CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004122
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA-binding protein modulo 
Protein Synonyms/Alias
  
Gene Name
 mod 
Gene Synonyms/Alias
 CG2050 
Created Date
 July 27, 2013 
Organism
 Drosophila melanogaster (Fruit fly) 
NCBI Taxa ID
 7227 
Lysine Modification
Position
Peptide
Type
References
20KATNGEEKPLAKRVTacetylation[1]
275NITKDDLKTFFEKVAacetylation[1]
360YSSDALEKIFKKFGDacetylation[1]
364ALEKIFKKFGDVEEIacetylation[1]
405LDGKTVNKFEWKLHRacetylation[1]
409TVNKFEWKLHRFERSacetylation[1]
515RKFQKDTKPNFGKKPacetylation[1]
520DTKPNFGKKPFNKRPacetylation[1]
534PAQENGGKSFVKRARacetylation[1]
Reference
 [1] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation.
 Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C.
 Sci Signal. 2011 Jul 26;4(183):ra48. [PMID: 21791702
Functional Description
 Its capacity to bind DNA and protein(s), and its differential expression during development suggest a role in the regulation of gene expression during Drosophila development. It could, in interaction with other factors, be required for the translation of instructions provided by pattern forming genes and controls, via chromatin changes, the activity of genes critical for the process of morphogenesis of several embryonic territories. 
Sequence Annotation
 DOMAIN 175 251 RRM 1.
 DOMAIN 258 331 RRM 2.
 DOMAIN 340 429 RRM 3.
 DOMAIN 420 489 RRM 4.
 MOD_RES 42 42 Phosphoserine.
 MOD_RES 44 44 Phosphoserine.
 MOD_RES 120 120 Phosphoserine.
 MOD_RES 129 129 Phosphoserine.
 MOD_RES 142 142 Phosphoserine.
 MOD_RES 304 304 Phosphoserine.
 MOD_RES 330 330 Phosphoserine; by PKA (Potential).
 MOD_RES 443 443 Phosphoserine.  
Keyword
 Complete proteome; DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 542 AA 
Protein Sequence
MAQKKAVTVK GKKATNGEEK PLAKRVTKST KVQEEETVVP QSPSKKSRKQ PVKEVPQFSE 60
EDESDVEEQN DEQPGDDSDF ETEEAAGLID DEAEEDEEYN SDDEEDDDDD ELEPGEVSKS 120
EGADEVDESD DDEEAPVEKP VSKKSEKANS EKSEENRGIP KVKVGKIPLG TPKNQIVFVT 180
NLPNEYLHKD LVALFAKFGR LSALQRFTNL NGNKSVLIAF DTSTGAEAVL QAKPKALTLG 240
DNVLSVSQPR NKEENNERTV VVGLIGPNIT KDDLKTFFEK VAPVEAVTIS SNRLMPRAFV 300
RLASVDDIPK ALKLHSTELF SRFITVRRIS QESISRTSEL TLVVENVGKH ESYSSDALEK 360
IFKKFGDVEE IDVVCSKAVL AFVTFKQSDA ATKALAQLDG KTVNKFEWKL HRFERSTSGR 420
AILVTNLTSD ATEADLRKVF NDSGEIESII MLGQKAVVKF KDDEGFCKSF LANESIVNNA 480
PIFIEPNSLL KHRLLKKRLA IGQTRAPRKF QKDTKPNFGK KPFNKRPAQE NGGKSFVKRA 540
RF 542 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:FlyBase.
 GO:0005730; C:nucleolus; IDA:FlyBase.
 GO:0043234; C:protein complex; IPI:FlyBase.
 GO:0003729; F:mRNA binding; ISS:FlyBase.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
 GO:0008283; P:cell proliferation; IMP:FlyBase.
 GO:0007286; P:spermatid development; IMP:FlyBase. 
Interpro
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 
Pfam
 PF00076; RRM_1 
SMART
 SM00360; RRM 
PROSITE
 PS50102; RRM 
PRINTS