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DnaJ homolog subfamily C member 2 (Gliosarcoma-related antigen MIDA1) (Zuotin-related factor 1)

 DNJC2_RAT               Reviewed;         621 AA.
Q7TQ20; Q5HZY5; Q7TQ18; Q9WVG4;
06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
23-MAY-2018, entry version 117.
RecName: Full=DnaJ homolog subfamily C member 2;
AltName: Full=Gliosarcoma-related antigen MIDA1;
AltName: Full=Zuotin-related factor 1;
Name=Dnajc2; Synonyms=Mida1, Zrf1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
STRAIN=Fischer 344; TISSUE=Thymus;
Yang T., Figallo L.A., Vujanovic N.L., Jenkins F.J., Okada H.,
Pollack I.F., Chambers W.H.;
"Characterization of Rat zuotin related factors (ZRFs).";
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-562.
STRAIN=Fischer 344;
PubMed=11289140;
Okada H., Attanucci J., Giezeman-Smits K.M., Brissette-Storkus C.,
Fellows W.K., Gambotto A., Pollack L.F., Pogue-Geile K., Lotze M.T.,
Bozik M.E., Chambers W.H.;
"Immunization with an antigen identified by cytokine tumor vaccine-
assisted SEREX (CAS) suppressed growth of the rat 9L glioma in vivo.";
Cancer Res. 61:2625-2631(2001).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-60 AND SER-183,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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. Specifically binds
DNA sequence 5'-GTCAAGC-3' (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts (via ZRF1-UBD region) with ID1. Component of
ribosome-associated complex (RAC), a heterodimer composed of
Hsp70/DnaK-type chaperone HSPA14 and Hsp40/DnaJ-type chaperone
DNAJC2 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00624}. Cytoplasm, cytosol
{ECO:0000250|UniProtKB:Q99543}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q7TQ20-1; Sequence=Displayed;
Name=2;
IsoId=Q7TQ20-2; Sequence=VSP_040720;
Note=No experimental confirmation available.;
-!- 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; AY322161; AAP84338.1; -; mRNA.
EMBL; AY322163; AAP84340.1; -; mRNA.
EMBL; BC088838; AAH88838.1; -; mRNA.
EMBL; AF118853; AAD45407.1; -; mRNA.
RefSeq; NP_446228.2; NM_053776.2.
RefSeq; XP_008760850.1; XM_008762628.2.
UniGene; Rn.11908; -.
ProteinModelPortal; Q7TQ20; -.
SMR; Q7TQ20; -.
CORUM; Q7TQ20; -.
STRING; 10116.ENSRNOP00000016909; -.
iPTMnet; Q7TQ20; -.
PhosphoSitePlus; Q7TQ20; -.
PaxDb; Q7TQ20; -.
PRIDE; Q7TQ20; -.
GeneID; 116456; -.
KEGG; rno:116456; -.
CTD; 27000; -.
RGD; 620524; Dnajc2.
eggNOG; KOG0724; Eukaryota.
eggNOG; COG5269; LUCA.
HOGENOM; HOG000006900; -.
HOVERGEN; HBG008782; -.
InParanoid; Q7TQ20; -.
KO; K09522; -.
PhylomeDB; Q7TQ20; -.
TreeFam; TF105834; -.
PRO; PR:Q7TQ20; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
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:0061649; F:ubiquitin modification-dependent histone binding; ISS:UniProtKB.
GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
GO; GO:0030308; P:negative regulation of cell growth; IDA:RGD.
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; Alternative splicing; 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_0000280179.
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:22673903}.
MOD_RES 49 49 Phosphoserine.
{ECO:0000250|UniProtKB:Q99543}.
MOD_RES 60 60 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 63 63 Phosphoserine.
{ECO:0000250|UniProtKB:Q99543}.
MOD_RES 183 183 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
VAR_SEQ 1 74 Missing (in isoform 2).
{ECO:0000303|Ref.1}.
/FTId=VSP_040720.
CONFLICT 446 446 G -> R (in Ref. 2; AAH88838).
{ECO:0000305}.
SEQUENCE 621 AA; 71769 MW; 06ED1C7AA56267A6 CRC64;
MLLLPSAAEG QGTAITHALT SASAVCQVEP VGRWFEAFVK RRNRNASTSF QELEDKKELS
EESEDEELQL EEFPMLKTLD PKDWKNQDHY AVLGLGHVRY KATQRQIKAA HKTMVLKHHP
DKRKAAGEPI KEGDNDYFTC ITKAYEMLSD PVKRRAFNSV DPTFDNSVPS KSEAKENFFQ
VFSPVFERNS RWSNKKNVPK LGDMNSSFED VDAFYSFWYN FDSWREFSYL DEEEKEKAEC
RDERKWIEKQ NRATRAQRKK EEMNRIRTLV DNAYSCDPRI KKFKEEGKAK KEAEKRAKAE
ARRKEQEAKE KQRQAELEAV RLAKEKEEEE VRQQALLAKK EKEIQKKAIK KERQKLRNSC
KNWNHFSDNE ADRVKMMEEV EKLCDRLELA SLQCLNEILA SSTREVGKAA LEKQIEEVNE
LMRKEKEEAD ARMRQASKNA EKSTGGSGSG SKNWSEDDLQ LLIKAVNLFP AGTNSRWEVI
ANYMNIHSSS GVKRTAKDVI GKAKSLQKLD PHQKDDINKK AFDKFKKEHG VAPQADSAAP
SERFEGPCID SIPWTTEEQK LLEQALKTYP VNTPERWEKI AEAVPGRTKK DCMRRYKELV
EMVKAKKAAQ EQVLNASRAR K


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