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Reviewed, UniProtKB/Swiss-Prot P09012 (SNRPA_HUMAN)

Last modified November 3, 2009. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    U1 small nuclear ribonucleoprotein A
      Short name=U1 snRNP protein A
      Short name=U1A protein
      Short name=U1-A
Gene names
Name: SNRPA
OrganismHomo sapiens (Human) [Complete 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

Binds stem loop II of U1 snRNA. It 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. In a snRNP-free form (SF-A) may be involved in coupled pre-mRNA splicing and polyadenylation process. Ref.5

Subunit structure

Belongs to the spliceosome where it is associated with snRNP U1. Interacts with SFPQ. Also 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.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentNucleus
Spliceosome
   DomainRepeat
   LigandRNA-binding
   Molecular functionRibonucleoprotein
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processnuclear mRNA splicing, via spliceosome

Inferred by curator. Source: HGNC

   Cellular componentspliceosomal complex

Inferred from direct assay. Source: HGNC

   Molecular functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide binding

Inferred from electronic annotation. Source: InterPro

protein binding Ref.5

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

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
Modified residue601N6-acetyllysine Ref.8
Modified residue1311Phosphothreonine Ref.6

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
P09012-1 [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: 1831431] [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: 2962859] [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: 15489334] [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, 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: 9848648] [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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-131, MASS SPECTROMETRY.
[7]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60, MASS SPECTROMETRY.
[9]"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: 2147232] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-95.
[10]"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: 7984237] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS).
[11]"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: 1826055] [Abstract]
Cited for: STRUCTURE BY NMR OF 11-94.
[12]"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: 8070414] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-102.
[13]"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: 8602269] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-102.
[14]"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: 8609632] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-117.
[15]"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: 9312034] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-102.
[16]"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: 9265619] [Abstract]
Cited for: STRUCTURE BY NMR OF 195-282.
[17]"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: 1833186] [Abstract]
Cited for: MUTAGENESIS, DETAILED STUDIES OF RNA-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
IPIIPI00012382.
PIRJQ1528.
RefSeqNP_004587.1.
UniGeneHs.466775

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1AUDNMR-A2-102[»]
1CX0X-ray2.30A4-97[»]
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-ray3.37A2-97[»]
2A3JNMR-A40-43[»]
2NZ4X-ray2.50A/B/C/D5-97[»]
2OIHX-ray2.40A2-99[»]
2OJ3X-ray2.90A2-99[»]
2U1ANMR-A197-282[»]
3BO2X-ray3.31A4-98[»]
3BO3X-ray3.40A4-98[»]
3BO4X-ray3.33A4-98[»]
3CULX-ray2.80A/B1-98[»]
3CUNX-ray3.00A/B1-98[»]
3EGZX-ray2.20A1-98[»]
3UTRmodel-B/D1-98[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP09012. 7 interactions.
STRINGP09012.

PTM databases

PhosphoSiteP09012.

Proteomic databases

PeptideAtlasP09012.
PRIDEP09012.

Genome annotation databases

EnsemblENST00000243563; ENSP00000243563; ENSG00000077312; Homo sapiens. [Genome view]
GeneID6626.
KEGGhsa:6626.
UCSCuc002ooz.1. human.

Organism-specific databases

CTD6626.
GeneCardsGC19P045948.
H-InvDBHIX0015143.
HGNCHGNC:11151. SNRPA.
HPACAB004652.
MIM182285. gene.
PharmGKBPA35993.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP09012.
HOVERGENP09012.
OMAMVEAKPG.

Enzyme and pathway databases

ReactomeREACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_6167. Influenza Infection.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP09012.
BgeeP09012.
CleanExHS_SNRPA.
GenevestigatorP09012.
GermOnlineENSG00000077312. Homo sapiens.

Family and domain databases

InterProIPR012677. a_b_plait_nuc_bd.
IPR000504. RRM_RNP1.
[Graphical view]
Gene3DG3DSA:3.30.70.330. a_b_plait_nuc_bd. 2 hits.
PfamPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTSM00360. RRM. 2 hits.
[Graphical view]
PROSITEPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio25809.
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: November 3, 2009
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 19

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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents