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P61978

- HNRPK_HUMAN

UniProt

P61978 - HNRPK_HUMAN

Protein

Heterogeneous nuclear ribonucleoprotein K

Gene

HNRNPK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 1 (07 Jun 2004)
      Previous versions | rss
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    Functioni

    One of the major pre-mRNA-binding proteins. Binds tenaciously to poly(C) sequences. Likely to play a role in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. Can also bind poly(C) single-stranded DNA. Plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. When sumoylated, acts as a transcriptional coactivator of p53/TP53, playing a role in p21/CDKN1A and 14-3-3 sigma/SFN induction By similarity. As far as transcription repression is concerned, acts by interacting with long intergenic RNA p21 (lincRNA-p21), a non-coding RNA induced by p53/TP53. This interaction is necessary for the induction of apoptosis, but not cell cycle arrest.By similarity3 Publications

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. RNA binding Source: ProtInc
    4. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: BHF-UCL
    5. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: BHF-UCL
    6. single-stranded DNA binding Source: BHF-UCL

    GO - Biological processi

    1. gene expression Source: Reactome
    2. mRNA splicing, via spliceosome Source: UniProtKB
    3. positive regulation of low-density lipoprotein particle receptor biosynthetic process Source: BHF-UCL
    4. positive regulation of receptor-mediated endocytosis Source: BHF-UCL
    5. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    6. regulation of lipid transport by positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    7. regulation of low-density lipoprotein particle clearance Source: BHF-UCL
    8. RNA processing Source: ProtInc
    9. RNA splicing Source: Reactome
    10. signal transduction Source: ProtInc
    11. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Repressor, Ribonucleoprotein

    Keywords - Biological processi

    Host-virus interaction, mRNA processing, mRNA splicing, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, 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 K
    Short name:
    hnRNP K
    Alternative name(s):
    Transformation up-regulated nuclear protein
    Short name:
    TUNP
    Gene namesi
    Name:HNRNPK
    Synonyms:HNRPK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:5044. HNRNPK.

    Subcellular locationi

    Cytoplasm. Nucleusnucleoplasm. Cell projectionpodosome
    Note: Recruited to p53/TP53-responsive promoters, in the presence of functional p53/TP53. In case of ASFV infection, there is a shift in the localization which becomes predominantly nuclear.

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. cell junction Source: UniProtKB-KW
    3. cell projection Source: UniProtKB-KW
    4. cytoplasm Source: ProtInc
    5. extracellular vesicular exosome Source: UniProt
    6. membrane Source: UniProtKB
    7. nuclear chromatin Source: BHF-UCL
    8. nucleoplasm Source: Reactome
    9. nucleus Source: HPA
    10. podosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell projection, Cytoplasm, Nucleus, Spliceosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi422 – 4221K → R: Loss of sumoylation. Loss of TP53 transcriptional stimulation. 1 Publication
    Mutagenesisi424 – 4241D → A: Loss of sumoylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA162391350.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 463463Heterogeneous nuclear ribonucleoprotein KPRO_0000050096Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine3 Publications
    Modified residuei116 – 1161Phosphoserine2 Publications
    Modified residuei198 – 1981N6-acetyllysineBy similarity
    Modified residuei214 – 2141Phosphoserine2 Publications
    Modified residuei216 – 2161Phosphoserine6 Publications
    Modified residuei284 – 2841Phosphoserine6 Publications
    Modified residuei379 – 3791Phosphoserine4 Publications
    Modified residuei380 – 3801Phosphotyrosine2 Publications
    Cross-linki422 – 422Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

    Post-translational modificationi

    Arg-296 and Arg-299 are dimethylated, probably to asymmetric dimethylarginine.
    Sumoylated by CBX4. Sumoylation is increased upon DNA damage, such as that produced by doxorubicin, etoposide, UV light and camptothecin, due to enhanced CBX4 phosphorylation by HIPK2 under these conditions.9 Publications
    Ubiquitinated by MDM2. Doxorubicin treatment does not affect monoubiquitination, but slightly decreases HNRNPK poly-ubiquitination.2 Publications
    O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.1 Publication

    Keywords - PTMi

    Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP61978.
    PaxDbiP61978.
    PRIDEiP61978.

    2D gel databases

    SWISS-2DPAGEP61978.

    PTM databases

    PhosphoSiteiP61978.

    Miscellaneous databases

    PMAP-CutDBP61978.

    Expressioni

    Inductioni

    By DNA damage, including ionizing radiations and phleomycin treatment or UV irradiation. This induction requires ATM kinase activity (ionizing radiations and phleomycin) or ATR activity (UV irradiation). Up-regulation is due to protein stabilization. Constitutive protein levels are controlled by MDM2-mediated ubiquitination and degradation via the proteasome pathway.1 Publication

    Gene expression databases

    ArrayExpressiP61978.
    BgeeiP61978.
    CleanExiHS_HNRNPK.
    GenevestigatoriP61978.

    Organism-specific databases

    HPAiCAB004435.
    CAB016225.
    HPA007644.
    HPA044105.

    Interactioni

    Subunit structurei

    Interacts with RBM42 and ZIK1. Interacts with BRDT By similarity. Identified in the spliceosome C complex. Interacts with ANKRD28. Interacts with HCV core protein. Interacts with ASFV p30 protein. Interacts with DDX1. Interacts with MDM2; this interaction leads to ubiquitination and proteasomal degradation. Interacts with p53/TP53.By similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P298469EBI-304185,EBI-8847394From a different organism.
    AURKAO149652EBI-304185,EBI-448680
    C'204LQ8V1E75EBI-304185,EBI-8068745From a different organism.
    EBNA-LPQ8AZK72EBI-304185,EBI-1185167From a different organism.
    MDM2Q009872EBI-304185,EBI-389668
    PRMT1Q998733EBI-304185,EBI-78738
    QKIQ96PU83EBI-304185,EBI-945792
    RBMXP381593EBI-304185,EBI-743526
    SRCP129316EBI-304185,EBI-621482
    TP53P046372EBI-304185,EBI-366083
    TP63Q9H3D42EBI-304185,EBI-2337775

    Protein-protein interaction databases

    BioGridi109431. 198 interactions.
    DIPiDIP-31805N.
    IntActiP61978. 99 interactions.
    MINTiMINT-225422.
    STRINGi9606.ENSP00000365439.

    Structurei

    Secondary structure

    1
    463
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi381 – 3844
    Beta strandi388 – 3958
    Turni396 – 3983
    Helixi399 – 4024
    Helixi405 – 4073
    Helixi408 – 41710
    Beta strandi420 – 4234
    Beta strandi430 – 43910
    Helixi441 – 45919

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1J5KNMR-A379-463[»]
    1KHMNMR-A379-463[»]
    1ZZIX-ray1.80A/B385-463[»]
    1ZZJX-ray2.30A/B/C385-463[»]
    1ZZKX-ray0.95A385-463[»]
    ProteinModelPortaliP61978.
    SMRiP61978. Positions 45-216, 385-463.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP61978.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini42 – 10463KH 1PROSITE-ProRule annotationAdd
    BLAST
    Repeati54 – 76231-1Add
    BLAST
    Repeati59 – 6243-1
    Domaini144 – 20966KH 2PROSITE-ProRule annotationAdd
    BLAST
    Repeati245 – 25062-1
    Repeati257 – 26043-2
    Repeati267 – 27043-3
    Repeati295 – 29843-4
    Repeati324 – 32962-2
    Domaini387 – 45165KH 3PROSITE-ProRule annotationAdd
    BLAST
    Repeati399 – 421231-2Add
    BLAST
    Repeati404 – 40743-5

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 276276Necessary for interaction with DDX1Add
    BLAST
    Regioni35 – 197163Interaction with ASFV p30Add
    BLAST
    Regioni54 – 4213682 X 22 AA approximate repeatsAdd
    BLAST
    Regioni59 – 4073495 X 4 AA repeats of G-X-G-GAdd
    BLAST
    Regioni209 – 337129Interaction with ZIK1By similarityAdd
    BLAST
    Regioni236 – 27338RNA-binding RGG-boxAdd
    BLAST
    Regioni245 – 329852 X 6 AA approximate repeatsAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi289 – 2946Poly-Pro
    Compositional biasi310 – 3156Poly-Pro

    Sequence similaritiesi

    Contains 3 KH domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG285495.
    HOVERGENiHBG051916.
    KOiK12886.
    OMAiKALRTDX.
    OrthoDBiEOG7CZK81.
    PhylomeDBiP61978.
    TreeFamiTF316335.

    Family and domain databases

    Gene3Di3.30.1370.10. 3 hits.
    InterProiIPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    IPR012987. ROK_N.
    [Graphical view]
    PfamiPF00013. KH_1. 3 hits.
    PF08067. ROKNT. 1 hit.
    [Graphical view]
    SMARTiSM00322. KH. 3 hits.
    [Graphical view]
    SUPFAMiSSF54791. SSF54791. 3 hits.
    PROSITEiPS50084. KH_TYPE_1. 3 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P61978-1) [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

    METEQPEETF PNTETNGEFG KRPAEDMEEE QAFKRSRNTD EMVELRILLQ    50
    SKNAGAVIGK GGKNIKALRT DYNASVSVPD SSGPERILSI SADIETIGEI 100
    LKKIIPTLEE GLQLPSPTAT SQLPLESDAV ECLNYQHYKG SDFDCELRLL 150
    IHQSLAGGII GVKGAKIKEL RENTQTTIKL FQECCPHSTD RVVLIGGKPD 200
    RVVECIKIIL DLISESPIKG RAQPYDPNFY DETYDYGGFT MMFDDRRGRP 250
    VGFPMRGRGG FDRMPPGRGG RPMPPSRRDY DDMSPRRGPP PPPPGRGGRG 300
    GSRARNLPLP PPPPPRGGDL MAYDRRGRPG DRYDGMVGFS ADETWDSAID 350
    TWSPSEWQMA YEPQGGSGYD YSYAGGRGSY GDLGGPIITT QVTIPKDLAG 400
    SIIGKGGQRI KQIRHESGAS IKIDEPLEGS EDRIITITGT QDQIQNAQYL 450
    LQNSVKQYSG KFF 463
    Length:463
    Mass (Da):50,976
    Last modified:June 7, 2004 - v1
    Checksum:i0F70EE169B2A064A
    GO
    Isoform 2 (identifier: P61978-2) [UniParc] [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         459-463: SGKFF → ADVEGF

    Show »
    Length:464
    Mass (Da):51,028
    Checksum:i0B4EC22FE4534A06
    GO
    Isoform 3 (identifier: P61978-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         111-134: Missing.
         459-463: SGKFF → ADVEGF

    Note: No experimental confirmation available.

    Show »
    Length:440
    Mass (Da):48,562
    Checksum:iC98A78A7462BF776
    GO

    Sequence cautioni

    The sequence BAD92799.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti32 – 321A → D in CAA51267. (PubMed:8107114)Curated

    Mass spectrometryi

    Isoform 1 : Molecular mass is 50976.25 Da from positions 1 - 463. Determined by MALDI. 1 Publication

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei111 – 13424Missing in isoform 3. 1 PublicationVSP_021669Add
    BLAST
    Alternative sequencei459 – 4635SGKFF → ADVEGF in isoform 2 and isoform 3. 2 PublicationsVSP_002822

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S74678 mRNA. Translation: AAB20770.1.
    X72727 mRNA. Translation: CAA51267.1.
    AB209562 mRNA. Translation: BAD92799.1. Different initiation.
    AL354733 Genomic DNA. Translation: CAI16020.1.
    CH471089 Genomic DNA. Translation: EAW62675.1.
    BC000355 mRNA. Translation: AAH00355.1.
    BC014980 mRNA. Translation: AAH14980.1.
    CCDSiCCDS6667.1.
    CCDS6668.1. [P61978-2]
    PIRiS43363.
    RefSeqiNP_002131.2. NM_002140.3. [P61978-2]
    NP_112552.1. NM_031262.2. [P61978-1]
    NP_112553.1. NM_031263.2. [P61978-2]
    XP_005252017.1. XM_005251960.1. [P61978-2]
    XP_005252018.1. XM_005251961.1. [P61978-1]
    XP_005252020.1. XM_005251963.2. [P61978-3]
    XP_005252021.1. XM_005251964.1. [P61978-3]
    XP_005252022.1. XM_005251965.1. [P61978-3]
    UniGeneiHs.522257.

    Genome annotation databases

    EnsembliENST00000351839; ENSP00000317788; ENSG00000165119. [P61978-1]
    ENST00000360384; ENSP00000353552; ENSG00000165119. [P61978-1]
    ENST00000376263; ENSP00000365439; ENSG00000165119. [P61978-2]
    ENST00000376281; ENSP00000365458; ENSG00000165119. [P61978-2]
    GeneIDi3190.
    KEGGihsa:3190.
    UCSCiuc004ang.4. human.
    uc004anh.4. human. [P61978-3]

    Polymorphism databases

    DMDMi48429103.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S74678 mRNA. Translation: AAB20770.1 .
    X72727 mRNA. Translation: CAA51267.1 .
    AB209562 mRNA. Translation: BAD92799.1 . Different initiation.
    AL354733 Genomic DNA. Translation: CAI16020.1 .
    CH471089 Genomic DNA. Translation: EAW62675.1 .
    BC000355 mRNA. Translation: AAH00355.1 .
    BC014980 mRNA. Translation: AAH14980.1 .
    CCDSi CCDS6667.1.
    CCDS6668.1. [P61978-2 ]
    PIRi S43363.
    RefSeqi NP_002131.2. NM_002140.3. [P61978-2 ]
    NP_112552.1. NM_031262.2. [P61978-1 ]
    NP_112553.1. NM_031263.2. [P61978-2 ]
    XP_005252017.1. XM_005251960.1. [P61978-2 ]
    XP_005252018.1. XM_005251961.1. [P61978-1 ]
    XP_005252020.1. XM_005251963.2. [P61978-3 ]
    XP_005252021.1. XM_005251964.1. [P61978-3 ]
    XP_005252022.1. XM_005251965.1. [P61978-3 ]
    UniGenei Hs.522257.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1J5K NMR - A 379-463 [» ]
    1KHM NMR - A 379-463 [» ]
    1ZZI X-ray 1.80 A/B 385-463 [» ]
    1ZZJ X-ray 2.30 A/B/C 385-463 [» ]
    1ZZK X-ray 0.95 A 385-463 [» ]
    ProteinModelPortali P61978.
    SMRi P61978. Positions 45-216, 385-463.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109431. 198 interactions.
    DIPi DIP-31805N.
    IntActi P61978. 99 interactions.
    MINTi MINT-225422.
    STRINGi 9606.ENSP00000365439.

    PTM databases

    PhosphoSitei P61978.

    Polymorphism databases

    DMDMi 48429103.

    2D gel databases

    SWISS-2DPAGE P61978.

    Proteomic databases

    MaxQBi P61978.
    PaxDbi P61978.
    PRIDEi P61978.

    Protocols and materials databases

    DNASUi 3190.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000351839 ; ENSP00000317788 ; ENSG00000165119 . [P61978-1 ]
    ENST00000360384 ; ENSP00000353552 ; ENSG00000165119 . [P61978-1 ]
    ENST00000376263 ; ENSP00000365439 ; ENSG00000165119 . [P61978-2 ]
    ENST00000376281 ; ENSP00000365458 ; ENSG00000165119 . [P61978-2 ]
    GeneIDi 3190.
    KEGGi hsa:3190.
    UCSCi uc004ang.4. human.
    uc004anh.4. human. [P61978-3 ]

    Organism-specific databases

    CTDi 3190.
    GeneCardsi GC09M086582.
    HGNCi HGNC:5044. HNRNPK.
    HPAi CAB004435.
    CAB016225.
    HPA007644.
    HPA044105.
    MIMi 600712. gene.
    neXtProti NX_P61978.
    PharmGKBi PA162391350.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG285495.
    HOVERGENi HBG051916.
    KOi K12886.
    OMAi KALRTDX.
    OrthoDBi EOG7CZK81.
    PhylomeDBi P61978.
    TreeFami TF316335.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi HNRNPK. human.
    EvolutionaryTracei P61978.
    GeneWikii HNRPK.
    GenomeRNAii 3190.
    NextBioi 12686.
    PMAP-CutDB P61978.
    PROi P61978.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P61978.
    Bgeei P61978.
    CleanExi HS_HNRNPK.
    Genevestigatori P61978.

    Family and domain databases

    Gene3Di 3.30.1370.10. 3 hits.
    InterProi IPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    IPR012987. ROK_N.
    [Graphical view ]
    Pfami PF00013. KH_1. 3 hits.
    PF08067. ROKNT. 1 hit.
    [Graphical view ]
    SMARTi SM00322. KH. 3 hits.
    [Graphical view ]
    SUPFAMi SSF54791. SSF54791. 3 hits.
    PROSITEi PS50084. KH_TYPE_1. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization and primary structure of the poly(C)-binding heterogeneous nuclear ribonucleoprotein complex K protein."
      Matunis M.J., Michael W.M., Dreyfuss G.
      Mol. Cell. Biol. 12:164-171(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
    2. "Identification, molecular cloning, expression and chromosome mapping of a family of transformation upregulated hnRNP-K proteins derived by alternative splicing."
      Dejgaard K., Leffers H., Rasmussen H.H., Madsen P., Kruse T.A., Gesser B., Nielsen H., Celis J.E.
      J. Mol. Biol. 236:33-48(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION.
    3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Brain.
    4. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORMS 1 AND 2).
      Tissue: Muscle.
    7. Bienvenut W.V., Vousden K.H., Lukashchuk N.
      Submitted (MAR-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-52; 70-103; 149-163; 192-201; 208-219; 317-325; 378-405 AND 423-456, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Lung carcinoma.
    8. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 38-46; 149-163; 208-219; 306-316 AND 378-396, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    9. "Hepatitis C virus core protein interacts with heterogeneous nuclear ribonucleoprotein K."
      Hsieh T.-Y., Matsumoto M., Chou H.-C., Schneider R., Hwang S.B., Lee A.S., Lai M.M.C.
      J. Biol. Chem. 273:17651-17659(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HCV CORE PROTEIN.
    10. "An RNA helicase, DDX1, interacting with poly(A) RNA and heterogeneous nuclear ribonucleoprotein K."
      Chen H.C., Lin W.C., Tsay Y.G., Lee S.C., Chang C.J.
      J. Biol. Chem. 277:40403-40409(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DDX1.
    11. "Cluster analysis of an extensive human breast cancer cell line protein expression map database."
      Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J.
      Proteomics 2:212-223(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MASS SPECTROMETRY.
      Tissue: Mammary cancer.
    12. "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.
    13. "hnRNP K: an HDM2 target and transcriptional coactivator of p53 in response to DNA damage."
      Moumen A., Masterson P., O'Connor M.J., Jackson S.P.
      Cell 123:1065-1078(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MDM2 AND TP53, SUBCELLULAR LOCATION, UBIQUITINATION, INDUCTION.
    14. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "PITK, a PP1 targeting subunit that modulates the phosphorylation of the transcriptional regulator hnRNP K."
      Kwiek N.C., Thacker D.F., Datto M.B., Megosh H.B., Haystead T.A.J.
      Cell. Signal. 18:1769-1778(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ANKRD28, PHOSPHORYLATION AT SER-284.
    16. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216 AND SER-379, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "African swine fever virus protein p30 interaction with heterogeneous nuclear ribonucleoprotein K (hnRNP-K) during infection."
      Hernaez B., Escribano J.M., Alonso C.
      FEBS Lett. 582:3275-3280(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ASFV PROTEIN P30.
    19. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-216 AND SER-284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216 AND TYR-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    23. "A large intergenic noncoding RNA induced by p53 mediates global gene repression in the p53 response."
      Huarte M., Guttman M., Feldser D., Garber M., Koziol M.J., Kenzelmann-Broz D., Khalil A.M., Zuk O., Amit I., Rabani M., Attardi L.D., Regev A., Lander E.S., Jacks T., Rinn J.L.
      Cell 142:409-419(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    24. "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-216; SER-284 AND SER-379, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "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-214; SER-216; SER-284 AND SER-379, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Characterization of O-GlcNAc cycling and proteomic identification of differentially O-GlcNAcylated proteins during G1/S transition."
      Drougat L., Olivier-Van Stichelen S., Mortuaire M., Foulquier F., Lacoste A.S., Michalski J.C., Lefebvre T., Vercoutter-Edouart A.S.
      Biochim. Biophys. Acta 1820:1839-1848(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION.
    28. "Proteomic analysis of podosome fractions from macrophages reveals similarities to spreading initiation centres."
      Cervero P., Himmel M., Kruger M., Linder S.
      Eur. J. Cell Biol. 91:908-922(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    29. "DNA damage-induced heterogeneous nuclear ribonucleoprotein K SUMOylation regulates p53 transcriptional activation."
      Pelisch F., Pozzi B., Risso G., Munoz M.J., Srebrow A.
      J. Biol. Chem. 287:30789-30799(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUMOYLATION AT LYS-422, UBIQUITINATION, MUTAGENESIS OF LYS-422 AND ASP-424.
    30. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. "High precision solution structure of the C-terminal KH domain of heterogeneous nuclear ribonucleoprotein K, a c-myc transcription factor."
      Baber J.L., Libutti D., Levens D., Tjandra N.
      J. Mol. Biol. 289:949-962(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 375-463.
    32. "Molecular basis of sequence-specific single-stranded DNA recognition by KH domains: solution structure of a complex between hnRNP K KH3 and single-stranded DNA."
      Braddock D.T., Baber J.L., Levens D., Clore G.M.
      EMBO J. 21:3476-3485(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 379-463 IN COMPLEX WITH SINGLE-STRANDED DNA.

    Entry informationi

    Entry nameiHNRPK_HUMAN
    AccessioniPrimary (citable) accession number: P61978
    Secondary accession number(s): Q07244
    , Q15671, Q59F98, Q5T6W4, Q60577, Q922Y7, Q96J62
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: June 7, 2004
    Last modified: October 1, 2014
    This is version 141 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 9
      Human chromosome 9: 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