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Q15287

- RNPS1_HUMAN

UniProt

Q15287 - RNPS1_HUMAN

Protein

RNA-binding protein with serine-rich domain 1

Gene

RNPS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Part of pre- and post-splicing multiprotein mRNP complexes. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP and PSAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. The ASAP complex can inhibit RNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Enhances the formation of the ATP-dependent A complex of the spliceosome. Involved in both constitutive splicing and, in association with SRP54 and TRA2B/SFRS10, in distinctive modulation of alternative splicing in a substrate-dependent manner. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function. Participates in mRNA 3'-end cleavage. Involved in UPF2-dependent nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Also mediates increase of mRNA abundance and translational efficiency. Binds spliced mRNA 20-25 nt upstream of exon-exon junctions.10 Publications

    GO - Molecular functioni

    1. mRNA 3'-UTR binding Source: UniProtKB
    2. nucleotide binding Source: InterPro
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: IntAct
    5. RNA binding Source: ProtInc

    GO - Biological processi

    1. gene expression Source: Reactome
    2. mRNA 3'-end processing Source: Reactome
    3. mRNA export from nucleus Source: Reactome
    4. mRNA metabolic process Source: Reactome
    5. mRNA splicing, via spliceosome Source: Reactome
    6. negative regulation of mRNA splicing, via spliceosome Source: UniProtKB
    7. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
    8. positive regulation of apoptotic process Source: UniProtKB
    9. regulation of alternative mRNA splicing, via spliceosome Source: UniProtKB
    10. RNA metabolic process Source: Reactome
    11. RNA splicing Source: Reactome
    12. termination of RNA polymerase II transcription Source: Reactome
    13. transcription, DNA-templated Source: ProtInc
    14. transcription from RNA polymerase II promoter Source: Reactome

    Keywords - Biological processi

    mRNA processing, mRNA splicing, Nonsense-mediated mRNA decay

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_1597. Transport of Mature mRNA derived from an Intron-Containing Transcript.
    REACT_1849. mRNA 3'-end processing.
    REACT_467. mRNA Splicing - Major Pathway.
    REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

    Protein family/group databases

    TCDBi3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RNA-binding protein with serine-rich domain 1
    Alternative name(s):
    SR-related protein LDC2
    Gene namesi
    Name:RNPS1
    Synonyms:LDC2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:10080. RNPS1.

    Subcellular locationi

    Nucleus. Nucleus speckle. Cytoplasm
    Note: Nucleocytoplasmic shuttling protein. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles.

    GO - Cellular componenti

    1. ASAP complex Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: Reactome
    4. nuclear speck Source: UniProtKB-SubCell
    5. nucleoplasm Source: Reactome
    6. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi53 – 531S → A: Abolishes phosphorylation by CSNK2A1 and partially reduces splicing stimulation. Does not abolish interaction with CSNK2A1 and subcellular localization. 1 Publication
    Mutagenesisi53 – 531S → E: Partially reduces splicing stimulation. Does not abolish interaction with CSNK2A1 and subcellular localization. 1 Publication
    Mutagenesisi171 – 1711N → R: Impairs interaction with SAP18. 1 Publication
    Mutagenesisi205 – 2051Y → A: Abolishes exon-skipping. 1 Publication
    Mutagenesisi207 – 2071Y → A: Abolishes exon-skipping. 1 Publication

    Organism-specific databases

    PharmGKBiPA34453.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 305305RNA-binding protein with serine-rich domain 1PRO_0000081816Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei53 – 531Phosphoserine; by CK21 Publication
    Modified residuei155 – 1551Phosphoserine1 Publication
    Modified residuei157 – 1571Phosphoserine1 Publication
    Modified residuei161 – 1611Phosphothreonine1 Publication
    Modified residuei218 – 2181N6-acetyllysine1 Publication

    Post-translational modificationi

    Phosphorylated on one or more of the four Ser/Thr residues (Ser-43, Thr-49, Ser-52 or Ser-53). Ser-53 phosphorylation site is important for splicing and translation stimulation activity in vitro.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ15287.
    PaxDbiQ15287.
    PRIDEiQ15287.

    PTM databases

    PhosphoSiteiQ15287.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiQ15287.
    BgeeiQ15287.
    CleanExiHS_RNPS1.
    GenevestigatoriQ15287.

    Organism-specific databases

    HPAiHPA044014.

    Interactioni

    Subunit structurei

    Found in mRNA splicing-dependent exon junction complexes (EJC). Found in a post-splicing complex with NXF1, RBM8A, UPF1, UPF2, UPF3A, UPF3B and RNPS1. Component of the heterotrimeric ASAP (apoptosis- and splicing-associated protein) and PSAP complexes consisting of RNPS1, SAP18 and either ACIN1 or PNN, respectively; the ASAP and PSAP complexes probably are formed mutually exclusive. Component of the active spliceosome. Associates with polysomes. Interacts with the cleaved p110 isoform of CDC2L1, CSNK2A1, PNN, SART3, SRP54, SRRM1 and TRA2B/SFRS10.14 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SART3Q150205EBI-395959,EBI-308619
    SRPK1Q96SB42EBI-395959,EBI-539478

    Protein-protein interaction databases

    BioGridi116125. 114 interactions.
    DIPiDIP-32943N.
    IntActiQ15287. 26 interactions.
    MINTiMINT-1474621.

    Structurei

    Secondary structure

    1
    305
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi162 – 1665
    Helixi174 – 1829
    Beta strandi187 – 1915
    Beta strandi198 – 2025
    Beta strandi204 – 2129
    Helixi213 – 22311
    Beta strandi234 – 2385

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4A8XX-ray1.90A159-244[»]
    ProteinModelPortaliQ15287.
    SMRiQ15287. Positions 157-244.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini161 – 24080RRMPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 220220Necessary for interaction with the cleaved p110 isoform of CDC2L1Add
    BLAST
    Regioni1 – 161161Necessary for interaction with SRP54, nuclear localization and exon-skippingAdd
    BLAST
    Regioni69 – 12153Necessary for interactions with UPF2 and UPF3B and UPF2-dependent NMDAdd
    BLAST
    Regioni156 – 24287Necessary for interaction with PNN and exon-skippingAdd
    BLAST
    Regioni159 – 24486Interaction with SAP18 and ACIN1Add
    BLAST
    Regioni238 – 30568Necessary for interaction with TRA2B, nuclear localization and exon-skippingAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi7 – 6458Lys-richAdd
    BLAST
    Compositional biasi67 – 14175Ser-richAdd
    BLAST
    Compositional biasi128 – 15427Arg-richAdd
    BLAST
    Compositional biasi241 – 29858Arg/Pro-richAdd
    BLAST

    Domaini

    The RRM domain is required for the formation of the ASAP complex.

    Sequence similaritiesi

    Belongs to the splicing factor SR family.Curated
    Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG331533.
    HOVERGENiHBG053138.
    InParanoidiQ15287.
    KOiK14325.
    OMAiMIDMPAD.
    OrthoDBiEOG7Q5HGF.
    PhylomeDBiQ15287.
    TreeFamiTF314165.

    Family and domain databases

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

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15287-1) [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

    MDLSGVKKKS LLGVKENNKK SSTRAPSPTK RKDRSDEKSK DRSKDKGATK    50
    ESSEKDRGRD KTRKRRSASS GSSSTRSRSS STSSSGSSTS TGSSSGSSSS 100
    SASSRSGSSS TSRSSSSSSS SGSPSPSRRR HDNRRRSRSK SKPPKRDEKE 150
    RKRRSPSPKP TKVHIGRLTR NVTKDHIMEI FSTYGKIKMI DMPVERMHPH 200
    LSKGYAYVEF ENPDEAEKAL KHMDGGQIDG QEITATAVLA PWPRPPPRRF 250
    SPPRRMLPPP PMWRRSPPRM RRRSRSPRRR SPVRRRSRSP GRRRHRSRSS 300
    SNSSR 305
    Length:305
    Mass (Da):34,208
    Last modified:November 1, 1996 - v1
    Checksum:i930C9D36C2486144
    GO
    Isoform 2 (identifier: Q15287-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2-24: Missing.

    Show »
    Length:282
    Mass (Da):31,709
    Checksum:iD3F7AAD16B6309F4
    GO
    Isoform 3 (identifier: Q15287-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2-24: Missing.
         69-82: Missing.

    Show »
    Length:268
    Mass (Da):30,354
    Checksum:i9058DEEC9B433103
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti32 – 321K → E in BAG56859. (PubMed:14702039)Curated
    Sequence conflicti66 – 661R → G in AAC39791. (PubMed:9580558)Curated
    Sequence conflicti249 – 2491R → G in BAG56859. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 2423Missing in isoform 2 and isoform 3. 2 PublicationsVSP_016243Add
    BLAST
    Alternative sequencei69 – 8214Missing in isoform 3. 1 PublicationVSP_037601Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L37368 mRNA. Translation: AAA92859.1.
    AF015608 mRNA. Translation: AAC39791.1.
    AF274003 mRNA. Translation: AAL56665.1.
    AK289955 mRNA. Translation: BAF82644.1.
    AK293343 mRNA. Translation: BAG56859.1.
    AK303100 mRNA. Translation: BAG64209.1.
    AK316132 mRNA. Translation: BAH14503.1.
    AC009065 Genomic DNA. No translation available.
    CH471112 Genomic DNA. Translation: EAW85516.1.
    BC001659 mRNA. Translation: AAH01659.1.
    BC001838 mRNA. Translation: AAH01838.1.
    BC108316 mRNA. Translation: AAI08317.1.
    AF247662 mRNA. Translation: AAF72519.1.
    CCDSiCCDS10465.1. [Q15287-1]
    CCDS66907.1. [Q15287-2]
    PIRiJC4525.
    RefSeqiNP_001273554.1. NM_001286625.1. [Q15287-1]
    NP_001273555.1. NM_001286626.1. [Q15287-2]
    NP_001273556.1. NM_001286627.1.
    NP_006702.1. NM_006711.4. [Q15287-1]
    NP_542161.1. NM_080594.3. [Q15287-1]
    XP_005255105.1. XM_005255048.1. [Q15287-1]
    XP_005255106.1. XM_005255049.1. [Q15287-1]
    UniGeneiHs.355643.
    Hs.507343.
    Hs.733012.

    Genome annotation databases

    EnsembliENST00000301730; ENSP00000301730; ENSG00000205937. [Q15287-1]
    ENST00000320225; ENSP00000315859; ENSG00000205937. [Q15287-1]
    ENST00000397086; ENSP00000380275; ENSG00000205937. [Q15287-1]
    ENST00000565678; ENSP00000457723; ENSG00000205937. [Q15287-1]
    ENST00000566458; ENSP00000456352; ENSG00000205937. [Q15287-2]
    ENST00000568631; ENSP00000457820; ENSG00000205937. [Q15287-1]
    GeneIDi10921.
    KEGGihsa:10921.
    UCSCiuc002cpt.3. human. [Q15287-1]
    uc002cpx.3. human. [Q15287-2]

    Polymorphism databases

    DMDMi74754492.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L37368 mRNA. Translation: AAA92859.1 .
    AF015608 mRNA. Translation: AAC39791.1 .
    AF274003 mRNA. Translation: AAL56665.1 .
    AK289955 mRNA. Translation: BAF82644.1 .
    AK293343 mRNA. Translation: BAG56859.1 .
    AK303100 mRNA. Translation: BAG64209.1 .
    AK316132 mRNA. Translation: BAH14503.1 .
    AC009065 Genomic DNA. No translation available.
    CH471112 Genomic DNA. Translation: EAW85516.1 .
    BC001659 mRNA. Translation: AAH01659.1 .
    BC001838 mRNA. Translation: AAH01838.1 .
    BC108316 mRNA. Translation: AAI08317.1 .
    AF247662 mRNA. Translation: AAF72519.1 .
    CCDSi CCDS10465.1. [Q15287-1 ]
    CCDS66907.1. [Q15287-2 ]
    PIRi JC4525.
    RefSeqi NP_001273554.1. NM_001286625.1. [Q15287-1 ]
    NP_001273555.1. NM_001286626.1. [Q15287-2 ]
    NP_001273556.1. NM_001286627.1.
    NP_006702.1. NM_006711.4. [Q15287-1 ]
    NP_542161.1. NM_080594.3. [Q15287-1 ]
    XP_005255105.1. XM_005255048.1. [Q15287-1 ]
    XP_005255106.1. XM_005255049.1. [Q15287-1 ]
    UniGenei Hs.355643.
    Hs.507343.
    Hs.733012.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4A8X X-ray 1.90 A 159-244 [» ]
    ProteinModelPortali Q15287.
    SMRi Q15287. Positions 157-244.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116125. 114 interactions.
    DIPi DIP-32943N.
    IntActi Q15287. 26 interactions.
    MINTi MINT-1474621.

    Protein family/group databases

    TCDBi 3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

    PTM databases

    PhosphoSitei Q15287.

    Polymorphism databases

    DMDMi 74754492.

    Proteomic databases

    MaxQBi Q15287.
    PaxDbi Q15287.
    PRIDEi Q15287.

    Protocols and materials databases

    DNASUi 10921.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000301730 ; ENSP00000301730 ; ENSG00000205937 . [Q15287-1 ]
    ENST00000320225 ; ENSP00000315859 ; ENSG00000205937 . [Q15287-1 ]
    ENST00000397086 ; ENSP00000380275 ; ENSG00000205937 . [Q15287-1 ]
    ENST00000565678 ; ENSP00000457723 ; ENSG00000205937 . [Q15287-1 ]
    ENST00000566458 ; ENSP00000456352 ; ENSG00000205937 . [Q15287-2 ]
    ENST00000568631 ; ENSP00000457820 ; ENSG00000205937 . [Q15287-1 ]
    GeneIDi 10921.
    KEGGi hsa:10921.
    UCSCi uc002cpt.3. human. [Q15287-1 ]
    uc002cpx.3. human. [Q15287-2 ]

    Organism-specific databases

    CTDi 10921.
    GeneCardsi GC16M002303.
    H-InvDB HIX0031789.
    HGNCi HGNC:10080. RNPS1.
    HPAi HPA044014.
    MIMi 606447. gene.
    neXtProti NX_Q15287.
    PharmGKBi PA34453.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG331533.
    HOVERGENi HBG053138.
    InParanoidi Q15287.
    KOi K14325.
    OMAi MIDMPAD.
    OrthoDBi EOG7Q5HGF.
    PhylomeDBi Q15287.
    TreeFami TF314165.

    Enzyme and pathway databases

    Reactomei REACT_1597. Transport of Mature mRNA derived from an Intron-Containing Transcript.
    REACT_1849. mRNA 3'-end processing.
    REACT_467. mRNA Splicing - Major Pathway.
    REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

    Miscellaneous databases

    ChiTaRSi RNPS1. human.
    GeneWikii RNPS1.
    GenomeRNAii 10921.
    NextBioi 41487.
    PROi Q15287.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15287.
    Bgeei Q15287.
    CleanExi HS_RNPS1.
    Genevestigatori Q15287.

    Family and domain databases

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

    Publicationsi

    1. "Identification and characterisation of a novel human RNA-binding protein."
      Badolato J., Gardiner E., Morrison N., Eisman J.
      Gene 166:323-327(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Brain.
    2. "The RNP protein, RNPS1, associates with specific isoforms of the p34cdc2-related PITSLRE protein kinases in vivo."
      Loyer P., Trembley J.H., Lahti J.M., Kidd V.J.
      J. Cell Sci. 111:1495-1506(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CDC2L1, SUBCELLULAR LOCATION.
      Tissue: B-cell.
    3. "Identification of an alternatively spliced form of RNPS1."
      Harada K., Yang D., Yamada A., Shichijo S., Itoh K.
      Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Thymus.
    4. "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] (ISOFORMS 1; 2 AND 3).
      Tissue: Hippocampus and Tongue.
    5. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Muscle and Skin.
    8. "Direct interaction of LDC2, a SR-related protein with pinin."
      Lee D.-C., Ouyang P.
      Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 78-305.
      Tissue: Kidney.
    9. "Purification and characterization of human RNPS1: a general activator of pre-mRNA splicing."
      Mayeda A., Badolato J., Kobayashi R., Zhang M.Q., Gardiner E.M., Krainer A.R.
      EMBO J. 18:4560-4570(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PRE-MRNA SPLICING, ASSOCIATION WITH THE SPLICEOSOME, SUBCELLULAR LOCATION.
    10. "The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions."
      Le Hir H., Izaurralde E., Maquat L.E., Moore M.J.
      EMBO J. 19:6860-6869(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC) WITH DEK; RBM8A; SRRM1 AND ALYREF/THOC4.
    11. "Binding of a SART3 tumor-rejection antigen to a pre-mRNA splicing factor RNPS1: a possible regulation of splicing by a complex formation."
      Harada K., Yamada A., Yang D., Itoh K., Shichijo S.
      Int. J. Cancer 93:623-628(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SART3, SUBCELLULAR LOCATION.
    12. "Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1."
      Lykke-Andersen J., Shu M.-D., Steitz J.A.
      Science 293:1836-1839(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, IDENTIFICATION IN A POST-SPLICING COMPLEX WITH NXF1; RBM8A; UPF1; UPF2; UPF3A AND UPF3B, RNA-BINDING, SUBCELLULAR LOCATION.
    13. "An evolutionarily conserved role for SRm160 in 3'-end processing that functions independently of exon junction complex formation."
      McCracken S., Longman D., Johnstone I.L., Caceres J.F., Blencowe B.J.
      J. Biol. Chem. 278:44153-44160(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MRNA 3'-END FORMATION, INTERACTION WITH SRRM1.
    14. "Nuclear Pnn/DRS protein binds to spliced mRNPs and participates in mRNA processing and export via interaction with RNPS1."
      Li C., Lin R.-I., Lai M.-C., Ouyang P., Tarn W.-Y.
      Mol. Cell. Biol. 23:7363-7376(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A MRNP COMPLEX WITH PNN, INTERACTION WITH PNN, SUBCELLULAR LOCATION.
    15. "Splicing enhances translation in mammalian cells: an additional function of the exon junction complex."
      Nott A., Le Hir H., Moore M.J.
      Genes Dev. 18:210-222(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRANSLATIONAL ACTIVITY AND NONSENSE-MEDIATED MRNA DECAY, ASSOCIATION WITH POLYSOMES.
    16. "A simple whole cell lysate system for in vitro splicing reveals a stepwise assembly of the exon-exon junction complex."
      Kataoka N., Dreyfuss G.
      J. Biol. Chem. 279:7009-7013(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC) WITH RBM8A AND SRRM1.
    17. "Human RNPS1 and its associated factors: a versatile alternative pre-mRNA splicing regulator in vivo."
      Sakashita E., Tatsumi S., Werner D., Endo H., Mayeda A.
      Mol. Cell. Biol. 24:1174-1187(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ALTERNATIVE PRE-MRNA SPLICING, INTERACTION WITH PNN; SRP54 AND TRA2B, MUTAGENESIS OF TYR-205 AND TYR-207, SUBCELLULAR LOCATION.
    18. "Activation of pre-mRNA splicing by human RNPS1 is regulated by CK2 phosphorylation."
      Trembley J.H., Tatsumi S., Sakashita E., Loyer P., Slaughter C.A., Suzuki H., Endo H., Kidd V.J., Mayeda A.
      Mol. Cell. Biol. 25:1446-1457(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PRE-MRNA SPLICING, ASSOCIATION WITH THE ACTIVE SPLICEOSOME, PHOSPHORYLATION AT SER-53, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CSNK2A1, MUTAGENESIS OF SER-53, SUBCELLULAR LOCATION.
    19. "Exon-junction complex components specify distinct routes of nonsense-mediated mRNA decay with differential cofactor requirements."
      Gehring N.H., Kunz J.B., Neu-Yilik G., Breit S., Viegas M.H., Hentze M.W., Kulozik A.E.
      Mol. Cell 20:65-75(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN A RENT2-DEPENDENT NONSENSE-MEDIATED MRNA DECAY, IDENTIFICATION IN A COMPLEX WITH UPF2 AND UPF3B.
    20. Cited for: IDENTIFICATION IN THE ASAP COMPLEX, FUNCTION OF THE ASAP COMPLEX.
    21. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein core."
      Tange T.O., Shibuya T., Jurica M.S., Moore M.J.
      RNA 11:1869-1883(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX, IDENTIFICATION IN THE ASAP COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    23. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. "The abundance of RNPS1, a protein component of the exon junction complex, can determine the variability in efficiency of the nonsense mediated decay pathway."
      Viegas M.H., Gehring N.H., Breit S., Hentze M.W., Kulozik A.E.
      Nucleic Acids Res. 35:4542-4551(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY (NMD).
    25. "Assembly and mobility of exon-exon junction complexes in living cells."
      Schmidt U., Im K.-B., Benzing C., Janjetovic S., Rippe K., Lichter P., Wachsmuth M.
      RNA 15:862-876(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    26. "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-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Human SAP18 mediates assembly of a splicing regulatory multiprotein complex via its ubiquitin-like fold."
      Singh K.K., Erkelenz S., Rattay S., Dehof A.K., Hildebrandt A., Schulze-Osthoff K., Schaal H., Schwerk C.
      RNA 16:2442-2454(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SAP18 AND ACIN1.
    28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "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-155; SER-157 AND THR-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "Proteins associated with the exon junction complex also control the alternative splicing of apoptotic regulators."
      Michelle L., Cloutier A., Toutant J., Shkreta L., Thibault P., Durand M., Garneau D., Gendron D., Lapointe E., Couture S., Le Hir H., Klinck R., Elela S.A., Prinos P., Chabot B.
      Mol. Cell. Biol. 32:954-967(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    31. "The structure of the ASAP core complex reveals the existence of a Pinin-containing PSAP complex."
      Murachelli A.G., Ebert J., Basquin C., Le Hir H., Conti E.
      Nat. Struct. Mol. Biol. 19:378-386(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF THE ASAP COMPLEX, IDENTIFICATION IN THE PSAP COMPLEX, INTERACTION WITH SAP18, MUTAGENESIS OF ASN-171.

    Entry informationi

    Entry nameiRNPS1_HUMAN
    AccessioniPrimary (citable) accession number: Q15287
    Secondary accession number(s): A8K1P0
    , B4DDU8, B4DZU7, B7ZA17, O75308, Q32P25, Q8WY42, Q9NYG3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 22, 2005
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 142 of the entry and version 1 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, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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