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P09012

- SNRPA_HUMAN

UniProt

P09012 - SNRPA_HUMAN

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Protein

U1 small nuclear ribonucleoprotein A

Gene

SNRPA

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

Functioni

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.1 Publication

GO - Molecular functioni

  1. nucleotide binding Source: InterPro
  2. poly(A) RNA binding Source: UniProtKB
  3. RNA binding Source: UniProtKB
  4. snRNA binding Source: InterPro

GO - Biological processi

  1. gene expression Source: Reactome
  2. mRNA splicing, via spliceosome Source: HGNC
  3. 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:
U1 small nuclear ribonucleoprotein A
Short name:
U1 snRNP A
Short name:
U1-A
Short name:
U1A
Gene namesi
Name:SNRPA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:11151. SNRPA.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleolus Source: HPA
  3. nucleoplasm Source: Reactome
  4. nucleus Source: HPA
  5. spliceosomal complex Source: HGNC
  6. U1 snRNP Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi11 – 111T → V: Abolishes RNA binding. 1 Publication
Mutagenesisi13 – 131Y → F: Substantially reduces RNA binding. 1 Publication
Mutagenesisi15 – 151N → V: Abolishes RNA binding. 1 Publication
Mutagenesisi16 – 161N → V: Substantially reduces RNA binding. 1 Publication
Mutagenesisi52 – 521R → Q: Abolishes RNA binding. 1 Publication

Organism-specific databases

PharmGKBiPA35993.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 282281U1 small nuclear ribonucleoprotein APRO_0000081887Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei60 – 601N6-acetyllysine1 Publication
Modified residuei131 – 1311Phosphothreonine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP09012.
PaxDbiP09012.
PeptideAtlasiP09012.
PRIDEiP09012.

PTM databases

PhosphoSiteiP09012.

Expressioni

Gene expression databases

BgeeiP09012.
CleanExiHS_SNRPA.
ExpressionAtlasiP09012. baseline and differential.
GenevestigatoriP09012.

Organism-specific databases

HPAiCAB004652.
HPA046440.
HPA054834.

Interactioni

Subunit structurei

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SFPQP232464EBI-607085,EBI-355453
U2AF2P263682EBI-607085,EBI-742339

Protein-protein interaction databases

BioGridi112510. 67 interactions.
DIPiDIP-29407N.
IntActiP09012. 24 interactions.
MINTiMINT-125665.
STRINGi9606.ENSP00000243563.

Structurei

Secondary structure

1
282
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 167Combined sources
Beta strandi19 – 213Combined sources
Helixi23 – 3412Combined sources
Helixi35 – 373Combined sources
Beta strandi40 – 445Combined sources
Helixi47 – 515Combined sources
Beta strandi55 – 617Combined sources
Helixi62 – 7211Combined sources
Beta strandi77 – 804Combined sources
Beta strandi83 – 864Combined sources
Helixi93 – 964Combined sources
Helixi97 – 1004Combined sources
Beta strandi208 – 2136Combined sources
Helixi221 – 2299Combined sources
Beta strandi234 – 2385Combined sources
Beta strandi246 – 2538Combined sources
Helixi254 – 26310Combined sources
Turni264 – 2663Combined sources
Helixi269 – 2713Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP09012.
SMRiP09012. Positions 2-117, 195-282.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09012.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 8980RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini208 – 28275RRM 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi140 – 20667Pro-richAdd
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.
InParanoidiP09012.
KOiK11091.
OMAiVQPVPGM.
PhylomeDBiP09012.
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. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09012-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAVPETRPNH TIYINNLNEK IKKDELKKSL YAIFSQFGQI LDILVSRSLK
60 70 80 90 100
MRGQAFVIFK EVSSATNALR SMQGFPFYDK PMRIQYAKTD SDIIAKMKGT
110 120 130 140 150
FVERDRKREK RKPKSQETPA TKKAVQGGGA TPVVGAVQGP VPGMPPMTQA
160 170 180 190 200
PRIMHHMPGQ PPYMPPPGMI PPPGLAPGQI PPGAMPPQQL MPGQMPPAQP
210 220 230 240 250
LSENPPNHIL FLTNLPEETN ELMLSMLFNQ FPGFKEVRLV PGRHDIAFVE
260 270 280
FDNEVQAGAA RDALQGFKIT QNNAMKISFA KK
Length:282
Mass (Da):31,280
Last modified:January 23, 2007 - v3
Checksum:i9426E83EE5A22894
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60784
, 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.
CCDSiCCDS12565.1.
PIRiJQ1528.
RefSeqiNP_004587.1. NM_004596.4.
UniGeneiHs.466775.

Genome annotation databases

EnsembliENST00000243563; ENSP00000243563; ENSG00000077312.
GeneIDi6626.
KEGGihsa:6626.
UCSCiuc002ooz.3. human.

Polymorphism databases

DMDMi134092.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60784
, 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 .
CCDSi CCDS12565.1.
PIRi JQ1528.
RefSeqi NP_004587.1. NM_004596.4.
UniGenei Hs.466775.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AUD NMR - A 2-102 [» ]
1CX0 X-ray 2.30 A 4-98 [» ]
1DRZ X-ray 2.30 A 2-98 [» ]
1DZ5 NMR - A/B 2-102 [» ]
1FHT NMR - A 2-117 [» ]
1M5K X-ray 2.40 C/F 1-100 [» ]
1M5O X-ray 2.20 C/F 1-100 [» ]
1M5P X-ray 2.60 C/F 1-100 [» ]
1M5V X-ray 2.40 C/F 1-100 [» ]
1NU4 X-ray 1.80 A/B 2-98 [» ]
1OIA X-ray 2.40 A/B 1-95 [» ]
1SJ3 X-ray 2.20 P 1-100 [» ]
1SJ4 X-ray 2.70 P 1-100 [» ]
1SJF X-ray 2.75 A 1-100 [» ]
1U6B X-ray 3.10 A 1-98 [» ]
1URN X-ray 1.92 A/B/C 2-98 [» ]
1VBX X-ray 2.70 A 1-100 [» ]
1VBY X-ray 2.90 A 1-100 [» ]
1VBZ X-ray 2.80 A 1-100 [» ]
1VC0 X-ray 2.50 A 1-100 [» ]
1VC5 X-ray 3.40 A 1-100 [» ]
1VC6 X-ray 2.80 A 1-100 [» ]
1VC7 X-ray 2.45 A 1-100 [» ]
1ZZN X-ray 3.37 A 1-98 [» ]
2A3J NMR - A 3-80 [» ]
2NZ4 X-ray 2.50 A/B/C/D 5-98 [» ]
2OIH X-ray 2.40 A 2-100 [» ]
2OJ3 X-ray 2.90 A 2-100 [» ]
2U1A NMR - A 195-282 [» ]
3BO2 X-ray 3.31 A 4-98 [» ]
3BO3 X-ray 3.40 A 4-98 [» ]
3BO4 X-ray 3.33 A 4-98 [» ]
3CUL X-ray 2.80 A/B 1-96 [» ]
3CUN X-ray 3.00 A/B 1-98 [» ]
3EGZ X-ray 2.20 A 1-98 [» ]
3G8S X-ray 3.10 A/B/C/D 1-98 [» ]
3G8T X-ray 3.00 A/B/C/D 1-98 [» ]
3G96 X-ray 3.01 A/B/C/D 1-98 [» ]
3G9C X-ray 2.90 A/B/C/D 1-98 [» ]
3HHN X-ray 2.99 B/D 2-98 [» ]
3IIN X-ray 4.18 A 4-98 [» ]
3IRW X-ray 2.70 P 1-98 [» ]
3IWN X-ray 3.20 C/D 6-96 [» ]
3K0J X-ray 3.10 A/B/C/D 2-97 [» ]
3L3C X-ray 2.85 A/B/C/D 7-96 [» ]
3MUM X-ray 2.90 P 1-98 [» ]
3MUR X-ray 3.00 P 1-98 [» ]
3MUT X-ray 3.00 P 1-98 [» ]
3MUV X-ray 3.20 P 1-98 [» ]
3MXH X-ray 2.30 P 1-98 [» ]
3P49 X-ray 3.55 B 1-98 [» ]
3PGW X-ray 4.40 A/P 1-282 [» ]
3R1H X-ray 3.15 A/D 1-98 [» ]
3R1L X-ray 3.12 A/D 1-98 [» ]
3UCU X-ray 2.80 P 1-98 [» ]
3UCZ X-ray 2.80 P 1-98 [» ]
3UD3 X-ray 3.10 P 1-98 [» ]
3UD4 X-ray 2.70 P 1-98 [» ]
3UTR model - B/D 1-98 [» ]
4C4W X-ray 2.95 A/B/E/F 1-102 [» ]
ProteinModelPortali P09012.
SMRi P09012. Positions 2-117, 195-282.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112510. 67 interactions.
DIPi DIP-29407N.
IntActi P09012. 24 interactions.
MINTi MINT-125665.
STRINGi 9606.ENSP00000243563.

PTM databases

PhosphoSitei P09012.

Polymorphism databases

DMDMi 134092.

Proteomic databases

MaxQBi P09012.
PaxDbi P09012.
PeptideAtlasi P09012.
PRIDEi P09012.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000243563 ; ENSP00000243563 ; ENSG00000077312 .
GeneIDi 6626.
KEGGi hsa:6626.
UCSCi uc002ooz.3. human.

Organism-specific databases

CTDi 6626.
GeneCardsi GC19P041256.
HGNCi HGNC:11151. SNRPA.
HPAi CAB004652.
HPA046440.
HPA054834.
MIMi 182285. gene.
neXtProti NX_P09012.
PharmGKBi PA35993.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG317159.
GeneTreei ENSGT00390000007046.
HOGENOMi HOG000217519.
HOVERGENi HBG000895.
InParanoidi P09012.
KOi K11091.
OMAi VQPVPGM.
PhylomeDBi P09012.
TreeFami TF313834.

Enzyme and pathway databases

Reactomei REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSi SNRPA. human.
EvolutionaryTracei P09012.
GeneWikii Small_nuclear_ribonucleoprotein_polypeptide_A.
GenomeRNAii 6626.
NextBioi 25809.
PROi P09012.
SOURCEi Search...

Gene expression databases

Bgeei P09012.
CleanExi HS_SNRPA.
ExpressionAtlasi P09012. baseline and differential.
Genevestigatori P09012.

Family and domain databases

Gene3Di 3.30.70.330. 2 hits.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR024888. U1_snRNP_A/U2_snRNP_B''.
[Graphical view ]
PANTHERi PTHR10501. PTHR10501. 1 hit.
Pfami PF00076. RRM_1. 2 hits.
[Graphical view ]
SMARTi SM00360. RRM. 2 hits.
[Graphical view ]
PROSITEi PS50102. RRM. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiSNRPA_HUMAN
AccessioniPrimary (citable) accession number: P09012
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 179 of the entry and version 3 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3