DNJC2_MOUSE
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 03-AUG-2022, entry version 165.
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}.
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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_009584.4.
DR AlphaFoldDB; P54103; -.
DR SMR; P54103; -.
DR BioGRID; 204711; 7.
DR IntAct; P54103; 1.
DR MINT; P54103; -.
DR STRING; 10090.ENSMUSP00000030771; -.
DR iPTMnet; P54103; -.
DR PhosphoSitePlus; P54103; -.
DR EPD; P54103; -.
DR jPOST; P54103; -.
DR MaxQB; P54103; -.
DR PaxDb; P54103; -.
DR PeptideAtlas; P54103; -.
DR PRIDE; P54103; -.
DR ProteomicsDB; 277352; -.
DR Antibodypedia; 9291; 188 antibodies from 30 providers.
DR DNASU; 22791; -.
DR Ensembl; ENSMUST00000030771; ENSMUSP00000030771; ENSMUSG00000029014.
DR GeneID; 22791; -.
DR KEGG; mmu:22791; -.
DR UCSC; uc008wpa.1; mouse.
DR CTD; 27000; -.
DR MGI; MGI:99470; Dnajc2.
DR VEuPathDB; HostDB:ENSMUSG00000029014; -.
DR eggNOG; KOG0724; Eukaryota.
DR GeneTree; ENSGT00940000155441; -.
DR InParanoid; P54103; -.
DR OMA; QNGVDHK; -.
DR OrthoDB; 1392575at2759; -.
DR PhylomeDB; P54103; -.
DR TreeFam; TF105834; -.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR BioGRID-ORCS; 22791; 26 hits in 76 CRISPR screens.
DR ChiTaRS; Dnajc2; mouse.
DR PRO; PR:P54103; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P54103; protein.
DR Bgee; ENSMUSG00000029014; Expressed in embryonic post-anal tail and 260 other tissues.
DR ExpressionAtlas; P54103; baseline and differential.
DR Genevisible; P54103; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:MGI.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0061649; F:ubiquitin modification-dependent histone binding; ISS:UniProtKB.
DR GO; GO:0051083; P:'de novo' cotranslational protein folding; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IMP:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR GO; GO:2000279; P:negative regulation of DNA biosynthetic process; IMP:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd00167; SANT; 2.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 1.10.8.840; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR009057; Homeobox-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; IPR044634; Zuotin/DnaJC2.
DR PANTHER; PTHR43999; PTHR43999; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF00249; Myb_DNA-binding; 2.
DR Pfam; PF16717; RAC_head; 1.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF46689; SSF46689; 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..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..453
FT /note="Polar 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
