CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011357
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Multiple RNA-binding domain-containing protein 1 
Protein Synonyms/Alias
  
Gene Name
 MRD1 
Gene Synonyms/Alias
 YPR112C 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
768KSGKIIVKNLPFEATacetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919
Functional Description
 Involved in pre-rRNA processing. Required for maintaining steady-state levels of 40S ribosomal subunit. Required for the initial processing of pre-rRNA at the A0 to A2 sites, leading to the processing of the 23S pre-rRNA intermediate to the 18S rRNA. 
Sequence Annotation
 DOMAIN 2 94 RRM 1.
 DOMAIN 345 423 RRM 2.
 DOMAIN 532 604 RRM 3.
 DOMAIN 663 746 RRM 4.
 DOMAIN 763 840 RRM 5.
 MOD_RES 220 220 Phosphoserine.
 MOD_RES 264 264 Phosphoserine.  
Keyword
 Complete proteome; Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; rRNA processing. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 887 AA 
Protein Sequence
MSRIIVKGLP VYLTDDNLRE HFTKRLRQKH SHQAVNGSGP DLITDVKILR DRNGESRRFG 60
FIGYRNEEDA FDAVEYFNGS FINTSKIEVS MAKSFADPRV PQPMKEKRRE ALKRFREKEE 120
KLLQEENRKK KKVDENKHSN IDDEIRKNKQ LQEFMETMKP SSQVTSWEKV GIDKSIEDEK 180
LKREEEDSSV QGNSLLAHAL ALKEENNKDE APNLVIENES DDEYSALNRN RDEDQEDAGE 240
EEKMISISNL KDTDIGLVND DANSDEKENE KRRNLAQDEK VSDLDWFKQR RVRIKESEAE 300
TREKSSSYAT EQNESLDTKK EEQPERAVPQ KTDEELAIEK INQTGRLFLR NILYTSKEED 360
FRKLFSPFGE LEEVHVALDT RTGQSKGFAY VLFKDSKNAV NAYVELDKQI FQGRLLHILP 420
GEEKKSHRLD EFDLKNMPLK KQKELKRKAA ASRQTFSWNS LYMNQDAVLG SVAAKLGLEK 480
SQLIDAENSS SAVKQALAEA HVIGDVRKYF ESKGVDLTKF SQLKSTNQRD DKVILVKNFP 540
FGTTREELGE MFLPYGKLER LLMPPAGTIA IVQFRDTTSA RAAFTKLSYK RFKDGIIYLE 600
RGPKDCFTKP AEADDLINNT SAKEEENPVE VKPSSNDLME ANKDVTEGSS NAHDEDVIDG 660
PTVSIFIKNL NFSTTNQNLT DRFKVFTGFV VAQVKTKPDP KHQGKTLSMG FGFVEFRTKE 720
QANAVIAAMD GTVIDGHKIQ LKLSHRQASQ SGNTKTKSNK KSGKIIVKNL PFEATRKDVF 780
ELFNSFGQLK SVRVPKKFDK SARGFAFVEF LLPKEAENAM DQLHGVHLLG RRLVMQYAEE 840
DAVDAEEEIA RMTKKVRKQV ATNEMAALRN GGGRKKLDVD DEENEGF 887 
Gene Ontology
 GO:0030686; C:90S preribosome; IDA:SGD.
 GO:0005730; C:nucleolus; IDA:SGD.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0042134; F:rRNA primary transcript binding; IDA:SGD.
 GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
 GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
 GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
 GO:0034462; P:small-subunit processome assembly; IMP:SGD. 
Interpro
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 
Pfam
 PF00076; RRM_1 
SMART
 SM00360; RRM 
PROSITE
 PS50102; RRM 
PRINTS