CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019727
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DnaJ homolog subfamily C member 2 
Protein Synonyms/Alias
 M-phase phosphoprotein 11; Zuotin-related factor 1 
Gene Name
 DNAJC2 
Gene Synonyms/Alias
 MPHOSPH11; MPP11; ZRF1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
40RWFEAFVKRRNRNASubiquitination[1]
514QKLDPHQKDDINKKAubiquitination[2]
567KLLEQALKTYPVNTPubiquitination[2]
Reference
 [1] 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]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983
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. Specifically binds DNA sequence 5'-GTCAAGC-3'. 
Sequence Annotation
 DOMAIN 88 161 J.
 DOMAIN 449 511 SANT 1.
 DOMAIN 549 604 SANT 2.
 REGION 23 31 Epitope (recognized by CD8(+) cytotoxic
 REGION 160 250 ZRF1-UBD.
 MOD_RES 47 47 Phosphoserine.
 MOD_RES 49 49 Phosphoserine.
 MOD_RES 60 60 Phosphoserine.
 MOD_RES 63 63 Phosphoserine.  
Keyword
 3D-structure; Activator; Alternative splicing; Chaperone; Chromatin regulator; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 621 AA 
Protein Sequence
MLLLPSAADG RGTAITHALT SASTLCQVEP VGRWFEAFVK RRNRNASASF QELEDKKELS 60
EESEDEELQL EEFPMLKTLD PKDWKNQDHY AVLGLGHVRY KATQRQIKAA HKAMVLKHHP 120
DKRKAAGEPI KEGDNDYFTC ITKAYEMLSD PVKRRAFNSV DPTFDNSVPS KSEAKDNFFE 180
VFTPVFERNS RWSNKKNVPK LGDMNSSFED VDIFYSFWYN FDSWREFSYL DEEEKEKAEC 240
RDERRWIEKQ NRATRAQRKK EEMNRIRTLV DNAYSCDPRI KKFKEEEKAK KEAEKKAKAE 300
AKRKEQEAKE KQRQAELEAA RLAKEKEEEE VRQQALLAKK EKDIQKKAIK KERQKLRNSC 360
KTWNHFSDNE AERVKMMEEV EKLCDRLELA SLQCLNETLT SCTKEVGKAA LEKQIEEINE 420
QIRKEKEEAE ARMRQASKNT EKSTGGGGNG SKNWSEDDLQ LLIKAVNLFP AGTNSRWEVI 480
ANYMNIHSSS GVKRTAKDVI GKAKSLQKLD PHQKDDINKK AFDKFKKEHG VVPQADNATP 540
SERFEGPYTD FTPWTTEEQK LLEQALKTYP VNTPERWEKI AEAVPGRTKK DCMKRYKELV 600
EMVKAKKAAQ EQVLNASRAK K 621 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0031965; C:nuclear membrane; IDA:HPA.
 GO:0003682; F:chromatin binding; IDA:UniProtKB.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0042393; F:histone binding; IDA:UniProtKB.
 GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
 GO:0051083; P:'de novo' cotranslational protein folding; TAS:UniProtKB.
 GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
 GO:0006260; P:DNA replication; IEA:Compara.
 GO:0000085; P:G2 phase of mitotic cell cycle; IEA:Compara.
 GO:0030308; P:negative regulation of cell growth; IEA:Compara.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR001623; DnaJ_domain.
 IPR018253; DnaJ_domain_CS.
 IPR009057; Homeodomain-like.
 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