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P09661

- RU2A_HUMAN

UniProt

P09661 - RU2A_HUMAN

Protein

U2 small nuclear ribonucleoprotein A'

Gene

SNRPA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 2 (23 May 2003)
      Previous versions | rss
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    Functioni

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

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. gene expression Source: Reactome
    2. mRNA splicing, via spliceosome Source: UniProtKB
    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:
    U2 small nuclear ribonucleoprotein A'
    Short name:
    U2 snRNP A'
    Gene namesi
    Name:SNRPA1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:11152. SNRPA1.

    Subcellular locationi

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. nucleoplasm Source: Reactome
    3. nucleus Source: HPA
    4. small nuclear ribonucleoprotein complex Source: ProtInc
    5. spliceosomal complex Source: HGNC
    6. U2 snRNP Source: ProtInc

    Keywords - Cellular componenti

    Nucleus, Spliceosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35994.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 255254U2 small nuclear ribonucleoprotein A'PRO_0000074173Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei172 – 1721N6-acetyllysine1 Publication
    Modified residuei178 – 1781Phosphoserine1 Publication
    Modified residuei197 – 1971Phosphoserine3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP09661.
    PaxDbiP09661.
    PeptideAtlasiP09661.
    PRIDEiP09661.

    PTM databases

    PhosphoSiteiP09661.

    Expressioni

    Gene expression databases

    BgeeiP09661.
    CleanExiHS_SNRPA1.
    GenevestigatoriP09661.

    Organism-specific databases

    HPAiHPA045622.
    HPA048499.

    Interactioni

    Subunit structurei

    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.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SNRPB2P085792EBI-876439,EBI-1053651

    Protein-protein interaction databases

    BioGridi112511. 93 interactions.
    DIPiDIP-625N.
    IntActiP09661. 13 interactions.
    MINTiMINT-3007227.
    STRINGi9606.ENSP00000254193.

    Structurei

    Secondary structure

    1
    255
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 105
    Beta strandi14 – 163
    Beta strandi22 – 254
    Helixi37 – 404
    Beta strandi45 – 484
    Beta strandi68 – 703
    Helixi83 – 864
    Beta strandi92 – 943
    Helixi103 – 1119
    Beta strandi117 – 1193
    Helixi124 – 1274
    Helixi131 – 1388
    Beta strandi143 – 1453
    Helixi152 – 1609

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A9NX-ray2.38A/C1-176[»]
    ProteinModelPortaliP09661.
    SMRiP09661. Positions 2-175.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09661.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati20 – 4122LRR 1Add
    BLAST
    Repeati43 – 6422LRR 2Add
    BLAST
    Repeati65 – 8622LRR 3Add
    BLAST
    Repeati89 – 11022LRR 4Add
    BLAST
    Domaini123 – 16139LRRCTAdd
    BLAST

    Sequence similaritiesi

    Contains 4 LRR (leucine-rich) repeats.Curated
    Contains 1 LRRCT domain.Curated

    Keywords - Domaini

    Leucine-rich repeat, Repeat

    Phylogenomic databases

    eggNOGiCOG4886.
    HOGENOMiHOG000175472.
    HOVERGENiHBG007330.
    InParanoidiP09661.
    KOiK11092.
    OMAiSMQYINP.
    OrthoDBiEOG7966HF.
    PhylomeDBiP09661.
    TreeFamiTF313776.

    Family and domain databases

    InterProiIPR001611. Leu-rich_rpt.
    IPR003603. U2A'_phosphoprotein32A_C.
    [Graphical view]
    SMARTiSM00446. LRRcap. 1 hit.
    [Graphical view]
    PROSITEiPS51450. LRR. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P09661-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVKLTAELIE QAAQYTNAVR DRELDLRGYK IPVIENLGAT LDQFDAIDFS    50
    DNEIRKLDGF PLLRRLKTLL VNNNRICRIG EGLDQALPCL TELILTNNSL 100
    VELGDLDPLA SLKSLTYLSI LRNPVTNKKH YRLYVIYKVP QVRVLDFQKV 150
    KLKERQEAEK MFKGKRGAQL AKDIARRSKT FNPGAGLPTD KKKGGPSPGD 200
    VEAIKNAIAN ASTLAEVERL KGLLQSGQIP GRERRSGPTD DGEEEMEEDT 250
    VTNGS 255
    Length:255
    Mass (Da):28,416
    Last modified:May 23, 2003 - v2
    Checksum:i25902F07992B7209
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti193 – 1931K → R in CAA31838. (PubMed:2928112)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti234 – 2341R → H.
    Corresponds to variant rs1050843 [ dbSNP | Ensembl ].
    VAR_052030

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS10391.1.
    PIRiS03616.
    RefSeqiNP_003081.2. NM_003090.2.
    UniGeneiHs.528763.

    Genome annotation databases

    EnsembliENST00000254193; ENSP00000254193; ENSG00000131876.
    GeneIDi6627.
    KEGGihsa:6627.
    UCSCiuc002bww.3. human.

    Polymorphism databases

    DMDMi31077165.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS10391.1.
    PIRi S03616.
    RefSeqi NP_003081.2. NM_003090.2.
    UniGenei Hs.528763.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A9N X-ray 2.38 A/C 1-176 [» ]
    ProteinModelPortali P09661.
    SMRi P09661. Positions 2-175.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112511. 93 interactions.
    DIPi DIP-625N.
    IntActi P09661. 13 interactions.
    MINTi MINT-3007227.
    STRINGi 9606.ENSP00000254193.

    PTM databases

    PhosphoSitei P09661.

    Polymorphism databases

    DMDMi 31077165.

    Proteomic databases

    MaxQBi P09661.
    PaxDbi P09661.
    PeptideAtlasi P09661.
    PRIDEi P09661.

    Protocols and materials databases

    DNASUi 6627.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000254193 ; ENSP00000254193 ; ENSG00000131876 .
    GeneIDi 6627.
    KEGGi hsa:6627.
    UCSCi uc002bww.3. human.

    Organism-specific databases

    CTDi 6627.
    GeneCardsi GC15M101821.
    H-InvDB HIX0203213.
    HGNCi HGNC:11152. SNRPA1.
    HPAi HPA045622.
    HPA048499.
    MIMi 603521. gene.
    neXtProti NX_P09661.
    PharmGKBi PA35994.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4886.
    HOGENOMi HOG000175472.
    HOVERGENi HBG007330.
    InParanoidi P09661.
    KOi K11092.
    OMAi SMQYINP.
    OrthoDBi EOG7966HF.
    PhylomeDBi P09661.
    TreeFami TF313776.

    Enzyme and pathway databases

    Reactomei REACT_467. mRNA Splicing - Major Pathway.

    Miscellaneous databases

    EvolutionaryTracei P09661.
    GeneWikii SNRPA1.
    GenomeRNAii 6627.
    NextBioi 25813.
    PROi P09661.
    SOURCEi Search...

    Gene expression databases

    Bgeei P09661.
    CleanExi HS_SNRPA1.
    Genevestigatori P09661.

    Family and domain databases

    InterProi IPR001611. Leu-rich_rpt.
    IPR003603. U2A'_phosphoprotein32A_C.
    [Graphical view ]
    SMARTi SM00446. LRRcap. 1 hit.
    [Graphical view ]
    PROSITEi PS51450. LRR. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. 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.

    Entry informationi

    Entry nameiRU2A_HUMAN
    AccessioniPrimary (citable) accession number: P09661
    Secondary accession number(s): B2R5I6, Q8TBD2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: May 23, 2003
    Last modified: October 1, 2014
    This is version 149 of the entry and version 2 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 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3