UniProt Accession

 HNRPD_HUMAN; Q14103; A8K9J2; P07029; Q01858; Q14100; Q14101; Q14102; Q4W5A1; Q9UCE8; Q9UCE9 

Genbank Protein ID

 D55671; D55672; D55673; D55674; AF026126; AF026126; AF026126; AK292707; AC124016; CH471057; BC002401; BC023977; BC026015; X03910; AF039575; M94630 

Genbank Nucleotide ID

 BAA09522.1; BAA09523.1; BAA09524.1; BAA09525.1; AAC23474.1; AAC23475.1; AAC23476.1; BAF85396.1; AAY40913.1; EAX05874.1; AAH02401.1; AAH23977.1; AAH26015.1; CAA27544.1; AAB96683.1; AAA35781.1 

Protein Name

 Heterogeneous nuclear ribonucleoprotein D0 

Protein Synonyms/Alias

 hnRNP D0; AU-rich element RNA-binding protein 1 

Gene Name

 HNRNPD 

Gene Synonyms/Alias

 AUF1; HNRPD 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
110	GLSWDTTKKDLKDYF	ubiquitination	[1]
111	LSWDTTKKDLKDYFS	ubiquitination	[1]
114	DTTKKDLKDYFSKFG	ubiquitination	[1]
119	DLKDYFSKFGEVVDC	ubiquitination	[1]
129	EVVDCTLKLDPITGR	ubiquitination	[1]
153	KESESVDKVMDQKEH	ubiquitination	[1]
161	VMDQKEHKLNGKVID	ubiquitination	[1]
165	KEHKLNGKVIDPKRA	ubiquitination	[1]
197	SPDTPEEKIREYFGG	ubiquitination	[1]
218	IELPMDNKTNKRRGF	ubiquitination	[1]
251	YHNVGLSKCEIKVAM	ubiquitination	[1]
260	EIKVAMSKEQYQQQQ	ubiquitination	[1]
292	DQQSGYGKVSRRGGH	ubiquitination	[1]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961] 

Functional Description

 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. 

Sequence Annotation

 DOMAIN 97 179 RRM 1.
 DOMAIN 182 261 RRM 2.
 MOD_RES 71 71 Phosphoserine.
 MOD_RES 80 80 Phosphoserine.
 MOD_RES 82 82 Phosphoserine.
 MOD_RES 83 83 Phosphoserine.
 MOD_RES 119 119 N6-methyllysine.
 MOD_RES 165 165 N6-acetyllysine.
 MOD_RES 190 190 Phosphoserine.
 MOD_RES 193 193 Phosphothreonine.
 MOD_RES 251 251 N6-acetyllysine.
 MOD_RES 345 345 Dimethylated arginine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; Transcription; Transcription regulation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 355 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IDA:UniProtKB.
 GO:0042162; F:telomeric DNA binding; IDA:UniProtKB.
 GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; NAS:UniProtKB.
 GO:0043488; P:regulation of mRNA stability; IEA:Compara.
 GO:0006401; P:RNA catabolic process; TAS:ProtInc.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 

Interpro

 IPR012956; CARG-binding_factor_N.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 

Pfam

 PF08143; CBFNT
 PF00076; RRM_1 

SMART

 SM00360; RRM 

PROSITE

 PS50102; RRM 

PRINTS