Q60668 (HNRPD_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 113.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Heterogeneous nuclear ribonucleoprotein D0 Short name=hnRNP D0 Alternative name(s): AU-rich element RNA-binding protein 1 | ||||
| Gene names |
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| Organism | Mus musculus (Mouse) | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus |
Protein attributes
| Sequence length | 355 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | 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 By similarity. |
| Subunit structure | Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and 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 By similarity. |
| Subcellular location | Nucleus By similarity. Cytoplasm By similarity. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Component of ribonucleosomes By similarity. |
| Post-translational modification | Methylated by PRMT1, in an insulin dependent manner. The PRMT1-mediated methylation regulates its phosphorylation By similarity. |
| Sequence similarities | Contains 2 RRM (RNA recognition motif) domains. |
| Sequence caution | The sequence AAA64653.1 differs from that shown. Reason: Frameshift at several positions. The sequence AAA64653.1 differs from that shown. Reason: Contaminating sequence. The sequence AAA64654.1 differs from that shown. Reason: Frameshift at several positions. The sequence AAA64654.1 differs from that shown. Reason: Contaminating sequence. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| Ldha | P06151 | 2 | EBI-299932,EBI-444940 |
Alternative products
| This entry describes 4 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q60668-1) 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. | ||||||
| Isoform 2 (identifier: Q60668-2) The sequence of this isoform differs from the canonical sequence as follows: 74-92: Missing. | ||||||
| Isoform 3 (identifier: Q60668-3) Also known as: muAUF1-3; The sequence of this isoform differs from the canonical sequence as follows: 285-334: GPSQNWNQGYSNYWNQGYGNYGYNSQGYGGYGGYDYTGYNNYYGYGDYSN → D | ||||||
| Isoform 4 (identifier: Q60668-4) The sequence of this isoform differs from the canonical sequence as follows: 74-92: Missing. 285-334: GPSQNWNQGYSNYWNQGYGNYGYNSQGYGGYGGYDYTGYNNYYGYGDYSN → D | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 355 | 355 | Heterogeneous nuclear ribonucleoprotein D0 | PRO_0000081850 | |||||
Regions | |||||||||
| Domain | 97 – 179 | 83 | RRM 1 | ||||||
| Domain | 182 – 261 | 80 | RRM 2 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 80 | 1 | Phosphoserine Ref.4 | ||||||
| Modified residue | 82 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 83 | 1 | Phosphoserine Ref.4 | ||||||
| Modified residue | 119 | 1 | N6-methyllysine By similarity | ||||||
| Modified residue | 165 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 190 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 193 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 251 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 341 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 345 | 1 | Asymmetric dimethylarginine By similarity | ||||||
| Modified residue | 353 | 1 | N6-acetyllysine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 74 – 92 | 19 | Missing in isoform 2 and isoform 4. | VSP_007940 | |||||
| Alternative sequence | 285 – 334 | 50 | GPSQN…GDYSN → D in isoform 3 and isoform 4. | VSP_007941 | |||||
Experimental info | |||||||||
| Sequence conflict | 22 – 23 | 2 | SA → G in AAA64653. Ref.1 | ||||||
| Sequence conflict | 35 – 38 | 4 | AQGP → RRA in AAA64654. Ref.1 | ||||||
| Sequence conflict | 35 – 37 | 3 | AQG → RR in AAA64653. Ref.1 | ||||||
| Sequence conflict | 50 – 53 | 4 | GSAA → LCG in AAA64654. Ref.1 | ||||||
| Sequence conflict | 217 | 1 | N → K in AAA64654. Ref.1 | ||||||
| Sequence conflict | 227 – 228 | 2 | FI → ID in AAA64653. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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: 7959009] [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: 15489334] [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, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus. |
| [4] | "Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-83, MASS SPECTROMETRY. Tissue: Melanoma. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U11273 mRNA. Translation: AAA64653.1. Sequence problems. U11274 mRNA. Translation: AAA64654.1. Sequence problems. BC011172 mRNA. Translation: AAH11172.2. BC049098 mRNA. Translation: AAH49098.1. |
| IPI | IPI00230086. IPI00330958. IPI00336873. IPI00336874. |
| PIR | I49069. I49070. |
| RefSeq | NP_001070733.1. NM_001077265.1. NP_001070734.1. NM_001077266.1. NP_001070735.1. NM_001077267.1. NP_031542.2. NM_007516.2. |
| UniGene | Mm.150231. |
3D structure databases | |
| ProteinModelPortal | Q60668. |
| SMR | Q60668. Positions 95-260. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q60668. 4 interactions. |
| STRING | Q60668. |
PTM databases | |
| PhosphoSite | Q60668. |
Proteomic databases | |
| PRIDE | Q60668. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000019128; ENSMUSP00000019128; ENSMUSG00000000568. ENSMUST00000172361; ENSMUSP00000132735; ENSMUSG00000000568. |
| GeneID | 11991. |
| KEGG | mmu:11991. |
| UCSC | uc008ygt.1. mouse. uc008ygu.1. mouse. |
Organism-specific databases | |
| CTD | 3184. |
| MGI | MGI:101947. Hnrnpd. |
Phylogenomic databases | |
| GeneTree | ENSGT00560000076532. |
| HOGENOM | HBG756718. |
| HOVERGEN | HBG002295. |
| InParanoid | Q60668. |
| OMA | NEEDEGX. |
| OrthoDB | EOG49W2FZ. |
| PhylomeDB | Q60668. |
Gene expression databases | |
| ArrayExpress | Q60668. |
| Bgee | Q60668. |
| Genevestigator | Q60668. |
| GermOnline | ENSMUSG00000000568. Mus musculus. |
Family and domain databases | |
| InterPro | IPR012956. CARG-binding_factor_N. IPR012677. Nucleotide-bd_a/b_plait. IPR000504. RRM_dom. [Graphical view] |
| Gene3D | G3DSA:3.30.70.330. a_b_plait_nuc_bd. 2 hits. |
| KO | K13044. |
| Pfam | PF08143. CBFNT. 1 hit. PF00076. RRM_1. 2 hits. [Graphical view] |
| SMART | SM00360. RRM. 2 hits. [Graphical view] |
| PROSITE | PS50102. RRM. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 280159. |
| SOURCE | Search... |
Entry information
| Entry name | HNRPD_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q60668 Secondary accession number(s): Q60667, Q80ZJ0, Q91X94 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with