CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014239
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
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
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
110GLSWDTTKKDLKDYFubiquitination[1]
114DTTKKDLKDYFSKFGubiquitination[1]
119DLKDYFSKFGEVVDCubiquitination[1]
153KESESVDKVMDQKEHubiquitination[1]
197SPDTPEEKIREYFGGubiquitination[1]
218IELPMDNKTNKRRGFubiquitination[1]
237FKEEEPVKKIMEKKYubiquitination[1]
251YHNVGLSKCEIKVAMubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
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 (By similarity). 
Sequence Annotation
 DOMAIN 97 179 RRM 1.
 DOMAIN 182 261 RRM 2.
 MOD_RES 71 71 Phosphoserine (By similarity).
 MOD_RES 80 80 Phosphoserine.
 MOD_RES 82 82 Phosphoserine (By similarity).
 MOD_RES 83 83 Phosphoserine.
 MOD_RES 119 119 N6-methyllysine (By similarity).
 MOD_RES 165 165 N6-acetyllysine (By similarity).
 MOD_RES 190 190 Phosphoserine (By similarity).
 MOD_RES 193 193 Phosphothreonine (By similarity).
 MOD_RES 251 251 N6-acetyllysine (By similarity).
 MOD_RES 345 345 Dimethylated arginine (By similarity).  
Keyword
 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
MSEEQFGGDG AAAAATAAVG GSAGEQEGAM VAAAAQGPAA AAGSGSGGGG SAAGGTEGGS 60
AEAEGAKIDA SKNEEDEGHS NSSPRHTEAA AAQREEWKMF IGGLSWDTTK KDLKDYFSKF 120
GEVVDCTLKL DPITGRSRGF GFVLFKESES VDKVMDQKEH KLNGKVIDPK RAKAMKTKEP 180
VKKIFVGGLS PDTPEEKIRE YFGGFGEVES IELPMDNKTN KRRGFCFITF KEEEPVKKIM 240
EKKYHNVGLS KCEIKVAMSK EQYQQQQQWG SRGGFAGRAR GRGGGPSQNW NQGYSNYWNQ 300
GYGNYGYNSQ GYGGYGGYDY TGYNNYYGYG DYSNQQSGYG KVSRRGGHQN SYKPY 355 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0030529; C:ribonucleoprotein complex; ISS:UniProtKB.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; ISS:UniProtKB.
 GO:0042162; F:telomeric DNA binding; ISS:UniProtKB.
 GO:0043488; P:regulation of mRNA stability; IMP:MGI.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 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