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P08621

- RU17_HUMAN

UniProt

P08621 - RU17_HUMAN

Protein

U1 small nuclear ribonucleoprotein 70 kDa

Gene

SNRNP70

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 174 (01 Oct 2014)
      Sequence version 2 (01 Aug 1988)
      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. SNRNP70 binds to the loop I region of U1-snRNA. The truncated isoforms cannot bind U1-snRNA.

    GO - Molecular functioni

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

    GO - Biological processi

    1. gene expression Source: Reactome
    2. mRNA processing Source: ProtInc
    3. mRNA splicing, via spliceosome Source: UniProtKB
    4. regulation of RNA splicing Source: UniProtKB
    5. RNA splicing Source: Reactome

    Keywords - Molecular functioni

    Ribonucleoprotein

    Keywords - Biological processi

    mRNA processing

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_467. mRNA Splicing - Major Pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    U1 small nuclear ribonucleoprotein 70 kDa
    Short name:
    U1 snRNP 70 kDa
    Short name:
    U1-70K
    Short name:
    snRNP70
    Gene namesi
    Name:SNRNP70
    Synonyms:RNPU1Z, RPU1, SNRP70, U1AP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:11150. SNRNP70.

    Subcellular locationi

    Nucleus. Nucleus speckle By similarity. Nucleusnucleoplasm By similarity
    Note: Colocalizes with SCNM1 and LUC7L2 in nuclear speckles.By similarity

    GO - Cellular componenti

    1. nuclear speck Source: UniProtKB-SubCell
    2. nucleoplasm Source: Reactome
    3. nucleus Source: HPA
    4. spliceosomal complex Source: UniProtKB
    5. U1 snRNP Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35992.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 437436U1 small nuclear ribonucleoprotein 70 kDaPRO_0000081880Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine2 Publications
    Modified residuei118 – 1181N6-acetyllysine1 Publication
    Modified residuei226 – 2261Phosphoserine8 Publications
    Modified residuei268 – 2681Phosphoserine2 Publications
    Modified residuei320 – 3201Phosphoserine5 Publications
    Modified residuei410 – 4101Phosphoserine7 Publications

    Post-translational modificationi

    The N-terminus is blocked.
    Extensively phosphorylated on serine residues in the C-terminal region.11 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP08621.
    PaxDbiP08621.
    PRIDEiP08621.

    PTM databases

    PhosphoSiteiP08621.

    Miscellaneous databases

    PMAP-CutDBP08621.

    Expressioni

    Gene expression databases

    ArrayExpressiP08621.
    BgeeiP08621.
    GenevestigatoriP08621.

    Organism-specific databases

    HPAiCAB001718.
    HPA042050.
    HPA043516.

    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 SCNM1. 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/SFRS10. Interacts with dephosphorylated SFRS13A and SFPQ. Interacts with NUDT21/CPSF5, CPSF6, SCAF11, and ZRANB2.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CLK2P497602EBI-1049228,EBI-750020
    SRPK2P783623EBI-1049228,EBI-593303

    Protein-protein interaction databases

    BioGridi112509. 105 interactions.
    DIPiDIP-29406N.
    IntActiP08621. 44 interactions.
    MINTiMINT-5004037.

    Structurei

    Secondary structure

    1
    437
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni139 – 1413
    Turni142 – 1509

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2L5INMR-A131-151[»]
    2L5JNMR-A131-151[»]
    3CW1X-ray5.496/7/8/K1-216[»]
    3PGWX-ray4.40L/S1-437[»]
    ProteinModelPortaliP08621.
    SMRiP08621. Positions 114-177.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08621.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini103 – 18179RRMPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi231 – 31080Arg/Glu-rich (mixed charge)Add
    BLAST
    Compositional biasi311 – 3144Poly-Gly
    Compositional biasi344 – 39350Arg/Asp/Glu-rich (mixed charge)Add
    BLAST
    Compositional biasi394 – 3985Poly-Gly

    Sequence similaritiesi

    Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0724.
    InParanoidiP08621.
    KOiK11093.
    OMAiDGRDMYM.
    OrthoDBiEOG79W96V.
    PhylomeDBiP08621.
    TreeFamiTF314215.

    Family and domain databases

    Gene3Di3.30.70.330. 1 hit.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR022023. U1snRNP70_N.
    [Graphical view]
    PfamiPF00076. RRM_1. 1 hit.
    PF12220. U1snRNP70_N. 1 hit.
    [Graphical view]
    SMARTiSM00360. RRM. 1 hit.
    [Graphical view]
    PROSITEiPS50102. RRM. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P08621-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MTQFLPPNLL ALFAPRDPIP YLPPLEKLPH EKHHNQPYCG IAPYIREFED    50
    PRDAPPPTRA ETREERMERK RREKIERRQQ EVETELKMWD PHNDPNAQGD 100
    AFKTLFVARV NYDTTESKLR REFEVYGPIK RIHMVYSKRS GKPRGYAFIE 150
    YEHERDMHSA YKHADGKKID GRRVLVDVER GRTVKGWRPR RLGGGLGGTR 200
    RGGADVNIRH SGRDDTSRYD ERPGPSPLPH RDRDRDRERE RRERSRERDK 250
    ERERRRSRSR DRRRRSRSRD KEERRRSRER SKDKDRDRKR RSSRSRERAR 300
    RERERKEELR GGGGDMAEPS EAGDAPPDDG PPGELGPDGP DGPEEKGRDR 350
    DRERRRSHRS ERERRRDRDR DRDRDREHKR GERGSERGRD EARGGGGGQD 400
    NGLEGLGNDS RDMYMESEGG DGYLAPENGY LMEAAPE 437
    Length:437
    Mass (Da):51,557
    Last modified:August 1, 1988 - v2
    Checksum:iF1020BF5C40CF97D
    GO
    Isoform 2 (identifier: P08621-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         223-231: Missing.

    Show »
    Length:428
    Mass (Da):50,618
    Checksum:iEEBC1CE4E8B9DBDA
    GO
    Isoform 3 (identifier: P08621-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         160-166: AYKHADG → TTQLACS
         167-437: Missing.

    Show »
    Length:166
    Mass (Da):19,790
    Checksum:iE90F034A08D3E79C
    GO
    Isoform 4 (identifier: P08621-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-159: MTQFLPPNLL...EYEHERDMHS → MEQALHRFGR...PLPLPTSVTA

    Show »
    Length:341
    Mass (Da):39,191
    Checksum:i390967CC272E50E9
    GO

    Sequence cautioni

    The sequence CAA28352.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAA29964.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAA29966.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 159159MTQFL…RDMHS → MEQALHRFGRGLVWLSVAWL SVGRVRVRDDGDTGRGFCRA GPVLTRGPSGDSSPLPLPTS VTA in isoform 4. 1 PublicationVSP_005847Add
    BLAST
    Alternative sequencei160 – 1667AYKHADG → TTQLACS in isoform 3. 1 PublicationVSP_005848
    Alternative sequencei167 – 437271Missing in isoform 3. 1 PublicationVSP_005849Add
    BLAST
    Alternative sequencei223 – 2319Missing in isoform 2. CuratedVSP_005850

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04654 mRNA. Translation: CAA28352.1. Different initiation.
    X06814 mRNA. Translation: CAA29963.1.
    X06815 mRNA. Translation: CAA29964.1. Different initiation.
    X06817 mRNA. Translation: CAA29966.1. Different initiation.
    X07402 mRNA. Translation: CAA30304.1.
    X06816 mRNA. Translation: CAA29965.1.
    X06812 mRNA. Translation: CAA29961.1.
    X06811 mRNA. Translation: CAA29960.1.
    X07401 mRNA. Translation: CAA30303.1.
    X07403 mRNA. Translation: CAA30305.1.
    M22636 mRNA. Translation: AAA03001.1.
    M57939
    , M57929, M57930, M57932, M57934, M57937 Genomic DNA. Translation: AAA36572.1.
    M57939
    , M57929, M57930, M57932, M57934, M57937 Genomic DNA. Translation: AAA36573.1.
    M57935
    , M57929, M57930, M57932, M57934 Genomic DNA. Translation: AAA36571.1.
    AK096783 mRNA. Translation: BAG53365.1.
    X84841 mRNA. Translation: CAA59278.1.
    AL117507 mRNA. Translation: CAB55969.1.
    CH471177 Genomic DNA. Translation: EAW52449.1.
    BC001315 mRNA. Translation: AAH01315.1.
    CCDSiCCDS12756.1. [P08621-1]
    PIRiA25707.
    S00674.
    RefSeqiNP_003080.2. NM_003089.4. [P08621-1]
    XP_005259234.1. XM_005259177.1. [P08621-2]
    UniGeneiHs.467097.

    Genome annotation databases

    EnsembliENST00000221448; ENSP00000221448; ENSG00000104852. [P08621-2]
    ENST00000401730; ENSP00000385077; ENSG00000104852. [P08621-3]
    ENST00000595231; ENSP00000471006; ENSG00000104852. [P08621-3]
    ENST00000598441; ENSP00000472998; ENSG00000104852. [P08621-1]
    ENST00000601065; ENSP00000468952; ENSG00000104852. [P08621-3]
    GeneIDi6625.
    KEGGihsa:6625.
    UCSCiuc002pmk.3. human. [P08621-1]

    Polymorphism databases

    DMDMi13635663.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04654 mRNA. Translation: CAA28352.1 . Different initiation.
    X06814 mRNA. Translation: CAA29963.1 .
    X06815 mRNA. Translation: CAA29964.1 . Different initiation.
    X06817 mRNA. Translation: CAA29966.1 . Different initiation.
    X07402 mRNA. Translation: CAA30304.1 .
    X06816 mRNA. Translation: CAA29965.1 .
    X06812 mRNA. Translation: CAA29961.1 .
    X06811 mRNA. Translation: CAA29960.1 .
    X07401 mRNA. Translation: CAA30303.1 .
    X07403 mRNA. Translation: CAA30305.1 .
    M22636 mRNA. Translation: AAA03001.1 .
    M57939
    , M57929 , M57930 , M57932 , M57934 , M57937 Genomic DNA. Translation: AAA36572.1 .
    M57939
    , M57929 , M57930 , M57932 , M57934 , M57937 Genomic DNA. Translation: AAA36573.1 .
    M57935
    , M57929 , M57930 , M57932 , M57934 Genomic DNA. Translation: AAA36571.1 .
    AK096783 mRNA. Translation: BAG53365.1 .
    X84841 mRNA. Translation: CAA59278.1 .
    AL117507 mRNA. Translation: CAB55969.1 .
    CH471177 Genomic DNA. Translation: EAW52449.1 .
    BC001315 mRNA. Translation: AAH01315.1 .
    CCDSi CCDS12756.1. [P08621-1 ]
    PIRi A25707.
    S00674.
    RefSeqi NP_003080.2. NM_003089.4. [P08621-1 ]
    XP_005259234.1. XM_005259177.1. [P08621-2 ]
    UniGenei Hs.467097.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2L5I NMR - A 131-151 [» ]
    2L5J NMR - A 131-151 [» ]
    3CW1 X-ray 5.49 6/7/8/K 1-216 [» ]
    3PGW X-ray 4.40 L/S 1-437 [» ]
    ProteinModelPortali P08621.
    SMRi P08621. Positions 114-177.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112509. 105 interactions.
    DIPi DIP-29406N.
    IntActi P08621. 44 interactions.
    MINTi MINT-5004037.

    PTM databases

    PhosphoSitei P08621.

    Polymorphism databases

    DMDMi 13635663.

    Proteomic databases

    MaxQBi P08621.
    PaxDbi P08621.
    PRIDEi P08621.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000221448 ; ENSP00000221448 ; ENSG00000104852 . [P08621-2 ]
    ENST00000401730 ; ENSP00000385077 ; ENSG00000104852 . [P08621-3 ]
    ENST00000595231 ; ENSP00000471006 ; ENSG00000104852 . [P08621-3 ]
    ENST00000598441 ; ENSP00000472998 ; ENSG00000104852 . [P08621-1 ]
    ENST00000601065 ; ENSP00000468952 ; ENSG00000104852 . [P08621-3 ]
    GeneIDi 6625.
    KEGGi hsa:6625.
    UCSCi uc002pmk.3. human. [P08621-1 ]

    Organism-specific databases

    CTDi 6625.
    GeneCardsi GC19P049588.
    HGNCi HGNC:11150. SNRNP70.
    HPAi CAB001718.
    HPA042050.
    HPA043516.
    MIMi 180740. gene.
    neXtProti NX_P08621.
    PharmGKBi PA35992.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0724.
    InParanoidi P08621.
    KOi K11093.
    OMAi DGRDMYM.
    OrthoDBi EOG79W96V.
    PhylomeDBi P08621.
    TreeFami TF314215.

    Enzyme and pathway databases

    Reactomei REACT_467. mRNA Splicing - Major Pathway.

    Miscellaneous databases

    ChiTaRSi SNRNP70. human.
    EvolutionaryTracei P08621.
    GeneWikii SnRNP70.
    GenomeRNAii 6625.
    NextBioi 25805.
    PMAP-CutDB P08621.
    PROi P08621.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P08621.
    Bgeei P08621.
    Genevestigatori P08621.

    Family and domain databases

    Gene3Di 3.30.70.330. 1 hit.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR022023. U1snRNP70_N.
    [Graphical view ]
    Pfami PF00076. RRM_1. 1 hit.
    PF12220. U1snRNP70_N. 1 hit.
    [Graphical view ]
    SMARTi SM00360. RRM. 1 hit.
    [Graphical view ]
    PROSITEi PS50102. RRM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of the human cDNA for the U1 RNA-associated 70K protein."
      Theissen H., Etzerodt M., Reuter R., Schneider C., Lottspeich F., Argos P., Luehrmann R., Philipson L.
      EMBO J. 5:3209-3217(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "The human U1-70K snRNP protein: cDNA cloning, chromosomal localization, expression, alternative splicing and RNA-binding."
      Spritz R.A., Strunk K., Surowy C.S., Hoch S.O., Barton D.E., Francke U.
      Nucleic Acids Res. 15:10373-10391(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
    3. "A common RNA recognition motif identified within a defined U1 RNA binding domain of the 70K U1 snRNP protein."
      Query C.C., Bentley R.C., Keene J.D.
      Cell 57:89-101(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), RNA-BINDING DOMAIN.
    4. "Human U1-70K ribonucleoprotein antigen gene: organization, nucleotide sequence, and mapping to locus 19q13.3."
      Spritz R.A., Strunk K., Surowy C.S., Mohrenweiser H.W.
      Genomics 8:371-379(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
    5. "Identification of an inhibitory element within the human 68-kDa (U1) ribonucleoprotein antigen."
      Northemann W., Berg H., Stahnke G., Walter M., Hunt N., Fenning S.
      Protein Expr. Purif. 6:748-756(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    6. "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] (ISOFORM 3).
      Tissue: Prostate.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Testis.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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] (ISOFORM 1).
      Tissue: Placenta.
    10. "Identification of an snRNP-associated kinase activity that phosphorylates arginine/serine rich domains typical of splicing factors."
      Woppmann A., Will C.L., Kornstaedt U., Zuo P., Manley J.L., Luehrmann R.
      Nucleic Acids Res. 21:2815-2822(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 219-348, PHOSPHORYLATION.
    11. Cited for: IDENTIFICATION IN A MRNA SPLICING COMPLEX WITH SFRS4; SFRS5; SNRPA1; SRRM1 AND SRRM2.
    12. "Sip1, a novel RS domain-containing protein essential for pre-mRNA splicing."
      Zhang W.-J., Wu J.Y.
      Mol. Cell. Biol. 18:676-684(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SCAF11.
    13. "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 SNRPA1; SRRM1 AND TRA2B.
    14. "ZNF265 -- a novel spliceosomal protein able to induce alternative splicing."
      Adams D.J., van der Weyden L., Mayeda A., Stamm S., Morris B.J., Rasko J.E.J.
      J. Cell Biol. 154:25-32(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZRANB2.
    15. "Nuclear relocalization of the pre-mRNA splicing factor PSF during apoptosis involves hyperphosphorylation, masking of antigenic epitopes, and changes in protein interactions."
      Shav-Tal Y., Cohen M., Lapter S., Dye B., Patton J.G., Vandekerckhove J., Zipori D.
      Mol. Biol. Cell 12:2328-2340(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SFPQ.
    16. "Association of polyadenylation cleavage factor I with U1 snRNP."
      Awasthi S., Alwine J.C.
      RNA 9:1400-1409(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NUDT21/CPSF5 AND CPSF6.
    17. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "Dephosphorylated SRp38 acts as a splicing repressor in response to heat shock."
      Shin C., Feng Y., Manley J.L.
      Nature 427:553-558(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SFRS13A.
    19. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-320 AND SER-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. "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 THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    25. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "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-320 AND SER-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    27. "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-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "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-226; SER-268; SER-320 AND SER-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-320 AND SER-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. "Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution."
      Pomeranz Krummel D.A., Oubridge C., Leung A.K., Li J., Nagai K.
      Nature 458:475-480(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (5.49 ANGSTROMS) OF 1-216 IN SPLICEOSOMAL U1 SNRNP.

    Entry informationi

    Entry nameiRU17_HUMAN
    AccessioniPrimary (citable) accession number: P08621
    Secondary accession number(s): B3KUA3
    , P78493, P78494, Q15364, Q15686, Q15687, Q15689, Q99377, Q9UE45, Q9UE46, Q9UE47, Q9UE48, Q9UFQ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 174 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

    Miscellaneous

    Major ribonucleoprotein antigen recognized by the sera from patients with autoimmune diseases, such as systemic lupus erythematosus.

    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