CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017256
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Iron-sulfur cluster co-chaperone protein HscB, mitochondrial 
Protein Synonyms/Alias
 Hsc20 
Gene Name
 Hscb 
Gene Synonyms/Alias
 Hsc20 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
209FEQGDFEKAKELLTKacetylation[1]
Reference
 [1] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379
Functional Description
 Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria (By similarity). 
Sequence Annotation
 DOMAIN 71 143 J.
 METAL 40 40 Divalent metal cation (By similarity).
 METAL 43 43 Divalent metal cation (By similarity).
 METAL 57 57 Divalent metal cation (By similarity).
 METAL 60 60 Divalent metal cation (By similarity).  
Keyword
 Chaperone; Complete proteome; Cytoplasm; Metal-binding; Mitochondrion; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 234 AA 
Protein Sequence
MWGCGARALL GVWEVRLAGF LGRRLLGSNA AAGKSIAPQC WNCGHAREAG CGDEFFCSHC 60
RALQPPDPTR DYFSLMNCNR SFRVDVTKLQ HRYQQLQRLV HPDFFSQKSQ TEKHFSDKHS 120
TLVNDAYKTL QAPLTRGLYL LKLQGIEIPE GTDYKADSQF LVEIMEINER LADAQSEAAM 180
EEIEATVRAK QKEFTDNINS AFEQGDFEKA KELLTKMRYF SNIEEKIKLS KTPL 234 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0016226; P:iron-sulfur cluster assembly; IEA:Compara.
 GO:0006457; P:protein folding; IEA:InterPro.
 GO:0051259; P:protein oligomerization; IEA:InterPro. 
Interpro
 IPR001623; DnaJ_domain.
 IPR004640; HscB.
 IPR009073; HscB_oligo_C. 
Pfam
 PF00226; DnaJ
 PF07743; HSCB_C 
SMART
 SM00271; DnaJ 
PROSITE
 PS00636; DNAJ_1
 PS50076; DNAJ_2 
PRINTS