Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q60668

- HNRPD_MOUSE

UniProt

Q60668 - HNRPD_MOUSE

Protein

Heterogeneous nuclear ribonucleoprotein D0

Gene

Hnrnpd

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (04 Aug 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Binds with high affinity to RNA molecules that contain AU-rich elements (AREs) found within the 3'-UTR of many proto-oncogenes and cytokine mRNAs. Also binds to double- and single-stranded DNA sequences in a specific manner and functions a transcription factor. Each of the RNA-binding domains specifically can bind solely to a single-stranded non-monotonous 5'-UUAG-3' sequence and also weaker to the single-stranded 5'-TTAGGG-3' telomeric DNA repeat. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats. Binding of RRM1 to DNA inhibits the formation of DNA quadruplex structure which may play a role in telomere elongation. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. May play a role in the regulation of the rhythmic expression of circadian clock core genes. Directly binds to the 3'UTR of CRY1 mRNA and induces CRY1 rhythmic translation. May also be involved in the regulation of PER2 translation By similarity.By similarity

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. protein binding Source: IntAct
    3. RNA binding Source: UniProtKB
    4. telomeric DNA binding Source: UniProtKB

    GO - Biological processi

    1. circadian regulation of translation Source: UniProtKB
    2. positive regulation of translation Source: UniProtKB
    3. regulation of circadian rhythm Source: UniProtKB
    4. regulation of mRNA stability Source: MGI
    5. regulation of transcription, DNA-templated Source: UniProtKB-KW
    6. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ribonucleoprotein

    Keywords - Biological processi

    Biological rhythms, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_198693. AUF1 (hnRNP D0) destabilizes mRNA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heterogeneous nuclear ribonucleoprotein D0
    Short name:
    hnRNP D0
    Alternative name(s):
    AU-rich element RNA-binding protein 1
    Gene namesi
    Name:Hnrnpd
    Synonyms:Auf1, Hnrpd
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:101947. Hnrnpd.

    Subcellular locationi

    Nucleus By similarity. Cytoplasm By similarity
    Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Component of ribonucleosomes. Cytoplasmic localization oscillates diurnally By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell
    3. ribonucleoprotein complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 355355Heterogeneous nuclear ribonucleoprotein D0PRO_0000081850Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei71 – 711PhosphoserineBy similarity
    Modified residuei80 – 801PhosphoserineBy similarity
    Modified residuei82 – 821PhosphoserineBy similarity
    Modified residuei83 – 831Phosphoserine1 Publication
    Modified residuei119 – 1191N6-methyllysineBy similarity
    Modified residuei165 – 1651N6-acetyllysineBy similarity
    Modified residuei190 – 1901PhosphoserineBy similarity
    Modified residuei193 – 1931PhosphothreonineBy similarity
    Modified residuei243 – 2431N6-acetyllysine1 Publication
    Modified residuei251 – 2511N6-acetyllysineBy similarity
    Modified residuei345 – 3451Dimethylated arginineBy similarity

    Post-translational modificationi

    Methylated by PRMT1, in an insulin dependent manner. The PRMT1-mediated methylation regulates its phosphorylation By similarity.By similarity

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ60668.
    PaxDbiQ60668.
    PRIDEiQ60668.

    PTM databases

    PhosphoSiteiQ60668.

    Expressioni

    Gene expression databases

    ArrayExpressiQ60668.
    BgeeiQ60668.
    GenevestigatoriQ60668.

    Interactioni

    Subunit structurei

    Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Part of a complex associated with the FOS mCRD domain and consisting of PABPC1, PAIP1, CSDE1/UNR and SYNCRIP. Interacts with IGF2BP2. Interacts with GTPBP1. Interacts with EIF4G1; the interaction requires RNA. Interacts with EIF3B and RPS3 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LdhaP061512EBI-299932,EBI-444940

    Protein-protein interaction databases

    BioGridi198279. 5 interactions.
    DIPiDIP-31411N.
    IntActiQ60668. 7 interactions.
    MINTiMINT-1864708.
    STRINGi10090.ENSMUSP00000019128.

    Structurei

    3D structure databases

    ProteinModelPortaliQ60668.
    SMRiQ60668. Positions 98-259.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini97 – 17983RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini182 – 26180RRM 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0724.
    GeneTreeiENSGT00730000110184.
    HOGENOMiHOG000234441.
    HOVERGENiHBG002295.
    InParanoidiQ60668.
    KOiK13044.
    OMAiRGGPNQN.
    OrthoDBiEOG715Q6V.
    PhylomeDBiQ60668.
    TreeFamiTF314808.

    Family and domain databases

    Gene3Di3.30.70.330. 2 hits.
    InterProiIPR012956. CARG-binding_factor_N.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF08143. CBFNT. 1 hit.
    PF00076. RRM_1. 2 hits.
    [Graphical view]
    SMARTiSM00360. RRM. 2 hits.
    [Graphical view]
    PROSITEiPS50102. RRM. 2 hits.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q60668-1) [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

    MSEEQFGGDG AAAAATAAVG GSAGEQEGAM VAAAAQGPAA AAGSGSGGGG    50
    SAAGGTEGGS AEAEGAKIDA SKNEEDEGHS NSSPRHTEAA AAQREEWKMF 100
    IGGLSWDTTK KDLKDYFSKF GEVVDCTLKL DPITGRSRGF GFVLFKESES 150
    VDKVMDQKEH KLNGKVIDPK RAKAMKTKEP VKKIFVGGLS PDTPEEKIRE 200
    YFGGFGEVES IELPMDNKTN KRRGFCFITF KEEEPVKKIM EKKYHNVGLS 250
    KCEIKVAMSK EQYQQQQQWG SRGGFAGRAR GRGGGPSQNW NQGYSNYWNQ 300
    GYGNYGYNSQ GYGGYGGYDY TGYNNYYGYG DYSNQQSGYG KVSRRGGHQN 350
    SYKPY 355
    Length:355
    Mass (Da):38,354
    Last modified:August 4, 2003 - v2
    Checksum:i5941DFC6F65B88DF
    GO
    Isoform 2 (identifier: Q60668-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         74-92: Missing.

    Show »
    Length:336
    Mass (Da):36,377
    Checksum:i7DB919DCCEDAFC1C
    GO
    Isoform 3 (identifier: Q60668-3) [UniParc]FASTAAdd to Basket

    Also known as: muAUF1-3

    The sequence of this isoform differs from the canonical sequence as follows:
         285-334: GPSQNWNQGYSNYWNQGYGNYGYNSQGYGGYGGYDYTGYNNYYGYGDYSN → D

    Show »
    Length:306
    Mass (Da):32,754
    Checksum:iB6E5DE4E2D4C2275
    GO
    Isoform 4 (identifier: Q60668-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         74-92: Missing.
         285-334: GPSQNWNQGYSNYWNQGYGNYGYNSQGYGGYGGYDYTGYNNYYGYGDYSN → D

    Note: No experimental confirmation available.

    Show »
    Length:287
    Mass (Da):30,778
    Checksum:iE6678C4248543031
    GO

    Sequence cautioni

    The sequence AAA64653.1 differs from that shown. Reason: Contaminating sequence.
    The sequence AAA64654.1 differs from that shown. Reason: Contaminating sequence.
    The sequence AAA64653.1 differs from that shown. Reason: Frameshift at several positions.
    The sequence AAA64654.1 differs from that shown. Reason: Frameshift at several positions.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 232SA → G in AAA64653. (PubMed:7959009)Curated
    Sequence conflicti35 – 384AQGP → RRA in AAA64654. (PubMed:7959009)Curated
    Sequence conflicti35 – 373AQG → RR in AAA64653. (PubMed:7959009)Curated
    Sequence conflicti50 – 534GSAA → LCG in AAA64654. (PubMed:7959009)Curated
    Sequence conflicti217 – 2171N → K in AAA64654. (PubMed:7959009)Curated
    Sequence conflicti227 – 2282FI → ID in AAA64653. (PubMed:7959009)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei74 – 9219Missing in isoform 2 and isoform 4. CuratedVSP_007940Add
    BLAST
    Alternative sequencei285 – 33450GPSQN…GDYSN → D in isoform 3 and isoform 4. 2 PublicationsVSP_007941Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U11273 mRNA. Translation: AAA64653.1. Sequence problems.
    U11274 mRNA. Translation: AAA64654.1. Sequence problems.
    BC011172 mRNA. Translation: AAH11172.2.
    BC049098 mRNA. Translation: AAH49098.1.
    CCDSiCCDS39180.1. [Q60668-2]
    CCDS39181.1. [Q60668-3]
    CCDS39182.1. [Q60668-1]
    CCDS51571.1. [Q60668-4]
    PIRiI49069.
    I49070.
    RefSeqiNP_001070733.1. NM_001077265.2. [Q60668-1]
    NP_001070734.1. NM_001077266.2.
    NP_001070735.1. NM_001077267.2.
    NP_031542.2. NM_007516.3. [Q60668-3]
    XP_006534798.1. XM_006534735.1. [Q60668-1]
    UniGeneiMm.150231.

    Genome annotation databases

    EnsembliENSMUST00000019128; ENSMUSP00000019128; ENSMUSG00000000568. [Q60668-3]
    ENSMUST00000172361; ENSMUSP00000132735; ENSMUSG00000000568. [Q60668-1]
    GeneIDi11991.
    KEGGimmu:11991.
    UCSCiuc008ygt.1. mouse. [Q60668-1]
    uc008ygu.1. mouse. [Q60668-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U11273 mRNA. Translation: AAA64653.1 . Sequence problems.
    U11274 mRNA. Translation: AAA64654.1 . Sequence problems.
    BC011172 mRNA. Translation: AAH11172.2 .
    BC049098 mRNA. Translation: AAH49098.1 .
    CCDSi CCDS39180.1. [Q60668-2 ]
    CCDS39181.1. [Q60668-3 ]
    CCDS39182.1. [Q60668-1 ]
    CCDS51571.1. [Q60668-4 ]
    PIRi I49069.
    I49070.
    RefSeqi NP_001070733.1. NM_001077265.2. [Q60668-1 ]
    NP_001070734.1. NM_001077266.2.
    NP_001070735.1. NM_001077267.2.
    NP_031542.2. NM_007516.3. [Q60668-3 ]
    XP_006534798.1. XM_006534735.1. [Q60668-1 ]
    UniGenei Mm.150231.

    3D structure databases

    ProteinModelPortali Q60668.
    SMRi Q60668. Positions 98-259.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198279. 5 interactions.
    DIPi DIP-31411N.
    IntActi Q60668. 7 interactions.
    MINTi MINT-1864708.
    STRINGi 10090.ENSMUSP00000019128.

    PTM databases

    PhosphoSitei Q60668.

    Proteomic databases

    MaxQBi Q60668.
    PaxDbi Q60668.
    PRIDEi Q60668.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000019128 ; ENSMUSP00000019128 ; ENSMUSG00000000568 . [Q60668-3 ]
    ENSMUST00000172361 ; ENSMUSP00000132735 ; ENSMUSG00000000568 . [Q60668-1 ]
    GeneIDi 11991.
    KEGGi mmu:11991.
    UCSCi uc008ygt.1. mouse. [Q60668-1 ]
    uc008ygu.1. mouse. [Q60668-3 ]

    Organism-specific databases

    CTDi 3184.
    MGIi MGI:101947. Hnrnpd.

    Phylogenomic databases

    eggNOGi COG0724.
    GeneTreei ENSGT00730000110184.
    HOGENOMi HOG000234441.
    HOVERGENi HBG002295.
    InParanoidi Q60668.
    KOi K13044.
    OMAi RGGPNQN.
    OrthoDBi EOG715Q6V.
    PhylomeDBi Q60668.
    TreeFami TF314808.

    Enzyme and pathway databases

    Reactomei REACT_198693. AUF1 (hnRNP D0) destabilizes mRNA.

    Miscellaneous databases

    ChiTaRSi HNRNPD. mouse.
    NextBioi 280159.
    PROi Q60668.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q60668.
    Bgeei Q60668.
    Genevestigatori Q60668.

    Family and domain databases

    Gene3Di 3.30.70.330. 2 hits.
    InterProi IPR012956. CARG-binding_factor_N.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF08143. CBFNT. 1 hit.
    PF00076. RRM_1. 2 hits.
    [Graphical view ]
    SMARTi SM00360. RRM. 2 hits.
    [Graphical view ]
    PROSITEi PS50102. RRM. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of cDNAs encoding the murine A+U-rich RNA-binding protein AUF1."
      Ehrenman K., Long L., Wagner B.J., Brewer G.
      Gene 149:315-319(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-228 (ISOFORMS 2/4), NUCLEOTIDE SEQUENCE [MRNA] OF 25-355 (ISOFORM 3).
      Strain: BALB/c.
      Tissue: Embryo.
    2. "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 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-355 (ISOFORM 1).
      Tissue: Brain and Salivary gland.
    3. Lubec G., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 184-197, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    4. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiHNRPD_MOUSE
    AccessioniPrimary (citable) accession number: Q60668
    Secondary accession number(s): Q60667, Q80ZJ0, Q91X94
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 4, 2003
    Last sequence update: August 4, 2003
    Last modified: October 1, 2014
    This is version 137 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3