P08579 (RU2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
U2 small nuclear ribonucleoprotein B''
Short name=U2 snRNP B''

Gene names

Name:

SNRPB2

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 › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	225 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in pre-mRNA splicing. This protein is associated with snRNP U2. It binds stem loop IV of U2 snRNA only in presence of the U2A' protein.
Subunit structure	Identified in the spliceosome C complex. Present in a spliceosome complex assembled in vitro, and composed of SNRPB2, HPRP8BP and CRNKL1. Ref.6 Ref.7
Subcellular location	Nucleus.
Miscellaneous	Patients with systemic lupus erythematosus produce antibodies which interact with snRNP proteins.
Sequence similarities	Belongs to the RRM U1 A/B'' family. Contains 2 RRM (RNA recognition motif) domains.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Nucleus Spliceosome
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	RNA-binding
Molecular function	Ribonucleoprotein
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mRNA splicing, via spliceosome Inferred by curator Ref.7. Source: UniProtKB
Cellular_component	U2 snRNP Traceable author statement Ref.1. Source: ProtInc catalytic step 2 spliceosome Inferred from direct assay Ref.7. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	nucleotide binding Inferred from electronic annotation. Source: InterPro snRNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 225

225

U2 small nuclear ribonucleoprotein B''

PRO_0000081892

Regions

Domain

7 – 86

80

RRM 1

Domain

151 – 225

75

RRM 2

Amino acid modifications

Modified residue

151

1

Phosphotyrosine Ref.8

Natural variations

Natural variant

19

1

K → Q in a colorectal cancer sample; somatic mutation. Ref.11

VAR_035487

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

225

Helix Strand Turn

Details...

Beta strand

7 – 13

7

Helix

20 – 32

13

Beta strand

37 – 41

5

Turn

46 – 50

5

Beta strand

52 – 58

7

Helix

59 – 68

10

Beta strand

80 – 83

4

Helix

89 – 95

7

Sequences

	Sequence		Length	Mass (Da)
	P08579 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: 67C949CC7E14A92A	FASTA	225	25,486
	10 20 30 40 50 60 MDIRPNHTIY INNMNDKIKK EELKRSLYAL FSQFGHVVDI VALKTMKMRG QAFVIFKELG 70 80 90 100 110 120 SSTNALRQLQ GFPFYGKPMR IQYAKTDSDI ISKMRGTFAD KEKKKEKKKA KTVEQTATTT 130 140 150 160 170 180 NKKPGQGTPN SANTQGNSTP NPQVPDYPPN YILFLNNLPE ETNEMMLSML FNQFPGFKEV 190 200 210 220 RLVPGRHDIA FVEFENDGQA GAARDALQGF KITPSHAMKI TYAKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of a cDNA clone expressing a human autoimmune antigen: full-length sequence of the U2 small nuclear RNA-associated B' antigen." Habets W.J., Sillekens P.T.G., Hoet M.H., Schalken J.A., Roebroek A.J.M., Leunissen J.A.M., de Ven W.J.M., van Venrooij W.J. Proc. Natl. Acad. Sci. U.S.A. 84:2421-2425(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cerebellum.
[3]	"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].
[4]	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].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Uterus.
[6]	"Crooked neck is a component of the human spliceosome and implicated in the splicing process." Chung S., Zhou Z., Huddleston K.A., Harrison D.A., Reed R., Coleman T.A., Rymond B.C. Biochim. Biophys. Acta 1576:287-297(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN SPLICEOSOMAL COMPLEX WITH HPRP8BP AND CRNKL1.
[7]	"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.
[8]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-151, MASS SPECTROMETRY.
[9]	"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].
[10]	"Crystal structure of the spliceosomal U2B'-U2A' protein complex bound to a fragment of U2 small nuclear RNA." Price S.R., Evans P.R., Nagai K. Nature 394:645-650(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 1-96.
[11]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-19.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M15841 mRNA. Translation: AAA36796.1.
AK313004 mRNA. Translation: BAG35840.1.
AL034428 Genomic DNA. Translation: CAB38777.2.
CH471133 Genomic DNA. Translation: EAX10284.1.
CH471133 Genomic DNA. Translation: EAX10285.1.
BC018022 mRNA. Translation: AAH18022.1.
BC036737 mRNA. Translation: AAH36737.1.

IPI

IPI00029267.

PIR

A25910.

RefSeq

NP_003083.1. NM_003092.4.
NP_937863.1. NM_198220.2.

UniGene

Hs.280378.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A9N	X-ray	2.38	B/D	1-96	[»]

ProteinModelPortal

P08579.

ModBase

Search...

Protein-protein interaction databases

IntAct

P08579. 6 interactions.

MINT

MINT-156501.

STRING

9606.ENSP00000246071.

PTM databases

PhosphoSite

P08579.

Polymorphism databases

DMDM

134095.

Proteomic databases

PaxDb

P08579.

PeptideAtlas

P08579.

PRIDE

P08579.

Protocols and materials databases

DNASU

6629.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000246071; ENSP00000246071; ENSG00000125870.
ENST00000377943; ENSP00000367178; ENSG00000125870.

GeneID

6629.

KEGG

hsa:6629.

UCSC

uc002wph.2. human.

Organism-specific databases

CTD

6629.

GeneCards

GC20P016658.

HGNC

HGNC:11155. SNRPB2.

MIM

603520. gene.

neXtProt

NX_P08579.

PharmGKB

PA35996.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG317159.

HOGENOM

HOG000217519.

HOVERGEN

HBG000895.

InParanoid

P08579.

KO

K11094.

OMA

TTANKKP.

OrthoDB

EOG4H72CH.

PhylomeDB

P08579.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_71. Gene Expression.

Gene expression databases

Bgee

P08579.

CleanEx

HS_SNRPB2.

Genevestigator

P08579.

GermOnline

ENSG00000125870. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 2 hits.

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR024888. U1_snRNP_A/U2_snRNP_B''.
[Graphical view]

PANTHER

PTHR10501. PTHR10501. 1 hit.

Pfam

PF00076. RRM_1. 1 hit.
[Graphical view]

SMART

SM00360. RRM. 2 hits.
[Graphical view]

PROSITE

PS50102. RRM. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P08579.

GenomeRNAi

6629.

NextBio

25823.

SOURCE

Search...

Entry information

Entry name

RU2B_HUMAN

Accession

Primary (citable) accession number: P08579
Secondary accession number(s): B2R7J3, D3DW21, Q9UJD4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	May 1, 2013
This is version 144 of the entry and version 1 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.