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O43390

- HNRPR_HUMAN

UniProt

O43390 - HNRPR_HUMAN

Protein

Heterogeneous nuclear ribonucleoprotein R

Gene

HNRNPR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    Functioni

    Component of ribonucleosomes, which are complexes of at least 20 other different heterogenious nuclear ribonucleoproteins (hnRNP). hnRNP play an important role in processing of precursor mRNA in the nucleus.

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Molecular functioni

    Ribonucleoprotein

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_125. Processing of Capped Intron-Containing Pre-mRNA.
    REACT_467. mRNA Splicing - Major Pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heterogeneous nuclear ribonucleoprotein R
    Short name:
    hnRNP R
    Gene namesi
    Name:HNRNPR
    Synonyms:HNRPR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:5047. HNRNPR.

    Subcellular locationi

    Nucleusnucleoplasm 1 Publication. Cytoplasm 1 Publication
    Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. cytoplasm Source: UniProtKB-SubCell
    3. nucleoplasm Source: UniProtKB
    4. nucleus Source: HPA
    5. ribonucleoprotein complex Source: UniProtKB
    6. spliceosomal complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Spliceosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162391459.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 633632Heterogeneous nuclear ribonucleoprotein RPRO_0000081870Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei366 – 3661N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO43390.
    PaxDbiO43390.
    PeptideAtlasiO43390.
    PRIDEiO43390.

    PTM databases

    PhosphoSiteiO43390.

    Miscellaneous databases

    PMAP-CutDBO43390.

    Expressioni

    Gene expression databases

    ArrayExpressiO43390.
    BgeeiO43390.
    CleanExiHS_HNRNPR.
    GenevestigatoriO43390.

    Organism-specific databases

    HPAiCAB011687.
    HPA026092.

    Interactioni

    Subunit structurei

    Identified in the spliceosome C complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with GTPBP1.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NCK1P163332EBI-713419,EBI-389883

    Protein-protein interaction databases

    BioGridi115530. 154 interactions.
    IntActiO43390. 44 interactions.
    MINTiMINT-2796101.
    STRINGi9606.ENSP00000363745.

    Structurei

    Secondary structure

    1
    633
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi334 – 3385
    Beta strandi342 – 3476
    Helixi354 – 3629
    Beta strandi367 – 3737
    Beta strandi376 – 3838
    Helixi384 – 39411
    Beta strandi405 – 4084

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DK2NMR-A333-416[»]
    ProteinModelPortaliO43390.
    SMRiO43390. Positions 99-416.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO43390.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini165 – 24480RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini246 – 32883RRM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini341 – 41171RRM 3PROSITE-ProRule annotationAdd
    BLAST
    Repeati462 – 471101; approximate
    Repeati472 – 482112Add
    BLAST
    Repeati488 – 497103; approximate

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni447 – 567121RNA-binding RGG-boxAdd
    BLAST
    Regioni462 – 497363 X 11 AA approximate repeats of D-D-Y-Y-G-Y-D-Y-H-D-YAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi412 – 4187Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi2 – 153152Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi579 – 63355Asn/Gln-richAdd
    BLAST

    Sequence similaritiesi

    Contains 3 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG258596.
    HOGENOMiHOG000186082.
    HOVERGENiHBG051917.
    KOiK13161.
    OMAiYYPPPRM.
    OrthoDBiEOG73JKW2.
    PhylomeDBiO43390.
    TreeFamiTF314932.

    Family and domain databases

    Gene3Di3.30.70.330. 2 hits.
    InterProiIPR006535. HnRNP_R/Q_splicing_fac.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF00076. RRM_1. 3 hits.
    [Graphical view]
    SMARTiSM00360. RRM. 3 hits.
    [Graphical view]
    TIGRFAMsiTIGR01648. hnRNP-R-Q. 1 hit.
    PROSITEiPS50102. RRM. 3 hits.
    [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: O43390-1) [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

    MANQVNGNAV QLKEEEEPMD TSSVTHTEHY KTLIEAGLPQ KVAERLDEIF    50
    QTGLVAYVDL DERAIDALRE FNEEGALSVL QQFKESDLSH VQNKSAFLCG 100
    VMKTYRQREK QGSKVQESTK GPDEAKIKAL LERTGYTLDV TTGQRKYGGP 150
    PPDSVYSGVQ PGIGTEVFVG KIPRDLYEDE LVPLFEKAGP IWDLRLMMDP 200
    LSGQNRGYAF ITFCGKEAAQ EAVKLCDSYE IRPGKHLGVC ISVANNRLFV 250
    GSIPKNKTKE NILEEFSKVT EGLVDVILYH QPDDKKKNRG FCFLEYEDHK 300
    SAAQARRRLM SGKVKVWGNV VTVEWADPVE EPDPEVMAKV KVLFVRNLAT 350
    TVTEEILEKS FSEFGKLERV KKLKDYAFVH FEDRGAAVKA MDEMNGKEIE 400
    GEEIEIVLAK PPDKKRKERQ AARQASRSTA YEDYYYHPPP RMPPPIRGRG 450
    RGGGRGGYGY PPDYYGYEDY YDDYYGYDYH DYRGGYEDPY YGYDDGYAVR 500
    GRGGGRGGRG APPPPRGRGA PPPRGRAGYS QRGAPLGPPR GSRGGRGGPA 550
    QQQRGRGSRG SRGNRGGNVG GKRKADGYNQ PDSKRRQTNN QQNWGSQPIA 600
    QQPLQQGGDY SGNYGYNNDN QEFYQDTYGQ QWK 633
    Length:633
    Mass (Da):70,943
    Last modified:June 1, 1998 - v1
    Checksum:i088341F6465ED46F
    GO
    Isoform 2 (identifier: O43390-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         269-269: V → VTGL

    Show »
    Length:636
    Mass (Da):71,214
    Checksum:i4319EA79A1A6DED2
    GO
    Isoform 3 (identifier: O43390-3) [UniParc]FASTAAdd to Basket

    Also known as: hnRNP-R2

    The sequence of this isoform differs from the canonical sequence as follows:
         129-166: Missing.

    Note: Expression is low and neural-specific.

    Show »
    Length:595
    Mass (Da):66,980
    Checksum:iC9C67D917E7BCC44
    GO
    Isoform 4 (identifier: O43390-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-101: Missing.
         269-269: V → VTGL

    Note: No experimental confirmation available. Gene prediction based on EST data.

    Show »
    Length:535
    Mass (Da):59,953
    Checksum:iEDEE799FB18DE444
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 101101Missing in isoform 4. CuratedVSP_054703Add
    BLAST
    Alternative sequencei129 – 16638Missing in isoform 3. 1 PublicationVSP_047647Add
    BLAST
    Alternative sequencei269 – 2691V → VTGL in isoform 2 and isoform 4. 1 PublicationVSP_038360

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF000364 mRNA. Translation: AAC39540.1.
    DQ351905 mRNA. Translation: ABC73063.1.
    AL109936 Genomic DNA. Translation: CAI19026.1.
    AL109936 Genomic DNA. Translation: CAI19027.1.
    BC001449 mRNA. Translation: AAH01449.1.
    CCDSiCCDS232.1. [O43390-1]
    CCDS44085.1. [O43390-2]
    CCDS60020.1. [O43390-4]
    PIRiT02673.
    RefSeqiNP_001095867.1. NM_001102397.1.
    NP_001095868.1. NM_001102398.1. [O43390-2]
    NP_005817.1. NM_005826.3. [O43390-1]
    XP_005245768.1. XM_005245711.2. [O43390-1]
    XP_005245769.1. XM_005245712.2. [O43390-3]
    XP_005245770.1. XM_005245713.2. [O43390-3]
    UniGeneiHs.373763.

    Genome annotation databases

    EnsembliENST00000302271; ENSP00000304405; ENSG00000125944. [O43390-1]
    ENST00000374612; ENSP00000363741; ENSG00000125944. [O43390-1]
    ENST00000374616; ENSP00000363745; ENSG00000125944. [O43390-2]
    ENST00000427764; ENSP00000392799; ENSG00000125944. [O43390-3]
    ENST00000478691; ENSP00000474437; ENSG00000125944. [O43390-4]
    GeneIDi10236.
    KEGGihsa:10236.
    UCSCiuc001bgp.4. human. [O43390-2]
    uc001bgr.4. human. [O43390-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF000364 mRNA. Translation: AAC39540.1 .
    DQ351905 mRNA. Translation: ABC73063.1 .
    AL109936 Genomic DNA. Translation: CAI19026.1 .
    AL109936 Genomic DNA. Translation: CAI19027.1 .
    BC001449 mRNA. Translation: AAH01449.1 .
    CCDSi CCDS232.1. [O43390-1 ]
    CCDS44085.1. [O43390-2 ]
    CCDS60020.1. [O43390-4 ]
    PIRi T02673.
    RefSeqi NP_001095867.1. NM_001102397.1.
    NP_001095868.1. NM_001102398.1. [O43390-2 ]
    NP_005817.1. NM_005826.3. [O43390-1 ]
    XP_005245768.1. XM_005245711.2. [O43390-1 ]
    XP_005245769.1. XM_005245712.2. [O43390-3 ]
    XP_005245770.1. XM_005245713.2. [O43390-3 ]
    UniGenei Hs.373763.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DK2 NMR - A 333-416 [» ]
    ProteinModelPortali O43390.
    SMRi O43390. Positions 99-416.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115530. 154 interactions.
    IntActi O43390. 44 interactions.
    MINTi MINT-2796101.
    STRINGi 9606.ENSP00000363745.

    PTM databases

    PhosphoSitei O43390.

    Proteomic databases

    MaxQBi O43390.
    PaxDbi O43390.
    PeptideAtlasi O43390.
    PRIDEi O43390.

    Protocols and materials databases

    DNASUi 10236.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000302271 ; ENSP00000304405 ; ENSG00000125944 . [O43390-1 ]
    ENST00000374612 ; ENSP00000363741 ; ENSG00000125944 . [O43390-1 ]
    ENST00000374616 ; ENSP00000363745 ; ENSG00000125944 . [O43390-2 ]
    ENST00000427764 ; ENSP00000392799 ; ENSG00000125944 . [O43390-3 ]
    ENST00000478691 ; ENSP00000474437 ; ENSG00000125944 . [O43390-4 ]
    GeneIDi 10236.
    KEGGi hsa:10236.
    UCSCi uc001bgp.4. human. [O43390-2 ]
    uc001bgr.4. human. [O43390-1 ]

    Organism-specific databases

    CTDi 10236.
    GeneCardsi GC01M023630.
    HGNCi HGNC:5047. HNRNPR.
    HPAi CAB011687.
    HPA026092.
    MIMi 607201. gene.
    neXtProti NX_O43390.
    PharmGKBi PA162391459.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG258596.
    HOGENOMi HOG000186082.
    HOVERGENi HBG051917.
    KOi K13161.
    OMAi YYPPPRM.
    OrthoDBi EOG73JKW2.
    PhylomeDBi O43390.
    TreeFami TF314932.

    Enzyme and pathway databases

    Reactomei REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
    REACT_467. mRNA Splicing - Major Pathway.

    Miscellaneous databases

    ChiTaRSi HNRNPR. human.
    EvolutionaryTracei O43390.
    GeneWikii HNRNPR.
    GenomeRNAii 10236.
    NextBioi 38770.
    PMAP-CutDB O43390.
    PROi O43390.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43390.
    Bgeei O43390.
    CleanExi HS_HNRNPR.
    Genevestigatori O43390.

    Family and domain databases

    Gene3Di 3.30.70.330. 2 hits.
    InterProi IPR006535. HnRNP_R/Q_splicing_fac.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF00076. RRM_1. 3 hits.
    [Graphical view ]
    SMARTi SM00360. RRM. 3 hits.
    [Graphical view ]
    TIGRFAMsi TIGR01648. hnRNP-R-Q. 1 hit.
    PROSITEi PS50102. RRM. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular definition of heterogeneous nuclear ribonucleoprotein R (hnRNP R) using autoimmune antibody: immunological relationship with hnRNP P."
      Hassfeld W., Chan E.K.L., Mathison D.A., Portman D., Dreyfuss G., Steiner G., Tan E.M.
      Nucleic Acids Res. 26:439-445(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Cloning and expression of a novel isoform of heterogeneous nuclear ribonucleoprotein-R."
      Huang J., Chen X.H., Wu K., Xu P.
      NeuroReport 16:727-730(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
      Tissue: Brain.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 2).
      Tissue: Placenta.
    5. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-13; 32-41; 70-84; 95-103; 134-145; 175-216; 225-255; 258-285; 290-300; 347-366; 373-384; 398-414 AND 428-441, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Ovarian carcinoma.
    6. Lubec G., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 32-41 AND 347-359, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain.
    7. "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.
    8. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Modulation of exosome-mediated mRNA turnover by interaction of GTP-binding protein 1 (GTPBP1) with its target mRNAs."
      Woo K.C., Kim T.D., Lee K.H., Kim D.Y., Kim S., Lee H.R., Kang H.J., Chung S.J., Senju S., Nishimura Y., Kim K.T.
      FASEB J. 25:2757-2769(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GTPBP1.
    13. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Solution structure of RRM domain in heterogeneous nuclear ribonucleoprotein R (HNRNP R)."
      RIKEN structural genomics initiative (RSGI)
      Submitted (OCT-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 333-416.

    Entry informationi

    Entry nameiHNRPR_HUMAN
    AccessioniPrimary (citable) accession number: O43390
    Secondary accession number(s): Q2L7G6
    , Q5TEH1, Q9BV64, S4R3J4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 150 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 1
      Human chromosome 1: 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