DNJC9_MOUSE
ID DNJC9_MOUSE Reviewed; 259 AA.
AC Q91WN1; Q3TSG3; Q8R0E3;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=DnaJ homolog subfamily C member 9;
GN Name=Dnajc9;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Egg, and Pituitary;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Eye, and Mammary tumor;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, 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 as a dual histone chaperone and heat shock co-chaperone
CC (By similarity). As a histone chaperone, forms a co-chaperone complex
CC with MCM2 and histone H3-H4 heterodimers; and may thereby assist MCM2
CC in histone H3-H4 heterodimer recognition and facilitate the assembly of
CC histones into nucleosomes (By similarity). May also act as a histone
CC co-chaperone together with TONSL (By similarity). May recruit histone
CC chaperones ASF1A, NASP and SPT2 to histone H3-H4 heterodimers (By
CC similarity). Also plays a role as co-chaperone of the HSP70 family of
CC molecular chaperone proteins, such as HSPA1A, HSPA1B and HSPA8 (By
CC similarity). As a co-chaperone, may play a role in the recruitment of
CC HSP70-type molecular chaperone machinery to histone H3-H4 substrates,
CC thereby maintaining the histone structural integrity (By similarity).
CC Exhibits activity to assemble histones onto DNA in vitro (By
CC similarity). {ECO:0000250|UniProtKB:Q8WXX5}.
CC -!- SUBUNIT: Forms a co-chaperone complex with MCM2 and histone H3.3-H4
CC dimers (By similarity). Within the complex, interacts (via C-terminus)
CC with MCM2 (via N-terminus); the interaction is histone-dependent (By
CC similarity). Within the complex, interacts (via C-terminus) with
CC histone H3.3-H4 heterodimers; the interaction is direct (By
CC similarity). Interacts with histones H4, H3.3, H3.2 and H3.1, but not
CC with CENPA or the testis-specific histone H3.1t (By similarity).
CC Interacts (via J domain) with HSPA1A, HSPA1B and HSPA8 (By similarity).
CC May interact with TONSL; the interaction seems to be histone-dependent
CC (By similarity). May interact with HSPA8 and BAG2; the interactions
CC seem to be histone-dependent (By similarity).
CC {ECO:0000250|UniProtKB:Q8WXX5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WXX5}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8WXX5}. Cell membrane
CC {ECO:0000250|UniProtKB:Q8WXX5}. Note=Predominantly nuclear.
CC Translocates to the cytoplasm and membrane after heat shock.
CC {ECO:0000250|UniProtKB:Q8WXX5}.
CC -!- DOMAIN: The functional J domain is required for the release from
CC histone-dependent chromatin-binding. {ECO:0000250|UniProtKB:Q8WXX5}.
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DR EMBL; AK075979; BAC36092.1; -; mRNA.
DR EMBL; AK077324; BAC36750.1; -; mRNA.
DR EMBL; AK153033; BAE31665.1; -; mRNA.
DR EMBL; AK162075; BAE36712.1; -; mRNA.
DR EMBL; BC014686; AAH14686.2; -; mRNA.
DR EMBL; BC023787; AAH23787.1; -; mRNA.
DR EMBL; BC027012; AAH27012.1; -; mRNA.
DR CCDS; CCDS26844.1; -.
DR RefSeq; NP_598842.1; NM_134081.5.
DR AlphaFoldDB; Q91WN1; -.
DR SMR; Q91WN1; -.
DR BioGRID; 224364; 8.
DR IntAct; Q91WN1; 5.
DR STRING; 10090.ENSMUSP00000022345; -.
DR iPTMnet; Q91WN1; -.
DR PhosphoSitePlus; Q91WN1; -.
DR REPRODUCTION-2DPAGE; Q91WN1; -.
DR EPD; Q91WN1; -.
DR jPOST; Q91WN1; -.
DR MaxQB; Q91WN1; -.
DR PaxDb; Q91WN1; -.
DR PeptideAtlas; Q91WN1; -.
DR PRIDE; Q91WN1; -.
DR ProteomicsDB; 279461; -.
DR Antibodypedia; 29351; 139 antibodies from 25 providers.
DR DNASU; 108671; -.
DR Ensembl; ENSMUST00000022345; ENSMUSP00000022345; ENSMUSG00000021811.
DR GeneID; 108671; -.
DR KEGG; mmu:108671; -.
DR UCSC; uc007sjn.2; mouse.
DR CTD; 23234; -.
DR MGI; MGI:1915326; Dnajc9.
DR VEuPathDB; HostDB:ENSMUSG00000021811; -.
DR eggNOG; KOG0719; Eukaryota.
DR GeneTree; ENSGT00390000014549; -.
DR HOGENOM; CLU_055868_1_0_1; -.
DR InParanoid; Q91WN1; -.
DR OMA; DLWSKIF; -.
DR OrthoDB; 1416483at2759; -.
DR PhylomeDB; Q91WN1; -.
DR TreeFam; TF105168; -.
DR BioGRID-ORCS; 108671; 24 hits in 70 CRISPR screens.
DR PRO; PR:Q91WN1; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q91WN1; protein.
DR Bgee; ENSMUSG00000021811; Expressed in embryonic post-anal tail and 127 other tissues.
DR Genevisible; Q91WN1; MM.
DR GO; GO:0101031; C:chaperone complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0051087; F:chaperone binding; ISS:UniProtKB.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISO:MGI.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Chaperone; Cytoplasm; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..259
FT /note="DnaJ homolog subfamily C member 9"
FT /id="PRO_0000071064"
FT DOMAIN 15..82
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 171..248
FT /note="Required for histone binding"
FT /evidence="ECO:0000250|UniProtKB:Q8WXX5"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 259 AA; 30059 MW; ED959F4CC5B94343 CRC64;
MGLLELCEQV FGTADLYQVL GVRREASDGE VRRGYHKVSL QVHPDRVEED QKEDATRRFQ
ILGRVYAVLS DKEQKAVYDE QGTVDEDSAG LNQDRDWDAY WRLLFKKISL EDIQAFEKTY
KGSEEELNDI KQAYLDFKGD MDQIMESVLC VQYTDEPRIR NIIQKAIESK EIPAYSAFVK
ESKQKMNARK RRAQEEAKEA ELSRKELGLE EGVDNLKALI QSRQKDRQKE MDSFLAQMEA
KYCKPSKGGK RTALKKEKK
