CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008830
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DnaJ homolog subfamily C member 2 
Protein Synonyms/Alias
 Mouse Id associate 1; MIDA1; Zuotin-related factor 1 
Gene Name
 Dnajc2 
Gene Synonyms/Alias
 Mida1; Zrf1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
413VGKAALEKQIEEVNEubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
 Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb- repressed genes to an active state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex from chromatin, thereby facilitating transcription activation (By similarity). Specifically binds DNA sequence 5'-GTCAAGC-3'. 
Sequence Annotation
 DOMAIN 88 161 J.
 DOMAIN 449 511 SANT 1.
 DOMAIN 549 604 SANT 2.
 REGION 160 250 ZRF1-UBD.
 MOD_RES 47 47 Phosphoserine.
 MOD_RES 48 48 Phosphothreonine.
 MOD_RES 49 49 Phosphoserine.
 MOD_RES 60 60 Phosphoserine.
 MOD_RES 63 63 Phosphoserine.  
Keyword
 Activator; Chaperone; Chromatin regulator; Complete proteome; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 621 AA 
Protein Sequence
MLLLPSAAEG QGTAITHALT SASSVCQVEP VGRWFEAFVK RRNRNASTSF QELEDKKELS 60
EESEDEELQL EEFPMLKTLD PKDWKNQDHY AVLGLGHVRY TATQRQIKAA HKAMVLKHHP 120
DKRKAAGEPI KEGDNDYFTC ITKAYEMLSD PVKRRAFNSV DPTFDNSVPS KSEAKDNFFQ 180
VFSPVFERNS RWSNKKNVPK LGDMNSSFED VDAFYSFWYN FDSWREFSYL DEEEKEKAEC 240
RDERKWIEKQ NRATRAQRKK EEMNRIRTLV DNAYSCDPRI KKFKEEEKAK KEAEKKAKAE 300
ARRKEQEAKE KQRQAELEAV RLAKEKEEEE VRQQALLAKK EKDIQKKAIK KERQKLRNSC 360
KSWNHFSDNE ADRVKMMEEV EKLCDRLELA SLQGLNEILA SSTREVGKAA LEKQIEEVNE 420
QMRREKEEAD ARMRQASKNA EKSTGGSGSG SKNWSEDDLQ LLIKAVNLFP AGTNSRWEVI 480
ANYMNIHSSS GVKRTAKDVI SKAKSLQKLD PHQKDDINKK AFDKFKKEHG VASQADSAAP 540
SERFEGPCID STPWTTEEQK LLEQALKTYP VNTPERWEKI AEAVPGRTKK DCMRRYKELV 600
EMVKAKKAAQ EQVLNASRAR K 621 
Gene Ontology
 GO:0005829; C:cytosol; ISS:UniProtKB.
 GO:0031965; C:nuclear membrane; IEA:Compara.
 GO:0005634; C:nucleus; ISS:UniProtKB.
 GO:0003682; F:chromatin binding; ISS:UniProtKB.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0042393; F:histone binding; ISS:UniProtKB.
 GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
 GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
 GO:0006260; P:DNA replication; IMP:MGI.
 GO:0030308; P:negative regulation of cell growth; IEA:Compara.
 GO:2000279; P:negative regulation of DNA biosynthetic process; IMP:MGI.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; ISS:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR001623; DnaJ_domain.
 IPR018253; DnaJ_domain_CS.
 IPR009057; Homeodomain-like.
 IPR017930; Myb_dom.
 IPR001005; SANT/Myb.
 IPR017884; SANT_dom. 
Pfam
 PF00226; DnaJ
 PF00249; Myb_DNA-binding 
SMART
 SM00271; DnaJ
 SM00717; SANT 
PROSITE
 PS00636; DNAJ_1
 PS50076; DNAJ_2
 PS51293; SANT 
PRINTS