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Q60668 (HNRPD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heterogeneous nuclear ribonucleoprotein D0

Short name=hnRNP D0
Alternative name(s):
AU-rich element RNA-binding protein 1
Gene names
Name:Hnrnpd
Synonyms:Auf1, Hnrpd
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length355 AA.
Sequence statusComplete.
Protein existenceEvidence 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 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 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LdhaP061512EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 355355Heterogeneous nuclear ribonucleoprotein D0
PRO_0000081850

Regions

Domain97 – 17983RRM 1
Domain182 – 26180RRM 2

Amino acid modifications

Modified residue711Phosphoserine By similarity
Modified residue801Phosphoserine By similarity
Modified residue821Phosphoserine By similarity
Modified residue831Phosphoserine Ref.4
Modified residue1191N6-methyllysine By similarity
Modified residue1651N6-acetyllysine By similarity
Modified residue1901Phosphoserine By similarity
Modified residue1931Phosphothreonine By similarity
Modified residue2431N6-acetyllysine Ref.5
Modified residue2511N6-acetyllysine By similarity
Modified residue3451Dimethylated arginine By similarity

Natural variations

Alternative sequence74 – 9219Missing in isoform 2 and isoform 4.
VSP_007940
Alternative sequence285 – 33450GPSQN…GDYSN → D in isoform 3 and isoform 4.
VSP_007941

Experimental info

Sequence conflict22 – 232SA → G in AAA64653. Ref.1
Sequence conflict35 – 384AQGP → RRA in AAA64654. Ref.1
Sequence conflict35 – 373AQG → RR in AAA64653. Ref.1
Sequence conflict50 – 534GSAA → LCG in AAA64654. Ref.1
Sequence conflict2171N → K in AAA64654. Ref.1
Sequence conflict227 – 2282FI → ID in AAA64653. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 4, 2003. Version 2.
Checksum: 5941DFC6F65B88DF

FASTA35538,354
        10         20         30         40         50         60 
MSEEQFGGDG AAAAATAAVG GSAGEQEGAM VAAAAQGPAA AAGSGSGGGG SAAGGTEGGS 

        70         80         90        100        110        120 
AEAEGAKIDA SKNEEDEGHS NSSPRHTEAA AAQREEWKMF IGGLSWDTTK KDLKDYFSKF 

       130        140        150        160        170        180 
GEVVDCTLKL DPITGRSRGF GFVLFKESES VDKVMDQKEH KLNGKVIDPK RAKAMKTKEP 

       190        200        210        220        230        240 
VKKIFVGGLS PDTPEEKIRE YFGGFGEVES IELPMDNKTN KRRGFCFITF KEEEPVKKIM 

       250        260        270        280        290        300 
EKKYHNVGLS KCEIKVAMSK EQYQQQQQWG SRGGFAGRAR GRGGGPSQNW NQGYSNYWNQ 

       310        320        330        340        350 
GYGNYGYNSQ GYGGYGGYDY TGYNNYYGYG DYSNQQSGYG KVSRRGGHQN SYKPY 

« Hide

Isoform 2 [UniParc].

Checksum: 7DB919DCCEDAFC1C
Show »

FASTA33636,377
Isoform 3 (muAUF1-3) [UniParc].

Checksum: B6E5DE4E2D4C2275
Show »

FASTA30632,754
Isoform 4 [UniParc].

Checksum: E6678C4248543031
Show »

FASTA28730,778

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] [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.
+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.
PIRI49069.
I49070.
RefSeqNP_001070733.1. NM_001077265.2.
NP_001070734.1. NM_001077266.2.
NP_001070735.1. NM_001077267.2.
NP_031542.2. NM_007516.3.
XP_006534798.1. XM_006534735.1.
UniGeneMm.150231.

3D structure databases

ProteinModelPortalQ60668.
SMRQ60668. Positions 98-259.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198279. 4 interactions.
DIPDIP-31411N.
IntActQ60668. 7 interactions.
MINTMINT-1864708.
STRING10090.ENSMUSP00000019128.

PTM databases

PhosphoSiteQ60668.

Proteomic databases

PaxDbQ60668.
PRIDEQ60668.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000019128; ENSMUSP00000019128; ENSMUSG00000000568. [Q60668-3]
ENSMUST00000172361; ENSMUSP00000132735; ENSMUSG00000000568. [Q60668-1]
GeneID11991.
KEGGmmu:11991.
UCSCuc008ygt.1. mouse. [Q60668-1]
uc008ygu.1. mouse. [Q60668-3]

Organism-specific databases

CTD3184.
MGIMGI:101947. Hnrnpd.

Phylogenomic databases

eggNOGCOG0724.
GeneTreeENSGT00730000110184.
HOGENOMHOG000234441.
HOVERGENHBG002295.
InParanoidQ60668.
KOK13044.
OMANEEDEGX.
OrthoDBEOG715Q6V.
PhylomeDBQ60668.
TreeFamTF314808.

Gene expression databases

ArrayExpressQ60668.
BgeeQ60668.
GenevestigatorQ60668.

Family and domain databases

Gene3D3.30.70.330. 2 hits.
InterProIPR012956. CARG-binding_factor_N.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF08143. CBFNT. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view]
SMARTSM00360. RRM. 2 hits.
[Graphical view]
PROSITEPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHNRNPD. mouse.
NextBio280159.
PROQ60668.
SOURCESearch...

Entry information

Entry nameHNRPD_MOUSE
AccessionPrimary (citable) accession number: Q60668
Secondary accession number(s): Q60667, Q80ZJ0, Q91X94
Entry history
Integrated into UniProtKB/Swiss-Prot: August 4, 2003
Last sequence update: August 4, 2003
Last modified: April 16, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot