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Protein

U2 small nuclear ribonucleoprotein B''

Gene

SNRPB2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. nucleotide binding Source: InterPro
  2. snRNA binding Source: InterPro

GO - Biological processi

  1. gene expression Source: Reactome
  2. mRNA processing Source: ProtInc
  3. mRNA splicing, via spliceosome Source: UniProtKB
  4. RNA splicing Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
U2 small nuclear ribonucleoprotein B''
Short name:
U2 snRNP B''
Gene namesi
Name:SNRPB2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:11155. SNRPB2.

Subcellular locationi

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. nucleolus Source: HPA
  3. nucleoplasm Source: HPA
  4. spliceosomal complex Source: HGNC
  5. U2 snRNP Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35996.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 225225U2 small nuclear ribonucleoprotein B''PRO_0000081892Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei111 – 1111N6-acetyllysineBy similarity
Modified residuei151 – 1511Phosphotyrosine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP08579.
PaxDbiP08579.
PeptideAtlasiP08579.
PRIDEiP08579.

PTM databases

PhosphoSiteiP08579.

Expressioni

Gene expression databases

BgeeiP08579.
CleanExiHS_SNRPB2.
GenevestigatoriP08579.

Interactioni

Subunit structurei

Identified in the spliceosome C complex. Present in a spliceosome complex assembled in vitro, and composed of SNRPB2, HPRP8BP and CRNKL1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SNRPA1P096612EBI-1053651,EBI-876439

Protein-protein interaction databases

BioGridi112513. 54 interactions.
IntActiP08579. 12 interactions.
MINTiMINT-156501.
STRINGi9606.ENSP00000246071.

Structurei

Secondary structure

1
225
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 137Combined sources
Helixi20 – 3213Combined sources
Beta strandi37 – 415Combined sources
Turni46 – 505Combined sources
Beta strandi52 – 587Combined sources
Helixi59 – 6810Combined sources
Beta strandi80 – 834Combined sources
Helixi89 – 957Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A9NX-ray2.38B/D1-96[»]
ProteinModelPortaliP08579.
SMRiP08579. Positions 3-96, 146-225.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08579.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 8680RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini151 – 22575RRM 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the RRM U1 A/B'' family.Curated
Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG317159.
GeneTreeiENSGT00390000007046.
HOGENOMiHOG000217519.
HOVERGENiHBG000895.
KOiK11094.
OMAiIMDIRPN.
OrthoDBiEOG77DJ77.
PhylomeDBiP08579.
TreeFamiTF313834.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR024888. U1_snRNP_A/U2_snRNP_B''.
[Graphical view]
PANTHERiPTHR10501. PTHR10501. 1 hit.
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P08579-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDIRPNHTIY INNMNDKIKK EELKRSLYAL FSQFGHVVDI VALKTMKMRG
60 70 80 90 100
QAFVIFKELG SSTNALRQLQ GFPFYGKPMR IQYAKTDSDI ISKMRGTFAD
110 120 130 140 150
KEKKKEKKKA KTVEQTATTT NKKPGQGTPN SANTQGNSTP NPQVPDYPPN
160 170 180 190 200
YILFLNNLPE ETNEMMLSML FNQFPGFKEV RLVPGRHDIA FVEFENDGQA
210 220
GAARDALQGF KITPSHAMKI TYAKK
Length:225
Mass (Da):25,486
Last modified:August 1, 1988 - v1
Checksum:i67C949CC7E14A92A
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti19 – 191K → Q in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035487

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13123.1.
PIRiA25910.
RefSeqiNP_003083.1. NM_003092.4.
NP_937863.1. NM_198220.2.
UniGeneiHs.280378.

Genome annotation databases

EnsembliENST00000246071; ENSP00000246071; ENSG00000125870.
ENST00000377943; ENSP00000367178; ENSG00000125870.
GeneIDi6629.
KEGGihsa:6629.
UCSCiuc002wph.2. human.

Polymorphism databases

DMDMi134095.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13123.1.
PIRiA25910.
RefSeqiNP_003083.1. NM_003092.4.
NP_937863.1. NM_198220.2.
UniGeneiHs.280378.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A9NX-ray2.38B/D1-96[»]
ProteinModelPortaliP08579.
SMRiP08579. Positions 3-96, 146-225.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112513. 54 interactions.
IntActiP08579. 12 interactions.
MINTiMINT-156501.
STRINGi9606.ENSP00000246071.

PTM databases

PhosphoSiteiP08579.

Polymorphism databases

DMDMi134095.

Proteomic databases

MaxQBiP08579.
PaxDbiP08579.
PeptideAtlasiP08579.
PRIDEiP08579.

Protocols and materials databases

DNASUi6629.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000246071; ENSP00000246071; ENSG00000125870.
ENST00000377943; ENSP00000367178; ENSG00000125870.
GeneIDi6629.
KEGGihsa:6629.
UCSCiuc002wph.2. human.

Organism-specific databases

CTDi6629.
GeneCardsiGC20P016658.
HGNCiHGNC:11155. SNRPB2.
MIMi603520. gene.
neXtProtiNX_P08579.
PharmGKBiPA35996.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG317159.
GeneTreeiENSGT00390000007046.
HOGENOMiHOG000217519.
HOVERGENiHBG000895.
KOiK11094.
OMAiIMDIRPN.
OrthoDBiEOG77DJ77.
PhylomeDBiP08579.
TreeFamiTF313834.

Enzyme and pathway databases

ReactomeiREACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSiSNRPB2. human.
EvolutionaryTraceiP08579.
GeneWikiiSNRPB2.
GenomeRNAii6629.
NextBioi25823.
PROiP08579.
SOURCEiSearch...

Gene expression databases

BgeeiP08579.
CleanExiHS_SNRPB2.
GenevestigatoriP08579.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR024888. U1_snRNP_A/U2_snRNP_B''.
[Graphical view]
PANTHERiPTHR10501. PTHR10501. 1 hit.
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-19.

Entry informationi

Entry nameiRU2B_HUMAN
AccessioniPrimary (citable) accession number: P08579
Secondary accession number(s): B2R7J3, D3DW21, Q9UJD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: March 4, 2015
This is version 161 of the entry and version 1 of the sequence. [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

Miscellaneous

Patients with systemic lupus erythematosus produce antibodies which interact with snRNP proteins.

Keywords - Technical termi

3D-structure, Complete proteome, 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

External Data

Dasty 3

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 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.