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Q9UMS4

- PRP19_HUMAN

UniProt

Q9UMS4 - PRP19_HUMAN

Protein

Pre-mRNA-processing factor 19

Gene

PRPF19

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Plays a role in DNA double-strand break (DSB) repair. Binds double-stranded DNA in a sequence-nonspecific manner. Acts as a structural component of the nuclear framework. May also serve as a support for spliceosome binding and activity. Essential for spliceosome assembly in a oligomerization-dependent manner and might also be important for spliceosome stability. May have E3 ubiquitin ligase activity. The PSO4 complex is required in the DNA interstrand cross-links (ICLs) repair process. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing.6 Publications

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. identical protein binding Source: BHF-UCL
    3. protein binding Source: UniProtKB
    4. ubiquitin-protein transferase activity Source: MGI
    5. ubiquitin-ubiquitin ligase activity Source: MGI

    GO - Biological processi

    1. DNA repair Source: UniProtKB-KW
    2. inner cell mass cell proliferation Source: Ensembl
    3. lipid biosynthetic process Source: Ensembl
    4. mRNA splicing, via spliceosome Source: UniProtKB
    5. negative regulation of neuron differentiation Source: Ensembl
    6. positive regulation of astrocyte differentiation Source: Ensembl
    7. positive regulation of mRNA splicing, via spliceosome Source: Ensembl
    8. protein polyubiquitination Source: MGI
    9. spliceosomal complex assembly Source: BHF-UCL

    Keywords - Biological processi

    DNA damage, DNA repair, mRNA processing, mRNA splicing

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    SignaLinkiQ9UMS4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pre-mRNA-processing factor 19
    Alternative name(s):
    Nuclear matrix protein 200
    PRP19/PSO4 homolog
    Short name:
    hPso4
    Senescence evasion factor
    Gene namesi
    Name:PRPF19
    Synonyms:NMP200, PRP19, SNEV
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:17896. PRPF19.

    Subcellular locationi

    Nucleus. Nucleusnucleoplasm. Cytoplasmcytoskeletonspindle
    Note: Nucleoplasmic in interphase cells. Irregularly distributed in anaphase cells. In prophase cells, uniformly distributed, but not associated with condensing chromosomes. Found in extrachromosomal regions in metaphase cells. Mainly localized to the mitotic spindle apparatus when chromosomes segregate during anaphase. When nuclei reform during late telophase, uniformly distributed in daughter cells and displays no preferred association with decondensing chromatin.

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. cytoplasm Source: MGI
    3. lipid particle Source: Ensembl
    4. membrane Source: UniProtKB
    5. nuclear speck Source: BHF-UCL
    6. nucleus Source: UniProtKB
    7. Prp19 complex Source: UniProtKB
    8. spindle Source: UniProtKB-SubCell
    9. ubiquitin ligase complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus, Spliceosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134941355.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 504503Pre-mRNA-processing factor 19PRO_0000051145Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine4 Publications
    Modified residuei122 – 1221N6-acetyllysine1 Publication
    Modified residuei179 – 1791N6-acetyllysineBy similarity
    Modified residuei244 – 2441N6-acetyllysineBy similarity
    Modified residuei261 – 2611N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9UMS4.
    PaxDbiQ9UMS4.
    PeptideAtlasiQ9UMS4.
    PRIDEiQ9UMS4.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00004968.
    SWISS-2DPAGEQ9UMS4.

    PTM databases

    PhosphoSiteiQ9UMS4.

    Expressioni

    Tissue specificityi

    Ubiquitous. Weakly expressed in senescent cells of different tissue origins. Highly expressed in tumor cell lines.4 Publications

    Inductioni

    By gamma irradiation and chemical mutagens but not by UV irradiation.1 Publication

    Gene expression databases

    ArrayExpressiQ9UMS4.
    BgeeiQ9UMS4.
    CleanExiHS_PRPF19.
    GenevestigatoriQ9UMS4.

    Organism-specific databases

    HPAiCAB012448.
    HPA038051.

    Interactioni

    Subunit structurei

    Homooligomer. Identified in the spliceosome C complex. Component of the PSO4 complex, composed of PRPF19, CDC5L, PLRG1. Component of the PRP19-CDC5L splicing complex composed of a core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less stably associated proteins CTNNBL1, CWC15 and HSPA8. Interacts in the complex directly with CDC5L, PLRG1 and BCAS2. Interacts with APEX1, DNTT and PSMB4. Interacts with CWC22 and EIF4A3 in an RNA-independent manner.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BCAS2O759342EBI-395746,EBI-1050106
    CDC40O605082EBI-395746,EBI-2557812
    CDC5LQ994592EBI-395746,EBI-374880
    PRPF8Q6P2Q92EBI-395746,EBI-538479
    RBM10P981752EBI-395746,EBI-721525
    RBM5P527568EBI-395746,EBI-714003

    Protein-protein interaction databases

    BioGridi118151. 104 interactions.
    IntActiQ9UMS4. 32 interactions.
    MINTiMINT-1454442.
    STRINGi9606.ENSP00000227524.

    Structurei

    Secondary structure

    1
    504
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi201 – 2044
    Beta strandi208 – 2136
    Beta strandi219 – 2213
    Beta strandi224 – 2307
    Beta strandi233 – 2419
    Beta strandi246 – 2505
    Turni251 – 2544
    Beta strandi255 – 2606
    Beta strandi269 – 2724
    Beta strandi276 – 2827
    Beta strandi288 – 2925
    Turni293 – 2964
    Beta strandi297 – 3026
    Beta strandi309 – 3146
    Beta strandi318 – 3258
    Beta strandi328 – 3347
    Turni335 – 3373
    Beta strandi340 – 3456
    Turni347 – 3493
    Beta strandi353 – 3586
    Beta strandi362 – 3698
    Beta strandi374 – 3785
    Turni379 – 3824
    Beta strandi383 – 3886
    Beta strandi395 – 4006
    Beta strandi404 – 4118
    Beta strandi414 – 4207
    Turni421 – 4244
    Beta strandi425 – 4317
    Beta strandi438 – 4436
    Beta strandi447 – 46115
    Turni462 – 4654
    Beta strandi466 – 4716
    Beta strandi474 – 4763
    Beta strandi478 – 4836
    Helixi485 – 4873
    Beta strandi490 – 4945
    Beta strandi499 – 5035

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4LG8X-ray1.89A169-504[»]
    ProteinModelPortaliQ9UMS4.
    SMRiQ9UMS4. Positions 3-55, 195-504.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 7372U-boxAdd
    BLAST
    Repeati219 – 25941WD 1Add
    BLAST
    Repeati262 – 30140WD 2Add
    BLAST
    Repeati304 – 34542WD 3Add
    BLAST
    Repeati348 – 38740WD 4Add
    BLAST
    Repeati390 – 42940WD 5Add
    BLAST
    Repeati433 – 47240WD 6Add
    BLAST
    Repeati473 – 50331WD 7Add
    BLAST

    Sequence similaritiesi

    Belongs to the WD repeat PRP19 family.Curated
    Contains 1 U-box domain.Curated
    Contains 7 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    HOGENOMiHOG000177308.
    HOVERGENiHBG053697.
    InParanoidiQ9UMS4.
    KOiK10599.
    OMAiQWQELKV.
    OrthoDBiEOG7K9K2R.
    PhylomeDBiQ9UMS4.
    TreeFamiTF105919.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    3.30.40.10. 1 hit.
    InterProiIPR020472. G-protein_beta_WD-40_rep.
    IPR013915. Pre-mRNA_splic_Prp19.
    IPR000772. Ricin_B_lectin.
    IPR003613. Ubox_domain.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF08606. Prp19. 1 hit.
    PF04564. U-box. 1 hit.
    PF00400. WD40. 5 hits.
    [Graphical view]
    PRINTSiPR00320. GPROTEINBRPT.
    SMARTiSM00504. Ubox. 1 hit.
    SM00320. WD40. 7 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 1 hit.
    PROSITEiPS51698. U_BOX. 1 hit.
    PS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 4 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9UMS4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLICSISNE VPEHPCVSPV SNHVYERRLI EKYIAENGTD PINNQPLSEE    50
    QLIDIKVAHP IRPKPPSATS IPAILKALQD EWDAVMLHSF TLRQQLQTTR 100
    QELSHALYQH DAACRVIARL TKEVTAAREA LATLKPQAGL IVPQAVPSSQ 150
    PSVVGAGEPM DLGELVGMTP EIIQKLQDKA TVLTTERKKR GKTVPEELVK 200
    PEELSKYRQV ASHVGLHSAS IPGILALDLC PSDTNKILTG GADKNVVVFD 250
    KSSEQILATL KGHTKKVTSV VFHPSQDLVF SASPDATIRI WSVPNASCVQ 300
    VVRAHESAVT GLSLHATGDY LLSSSDDQYW AFSDIQTGRV LTKVTDETSG 350
    CSLTCAQFHP DGLIFGTGTM DSQIKIWDLK ERTNVANFPG HSGPITSIAF 400
    SENGYYLATA ADDSSVKLWD LRKLKNFKTL QLDNNFEVKS LIFDQSGTYL 450
    ALGGTDVQIY ICKQWTEILH FTEHSGLTTG VAFGHHAKFI ASTGMDRSLK 500
    FYSL 504
    Length:504
    Mass (Da):55,181
    Last modified:May 1, 2000 - v1
    Checksum:iB34C37496E8AA032
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ131186 mRNA. Translation: CAB51857.1.
    BC008719 mRNA. Translation: AAH08719.1.
    BC018665 mRNA. Translation: AAH18665.1.
    BC018698 mRNA. Translation: AAH18698.1.
    CCDSiCCDS7995.1.
    RefSeqiNP_055317.1. NM_014502.4.
    UniGeneiHs.502705.

    Genome annotation databases

    EnsembliENST00000227524; ENSP00000227524; ENSG00000110107.
    GeneIDi27339.
    KEGGihsa:27339.
    UCSCiuc001nqf.3. human.

    Polymorphism databases

    DMDMi55976619.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ131186 mRNA. Translation: CAB51857.1 .
    BC008719 mRNA. Translation: AAH08719.1 .
    BC018665 mRNA. Translation: AAH18665.1 .
    BC018698 mRNA. Translation: AAH18698.1 .
    CCDSi CCDS7995.1.
    RefSeqi NP_055317.1. NM_014502.4.
    UniGenei Hs.502705.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4LG8 X-ray 1.89 A 169-504 [» ]
    ProteinModelPortali Q9UMS4.
    SMRi Q9UMS4. Positions 3-55, 195-504.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118151. 104 interactions.
    IntActi Q9UMS4. 32 interactions.
    MINTi MINT-1454442.
    STRINGi 9606.ENSP00000227524.

    PTM databases

    PhosphoSitei Q9UMS4.

    Polymorphism databases

    DMDMi 55976619.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00004968.
    SWISS-2DPAGE Q9UMS4.

    Proteomic databases

    MaxQBi Q9UMS4.
    PaxDbi Q9UMS4.
    PeptideAtlasi Q9UMS4.
    PRIDEi Q9UMS4.

    Protocols and materials databases

    DNASUi 27339.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000227524 ; ENSP00000227524 ; ENSG00000110107 .
    GeneIDi 27339.
    KEGGi hsa:27339.
    UCSCi uc001nqf.3. human.

    Organism-specific databases

    CTDi 27339.
    GeneCardsi GC11M060658.
    HGNCi HGNC:17896. PRPF19.
    HPAi CAB012448.
    HPA038051.
    MIMi 608330. gene.
    neXtProti NX_Q9UMS4.
    PharmGKBi PA134941355.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2319.
    HOGENOMi HOG000177308.
    HOVERGENi HBG053697.
    InParanoidi Q9UMS4.
    KOi K10599.
    OMAi QWQELKV.
    OrthoDBi EOG7K9K2R.
    PhylomeDBi Q9UMS4.
    TreeFami TF105919.

    Enzyme and pathway databases

    SignaLinki Q9UMS4.

    Miscellaneous databases

    GeneWikii PRPF19.
    GenomeRNAii 27339.
    NextBioi 50404.
    PROi Q9UMS4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UMS4.
    Bgeei Q9UMS4.
    CleanExi HS_PRPF19.
    Genevestigatori Q9UMS4.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    3.30.40.10. 1 hit.
    InterProi IPR020472. G-protein_beta_WD-40_rep.
    IPR013915. Pre-mRNA_splic_Prp19.
    IPR000772. Ricin_B_lectin.
    IPR003613. Ubox_domain.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF08606. Prp19. 1 hit.
    PF04564. U-box. 1 hit.
    PF00400. WD40. 5 hits.
    [Graphical view ]
    PRINTSi PR00320. GPROTEINBRPT.
    SMARTi SM00504. Ubox. 1 hit.
    SM00320. WD40. 7 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 1 hit.
    PROSITEi PS51698. U_BOX. 1 hit.
    PS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 4 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "hNMP 200: a novel human common nuclear matrix protein combining structural and regulatory functions."
      Gotzmann J., Gerner C., Meissner M., Holzmann K., Grimm R., Mikulits W., Sauermann G.
      Exp. Cell Res. 261:166-179(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 32-40; 100-115; 179-187; 192-199 AND 334-342, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CHROMOSOMAL LOCATION.
      Tissue: Cervix.
    2. "Role of human Pso4 in mammalian DNA repair and association with terminal deoxynucleotidyl transferase."
      Mahajan K.N., Mitchell B.S.
      Proc. Natl. Acad. Sci. U.S.A. 100:10746-10751(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION, INTERACTION WITH DNTT.
    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: Muscle.
    4. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-27; 33-56; 77-93; 101-115; 193-206; 209-236; 252-261 AND 266-303, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma.
    5. Bienvenut W.V.
      Submitted (JAN-2010) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-27; 33-56; 63-93; 101-115; 193-206; 209-261; 266-303; 344-375 AND 429-439, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Ovarian carcinoma.
    6. "Reassembling proteins and chaperones in human nuclear matrix protein fractions."
      Gerner C., Holzmann K., Meissner M., Gotzmann J., Grimm R., Sauermann G.
      J. Cell. Biochem. 74:145-151(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 32-40, TISSUE SPECIFICITY.
      Tissue: Peripheral blood.
    7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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. "SNEV is an evolutionarily conserved splicing factor whose oligomerization is necessary for spliceosome assembly."
      Grillari J., Ajuh P., Stadler G., Loescher M., Voglauer R., Ernst W., Chusainow J., Eisenhaber F., Pokar M., Fortschegger K., Grey M., Lamond A.I., Katinger H.
      Nucleic Acids Res. 33:6868-6883(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    10. "Interaction of U-box E3 ligase SNEV with PSMB4, the beta7 subunit of the 20 S proteasome."
      Loescher M., Fortschegger K., Ritter G., Wostry M., Voglauer R., Schmid J.A., Watters S., Rivett A.J., Ajuh P., Lamond A.I., Katinger H., Grillari J.
      Biochem. J. 388:593-603(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PSMB4, FUNCTION.
    11. "The Pso4 mRNA splicing and DNA repair complex interacts with WRN for processing of DNA interstrand cross-links."
      Zhang N., Kaur R., Lu X., Shen X., Li L., Legerski R.J.
      J. Biol. Chem. 280:40559-40567(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    12. Cited for: FUNCTION, TISSUE SPECIFICITY.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in the rRNA quality control process."
      Vascotto C., Fantini D., Romanello M., Cesaratto L., Deganuto M., Leonardi A., Radicella J.P., Kelley M.R., D'Ambrosio C., Scaloni A., Quadrifoglio F., Tell G.
      Mol. Cell. Biol. 29:1834-1854(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APEX1, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    16. "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-122 AND LYS-261, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: IDENTIFICATION AS A COMPONENT OF THE PRP19-CDC5L SPLICING COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH CDC5L; PLRG1 AND BCAS2.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Human CWC22 escorts the helicase eIF4AIII to spliceosomes and promotes exon junction complex assembly."
      Barbosa I., Haque N., Fiorini F., Barrandon C., Tomasetto C., Blanchette M., Le Hir H.
      Nat. Struct. Mol. Biol. 19:983-990(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CWC22 AND EIF4A3.

    Entry informationi

    Entry nameiPRP19_HUMAN
    AccessioniPrimary (citable) accession number: Q9UMS4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 23, 2004
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 127 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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