ID DNJC2_MOUSE Reviewed; 621 AA. AC P54103; Q61866; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 06-MAR-2007, sequence version 2. DT 02-SEP-2026, entry version 184. DE RecName: Full=DnaJ homolog subfamily C member 2; DE AltName: Full=Mouse Id associate 1; DE Short=MIDA1; DE AltName: Full=Zuotin-related factor 1; GN Name=Dnajc2; Synonyms=Mida1, Zrf1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH ID1. RX PubMed=7559602; DOI=10.1074/jbc.270.42.24818; RA Shoji W., Inoue T., Yamamoto T., Obinata M.; RT "MIDA1, a protein associated with Id, regulates cell growth."; RL J. Biol. Chem. 270:24818-24825(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-514, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=8666407; DOI=10.1006/geno.1995.9969; RA Hughes R., Chan F.Y., White R.A., Zon L.I.; RT "Cloning and chromosomal localization of a mouse cDNA with homology to the RT Saccharomyces cerevisiae gene zuotin."; RL Genomics 29:546-550(1995). RN [5] RP INTERACTION WITH ID1. RX PubMed=10581180; DOI=10.1006/bbrc.1999.1779; RA Inoue T., Shoji W., Obinata M.; RT "MIDA1, an Id-associating protein, has two distinct DNA binding activities RT that are converted by the association with Id1: a novel function of Id RT protein."; RL Biochem. Biophys. Res. Commun. 266:147-151(1999). RN [6] RP DNA-BINDING. RX PubMed=10971652; DOI=10.1046/j.1365-2443.2000.00362.x; RA Inoue T., Shoji W., Obinata M.; RT "MIDA1 is a sequence specific DNA binding protein with novel DNA binding RT properties."; RL Genes Cells 5:699-709(2000). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60 AND SER-63, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Teratocarcinoma; RX PubMed=17622165; DOI=10.1021/pr070122r; RA Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.; RT "A differential phosphoproteomic analysis of retinoic acid-treated P19 RT cells."; RL J. Proteome Res. 6:3174-3186(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-49; SER-60; SER-63 RP AND SER-183, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Acts both as a chaperone in the cytosol and as a chromatin CC regulator in the nucleus. When cytosolic, acts as a molecular CC chaperone: component of the ribosome-associated complex (RAC), a CC complex involved in folding or maintaining nascent polypeptides in a CC folding-competent state. In the RAC complex, stimulates the ATPase CC activity of the ribosome-associated pool of Hsp70-type chaperones CC HSPA14 that bind to the nascent polypeptide chain. When nuclear, CC mediates the switching from polycomb-repressed genes to an active CC state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' CC (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex CC from chromatin, thereby facilitating transcription activation. CC {ECO:0000250|UniProtKB:Q99543}. CC -!- SUBUNIT: Component of ribosome-associated complex (RAC), a heterodimer CC composed of Hsp70/DnaK-type chaperone HSPA14 and Hsp40/DnaJ-type CC chaperone DNAJC2 (By similarity). Interacts (via ZRF1-UBD region) with CC ID1 (PubMed:10581180, PubMed:7559602). {ECO:0000250|UniProtKB:Q99543, CC ECO:0000269|PubMed:10581180, ECO:0000269|PubMed:7559602}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624, CC ECO:0000269|PubMed:8666407}. Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:Q99543}. CC -!- TISSUE SPECIFICITY: Expressed in all tissues. CC {ECO:0000269|PubMed:8666407}. CC -!- DOMAIN: The ZRF1-UBD region specifically recognizes and binds CC H2AK119ub. The ZRF1-UBD region is also involved in protein-protein CC interactions with other proteins, suggesting that it may be masked by CC some regulator, thereby preventing its association with H2AK119ub. CC {ECO:0000250|UniProtKB:Q99543}. CC -!- PTM: Phosphorylated in M (mitotic) phase. CC {ECO:0000250|UniProtKB:Q99543}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D63784; BAA09854.1; -; mRNA. DR EMBL; AK131964; BAE20907.1; -; mRNA. DR EMBL; BC052027; AAH52027.1; -; mRNA. DR EMBL; U53208; AAC52486.1; -; mRNA. DR CCDS; CCDS19107.1; -. DR PIR; A57591; A57591. DR RefSeq; NP_033610.1; NM_009584.5. DR AlphaFoldDB; P54103; -. DR SMR; P54103; -. DR BioGRID; 204711; 7. DR FunCoup; P54103; 5145. DR IntAct; P54103; 1. DR MINT; P54103; -. DR STRING; 10090.ENSMUSP00000030771; -. DR GlyGen; P54103; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P54103; -. DR PhosphoSitePlus; P54103; -. DR SwissPalm; P54103; -. DR jPOST; P54103; -. DR PaxDb; 10090-ENSMUSP00000030771; -. DR PeptideAtlas; P54103; -. DR ProteomicsDB; 277352; -. DR Pumba; P54103; -. DR Antibodypedia; 9291; 186 antibodies from 31 providers. DR DNASU; 22791; -. DR Ensembl; ENSMUST00000030771.12; ENSMUSP00000030771.6; ENSMUSG00000029014.15. DR GeneID; 22791; -. DR KEGG; mmu:22791; -. DR UCSC; uc008wpa.1; mouse. DR AGR; MGI:99470; -. DR CTD; 27000; -. DR MGI; MGI:99470; Dnajc2. DR VEuPathDB; HostDB:ENSMUSG00000029014; -. DR eggNOG; KOG0724; Eukaryota. DR GeneTree; ENSGT00940000155441; -. DR InParanoid; P54103; -. DR OMA; SFWYDFD; -. DR OrthoDB; 1690618at2759; -. DR PhylomeDB; P54103; -. DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response. DR BioGRID-ORCS; 22791; 28 hits in 82 CRISPR screens. DR PRO; PR:P54103; -. DR Proteomes; UP000000589; Chromosome 5. DR RNAct; P54103; protein. DR Bgee; ENSMUSG00000029014; Expressed in embryonic post-anal tail and 264 other cell types or tissues. DR ExpressionAtlas; P54103; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISO:GO_Central. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0031965; C:nuclear membrane; ISO:GO_Central. DR GO; GO:0005730; C:nucleolus; ISO:GO_Central. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0101031; C:protein folding chaperone complex; ISO:GO_Central. DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB. DR GO; GO:0042393; F:histone binding; ISS:UniProtKB. DR GO; GO:0030544; F:Hsp70 protein binding; ISO:GO_Central. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR GO; GO:0061649; F:ubiquitin-modified histone reader activity; ISS:UniProtKB. DR GO; GO:0051083; P:'de novo' cotranslational protein folding; IBA:GO_Central. DR GO; GO:0006260; P:DNA replication; IMP:MGI. DR GO; GO:0030308; P:negative regulation of cell growth; ISO:GO_Central. DR GO; GO:2000279; P:negative regulation of DNA biosynthetic process; IMP:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro. DR CDD; cd06257; DnaJ; 1. DR CDD; cd00167; SANT; 2. DR FunFam; 1.10.10.60:FF:000180; DnaJ (Hsp40) homolog, subfamily C, member 2; 1. DR FunFam; 1.10.287.110:FF:000024; DnaJ (Hsp40) homolog, subfamily C, member 2; 1. DR FunFam; 1.10.10.60:FF:000215; dnaJ homolog subfamily C member 2 isoform X1; 1. DR FunFam; 1.10.8.840:FF:000001; dnaJ homolog subfamily C member 2 isoform X1; 1. DR Gene3D; 1.10.287.110; DnaJ domain; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 2. DR Gene3D; 1.10.8.840; Ribosome-associated complex head domain; 1. DR InterPro; IPR001623; DnaJ_domain. DR InterPro; IPR018253; DnaJ_domain_CS. DR InterPro; IPR009057; Homeodomain-like_sf. DR InterPro; IPR036869; J_dom_sf. DR InterPro; IPR017930; Myb_dom. DR InterPro; IPR032003; RAC_head. DR InterPro; IPR042569; RAC_head_sf. DR InterPro; IPR001005; SANT/Myb. DR InterPro; IPR017884; SANT_dom. DR InterPro; IPR054076; ZUO1-like_ZHD. DR InterPro; IPR044634; Zuotin/DnaJC2. DR PANTHER; PTHR43999; DNAJ HOMOLOG SUBFAMILY C MEMBER 2; 1. DR PANTHER; PTHR43999:SF1; DNAJ HOMOLOG SUBFAMILY C MEMBER 2; 1. DR Pfam; PF00226; DnaJ; 1. DR Pfam; PF23082; Myb_DNA-binding_2; 2. DR Pfam; PF16717; RAC_head; 1. DR Pfam; PF21884; ZUO1-like_ZHD; 1. DR SMART; SM00271; DnaJ; 1. DR SMART; SM00717; SANT; 2. DR SUPFAM; SSF46565; Chaperone J-domain; 1. DR SUPFAM; SSF46689; Homeodomain-like; 2. DR PROSITE; PS00636; DNAJ_1; 1. DR PROSITE; PS50076; DNAJ_2; 1. DR PROSITE; PS51293; SANT; 1. PE 1: Evidence at protein level; KW Acetylation; Activator; Chaperone; Chromatin regulator; Cytoplasm; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Transcription; KW Transcription regulation. FT CHAIN 1..621 FT /note="DnaJ homolog subfamily C member 2" FT /id="PRO_0000071124" FT DOMAIN 88..161 FT /note="J" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286" FT DOMAIN 449..511 FT /note="SANT 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624" FT DOMAIN 549..604 FT /note="SANT 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624" FT REGION 160..250 FT /note="ZRF1-UBD" FT REGION 422..453 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 422..433 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:Q99543" FT MOD_RES 47 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 49 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 60 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17622165, FT ECO:0007744|PubMed:21183079" FT MOD_RES 63 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17622165, FT ECO:0007744|PubMed:21183079" FT MOD_RES 183 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT CONFLICT 473 FT /note="T -> R (in Ref. 4; AAC52486)" FT /evidence="ECO:0000305" FT CONFLICT 478 FT /note="E -> D (in Ref. 4; AAC52486)" FT /evidence="ECO:0000305" FT CONFLICT 502..514 FT /note="KAKSLQKLDPHQK -> EVRGPKSWGSSKR (in Ref. 4; FT AAC52486)" FT /evidence="ECO:0000305" SQ SEQUENCE 621 AA; 71722 MW; 0FFC511028EA1C41 CRC64; MLLLPSAAEG QGTAITHALT SASSVCQVEP VGRWFEAFVK RRNRNASTSF QELEDKKELS EESEDEELQL EEFPMLKTLD PKDWKNQDHY AVLGLGHVRY TATQRQIKAA HKAMVLKHHP DKRKAAGEPI KEGDNDYFTC ITKAYEMLSD PVKRRAFNSV DPTFDNSVPS KSEAKDNFFQ VFSPVFERNS RWSNKKNVPK LGDMNSSFED VDAFYSFWYN FDSWREFSYL DEEEKEKAEC RDERKWIEKQ NRATRAQRKK EEMNRIRTLV DNAYSCDPRI KKFKEEEKAK KEAEKKAKAE ARRKEQEAKE KQRQAELEAV RLAKEKEEEE VRQQALLAKK EKDIQKKAIK KERQKLRNSC KSWNHFSDNE ADRVKMMEEV EKLCDRLELA SLQGLNEILA SSTREVGKAA LEKQIEEVNE QMRREKEEAD ARMRQASKNA EKSTGGSGSG SKNWSEDDLQ LLIKAVNLFP AGTNSRWEVI ANYMNIHSSS GVKRTAKDVI SKAKSLQKLD PHQKDDINKK AFDKFKKEHG VASQADSAAP SERFEGPCID STPWTTEEQK LLEQALKTYP VNTPERWEKI AEAVPGRTKK DCMRRYKELV EMVKAKKAAQ EQVLNASRAR K //