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   16-NOV-2011, entry version 88.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH ID1.
RX   MEDLINE=96027574; 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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/6; 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
RT   project: 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   MEDLINE=96115610; 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
RT   the 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
RT   activities that are converted by the association with Id1: a novel
RT   function of Id 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
RT   binding properties.";
RL   Genes Cells 5:699-709(2000).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; THR-48; SER-49;
RP   SER-60 AND SER-63, AND MASS SPECTROMETRY.
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, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Acts both as a chaperone in the cytosol and as a
CC       chromatin regulator in the nucleus. When cytosolic, acts as a
CC       molecular chaperone: component of the ribosome-associated complex
CC       (RAC), a complex involved in folding or maintaining nascent
CC       polypeptides in a folding-competent state. In the RAC complex,
CC       stimulates the ATPase activity of the ribosome-associated pool of
CC       Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide
CC       chain. When nuclear, mediates the switching from polycomb-
CC       repressed genes to an active state: specifically recruited at
CC       histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes
CC       the displacement of the polycomb PRC1 complex from chromatin,
CC       thereby facilitating transcription activation (By similarity).
CC       Specifically binds DNA sequence 5'-GTCAAGC-3'.
CC   -!- SUBUNIT: Component of ribosome-associated complex (RAC), a
CC       heterodimer composed of Hsp70/DnaK-type chaperone HSPA14 and
CC       Hsp40/DnaJ-type chaperone DNAJC2 (By similarity). Interacts (via
CC       ZRF1-UBD region) with ID1.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytosol (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues.
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
CC       by some regulator, thereby preventing its association with
CC       H2AK119ub (By similarity).
CC   -!- PTM: Phosphorylated in M (mitotic) phase (By similarity).
CC   -!- SIMILARITY: Contains 1 J domain.
CC   -!- SIMILARITY: Contains 2 SANT domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs 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   IPI; IPI00126317; -.
DR   PIR; A57591; A57591.
DR   RefSeq; NP_033610.1; NM_009584.4.
DR   UniGene; Mm.266312; -.
DR   ProteinModelPortal; P54103; -.
DR   SMR; P54103; 85-162, 450-512, 543-601.
DR   STRING; P54103; -.
DR   PhosphoSite; P54103; -.
DR   PRIDE; P54103; -.
DR   Ensembl; ENSMUST00000030771; ENSMUSP00000030771; ENSMUSG00000029014.
DR   GeneID; 22791; -.
DR   KEGG; mmu:22791; -.
DR   UCSC; uc008woy.1; mouse.
DR   CTD; 27000; -.
DR   MGI; MGI:99470; Dnajc2.
DR   eggNOG; roNOG07168; -.
DR   HOGENOM; HBG383362; -.
DR   HOVERGEN; HBG008782; -.
DR   InParanoid; P54103; -.
DR   OMA; CKTWNHF; -.
DR   OrthoDB; EOG4D26PN; -.
DR   PhylomeDB; P54103; -.
DR   NextBio; 303379; -.
DR   ArrayExpress; P54103; -.
DR   Bgee; P54103; -.
DR   CleanEx; MM_DNAJC2; -.
DR   Genevestigator; P54103; -.
DR   GermOnline; ENSMUSG00000029014; Mus musculus.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR   GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IMP:MGI.
DR   GO; GO:0000085; P:G2 phase of mitotic cell cycle; IMP:MGI.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; ISS:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   InterPro; IPR001623; DnaJ_N.
DR   InterPro; IPR018253; Heat_shock_DnaJ_CS.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   InterPro; IPR014778; Myb_DNA-bd.
DR   InterPro; IPR001005; SANT_DNA-bd.
DR   InterPro; IPR017884; SANT_eukarya.
DR   InterPro; IPR017930; Tscrpt_reg_HTH_Myb-type.
DR   Gene3D; G3DSA:1.10.287.110; DnaJ_N; 1.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1.
DR   KO; K09522; -.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF00249; Myb_DNA-binding; 2.
DR   SMART; SM00271; DnaJ; 1.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF46565; DnaJ_N; 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   Activator; Chaperone; Chromatin regulator; Complete proteome;
KW   Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Transcription; Transcription regulation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    621       DnaJ homolog subfamily C member 2.
FT                                /FTId=PRO_0000071124.
FT   DOMAIN       88    161       J.
FT   DOMAIN      449    511       SANT 1.
FT   DOMAIN      549    604       SANT 2.
FT   REGION      160    250       ZRF1-UBD.
FT   MOD_RES      47     47       Phosphoserine.
FT   MOD_RES      48     48       Phosphothreonine.
FT   MOD_RES      49     49       Phosphoserine.
FT   MOD_RES      60     60       Phosphoserine.
FT   MOD_RES      63     63       Phosphoserine.
FT   CONFLICT    473    473       T -> R (in Ref. 4; AAC52486).
FT   CONFLICT    478    478       E -> D (in Ref. 4; AAC52486).
FT   CONFLICT    502    514       KAKSLQKLDPHQK -> EVRGPKSWGSSKR (in Ref.
FT                                4; AAC52486).
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
//