CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011524
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 mRNA-binding protein PUF3 
Protein Synonyms/Alias
 Pumilio homology domain family member 3 
Gene Name
 PUF3 
Gene Synonyms/Alias
 YLL013C; L1325 
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
528LRNSSSDKNSNSNMSubiquitination[1]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
Functional Description
 RNA-binding protein involved in post-transcriptional regulation. Negatively regulates expression of COX17 by binding to the 3'-UTR of COX17 mRNA. Promotes decay of COX17 mRNA by enhancing its rate of deadenylation and subsequent turnover. Predominantly binds to mRNAs encoding mitochondrial proteins and localizes them to the vicinity of mitochondria for translation. Regulates mitochondrial biogenesis, motility and morphology. 
Sequence Annotation
 DOMAIN 513 871 PUM-HD.
 REPEAT 538 573 Pumilio 1.
 REPEAT 574 609 Pumilio 2.
 REPEAT 610 645 Pumilio 3.
 REPEAT 646 681 Pumilio 4.
 REPEAT 682 717 Pumilio 5.
 REPEAT 718 759 Pumilio 6.
 REPEAT 760 795 Pumilio 7.
 REPEAT 807 844 Pumilio 8.
 MOD_RES 83 83 Phosphothreonine.
 MOD_RES 210 210 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Membrane; Mitochondrion; Mitochondrion outer membrane; Phosphoprotein; Reference proteome; Repeat; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 879 AA 
Protein Sequence
MEMNMDMDMD MELASIVSSL SALSHSNNNG GQAAAAGIVN GGAAGSQQIG GFRRSSFTTA 60
NEVDSEILLL HGSSESSPIF KKTALSVGTA PPFSTNSKKF FGNGGNYYQY RSTDTASLSS 120
ASYNNYHTHH TAANLGKNNK VNHLLGQYSA SIAGPVYYNG NDNNNSGGEG FFEKFGKSLI 180
DGTRELESQD RPDAVNTQSQ FISKSVSNAS LDTQNTFEQN VESDKNFNKL NRNTTNSGSL 240
YHSSSNSGSS ASLESENAHY PKRNIWNVAN TPVFRPSNNP AAVGATNVAL PNQQDGPANN 300
NFPPYMNGFP PNQFHQGPHY QNFPNYLIGS PSNFISQMIS VQIPANEDTE DSNGKKKKKA 360
NRPSSVSSPS SPPNNSPFPF AYPNPMMFMP PPPLSAPQQQ QQQQQQQQQE DQQQQQQQEN 420
PYIYYPTPNP IPVKMPKDEK TFKKRNNKNH PANNSNNANK QANPYLENSI PTKNTSKKNA 480
SSKSNESTAN NHKSHSHSHP HSQSLQQQQQ TYHRSPLLEQ LRNSSSDKNS NSNMSLKDIF 540
GHSLEFCKDQ HGSRFIQREL ATSPASEKEV IFNEIRDDAI ELSNDVFGNY VIQKFFEFGS 600
KIQKNTLVDQ FKGNMKQLSL QMYACRVIQK ALEYIDSNQR IELVLELSDS VLQMIKDQNG 660
NHVIQKAIET IPIEKLPFIL SSLTGHIYHL STHSYGCRVI QRLLEFGSSE DQESILNELK 720
DFIPYLIQDQ YGNYVIQYVL QQDQFTNKEM VDIKQEIIET VANNVVEYSK HKFASNVVEK 780
SILYGSKNQK DLIISKILPR DKNHALNLED DSPMILMIKD QFANYVIQKL VNVSEGEGKK 840
LIVIAIRAYL DKLNKSNSLG NRHLASVEKL AALVENAEV 879 
Gene Ontology
 GO:0032473; C:external side of mitochondrial outer membrane; IDA:SGD.
 GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
 GO:0003729; F:mRNA binding; IDA:SGD.
 GO:0009060; P:aerobic respiration; IMP:SGD.
 GO:0008298; P:intracellular mRNA localization; IMP:SGD.
 GO:0051646; P:mitochondrion localization; IMP:SGD.
 GO:0007005; P:mitochondrion organization; IMP:SGD.
 GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IMP:SGD. 
Interpro
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR001313; Pumilio_RNA-bd_rpt. 
Pfam
 PF00806; PUF 
SMART
 SM00025; Pumilio 
PROSITE
 PS50302; PUM
 PS50303; PUM_HD 
PRINTS