CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006161
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Zuotin 
Protein Synonyms/Alias
 DnaJ-related protein ZUO1; J protein ZUO1; Heat shock protein 40 homolog ZUO1; Ribosome-associated complex subunit ZUO1 
Gene Name
 ZUO1 
Gene Synonyms/Alias
 YGR285C 
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
34RPVEPVGKFFLQHAQacetylation[1]
34RPVEPVGKFFLQHAQubiquitination[2]
106YAAMGLSKLRFRATEubiquitination[2]
118ATESQIIKAHRKQVVacetylation[1]
131VVKYHPDKQSAAGGSacetylation[1]
150GFFKIIQKAFETLTDacetylation[1]
160ETLTDSNKRAQYDSCubiquitination[2]
274ADNARLVKLVERAVSacetylation[1]
408KANAAGAKEVLKESAubiquitination[2]
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]
 [2] 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, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
Functional Description
 Component of the ribosome-associated complex (RAC), a heterodimeric chaperone complex involved in regulation of accurate translation termination and in folding or maintaining nascent polypeptides in a folding-competent state. RAC stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones SSB1/SSB2 that bind to the nascent polypeptide chain. ZUO1 can act as a J-protein for SSB1/SSB2 only when associated with SSZ1. 
Sequence Annotation
 DOMAIN 98 170 J.
 MOD_RES 50 50 Phosphoserine.  
Keyword
 3D-structure; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 433 AA 
Protein Sequence
MFSLPTLTSD ITVEVNSSAT KTPFVRRPVE PVGKFFLQHA QRTLRNHTWS EFERIEAEKN 60
VKTVDESNVD PDELLFDTEL ADEDLLTHDA RDWKTADLYA AMGLSKLRFR ATESQIIKAH 120
RKQVVKYHPD KQSAAGGSLD QDGFFKIIQK AFETLTDSNK RAQYDSCDFV ADVPPPKKGT 180
DYDFYEAWGP VFEAEARFSK KTPIPSLGNK DSSKKEVEQF YAFWHRFDSW RTFEFLDEDV 240
PDDSSNRDHK RYIERKNKAA RDKKKTADNA RLVKLVERAV SEDPRIKMFK EEEKKEKERR 300
KWEREAGARA EAEAKAKAEA EAKAKAESEA KANASAKADK KKAKEAAKAA KKKNKRAIRN 360
SAKEADYFGD ADKATTIDEQ VGLIVDSLND EELVSTADKI KANAAGAKEV LKESAKTIVD 420
SGKLPSSLLS YFV 433 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0005730; C:nucleolus; IMP:SGD.
 GO:0005844; C:polysome; IDA:SGD.
 GO:0005840; C:ribosome; IDA:SGD.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0051082; F:unfolded protein binding; NAS:SGD.
 GO:0006457; P:protein folding; NAS:SGD.
 GO:0006450; P:regulation of translational fidelity; IMP:SGD.
 GO:0000054; P:ribosomal subunit export from nucleus; IMP:SGD.
 GO:0006364; P:rRNA processing; IMP:SGD. 
Interpro
 IPR001623; DnaJ_domain.
 IPR018253; DnaJ_domain_CS. 
Pfam
 PF00226; DnaJ 
SMART
 SM00271; DnaJ 
PROSITE
 PS00636; DNAJ_1
 PS50076; DNAJ_2 
PRINTS