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P09661 (RU2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
U2 small nuclear ribonucleoprotein A'

Short name=U2 snRNP A'
Gene names
Name:SNRPA1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length255 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein is associated with sn-RNP U2. It helps the A' protein to bind stem loop IV of U2 snRNA.

Subunit structure

Identified in the spliceosome C complex. 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. Ref.6 Ref.7 Ref.8

Subcellular location

Nucleus.

Sequence similarities

Belongs to the U2 small nuclear ribonucleoprotein A family.

Contains 4 LRR (leucine-rich) repeats.

Contains 1 LRRCT domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SNRPB2P085792EBI-876439,EBI-1053651

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 255254U2 small nuclear ribonucleoprotein A'
PRO_0000074173

Regions

Repeat20 – 4122LRR 1
Repeat43 – 6422LRR 2
Repeat65 – 8622LRR 3
Repeat89 – 11022LRR 4
Domain123 – 16139LRRCT

Amino acid modifications

Modified residue1721N6-acetyllysine Ref.12
Modified residue1781Phosphoserine Ref.9
Modified residue1971Phosphoserine Ref.10 Ref.11 Ref.13

Natural variations

Natural variant2341R → H.
Corresponds to variant rs1050843 [ dbSNP | Ensembl ].
VAR_052030

Experimental info

Sequence conflict1931K → R in CAA31838. Ref.1

Secondary structure

............................. 255
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09661 [UniParc].

Last modified May 23, 2003. Version 2.
Checksum: 25902F07992B7209

FASTA25528,416
        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 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of the cDNA for the human U2 snRNA-specific A' protein."
Sillekens P.T.G., Beijer R.P., Habets W.J., van Venrooij W.J.
Nucleic Acids Res. 17:1893-1906(1989) [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. expand/collapse author list , 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: Skeletal muscle.
[3]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: Muscle and Urinary bladder.
[5]Bienvenut W.V., Heiserich L., Gottlieb E.
Submitted (MAR-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-20; 114-122; 133-143 AND 222-232, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Colon carcinoma.
[6]"A coactivator of pre-mRNA splicing."
Blencowe B.J., Issner R., Nickerson J.A., Sharp P.A.
Genes Dev. 12:996-1009(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNA SPLICING COMPLEX WITH SFRS4; SFRS5; SNRNP70; SRRM1 AND SRRM2.
[7]"The SRm160/300 splicing coactivator is required for exon-enhancer function."
Eldridge A.G., Li Y., Sharp P.A., Blencowe B.J.
Proc. Natl. Acad. Sci. U.S.A. 96:6125-6130(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNA EXONIC SPLICING ENHANCER (ESE) COMPLEX WITH SNRNP70; SRRM1 AND TRA2B.
[8]"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.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-172, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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].
[15]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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 1-176.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X13482 mRNA. Translation: CAA31838.1.
AK312200 mRNA. Translation: BAG35133.1.
CH471101 Genomic DNA. Translation: EAX02300.1.
BC022816 mRNA. Translation: AAH22816.1.
BC071717 mRNA. Translation: AAH71717.1.
PIRS03616.
RefSeqNP_003081.2. NM_003090.2.
UniGeneHs.528763.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A9NX-ray2.38A/C1-176[»]
ProteinModelPortalP09661.
SMRP09661. Positions 2-175.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112511. 89 interactions.
DIPDIP-625N.
IntActP09661. 13 interactions.
MINTMINT-3007227.
STRING9606.ENSP00000254193.

PTM databases

PhosphoSiteP09661.

Polymorphism databases

DMDM31077165.

Proteomic databases

PaxDbP09661.
PeptideAtlasP09661.
PRIDEP09661.

Protocols and materials databases

DNASU6627.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000254193; ENSP00000254193; ENSG00000131876.
GeneID6627.
KEGGhsa:6627.
UCSCuc002bww.3. human.

Organism-specific databases

CTD6627.
GeneCardsGC15M101821.
H-InvDBHIX0203213.
HGNCHGNC:11152. SNRPA1.
HPAHPA045622.
HPA048499.
MIM603521. gene.
neXtProtNX_P09661.
PharmGKBPA35994.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4886.
HOGENOMHOG000175472.
HOVERGENHBG007330.
InParanoidP09661.
KOK11092.
OMASMQYINP.
OrthoDBEOG7966HF.
PhylomeDBP09661.
TreeFamTF313776.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

BgeeP09661.
CleanExHS_SNRPA1.
GenevestigatorP09661.

Family and domain databases

InterProIPR001611. Leu-rich_rpt.
IPR003603. U2A'_phosphoprotein32A_C.
[Graphical view]
SMARTSM00446. LRRcap. 1 hit.
[Graphical view]
PROSITEPS51450. LRR. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP09661.
GeneWikiSNRPA1.
GenomeRNAi6627.
NextBio25813.
PROP09661.
SOURCESearch...

Entry information

Entry nameRU2A_HUMAN
AccessionPrimary (citable) accession number: P09661
Secondary accession number(s): B2R5I6, Q8TBD2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: May 23, 2003
Last modified: April 16, 2014
This is version 144 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 15

Human chromosome 15: entries, gene names and cross-references to MIM