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P09012

- SNRPA_HUMAN

UniProt

P09012 - SNRPA_HUMAN

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
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    • History
      Entry version 177 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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. protein binding Source: IntAct
    4. RNA binding Source: UniProtKB
    5. snRNA binding Source: InterPro

    GO - Biological processi

    1. gene expression Source: Reactome
    2. mRNA splicing, via spliceosome Source: HGNC
    3. RNA splicing Source: Reactome

    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

    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

    ArrayExpressiP09012.
    BgeeiP09012.
    CleanExiHS_SNRPA.
    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 – 167
    Beta strandi19 – 213
    Helixi23 – 3412
    Helixi35 – 373
    Beta strandi40 – 445
    Helixi47 – 515
    Beta strandi55 – 617
    Helixi62 – 7211
    Beta strandi77 – 804
    Beta strandi83 – 864
    Helixi93 – 964
    Helixi97 – 1004
    Beta strandi208 – 2136
    Helixi221 – 2299
    Beta strandi234 – 2385
    Beta strandi246 – 2538
    Helixi254 – 26310
    Turni264 – 2663
    Helixi269 – 2713

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MAVPETRPNH TIYINNLNEK IKKDELKKSL YAIFSQFGQI LDILVSRSLK    50
    MRGQAFVIFK EVSSATNALR SMQGFPFYDK PMRIQYAKTD SDIIAKMKGT 100
    FVERDRKREK RKPKSQETPA TKKAVQGGGA TPVVGAVQGP VPGMPPMTQA 150
    PRIMHHMPGQ PPYMPPPGMI PPPGLAPGQI PPGAMPPQQL MPGQMPPAQP 200
    LSENPPNHIL FLTNLPEETN ELMLSMLFNQ FPGFKEVRLV PGRHDIAFVE 250
    FDNEVQAGAA RDALQGFKIT QNNAMKISFA KK 282
    Length:282
    Mass (Da):31,280
    Last modified:January 23, 2007 - v3
    Checksum:i9426E83EE5A22894
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    ArrayExpressi P09012.
    Bgeei P09012.
    CleanExi HS_SNRPA.
    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

    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: October 1, 2014
    This is version 177 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