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UniProtKB/Swiss-Prot entry P09661


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RU2A_HUMAN
Primary accession number P09661
Secondary accession number Q8TBD2
Integrated into Swiss-Prot on July 1, 1989
Sequence was last modified on May 23, 2003 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 95)
Name and origin of the protein
Protein name U2 small nuclear ribonucleoprotein A'
Synonym U2 snRNP-A'
Gene name
Name: SNRPA1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1093/nar/17.5.1893; PubMed=2928112 [NCBI, ExPASy, EBI, Israel, Japan]
Sillekens P.T.G., Beijer R.P., Habets W.J., van Venrooij W.J.;
"Molecular cloning of the cDNA for the human U2 snRNA-specific A' protein.";
Nucleic Acids Res. 17:1893-1906(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle, and Urinary bladder;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 2-20; 114-122; 133-143 AND 222-232, CLEAVAGE OF INITIATOR METHIONINE, AND MASS SPECTROMETRY.
TISSUE=Colon carcinoma;
Bienvenut W.V., Heiserich L., Gottlieb E.;
Submitted (MAR-2008) to UniProtKB.
[4]
IDENTIFICATION IN A MRNA SPLICING COMPLEX WITH SFRS4; SFRS5; SNRNP70; SRRM1 AND SRRM2.
PubMed=9531537 [NCBI, ExPASy, EBI, Israel, Japan]
Blencowe B.J., Issner R., Nickerson J.A., Sharp P.A.;
"A coactivator of pre-mRNA splicing.";
Genes Dev. 12:996-1009(1998).
[5]
IDENTIFICATION IN A MRNA EXONIC SPLICING ENHANCER (ESE) COMPLEX WITH SNRNP70; SRRM1 AND TRA2B.
DOI=10.1073/pnas.96.11.6125; PubMed=10339552 [NCBI, ExPASy, EBI, Israel, Japan]
Eldridge A.G., Li Y., Sharp P.A., Blencowe B.J.;
"The SRm160/300 splicing coactivator is required for exon-enhancer function.";
Proc. Natl. Acad. Sci. U.S.A. 96:6125-6130(1999).
[6]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPICEOSOMAL C COMPLEX.
DOI=10.1017/S1355838202021088; PubMed=11991638 [NCBI, ExPASy, EBI, Israel, Japan]
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.";
RNA 8:426-439(2002).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[10]
X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 1-176.
DOI=10.1038/29234; PubMed=9716128 [NCBI, ExPASy, EBI, Israel, Japan]
Price S.R., Evans P.R., Nagai K.;
"Crystal structure of the spliceosomal U2B'-U2A' protein complex bound to a fragment of U2 small nuclear RNA.";
Nature 394:645-650(1998).
Comments
  • FUNCTION: This protein is associated with sn-RNP U2. It helps the A' protein to bind stem loop IV of U2 snRNA.
  • SUBUNIT: Identified in the spliceosome C complex, at least composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23, DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1, GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRPH1, HNRPK, HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2, SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8. Found in a pre-mRNA splicing complex with SFRS4, SFRS5, SNRNP70, SNRPA1, SRRM1 and SRRM2. Found in a pre-mRNA exonic splicing enhancer (ESE) complex with SNRNP70, SNRPA1, SRRM1 and TRA2B.
  • INTERACTION:
    P20823:HNF1A; NbExp=1; IntAct=EBI-876439, EBI-636034;
  • SUBCELLULAR LOCATION: Nucleus.
  • SIMILARITY: Belongs to the U2 small nuclear ribonucleoprotein A family.
  • SIMILARITY: Contains 3 LRR (leucine-rich) repeats.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X13482; CAA31838.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC022816; AAH22816.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC071717; AAH71717.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00297477; -.
PIR S03616; S03616.
RefSeq NP_003081.2; -.
UniGene Hs.528763
3D structure databases
PDB
1A9N; X-ray; 2.38 A; A/C=1-176.[ExPASy / RCSB / EBI]
PDBsum 1A9N; -.
ModBase P09661.
Protein-protein interaction databases
DIP DIP:625N; -.
IntAct P09661; 11.
PTM databases
PhosphoSite P09661; -.
Enzyme and pathway databases
Reactome REACT_1675; mRNA Processing.
REACT_71; Gene Expression.
Organism-specific databases
GeneCards GC15M099639; -.
H-InvDB HIX0012630; -.
HIX0041327; -.
HGNC HGNC:11152; SNRPA1.
GenAtlas SNRPA1.
MIM 603521; gene. [NCBI / EBI]
PharmGKB PA35994; -.
Gene expression databases
Bgee P09661; -.
CleanEx HS_SNRPA1; -.
GermOnline ENSG00000131876; Homo sapiens.
Ontologies
GO
GO:0005686; Cellular component: snRNP U2 (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0003723; Molecular function: RNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0000398; Biological process: nuclear mRNA splicing, via spliceosome (inferred by curator from HGNC).
QuickGo view.
Family and domain databases
InterPro IPR003603; U2A'_phosphoprotein32A_C.
Graphical view of domain structure.
SMART SM00446; LRRcap; 1.
SMART graphical view of domain structure.
Proteomic databases
PeptideAtlas P09661; -.
PRIDE P09661; -.
Genome annotation databases
Ensembl ENSG00000131876; Homo sapiens. [Contig view]
GeneID 6627; -.
KEGG hsa:6627; -.
Phylogenomic databases
HOGENOM P09661; -.
HOVERGEN P09661; -.
OMA P09661; TADLIWK.
Other
NextBio 25813; -.
SOURCE SNRPA1; Homo sapiens.
ProtoNet P09661.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Leucine-rich repeat; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism; Repeat; Ribonucleoprotein; RNA-binding; Spliceosome.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   255  254     U2 small nuclear ribonucleoprotein A'. PRO_0000074173
REPEAT   41    63  23     LRR 1. 
REPEAT   64    86  23     LRR 2. 
REPEAT   88   111  24     LRR 3. 
MOD_RES   197   197        Phosphoserine. 
VARIANT   234   234  1     R -> H (in dbSNP:rs1050843 [NCBI]). VAR_052030 
CONFLICT   193   193        K -> R (in Ref. 1; CAA31838). 
HELIX   6    10  5      
STRAND   14    16  3      
STRAND   22    25  4      
HELIX   37    40  4      
STRAND   45    48  4      
STRAND   68    70  3      
HELIX   83    86  4      
STRAND   92    94  3      
HELIX   103   111  9      
STRAND   117   119  3      
HELIX   124   127  4      
HELIX   131   138  8      
STRAND   143   145  3      
HELIX   152   160  9      
HELIX   165   172  8      
Sequence information
Length: 255 AA [This is the length of the unprocessed precursor] Molecular weight: 28416 Da [This is the MW of the unprocessed precursor] CRC64: 25902F07992B7209 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVKLTAELIE QAAQYTNAVR DRELDLRGYK IPVIENLGAT LDQFDAIDFS DNEIRKLDGF 

        70         80         90        100        110        120 
PLLRRLKTLL VNNNRICRIG EGLDQALPCL TELILTNNSL VELGDLDPLA SLKSLTYLSI 

       130        140        150        160        170        180 
LRNPVTNKKH YRLYVIYKVP QVRVLDFQKV KLKERQEAEK MFKGKRGAQL AKDIARRSKT 

       190        200        210        220        230        240 
FNPGAGLPTD KKKGGPSPGD VEAIKNAIAN ASTLAEVERL KGLLQSGQIP GRERRSGPTD 

       250 
DGEEEMEEDT VTNGS 

P09661 in FASTA format

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