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P14866

- HNRPL_HUMAN

UniProt

P14866 - HNRPL_HUMAN

Protein

Heterogeneous nuclear ribonucleoprotein L

Gene

HNRNPL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 2 (25 Nov 2008)
      Previous versions | rss
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    Functioni

    Splicing factor binding to exonic or intronic sites and acting as either an activator or repressor of exon inclusion. Exhibits a binding preference for CA-rich elements. Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and associated with most nascent transcripts. Associates, together with APEX1, to the negative calcium responsive element (nCaRE) B2 of the APEX2 promoter.1 Publication

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. RNA binding Source: ProtInc
    5. transcription regulatory region DNA binding Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Ribonucleoprotein

    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 L
    Short name:
    hnRNP L
    Gene namesi
    Name:HNRNPL
    Synonyms:HNRPL
    ORF Names:P/OKcl.14
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:5045. HNRNPL.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt
    3. membrane Source: UniProtKB
    4. nucleoplasm Source: Reactome
    5. nucleus Source: MGI
    6. ribonucleoprotein complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi105 – 1051H → A: 6-fold decrease in RNA-binding affinity. 1 Publication
    Mutagenesisi132 – 1321V → A: 4-fold increase in RNA-binding affinity. 1 Publication
    Mutagenesisi141 – 1411L → A: 15-fold decrease in RNA-binding affinity; when associated with A-174. 1 Publication
    Mutagenesisi172 – 1721N → A: 1-fold increase in RNA-binding affinity. 1 Publication
    Mutagenesisi174 – 1741S → A: 15-fold decrease in RNA-binding affinity; when associated with A-174. 1 Publication
    Mutagenesisi504 – 5041H → A: Significant decrease in RNA-binding affinity. 1 Publication
    Mutagenesisi506 – 5061F → A: Significant decrease in RNA-binding affinity. 1 Publication

    Organism-specific databases

    PharmGKBiPA162391389.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 589589Heterogeneous nuclear ribonucleoprotein LPRO_0000081862Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei52 – 521Phosphoserine3 Publications
    Modified residuei101 – 1011Phosphoserine1 Publication
    Modified residuei185 – 1851Phosphoserine2 Publications
    Modified residuei269 – 2691N6-acetyllysine1 Publication
    Modified residuei291 – 2911Phosphoserine1 Publication
    Modified residuei298 – 2981Phosphoserine3 Publications
    Modified residuei544 – 5441Phosphoserine; by CaMK41 Publication

    Post-translational modificationi

    Several isoelectric forms of the L protein are probably the results of post-translational modifications.
    Phosphorylation at Ser-544 by CaMK4 enhances interaction with a CaMK4-responsive RNA element (CaRRE1), and prevents inclusion of the stress axis-regulated exon (STREX) of the KCNMA1 potassium channel transcripts upon membrane depolarization.4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP14866.
    PaxDbiP14866.
    PRIDEiP14866.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00027834.
    SWISS-2DPAGEP14866.

    PTM databases

    PhosphoSiteiP14866.

    Expressioni

    Gene expression databases

    ArrayExpressiP14866.
    BgeeiP14866.
    CleanExiHS_HNRNPL.
    GenevestigatoriP14866.

    Organism-specific databases

    HPAiCAB016326.
    HPA051748.

    Interactioni

    Subunit structurei

    Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with HNRNPLL. Interacts with APEX1; the interaction is DNA-dependent. Component of a complex with SETD2.4 Publications

    Protein-protein interaction databases

    BioGridi109432. 78 interactions.
    DIPiDIP-36355N.
    IntActiP14866. 30 interactions.
    MINTiMINT-1422378.
    STRINGi9606.ENSP00000221419.

    Structurei

    Secondary structure

    1
    589
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi102 – 1087
    Helixi115 – 1228
    Helixi123 – 1253
    Beta strandi128 – 1347
    Turni135 – 1384
    Beta strandi139 – 1468
    Helixi147 – 15913
    Beta strandi162 – 1643
    Beta strandi167 – 1737
    Beta strandi382 – 3876
    Turni391 – 3933
    Helixi396 – 4038
    Turni404 – 4063
    Beta strandi409 – 4146
    Beta strandi421 – 4288
    Helixi429 – 43911
    Beta strandi450 – 4534
    Beta strandi472 – 4765
    Helixi488 – 4914
    Beta strandi501 – 5088
    Helixi514 – 52411
    Beta strandi530 – 5345
    Beta strandi543 – 5486
    Helixi552 – 56211
    Beta strandi572 – 5743
    Beta strandi579 – 5824

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3R27X-ray2.04A/B90-180[»]
    3TO8X-ray1.82A380-589[»]
    ProteinModelPortaliP14866.
    SMRiP14866. Positions 97-290, 379-582.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini102 – 17675RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini193 – 27078RRM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini382 – 47897RRM 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini495 – 58389RRM 4PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi39 – 8951Gly-richAdd
    BLAST
    Compositional biasi335 – 38248Pro-richAdd
    BLAST

    Domaini

    RRM domain 2 has moderate RNA-binding affinity. RRM domains 3 and 4 may facilitate RNA looping when binding to two appropriately separated binding sites within the same target pre-mRNA (PubMed:23782695).1 Publication

    Sequence similaritiesi

    Contains 4 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG326285.
    HOGENOMiHOG000293298.
    HOVERGENiHBG105786.
    InParanoidiP14866.
    KOiK13159.
    OMAiPYEGRRM.
    OrthoDBiEOG7HMS2K.
    PhylomeDBiP14866.
    TreeFamiTF354318.

    Family and domain databases

    Gene3Di3.30.70.330. 4 hits.
    InterProiIPR006536. HnRNP-L_PTB.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    SMARTiSM00360. RRM. 3 hits.
    [Graphical view]
    TIGRFAMsiTIGR01649. hnRNP-L_PTB. 1 hit.
    PROSITEiPS50102. RRM. 3 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P14866-1) [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

    MSRRLLPRAE KRRRRLEQRQ QPDEQRRRSG AMVKMAAAGG GGGGGRYYGG    50
    GSEGGRAPKR LKTDNAGDQH GGGGGGGGGA GAAGGGGGGE NYDDPHKTPA 100
    SPVVHIRGLI DGVVEADLVE ALQEFGPISY VVVMPKKRQA LVEFEDVLGA 150
    CNAVNYAADN QIYIAGHPAF VNYSTSQKIS RPGDSDDSRS VNSVLLFTIL 200
    NPIYSITTDV LYTICNPCGP VQRIVIFRKN GVQAMVEFDS VQSAQRAKAS 250
    LNGADIYSGC CTLKIEYAKP TRLNVFKNDQ DTWDYTNPNL SGQGDPGSNP 300
    NKRQRQPPLL GDHPAEYGGP HGGYHSHYHD EGYGPPPPHY EGRRMGPPVG 350
    GHRRGPSRYG PQYGHPPPPP PPPEYGPHAD SPVLMVYGLD QSKMNCDRVF 400
    NVFCLYGNVE KVKFMKSKPG AAMVEMADGY AVDRAITHLN NNFMFGQKLN 450
    VCVSKQPAIM PGQSYGLEDG SCSYKDFSES RNNRFSTPEQ AAKNRIQHPS 500
    NVLHFFNAPL EVTEENFFEI CDELGVKRPS SVKVFSGKSE RSSSGLLEWE 550
    SKSDALETLG FLNHYQMKNP NGPYPYTLKL CFSTAQHAS 589
    Length:589
    Mass (Da):64,133
    Last modified:November 25, 2008 - v2
    Checksum:i31EEB51AF1C65F83
    GO
    Isoform 2 (identifier: P14866-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-133: Missing.

    Show »
    Length:456
    Mass (Da):50,561
    Checksum:i59DD6B10F1F41E68
    GO

    Sequence cautioni

    The sequence CAA34261.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti396 – 3961C → G in BAB18649. (PubMed:11280764)Curated
    Sequence conflicti396 – 3961C → G in CAA34261. (PubMed:2687284)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 133133Missing in isoform 2. 1 PublicationVSP_044301Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB044547 mRNA. Translation: BAB18649.1.
    AK292115 mRNA. Translation: BAF84804.1.
    AC008982 Genomic DNA. No translation available.
    CH471126 Genomic DNA. Translation: EAW56828.1.
    X16135 mRNA. Translation: CAA34261.1. Different initiation.
    CCDSiCCDS33015.1. [P14866-1]
    CCDS33016.1. [P14866-2]
    PIRiA33616.
    RefSeqiNP_001005335.1. NM_001005335.1. [P14866-2]
    NP_001524.2. NM_001533.2. [P14866-1]
    UniGeneiHs.644906.

    Genome annotation databases

    EnsembliENST00000221419; ENSP00000221419; ENSG00000104824. [P14866-1]
    ENST00000600873; ENSP00000470231; ENSG00000104824. [P14866-2]
    GeneIDi3191.
    KEGGihsa:3191.
    UCSCiuc002ojk.3. human. [P14866-2]
    uc021uuh.1. human. [P14866-1]

    Polymorphism databases

    DMDMi215274006.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB044547 mRNA. Translation: BAB18649.1 .
    AK292115 mRNA. Translation: BAF84804.1 .
    AC008982 Genomic DNA. No translation available.
    CH471126 Genomic DNA. Translation: EAW56828.1 .
    X16135 mRNA. Translation: CAA34261.1 . Different initiation.
    CCDSi CCDS33015.1. [P14866-1 ]
    CCDS33016.1. [P14866-2 ]
    PIRi A33616.
    RefSeqi NP_001005335.1. NM_001005335.1. [P14866-2 ]
    NP_001524.2. NM_001533.2. [P14866-1 ]
    UniGenei Hs.644906.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3R27 X-ray 2.04 A/B 90-180 [» ]
    3TO8 X-ray 1.82 A 380-589 [» ]
    ProteinModelPortali P14866.
    SMRi P14866. Positions 97-290, 379-582.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109432. 78 interactions.
    DIPi DIP-36355N.
    IntActi P14866. 30 interactions.
    MINTi MINT-1422378.
    STRINGi 9606.ENSP00000221419.

    PTM databases

    PhosphoSitei P14866.

    Polymorphism databases

    DMDMi 215274006.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00027834.
    SWISS-2DPAGE P14866.

    Proteomic databases

    MaxQBi P14866.
    PaxDbi P14866.
    PRIDEi P14866.

    Protocols and materials databases

    DNASUi 3191.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000221419 ; ENSP00000221419 ; ENSG00000104824 . [P14866-1 ]
    ENST00000600873 ; ENSP00000470231 ; ENSG00000104824 . [P14866-2 ]
    GeneIDi 3191.
    KEGGi hsa:3191.
    UCSCi uc002ojk.3. human. [P14866-2 ]
    uc021uuh.1. human. [P14866-1 ]

    Organism-specific databases

    CTDi 3191.
    GeneCardsi GC19M039327.
    H-InvDB HIX0174642.
    HGNCi HGNC:5045. HNRNPL.
    HPAi CAB016326.
    HPA051748.
    MIMi 164021. gene.
    603083. gene.
    neXtProti NX_P14866.
    PharmGKBi PA162391389.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG326285.
    HOGENOMi HOG000293298.
    HOVERGENi HBG105786.
    InParanoidi P14866.
    KOi K13159.
    OMAi PYEGRRM.
    OrthoDBi EOG7HMS2K.
    PhylomeDBi P14866.
    TreeFami TF354318.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi HNRNPL. human.
    GeneWikii HNRNPL.
    GenomeRNAii 3191.
    NextBioi 12694.
    PROi P14866.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P14866.
    Bgeei P14866.
    CleanExi HS_HNRNPL.
    Genevestigatori P14866.

    Family and domain databases

    Gene3Di 3.30.70.330. 4 hits.
    InterProi IPR006536. HnRNP-L_PTB.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    SMARTi SM00360. RRM. 3 hits.
    [Graphical view ]
    TIGRFAMsi TIGR01649. hnRNP-L_PTB. 1 hit.
    PROSITEi PS50102. RRM. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular basis of T cell-mediated recognition of pancreatic cancer cells."
      Ito M., Shichijo S., Tsuda N., Ochi M., Harashima N., Saito N., Itoh K.
      Cancer Res. 61:2038-2046(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Pancreatic cancer.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Synovium.
    3. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "A novel heterogeneous nuclear RNP protein with a unique distribution on nascent transcripts."
      Pinol-Roma S., Swanson M.S., Gall J.G., Dreyfuss G.
      J. Cell Biol. 109:2575-2587(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 23-589 (ISOFORM 1).
    6. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 67-76; 199-215; 218-233; 386-403; 425-448 AND 549-558, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    7. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
      Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
      Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
      Tissue: Keratinocyte.
    8. "Human AP-endonuclease 1 and hnRNP-L interact with a nCaRE-like repressor element in the AP-endonuclease 1 promoter."
      Kuninger D.T., Izumi T., Papaconstantinou J., Mitra S.
      Nucleic Acids Res. 30:823-829(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH APEX1.
    9. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Regulation of CD45 alternative splicing by heterogeneous ribonucleoprotein, hnRNPLL."
      Oberdoerffer S., Moita L.F., Neems D., Freitas R.P., Hacohen N., Rao A.
      Science 321:686-691(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HNRNPLL.
    12. "Heterogeneous nuclear ribonucleoprotein L is a subunit of human KMT3a/Set2 complex required for H3 Lys-36 trimethylation activity in vivo."
      Yuan W., Xie J., Long C., Erdjument-Bromage H., Ding X., Zheng Y., Tempst P., Chen S., Zhu B., Reinberg D.
      J. Biol. Chem. 284:15701-15707(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SETD2.
    13. "Auto- and cross-regulation of the hnRNP L proteins by alternative splicing."
      Rossbach O., Hung L.H., Schreiner S., Grishina I., Heiner M., Hui J., Bindereif A.
      Mol. Cell. Biol. 29:1442-1451(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING, MISCELLANEOUS.
    14. "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-269, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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-52; SER-185 AND SER-298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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-52; SER-101; SER-185; SER-291 AND SER-298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "A conserved serine of heterogeneous nuclear ribonucleoprotein L (hnRNP L) mediates depolarization-regulated alternative splicing of potassium channels."
      Liu G., Razanau A., Hai Y., Yu J., Sohail M., Lobo V.G., Chu J., Kung S.K., Xie J.
      J. Biol. Chem. 287:22709-22716(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-544.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Crystal structures and RNA-binding properties of the RNA recognition motifs of heterogeneous nuclear ribonucleoprotein L: insights into its roles in alternative splicing regulation."
      Zhang W., Zeng F., Liu Y., Zhao Y., Lv H., Niu L., Teng M., Li X.
      J. Biol. Chem. 288:22636-22649(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 90-180, X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 380-589, RRM DOMAINS, MUTAGENESIS OF HIS-105; VAL-132; LEU-141; ASN-172; SER-174; HIS-504 AND PHE-506.

    Entry informationi

    Entry nameiHNRPL_HUMAN
    AccessioniPrimary (citable) accession number: P14866
    Secondary accession number(s): A6ND69, A6NIT8, Q9H3P3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 158 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

    Excess hnRNP L activates NMD of its own mRNA by promoting the inclusion of a 'poison exon' containing a premature stop codon and leading to nonsense-mediated decay. It also cross-regulates inclusion of an analogous 'poison exon' in the hnRNP L-like pre-mRNA (PubMed:19124611).1 Publication

    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