CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018325
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DnaJ homolog subfamily A member 4 
Protein Synonyms/Alias
  
Gene Name
 DNAJA4 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
61AYRKLALKYHPDKNPubiquitination[1]
155LYNGVTKKLALQKNVubiquitination[2]
236AKVIREKKIIEVHVEubiquitination[2]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961
Functional Description
  
Sequence Annotation
 DOMAIN 4 70 J.
 REPEAT 135 142 CXXCXGXG motif.
 REPEAT 151 158 CXXCXGXG motif.
 REPEAT 178 185 CXXCXGXG motif.
 REPEAT 194 201 CXXCXGXG motif.
 ZN_FING 122 206 CR-type.
 METAL 135 135 Zinc 1 (By similarity).
 METAL 138 138 Zinc 1 (By similarity).
 METAL 151 151 Zinc 2 (By similarity).
 METAL 154 154 Zinc 2 (By similarity).
 METAL 178 178 Zinc 2 (By similarity).
 METAL 181 181 Zinc 2 (By similarity).
 METAL 194 194 Zinc 1 (By similarity).
 METAL 197 197 Zinc 1 (By similarity).
 MOD_RES 394 394 Cysteine methyl ester (By similarity).
 LIPID 394 394 S-farnesyl cysteine (By similarity).  
Keyword
 Alternative splicing; Chaperone; Complete proteome; Lipoprotein; Membrane; Metal-binding; Methylation; Polymorphism; Prenylation; Reference proteome; Repeat; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 397 AA 
Protein Sequence
MARGGSQSWS SGESDGQPKE QTPEKPRHKM VKETQYYDIL GVKPSASPEE IKKAYRKLAL 60
KYHPDKNPDE GEKFKLISQA YEVLSDPKKR DVYDQGGEQA IKEGGSGSPS FSSPMDIFDM 120
FFGGGGRMAR ERRGKNVVHQ LSVTLEDLYN GVTKKLALQK NVICEKCEGV GGKKGSVEKC 180
PLCKGRGMQI HIQQIGPGMV QQIQTVCIEC KGQGERINPK DRCESCSGAK VIREKKIIEV 240
HVEKGMKDGQ KILFHGEGDQ EPELEPGDVI IVLDQKDHSV FQRRGHDLIM KMKIQLSEAL 300
CGFKKTIKTL DNRILVITSK AGEVIKHGDL RCVRDEGMPI YKAPLEKGIL IIQFLVIFPE 360
KHWLSLEKLP QLEALLPPRQ KVRITDDMDQ VELKEFCPNE QNWRQHREAY EEDEDGPQAG 420
VQCQTA 426 
Gene Ontology
 GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006457; P:protein folding; IEA:InterPro.
 GO:0009408; P:response to heat; IEA:InterPro. 
Interpro
 IPR012724; DnaJ.
 IPR002939; DnaJ_C.
 IPR001623; DnaJ_domain.
 IPR018253; DnaJ_domain_CS.
 IPR008971; HSP40/DnaJ_pept-bd.
 IPR001305; HSP_DnaJ_Cys-rich_dom. 
Pfam
 PF00226; DnaJ
 PF01556; DnaJ_C
 PF00684; DnaJ_CXXCXGXG 
SMART
 SM00271; DnaJ 
PROSITE
 PS00636; DNAJ_1
 PS50076; DNAJ_2
 PS51188; ZF_CR 
PRINTS
 PR00625; JDOMAIN.