Hnrnpd
entrez
79256
canonical
uniprot
Q9JJ54
canonical
ensembl
ENSRNOG00000002292
resolver
ensp
ENSRNOP00000003158
resolver
ensp
ENSRNOP00000003173
resolver
ensp
ENSRNOP00000046491
resolver
genesymbol
Hnrnpd
resolver
genesymbol_syn
Auf1
resolver
genesymbol_syn
Hnrpd
resolver
uniprot
G3V9G2
resolver
uniprot
P17132
resolver
uniprot
Q9JJ51
resolver
uniprot
Q9JJ52
resolver
uniprot
Q9JJ53
resolver
uniprot_entry
HNRPD_RAT
resolver
uniprot_sec
G3V9G2
resolver
uniprot_sec
P17132
resolver
uniprot_sec
Q9JJ51
resolver
uniprot_sec
Q9JJ52
resolver
uniprot_sec
Q9JJ53
resolver
amino_acid_sequence
MSEEQFGGDGAAAAATAAVGGSAGEQEGAMVAAAQGAAAAAGSGSGGGSAPGGTEGGSTEAEGAKIDASKNEEDEGHSNSSPRHTEAATAQREEWKMFIGGLSWDTTKKDLKDYFSKFGDVVDCTLKLDPITGRSRGFGFVLFKESESVDKVMDQKEHKLNGKVIDPKRAKAMKTKEPVKKIFVGGLSPDTPEEKIREYFGGFGEVESIELPMDNKTNKRRGFCFITFKEEEPVKKIMEKKYHNVGLSKCEIKVAMSKEQYQQQQQWGSRGGFAGRARGRGGGPSQNWNQGYSNYWNQGYGSYGYNSQGYGGYGGYDYTGYNSYYGYGDYSNQQSGYGKVSRRGGHQNSYKPY
uniprot
proteins
function
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. 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. {ECO:0000250|UniProtKB:Q14103}.
uniprot
proteins
mass_dalton
38218
uniprot
proteins
post_translational_modification
PTM: Methylated by PRMT1, in an insulin-dependent manner. The PRMT1-mediated methylation regulates its phosphorylation. {ECO:0000269|PubMed:18492485}.; PTM: Arg-343 is dimethylated, probably to asymmetric dimethylarginine. {ECO:0000250|UniProtKB:Q14103}.
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
16396499
uniprot
proteins
pubmed
18492485
uniprot
proteins
pubmed
2088340
uniprot
proteins
pubmed
22673903
uniprot
proteins
sequence_length
353
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q14103}. Cytoplasm {ECO:0000250|UniProtKB:Q14103}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Component of ribonucleosomes. Cytoplasmic localization oscillates diurnally. {ECO:0000250|UniProtKB:Q14103}.
uniprot
proteins