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DnaJ homolog subfamily C member 2 (Mouse Id associate 1) (MIDA1) (Zuotin-related factor 1)

 DNJC2_MOUSE             Reviewed;         621 AA.
P54103; Q61866;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
06-MAR-2007, sequence version 2.
25-APR-2018, entry version 143.
RecName: Full=DnaJ homolog subfamily C member 2;
AltName: Full=Mouse Id associate 1;
Short=MIDA1;
AltName: Full=Zuotin-related factor 1;
Name=Dnajc2; Synonyms=Mida1, Zrf1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH ID1.
PubMed=7559602; DOI=10.1074/jbc.270.42.24818;
Shoji W., Inoue T., Yamamoto T., Obinata M.;
"MIDA1, a protein associated with Id, regulates cell growth.";
J. Biol. Chem. 270:24818-24825(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-514, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=8666407; DOI=10.1006/geno.1995.9969;
Hughes R., Chan F.Y., White R.A., Zon L.I.;
"Cloning and chromosomal localization of a mouse cDNA with homology to
the Saccharomyces cerevisiae gene zuotin.";
Genomics 29:546-550(1995).
[5]
INTERACTION WITH ID1.
PubMed=10581180; DOI=10.1006/bbrc.1999.1779;
Inoue T., Shoji W., Obinata M.;
"MIDA1, an Id-associating protein, has two distinct DNA binding
activities that are converted by the association with Id1: a novel
function of Id protein.";
Biochem. Biophys. Res. Commun. 266:147-151(1999).
[6]
DNA-BINDING.
PubMed=10971652; DOI=10.1046/j.1365-2443.2000.00362.x;
Inoue T., Shoji W., Obinata M.;
"MIDA1 is a sequence specific DNA binding protein with novel DNA
binding properties.";
Genes Cells 5:699-709(2000).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60 AND SER-63, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Teratocarcinoma;
PubMed=17622165; DOI=10.1021/pr070122r;
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
"A differential phosphoproteomic analysis of retinoic acid-treated P19
cells.";
J. Proteome Res. 6:3174-3186(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-49; SER-60;
SER-63 AND SER-183, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: 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'. {ECO:0000250}.
-!- SUBUNIT: Component of ribosome-associated complex (RAC), a
heterodimer composed of Hsp70/DnaK-type chaperone HSPA14 and
Hsp40/DnaJ-type chaperone DNAJC2 (By similarity). Interacts (via
ZRF1-UBD region) with ID1. {ECO:0000250,
ECO:0000269|PubMed:10581180, ECO:0000269|PubMed:7559602}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00624, ECO:0000269|PubMed:8666407}. Cytoplasm, cytosol
{ECO:0000250|UniProtKB:Q99543}.
-!- TISSUE SPECIFICITY: Expressed in all tissues.
{ECO:0000269|PubMed:8666407}.
-!- DOMAIN: The ZRF1-UBD region specifically recognizes and binds
H2AK119ub. The ZRF1-UBD region is also involved in protein-protein
interactions with other proteins, suggesting that it may be masked
by some regulator, thereby preventing its association with
H2AK119ub (By similarity). {ECO:0000250}.
-!- PTM: Phosphorylated in M (mitotic) phase. {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; D63784; BAA09854.1; -; mRNA.
EMBL; AK131964; BAE20907.1; -; mRNA.
EMBL; BC052027; AAH52027.1; -; mRNA.
EMBL; U53208; AAC52486.1; -; mRNA.
CCDS; CCDS19107.1; -.
PIR; A57591; A57591.
RefSeq; NP_033610.1; NM_009584.4.
UniGene; Mm.266312; -.
ProteinModelPortal; P54103; -.
SMR; P54103; -.
BioGrid; 204711; 2.
IntAct; P54103; 1.
MINT; P54103; -.
STRING; 10090.ENSMUSP00000030771; -.
iPTMnet; P54103; -.
PhosphoSitePlus; P54103; -.
EPD; P54103; -.
MaxQB; P54103; -.
PaxDb; P54103; -.
PeptideAtlas; P54103; -.
PRIDE; P54103; -.
Ensembl; ENSMUST00000030771; ENSMUSP00000030771; ENSMUSG00000029014.
GeneID; 22791; -.
KEGG; mmu:22791; -.
UCSC; uc008wpa.1; mouse.
CTD; 27000; -.
MGI; MGI:99470; Dnajc2.
eggNOG; KOG0724; Eukaryota.
eggNOG; COG5269; LUCA.
GeneTree; ENSGT00530000063419; -.
HOGENOM; HOG000006900; -.
HOVERGEN; HBG008782; -.
InParanoid; P54103; -.
KO; K09522; -.
OMA; TTPDRWD; -.
OrthoDB; EOG091G04S8; -.
PhylomeDB; P54103; -.
TreeFam; TF105834; -.
Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
PRO; PR:P54103; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000029014; -.
CleanEx; MM_DNAJC2; -.
ExpressionAtlas; P54103; baseline and differential.
Genevisible; P54103; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0031965; C:nuclear membrane; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0042393; F:histone binding; ISS:UniProtKB.
GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI.
GO; GO:0061649; F:ubiquitin modification-dependent histone binding; ISS:UniProtKB.
GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
GO; GO:0006260; P:DNA replication; IMP:MGI.
GO; GO:2000279; P:negative regulation of DNA biosynthetic process; IMP:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd06257; DnaJ; 1.
CDD; cd00167; SANT; 2.
Gene3D; 1.10.287.110; -; 1.
InterPro; IPR001623; DnaJ_domain.
InterPro; IPR018253; DnaJ_domain_CS.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR036869; J_dom_sf.
InterPro; IPR017930; Myb_dom.
InterPro; IPR032003; RAC_head.
InterPro; IPR001005; SANT/Myb.
InterPro; IPR017884; SANT_dom.
Pfam; PF00226; DnaJ; 1.
Pfam; PF00249; Myb_DNA-binding; 2.
Pfam; PF16717; RAC_head; 1.
SMART; SM00271; DnaJ; 1.
SMART; SM00717; SANT; 2.
SUPFAM; SSF46565; SSF46565; 1.
SUPFAM; SSF46689; SSF46689; 2.
PROSITE; PS00636; DNAJ_1; 1.
PROSITE; PS50076; DNAJ_2; 1.
PROSITE; PS51293; SANT; 1.
1: Evidence at protein level;
Acetylation; Activator; Chaperone; Chromatin regulator;
Complete proteome; Cytoplasm; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Transcription; Transcription regulation.
CHAIN 1 621 DnaJ homolog subfamily C member 2.
/FTId=PRO_0000071124.
DOMAIN 88 161 J. {ECO:0000255|PROSITE-
ProRule:PRU00286}.
DOMAIN 449 511 SANT 1. {ECO:0000255|PROSITE-
ProRule:PRU00624}.
DOMAIN 549 604 SANT 2. {ECO:0000255|PROSITE-
ProRule:PRU00624}.
REGION 160 250 ZRF1-UBD.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q99543}.
MOD_RES 47 47 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 49 49 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 60 60 Phosphoserine.
{ECO:0000244|PubMed:17622165,
ECO:0000244|PubMed:21183079}.
MOD_RES 63 63 Phosphoserine.
{ECO:0000244|PubMed:17622165,
ECO:0000244|PubMed:21183079}.
MOD_RES 183 183 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CONFLICT 473 473 T -> R (in Ref. 4; AAC52486).
{ECO:0000305}.
CONFLICT 478 478 E -> D (in Ref. 4; AAC52486).
{ECO:0000305}.
CONFLICT 502 514 KAKSLQKLDPHQK -> EVRGPKSWGSSKR (in Ref.
4; AAC52486). {ECO:0000305}.
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


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