,610
	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
	Isoform SM-B [UniParc]. Checksum: 5CB0BB2E75B93D4A	FASTA	231	23,656
	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 RGAPPPGMMG PPPGMRPPMG PPMGIPPGRG TPMGMPPPGM RPPPPGMRGL L
	Isoform SM-B1 [UniParc]. Checksum: 573E8A21414E2C22	FASTA	289	30,032
	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 RPPPPGGCEA FFDPWPQSME 250 260 270 280 VAPQRRGLDS SGPRYHRPVC FLCCCSWSLM GLSGFLTGPP PPGMRPPRP

References

	« Hide 'large scale' referencesShow '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. , 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. , 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 , 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.

PIR

S09377.

RefSeq

NP_003082.1. NM_003091.3.
NP_937859.1. NM_198216.1.

UniGene

Hs.83753.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D3B	X-ray	2.00	B/D/F/H/J/L	1-91	[»]
2Y9A	X-ray	3.60	A/H/O	1-95	[»]
2Y9B	X-ray	3.60	A/H/O	1-95	[»]
2Y9C	X-ray	3.60	A/H/O	1-95	[»]
2Y9D	X-ray	3.60	A/H/O	1-95	[»]
3CW1	X-ray	5.49	A/H/I/J	1-174	[»]
3PGW	X-ray	4.40	B/Q	1-229	[»]

ProteinModelPortal

P14678.

SMR

P14678. Positions 1-95.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

112512. 77 interactions.

DIP

DIP-31239N.

IntAct

P14678. 43 interactions.

MINT

MINT-124876.

STRING

9606.ENSP00000412566.

PTM databases

PhosphoSite

P14678.

Polymorphism databases

DMDM

134037.

Proteomic databases

PaxDb

P14678.

PRIDE

P14678.

Protocols and materials databases

DNASU

6628.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000381342; ENSP00000370746; ENSG00000125835. [P14678-2]
ENST00000438552; ENSP00000412566; ENSG00000125835. [P14678-1]

GeneID

6628.

KEGG

hsa:6628.

UCSC

uc002wfz.1. human. [P14678-1]

Organism-specific databases

CTD

6628.

GeneCards

GC20M002442.

HGNC

HGNC:11153. SNRPB.

HPA

CAB009610.
HPA003482.

MIM

182282. gene.

neXtProt

NX_P14678.

PharmGKB

PA35995.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1958.

HOGENOM

HOG000188899.

HOVERGEN

HBG001019.

KO

K11086.

OMA

KNNKMIQ.

OrthoDB

EOG7J70HT.

PhylomeDB

P14678.

TreeFam

TF314232.

Enzyme and pathway databases

Reactome

REACT_1788. Transcription.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpress

P14678.

Bgee

P14678.

CleanEx

HS_SNRPB.

Genevestigator

P14678.

Family and domain databases

InterPro

IPR010920. LSM_dom.
IPR001163. Ribonucl_LSM.
IPR006649. Ribonucl_LSM_euk/arc.
IPR017131. snRNP-assoc_SmB/SmN.
[Graphical view]

Pfam

PF01423. LSM. 1 hit.
[Graphical view]

PIRSF

PIRSF037187. snRNP_SmB/SmN. 1 hit.

SMART

SM00651. Sm. 1 hit.
[Graphical view]

SUPFAM

SSF50182. SSF50182. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

SNRPB. human.

EvolutionaryTrace

P14678.

GeneWiki

SNRPB.

GenomeRNAi

6628.

NextBio

25817.

PRO

P14678.

SOURCE

Search...

Entry information

Entry name

RSMB_HUMAN

Accession

Primary (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:	April 16, 2014
This is version 164 of the entry and version 2 of the sequence. [Complete history]

Entry status

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.