Tag | Content |
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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 |
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413 | VGKAALEKQIEEVNE | ubiquitination | [1] |
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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. |
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