CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017072
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 RNA-binding protein 12B 
Protein Synonyms/Alias
 RNA-binding motif protein 12B 
Gene Name
 RBM12B 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
151PRKTRPLKAENPYLFsumoylation[1]
319EQIRFLYKDENRTRYacetylation[2]
895FGRPEGGKFDFGKHNacetylation[2]
Reference
 [1] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
 Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
 Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional Description
  
Sequence Annotation
 DOMAIN 155 230 RRM 1.
 DOMAIN 284 360 RRM 2.
 DOMAIN 400 477 RRM 3.
 DOMAIN 925 1001 RRM 4.
 MOD_RES 250 250 Phosphoserine.
 MOD_RES 254 254 Phosphoserine.
 MOD_RES 276 276 Phosphothreonine.
 MOD_RES 278 278 Phosphoserine.
 MOD_RES 280 280 Phosphoserine.
 MOD_RES 319 319 N6-acetyllysine.
 MOD_RES 638 638 Phosphoserine.
 MOD_RES 640 640 Phosphothreonine.  
Keyword
 Acetylation; Complete proteome; Phosphoprotein; Polymorphism; Reference proteome; Repeat; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1001 AA 
Protein Sequence
MAVVIRLLGL PFIAGPVDIR HFFTGLTIPD GGVHIIGGEI GEAFIIFATD EDARRAISRS 60
GGFIKDSSVE LFLSSKAEMQ KTIEMKRTDR VGRGRPGSGT SGVDSLSNFI ESVKEEASNS 120
GYGSSINQDA GFHTNGTGHG NLRPRKTRPL KAENPYLFLR GLPYLVNEDD VRVFFSGLCV 180
DGVIFLKHHD GRNNGDAIVK FASCVDASGG LKCHRSFMGS RFIEVMQGSE QQWIEFGGNA 240
VKEGDVLRRS EEHSPPRGIN DRHFRKRSHS KSPRRTRSRS PLGFYVHLKN LSLSIDERDL 300
RNFFRGTDLT DEQIRFLYKD ENRTRYAFVM FKTLKDYNTA LSLHKTVLQY RPVHIDPISR 360
KQMLKFIARY EKKRSGSLER DRPGHVSQKY SQEGNSGQKL CIYIRNFPFD VTKVEVQKFF 420
ADFLLAEDDI YLLYDDKGVG LGEALVKFKS EEQAMKAERL NRRRFLGTEV LLRLISEAQI 480
QEFGVNFSVM SSEKMQARSQ SRERGDHSHL FDSKDPPIYS VGAFENFRHQ LEDLRQLDNF 540
KHPQRDFRQP DRHPPEDFRH SSEDFRFPPE DFRHSPEDFR RPREEDFRRP SEEDFRRPWE 600
EDFRRPPEDD FRHPREEDWR RPLEEDWRRP LEEDFRRSPT EDFRQLPEED FRQPPEEDLR 660
WLPEEDFRRP PEEDWRRPPE EDFRRPLQGE WRRPPEDDFR RPPEEDFRHS PEEDFRQSPQ 720
EHFRRPPQEH FRRPPPEHFR RPPPEHFRRP PPEHFRRPPP EHFRRPPPEH FRRPPPEHFR 780
RPPQEHFRRP PQEHFRRSRE EDFRHPPDED FRGPPDEDFR HPPDEDFRSP QEEDFRCPSD 840
EDFRQLPEED LREAPEEDPR LPDNFRPPGE DFRSPPDDFR SHRPFVNFGR PEGGKFDFGK 900
HNMGSFPEGR FMPDPKINCG SGRVTPIKIM NLPFKANVNE ILDFFHGYRI IPDSVSIQYN 960
EQGLPTGEAI VAMINYNEAM AAIKDLNDRP VGPRKVKLTL L 1001 
Gene Ontology
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW. 
Interpro
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 
Pfam
  
SMART
 SM00360; RRM 
PROSITE
 PS50102; RRM 
PRINTS