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P09012 (SNRPA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 175. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
U1 small nuclear ribonucleoprotein A

Short name=U1 snRNP A
Short name=U1-A
Short name=U1A
Gene names
Name:SNRPA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length282 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. U1 snRNP is the first snRNP to interact with pre-mRNA. This interaction is required for the subsequent binding of U2 snRNP and the U4/U6/U5 tri-snRNP. SNRPA binds stem loop II of U1 snRNA. In a snRNP-free form (SF-A) may be involved in coupled pre-mRNA splicing and polyadenylation process. May bind preferentially to the 5'-UGCAC-3' motif on RNAs. Ref.5

Subunit structure

U1 snRNP is 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. Interacts with SFPQ; component of a snRNP-free complex with SFPQ. Ref.5

Subcellular location

Nucleus.

Sequence similarities

Belongs to the RRM U1 A/B'' family.

Contains 2 RRM (RNA recognition motif) domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SFPQP232464EBI-607085,EBI-355453
U2AF2P263682EBI-607085,EBI-742339

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 282281U1 small nuclear ribonucleoprotein A
PRO_0000081887

Regions

Domain10 – 8980RRM 1
Domain208 – 28275RRM 2
Compositional bias140 – 20667Pro-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.4 Ref.7
Modified residue601N6-acetyllysine Ref.9
Modified residue1311Phosphothreonine Ref.6 Ref.10

Experimental info

Mutagenesis111T → V: Abolishes RNA binding.
Mutagenesis131Y → F: Substantially reduces RNA binding.
Mutagenesis151N → V: Abolishes RNA binding.
Mutagenesis161N → V: Substantially reduces RNA binding.
Mutagenesis521R → Q: Abolishes RNA binding.

Secondary structure

.................................. 282
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09012 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 9426E83EE5A22894

FASTA28231,280
        10         20         30         40         50         60 
MAVPETRPNH TIYINNLNEK IKKDELKKSL YAIFSQFGQI LDILVSRSLK MRGQAFVIFK 

        70         80         90        100        110        120 
EVSSATNALR SMQGFPFYDK PMRIQYAKTD SDIIAKMKGT FVERDRKREK RKPKSQETPA 

       130        140        150        160        170        180 
TKKAVQGGGA TPVVGAVQGP VPGMPPMTQA PRIMHHMPGQ PPYMPPPGMI PPPGLAPGQI 

       190        200        210        220        230        240 
PPGAMPPQQL MPGQMPPAQP LSENPPNHIL FLTNLPEETN ELMLSMLFNQ FPGFKEVRLV 

       250        260        270        280 
PGRHDIAFVE FDNEVQAGAA RDALQGFKIT QNNAMKISFA KK 

« Hide

References

« Hide 'large scale' references
[1]"Structure, chromosomal localization and evolutionary conservation of the gene encoding human U1 snRNP-specific A protein."
Nelissen R.L.H., Sillekens P.T.G., Beijer R.P., Geurts van Kessel A.H.M., van Venrooij W.J.
Gene 102:189-196(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Liver.
[2]"cDNA cloning of the human U1 snRNA-associated A protein: extensive homology between U1 and U2 snRNP-specific proteins."
Sillekens P.T.G., Habets W.J., Beijer R.P., van Venrooij W.J.
EMBO J. 6:3841-3848(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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: Lung and Lymph.
[4]Bienvenut W.V.
Submitted (JAN-2004) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-19, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[5]"The snRNP-free U1A (SF-A) complex(es): identification of the largest subunit as PSF, the polypyrimidine-tract binding protein-associated splicing factor."
Lutz C.S., Cooke C., O'Connor J.P., Kobayashi R., Alwine J.C.
RNA 4:1493-1499(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN COUPLED SPLICING, FUNCTION IN POLYADENYLATION PROCESS, INTERACTION WITH SFPQ, IDENTIFICATION IN A SNRNP-FREE COMPLEX WITH SFPQ.
[6]"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 THR-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Rapid and systematic analysis of the RNA recognition specificities of RNA-binding proteins."
Ray D., Kazan H., Chan E.T., Pena Castillo L., Chaudhry S., Talukder S., Blencowe B.J., Morris Q., Hughes T.R.
Nat. Biotechnol. 27:667-670(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA-BINDING.
[9]"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-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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 THR-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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].
[12]"Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A."
Nagai K., Oubridge C., Jessen T.-H., Li J., Evans P.R.
Nature 348:515-520(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-95.
[13]"Crystal structure at 1.92-A resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin."
Oubridge C., Ito N., Evans P.R., Teo C.-H., Nagai K.
Nature 372:432-438(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS).
[14]"RNA-binding domain of the A protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR spectroscopy is structurally similar to ribosomal proteins."
Hoffman D.W., Query C.C., Golden B.L., White S.W., Keene J.D.
Proc. Natl. Acad. Sci. U.S.A. 88:2495-2499(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 11-94.
[15]"NMR studies of U1 snRNA recognition by the N-terminal RNP domain of the human U1A protein."
Howe P.W.A., Nagai K., Neuhaus D., Varani G.
EMBO J. 13:3873-3881(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-102.
[16]"Specificity of ribonucleoprotein interaction determined by RNA folding during complex formulation."
Allain F.H.-T., Gubser C.C., Howe P.W.A., Nagai K., Neuhaus D., Varani G.
Nature 380:646-650(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-102.
[17]"Solution structure of the N-terminal RNP domain of U1A protein: the role of C-terminal residues in structure stability and RNA binding."
Avis J.M., Allain F.H.-T., Howe P.W.A., Varani G., Nagai K., Neuhaus D.
J. Mol. Biol. 257:398-411(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-117.
[18]"Structural basis of the RNA-binding specificity of human U1A protein."
Allain F.H.-T., Howe P.W., Neuhaus D., Varani G.
EMBO J. 16:5764-5772(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-102.
[19]"Tertiary structure of RBD2 and backbone dynamics of RBD1 and RBD2 of the human U1A protein determined by NMR spectroscopy."
Lu J., Hall K.B.
Biochemistry 36:10393-10405(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 195-282.
[20]"Identification of molecular contacts between the U1 A small nuclear ribonucleoprotein and U1 RNA."
Jessen T.-H., Oubridge C., Teo C.H., Pritchard C., Nagai K.
EMBO J. 10:3447-3456(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS, DETAILED STUDIES OF RNA-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M60784 expand/collapse EMBL AC list , M60779, M60780, M60781, M60782, M60783 Genomic DNA. Translation: AAA61245.1.
X06347 mRNA. Translation: CAA29653.1.
BC000405 mRNA. Translation: AAH00405.1.
BC008290 mRNA. Translation: AAH08290.1.
CCDSCCDS12565.1.
PIRJQ1528.
RefSeqNP_004587.1. NM_004596.4.
UniGeneHs.466775.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AUDNMR-A2-102[»]
1CX0X-ray2.30A4-98[»]
1DRZX-ray2.30A2-98[»]
1DZ5NMR-A/B2-102[»]
1FHTNMR-A2-117[»]
1M5KX-ray2.40C/F1-100[»]
1M5OX-ray2.20C/F1-100[»]
1M5PX-ray2.60C/F1-100[»]
1M5VX-ray2.40C/F1-100[»]
1NU4X-ray1.80A/B2-98[»]
1OIAX-ray2.40A/B1-95[»]
1SJ3X-ray2.20P1-100[»]
1SJ4X-ray2.70P1-100[»]
1SJFX-ray2.75A1-100[»]
1U6BX-ray3.10A1-98[»]
1URNX-ray1.92A/B/C2-98[»]
1VBXX-ray2.70A1-100[»]
1VBYX-ray2.90A1-100[»]
1VBZX-ray2.80A1-100[»]
1VC0X-ray2.50A1-100[»]
1VC5X-ray3.40A1-100[»]
1VC6X-ray2.80A1-100[»]
1VC7X-ray2.45A1-100[»]
1ZZNX-ray3.37A1-98[»]
2A3JNMR-A3-80[»]
2NZ4X-ray2.50A/B/C/D5-98[»]
2OIHX-ray2.40A2-100[»]
2OJ3X-ray2.90A2-100[»]
2U1ANMR-A195-282[»]
3BO2X-ray3.31A4-98[»]
3BO3X-ray3.40A4-98[»]
3BO4X-ray3.33A4-98[»]
3CULX-ray2.80A/B1-96[»]
3CUNX-ray3.00A/B1-98[»]
3EGZX-ray2.20A1-98[»]
3G8SX-ray3.10A/B/C/D1-98[»]
3G8TX-ray3.00A/B/C/D1-98[»]
3G96X-ray3.01A/B/C/D1-98[»]
3G9CX-ray2.90A/B/C/D1-98[»]
3HHNX-ray2.99B/D2-98[»]
3IINX-ray4.18A4-98[»]
3IRWX-ray2.70P1-98[»]
3IWNX-ray3.20C/D6-96[»]
3K0JX-ray3.10A/B/C/D2-97[»]
3L3CX-ray2.85A/B/C/D7-96[»]
3MUMX-ray2.90P1-98[»]
3MURX-ray3.00P1-98[»]
3MUTX-ray3.00P1-98[»]
3MUVX-ray3.20P1-98[»]
3MXHX-ray2.30P1-98[»]
3P49X-ray3.55B1-98[»]
3PGWX-ray4.40A/P1-282[»]
3R1HX-ray3.15A/D1-98[»]
3R1LX-ray3.12A/D1-98[»]
3UCUX-ray2.80P1-98[»]
3UCZX-ray2.80P1-98[»]
3UD3X-ray3.10P1-98[»]
3UD4X-ray2.70P1-98[»]
3UTRmodel-B/D1-98[»]
4C4WX-ray2.95A/B/E/F1-102[»]
ProteinModelPortalP09012.
SMRP09012. Positions 2-117, 195-282.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112510. 65 interactions.
DIPDIP-29407N.
IntActP09012. 24 interactions.
MINTMINT-125665.
STRING9606.ENSP00000243563.

PTM databases

PhosphoSiteP09012.

Polymorphism databases

DMDM134092.

Proteomic databases

MaxQBP09012.
PaxDbP09012.
PeptideAtlasP09012.
PRIDEP09012.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000243563; ENSP00000243563; ENSG00000077312.
GeneID6626.
KEGGhsa:6626.
UCSCuc002ooz.3. human.

Organism-specific databases

CTD6626.
GeneCardsGC19P041256.
HGNCHGNC:11151. SNRPA.
HPACAB004652.
HPA046440.
HPA054834.
MIM182285. gene.
neXtProtNX_P09012.
PharmGKBPA35993.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG317159.
HOGENOMHOG000217519.
HOVERGENHBG000895.
InParanoidP09012.
KOK11091.
OMAVQPVPGM.
PhylomeDBP09012.
TreeFamTF313834.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressP09012.
BgeeP09012.
CleanExHS_SNRPA.
GenevestigatorP09012.

Family and domain databases

Gene3D3.30.70.330. 2 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR024888. U1_snRNP_A/U2_snRNP_B''.
[Graphical view]
PANTHERPTHR10501. PTHR10501. 1 hit.
PfamPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTSM00360. RRM. 2 hits.
[Graphical view]
PROSITEPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSNRPA. human.
EvolutionaryTraceP09012.
GeneWikiSmall_nuclear_ribonucleoprotein_polypeptide_A.
GenomeRNAi6626.
NextBio25809.
PROP09012.
SOURCESearch...

Entry information

Entry nameSNRPA_HUMAN
AccessionPrimary (citable) accession number: P09012
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 175 of the entry and version 3 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 chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM