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Q00839

- HNRPU_HUMAN

UniProt

Q00839 - HNRPU_HUMAN

Protein

Heterogeneous nuclear ribonucleoprotein U

Gene

HNRNPU

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 6 (28 Jul 2009)
      Previous versions | rss
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    Functioni

    Component of the CRD-mediated complex that promotes MYC mRNA stabilization. Binds to pre-mRNA. Has high affinity for scaffold-attached region (SAR) DNA. Binds to double- and single-stranded DNA and RNA.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi504 – 5118ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA binding Source: ProtInc
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. RNA binding Source: ProtInc

    GO - Biological processi

    1. CRD-mediated mRNA stabilization Source: UniProtKB
    2. gene expression Source: Reactome
    3. mRNA splicing, via spliceosome Source: UniProtKB
    4. osteoblast differentiation Source: UniProt
    5. RNA processing Source: ProtInc
    6. RNA splicing Source: Reactome

    Keywords - Molecular functioni

    Ribonucleoprotein

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-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 U
    Short name:
    hnRNP U
    Alternative name(s):
    Scaffold attachment factor A
    Short name:
    SAF-A
    p120
    pp120
    Gene namesi
    Name:HNRNPU
    Synonyms:HNRPU, SAFA, U21.1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:5048. HNRNPU.

    Subcellular locationi

    Nucleus. Cytoplasm. Cell surface
    Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Component of ribonucleosomes. Also found associated with the cell surface.

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. cell surface Source: UniProtKB-SubCell
    3. CRD-mediated mRNA stability complex Source: UniProtKB
    4. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
    5. membrane Source: UniProtKB
    6. nucleoplasm Source: Reactome
    7. nucleus Source: UniProt
    8. ribonucleoprotein complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Spliceosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162391486.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed8 Publications
    Chaini2 – 825824Heterogeneous nuclear ribonucleoprotein UPRO_0000081872Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine; partial7 Publications
    Modified residuei4 – 41Phosphoserine3 Publications
    Modified residuei17 – 171N6-acetyllysineBy similarity
    Modified residuei21 – 211N6-acetyllysineBy similarity
    Modified residuei59 – 591Phosphoserine6 Publications
    Modified residuei66 – 661Phosphoserine5 Publications
    Modified residuei186 – 1861N6-acetyllysineBy similarity
    Modified residuei255 – 2551CitrullineBy similarity
    Modified residuei265 – 2651N6-acetyllysine1 Publication
    Modified residuei266 – 2661PhosphotyrosineBy similarity
    Modified residuei271 – 2711Phosphoserine6 Publications
    Modified residuei352 – 3521N6-acetyllysine1 Publication
    Modified residuei516 – 5161N6-acetyllysine1 Publication
    Modified residuei524 – 5241N6-acetyllysine1 Publication
    Modified residuei551 – 5511N6-acetyllysine1 Publication
    Modified residuei565 – 5651N6-acetyllysine1 Publication
    Modified residuei635 – 6351N6-acetyllysine1 Publication
    Modified residuei739 – 7391Dimethylated arginine; in A2780 ovarian carcinoma cell line1 Publication
    Modified residuei739 – 7391Omega-N-methylated arginine1 Publication
    Modified residuei814 – 8141N6-acetyllysine1 Publication

    Post-translational modificationi

    Extensively phosphorylated.8 Publications
    Arg-733 and Arg-739 are dimethylated, probably to asymmetric dimethylarginine.
    Citrullinated by PADI4.By similarity

    Keywords - PTMi

    Acetylation, Citrullination, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ00839.
    PaxDbiQ00839.
    PRIDEiQ00839.

    PTM databases

    PhosphoSiteiQ00839.

    Expressioni

    Gene expression databases

    ArrayExpressiQ00839.
    BgeeiQ00839.
    CleanExiHS_HNRNPU.
    GenevestigatoriQ00839.

    Organism-specific databases

    HPAiCAB011532.

    Interactioni

    Subunit structurei

    Identified in the spliceosome C complex. Component of the coding region determinant (CRD)-mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with IGF2BP1, IGF2BP2, IGF2BP3 and ERBB4. Ligand for CR2.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDKN2AP427712EBI-351126,EBI-375053

    Protein-protein interaction databases

    BioGridi109433. 269 interactions.
    DIPiDIP-684N.
    IntActiQ00839. 58 interactions.
    MINTiMINT-1654412.
    STRINGi9606.ENSP00000283179.

    Structurei

    Secondary structure

    1
    825
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni24 – 252

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZRJNMR-A23-42[»]
    ProteinModelPortaliQ00839.
    SMRiQ00839. Positions 3-48, 298-470.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ00839.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini8 – 4235SAPPROSITE-ProRule annotationAdd
    BLAST
    Domaini267 – 464198B30.2/SPRYPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni714 – 73926RNA-binding RGG-boxAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi2 – 160159Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi84 – 9411Poly-GluAdd
    BLAST
    Compositional biasi161 – 20949Gln-richAdd
    BLAST
    Compositional biasi703 – 825123Gly-richAdd
    BLAST
    Compositional biasi740 – 75011Poly-GlyAdd
    BLAST

    Sequence similaritiesi

    Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
    Contains 1 SAP domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG297571.
    HOGENOMiHOG000253920.
    HOVERGENiHBG061101.
    InParanoidiQ00839.
    KOiK12888.
    OMAiFKRQMAD.
    OrthoDBiEOG79CZ07.
    PhylomeDBiQ00839.
    TreeFamiTF317301.

    Family and domain databases

    Gene3Di1.10.720.30. 1 hit.
    3.40.50.300. 1 hit.
    InterProiIPR001870. B30.2/SPRY.
    IPR008985. ConA-like_lec_gl_sf.
    IPR026745. hnRNP_U.
    IPR027417. P-loop_NTPase.
    IPR003034. SAP_dom.
    IPR018355. SPla/RYanodine_receptor_subgr.
    IPR003877. SPRY_rcpt.
    [Graphical view]
    PANTHERiPTHR12381:SF11. PTHR12381:SF11. 1 hit.
    PfamiPF02037. SAP. 1 hit.
    PF00622. SPRY. 1 hit.
    [Graphical view]
    SMARTiSM00513. SAP. 1 hit.
    SM00449. SPRY. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS50188. B302_SPRY. 1 hit.
    PS50800. SAP. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: Q00839-1) [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

    MSSSPVNVKK LKVSELKEEL KKRRLSDKGL KAELMERLQA ALDDEEAGGR    50
    PAMEPGNGSL DLGGDSAGRS GAGLEQEAAA GGDEEEEEEE EEEEGISALD 100
    GDQMELGEEN GAAGAADSGP MEEEEAASED ENGDDQGFQE GEDELGDEEE 150
    GAGDENGHGE QQPQPPATQQ QQPQQQRGAA KEAAGKSSGP TSLFAVTVAP 200
    PGARQGQQQA GGKKKAEGGG GGGRPGAPAA GDGKTEQKGG DKKRGVKRPR 250
    EDHGRGYFEY IEENKYSRAK SPQPPVEEED EHFDDTVVCL DTYNCDLHFK 300
    ISRDRLSASS LTMESFAFLW AGGRASYGVS KGKVCFEMKV TEKIPVRHLY 350
    TKDIDIHEVR IGWSLTTSGM LLGEEEFSYG YSLKGIKTCN CETEDYGEKF 400
    DENDVITCFA NFESDEVELS YAKNGQDLGV AFKISKEVLA GRPLFPHVLC 450
    HNCAVEFNFG QKEKPYFPIP EEYTFIQNVP LEDRVRGPKG PEEKKDCEVV 500
    MMIGLPGAGK TTWVTKHAAE NPGKYNILGT NTIMDKMMVA GFKKQMADTG 550
    KLNTLLQRAP QCLGKFIEIA ARKKRNFILD QTNVSAAAQR RKMCLFAGFQ 600
    RKAVVVCPKD EDYKQRTQKK AEVEGKDLPE HAVLKMKGNF TLPEVAECFD 650
    EITYVELQKE EAQKLLEQYK EESKKALPPE KKQNTGSKKS NKNKSGKNQF 700
    NRGGGHRGRG GFNMRGGNFR GGAPGNRGGY NRRGNMPQRG GGGGGSGGIG 750
    YPYPRAPVFP GRGSYSNRGN YNRGGMPNRG NYNQNFRGRG NNRGYKNQSQ 800
    GYNQWQQGQF WGQKPWSQHY HQGYY 825
    Length:825
    Mass (Da):90,584
    Last modified:July 28, 2009 - v6
    Checksum:i5D4EC4188436831F
    GO
    Isoform Short (identifier: Q00839-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         213-231: Missing.

    Note: Contains a N6-acetyllysine at position 215.

    Show »
    Length:806
    Mass (Da):88,980
    Checksum:iBCE1AD365501EDC1
    GO

    Sequence cautioni

    The sequence AAC19382.1 differs from that shown. Reason: Aberrant splicing.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti603 – 6031A → V in AAH07950. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti712 – 7121F → L.2 Publications
    Corresponds to variant rs1052660 [ dbSNP | Ensembl ].
    VAR_014712

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei213 – 23119Missing in isoform Short. 3 PublicationsVSP_005846Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X65488 mRNA. Translation: CAA46472.1.
    AF068846 mRNA. Translation: AAC19382.1. Sequence problems.
    BX323046 Genomic DNA. Translation: CAI11058.1.
    BC003367 mRNA. Translation: AAH03367.1.
    BC003621 mRNA. Translation: AAH03621.1.
    BC007950 mRNA. Translation: AAH07950.2.
    BC024767 mRNA. Translation: AAH24767.1.
    BC034925 mRNA. Translation: AAH34925.1.
    CCDSiCCDS31081.1. [Q00839-2]
    CCDS41479.1. [Q00839-1]
    PIRiS22765.
    RefSeqiNP_004492.2. NM_004501.3. [Q00839-2]
    NP_114032.2. NM_031844.2. [Q00839-1]
    UniGeneiHs.106212.

    Genome annotation databases

    EnsembliENST00000283179; ENSP00000283179; ENSG00000153187. [Q00839-1]
    ENST00000444376; ENSP00000393151; ENSG00000153187. [Q00839-2]
    GeneIDi3192.
    KEGGihsa:3192.
    UCSCiuc001iaz.1. human. [Q00839-1]
    uc001iba.1. human. [Q00839-2]

    Polymorphism databases

    DMDMi254763463.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X65488 mRNA. Translation: CAA46472.1 .
    AF068846 mRNA. Translation: AAC19382.1 . Sequence problems.
    BX323046 Genomic DNA. Translation: CAI11058.1 .
    BC003367 mRNA. Translation: AAH03367.1 .
    BC003621 mRNA. Translation: AAH03621.1 .
    BC007950 mRNA. Translation: AAH07950.2 .
    BC024767 mRNA. Translation: AAH24767.1 .
    BC034925 mRNA. Translation: AAH34925.1 .
    CCDSi CCDS31081.1. [Q00839-2 ]
    CCDS41479.1. [Q00839-1 ]
    PIRi S22765.
    RefSeqi NP_004492.2. NM_004501.3. [Q00839-2 ]
    NP_114032.2. NM_031844.2. [Q00839-1 ]
    UniGenei Hs.106212.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ZRJ NMR - A 23-42 [» ]
    ProteinModelPortali Q00839.
    SMRi Q00839. Positions 3-48, 298-470.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109433. 269 interactions.
    DIPi DIP-684N.
    IntActi Q00839. 58 interactions.
    MINTi MINT-1654412.
    STRINGi 9606.ENSP00000283179.

    PTM databases

    PhosphoSitei Q00839.

    Polymorphism databases

    DMDMi 254763463.

    Proteomic databases

    MaxQBi Q00839.
    PaxDbi Q00839.
    PRIDEi Q00839.

    Protocols and materials databases

    DNASUi 3192.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000283179 ; ENSP00000283179 ; ENSG00000153187 . [Q00839-1 ]
    ENST00000444376 ; ENSP00000393151 ; ENSG00000153187 . [Q00839-2 ]
    GeneIDi 3192.
    KEGGi hsa:3192.
    UCSCi uc001iaz.1. human. [Q00839-1 ]
    uc001iba.1. human. [Q00839-2 ]

    Organism-specific databases

    CTDi 3192.
    GeneCardsi GC01M245013.
    HGNCi HGNC:5048. HNRNPU.
    HPAi CAB011532.
    MIMi 602869. gene.
    neXtProti NX_Q00839.
    PharmGKBi PA162391486.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG297571.
    HOGENOMi HOG000253920.
    HOVERGENi HBG061101.
    InParanoidi Q00839.
    KOi K12888.
    OMAi FKRQMAD.
    OrthoDBi EOG79CZ07.
    PhylomeDBi Q00839.
    TreeFami TF317301.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi HNRNPU. human.
    EvolutionaryTracei Q00839.
    GeneWikii HNRPU.
    GenomeRNAii 3192.
    NextBioi 12700.
    PROi Q00839.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q00839.
    Bgeei Q00839.
    CleanExi HS_HNRNPU.
    Genevestigatori Q00839.

    Family and domain databases

    Gene3Di 1.10.720.30. 1 hit.
    3.40.50.300. 1 hit.
    InterProi IPR001870. B30.2/SPRY.
    IPR008985. ConA-like_lec_gl_sf.
    IPR026745. hnRNP_U.
    IPR027417. P-loop_NTPase.
    IPR003034. SAP_dom.
    IPR018355. SPla/RYanodine_receptor_subgr.
    IPR003877. SPRY_rcpt.
    [Graphical view ]
    PANTHERi PTHR12381:SF11. PTHR12381:SF11. 1 hit.
    Pfami PF02037. SAP. 1 hit.
    PF00622. SPRY. 1 hit.
    [Graphical view ]
    SMARTi SM00513. SAP. 1 hit.
    SM00449. SPRY. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS50188. B302_SPRY. 1 hit.
    PS50800. SAP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure and binding activity of the hnRNP U protein: binding RNA through RGG box."
      Kiledjian M., Dreyfuss G.
      EMBO J. 11:2655-2664(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), RNA-BINDING DOMAIN, VARIANT LEU-712.
    2. "hnRNP-U/SAF-A is encoded by two differentially polyadenylated mRNAs in human cells."
      Fackelmayer F.O., Richter A.
      Biochim. Biophys. Acta 1217:232-234(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
    3. "A variant of human scaffold attachment factor A (SAF-A), also known as heterogeneous nuclear ribonucleoprotein U (hnRNP-U)."
      Fackelmayer F.O.
      Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANT LEU-712.
    4. "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].
    5. "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 SHORT).
      Tissue: Eye, Lymph, Placenta and Skin.
    6. "Major cell surface-located protein substrates of an ecto-protein kinase are homologs of known nuclear proteins."
      Jordan P., Heid H., Kinzel V., Kubler D.
      Biochemistry 33:14696-14706(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-7; 256-265 AND 463-476, PHOSPHORYLATION, SUBCELLULAR LOCATION.
    7. Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
      Submitted (MAY-2006) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-9; 186-194; 319-330; 399-409; 423-432; 452-461; 464-475 AND 524-535, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: T-cell.
    8. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-9; 13-21; 38-69; 187-204; 256-268; 306-324; 353-360; 424-433; 463-484; 495-510; 525-543; 552-558; 566-572; 576-590; 592-601; 627-635; 665-674 AND 734-755, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, METHYLATION AT ARG-739, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Ovarian carcinoma.
    9. "Purification of two isoforms of hnRNP-U and characterization of their nucleic acid binding activity."
      Fackelmayer F.O., Richter A.
      Biochemistry 33:10416-10422(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    10. "Binding sites of the Epstein-Barr virus and C3d receptor (CR2, CD21) for its three intracellular ligands, the p53 anti-oncoprotein, the p68 calcium binding protein and the nuclear p120 ribonucleoprotein."
      Barel M., Balbo M., Gauffre A., Frade R.
      Mol. Immunol. 32:389-397(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CR2.
    11. "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.
    12. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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-59 AND SER-271, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
      Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
      Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Prostate cancer.
    15. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    16. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 AND SER-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "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].
    19. "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs."
      Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.
      RNA 15:104-115(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COMPONENT OF THE CRD-MEDIATED MRNA STABILIZATION COMPLEX, IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    20. "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-59; SER-66 AND SER-271, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    21. "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-265; LYS-352; LYS-516; LYS-524; LYS-551; LYS-565; LYS-635 AND LYS-814, ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-215 (ISOFORM SHORT), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Interactions of ErbB4 and Kap1 connect the growth factor and DNA damage response pathways."
      Gilmore-Hebert M., Ramabhadran R., Stern D.F.
      Mol. Cancer Res. 8:1388-1398(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ERBB4, SUBCELLULAR LOCATION.
    23. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-59; SER-66 AND SER-271, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-59 AND SER-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "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].
    27. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "Subcellular localization and RNP formation of IGF2BPs (IGF2 mRNA-binding proteins) is modulated by distinct RNA-binding domains."
      Wachter K., Kohn M., Stohr N., Huttelmaier S.
      Biol. Chem. 394:1077-1090(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IGF2BP1; IGF2BP2 AND IGF2BP3.
    29. "Solution structure of the SAP domain of human E1B-55kDa-associated protein 5 isoform C."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JAN-2008) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 23-42.

    Entry informationi

    Entry nameiHNRPU_HUMAN
    AccessioniPrimary (citable) accession number: Q00839
    Secondary accession number(s): O75507
    , Q8N174, Q96HY9, Q9BQ09
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 166 of the entry and version 6 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. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3