ID DNJC9_HUMAN Reviewed; 260 AA. AC Q8WXX5; B2RMW6; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 167. DE RecName: Full=DnaJ homolog subfamily C member 9; DE Short=HDJC9 {ECO:0000303|PubMed:17182002}; DE AltName: Full=DnaJ protein SB73; GN Name=DNAJC9; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH HSPA1A; HSPA1B AND RP HSPA8, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION. RC TISSUE=Dendritic cell {ECO:0000303|PubMed:17182002}; RX PubMed=17182002; DOI=10.1016/j.bbrc.2006.12.013; RA Han C., Chen T., Li N., Yang M., Wan T., Cao X.; RT "HDJC9, a novel human type C DnaJ/HSP40 member interacts with and RT cochaperones HSP70 through the J domain."; RL Biochem. Biophys. Res. Commun. 353:280-285(2007). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC 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 [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 AND SER-215, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [12] {ECO:0007744|PDB:7CIZ, ECO:0007744|PDB:7CJ0} RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 171-249 MUTANT CYS-243 IN COMPLEX RP WITH MCM2 61-130 AND HISTONES H3.3 58-136 AND H4, IDENTIFICATION BY MASS RP SPECTROMETRY, FUNCTION, IDENTIFICATION IN A CO-CHAPERONE COMPLEX WITH MCM2 RP AND HISTONES H3.3 AND H4, INTERACTION WITH MCM2; H3.3; H3.2; H3.1; H4; RP TONSL; HSPA8; BAG2 AND HSPA1B, DOMAIN, AND MUTAGENESIS OF 43-HIS--ASP-45; RP 195-GLU--ALA-200; 216-LEU--ILE-220; 224-GLN--TYR-242; 224-GLN--ARG-227; RP ARG-227; 234-PHE-LEU-235; 238-MET--TYR-242 AND CYS-243. RX PubMed=33857403; DOI=10.1016/j.molcel.2021.03.041; RA Hammond C.M., Bao H., Hendriks I.A., Carraro M., Garcia-Nieto A., Liu Y., RA Reveron-Gomez N., Spanos C., Chen L., Rappsilber J., Nielsen M.L., RA Patel D.J., Huang H., Groth A.; RT "DNAJC9 integrates heat shock molecular chaperones into the histone RT chaperone network."; RL Mol. Cell 0:0-0(2021). CC -!- FUNCTION: Acts as a dual histone chaperone and heat shock co-chaperone CC (PubMed:33857403). 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 (PubMed:33857403). May also act as a histone CC co-chaperone together with TONSL (PubMed:33857403). May recruit histone CC chaperones ASF1A, NASP and SPT2 to histone H3-H4 heterodimers CC (PubMed:33857403). Also plays a role as co-chaperone of the HSP70 CC family of molecular chaperone proteins, such as HSPA1A, HSPA1B and CC HSPA8 (PubMed:17182002, PubMed:33857403). As a co-chaperone, may play a CC role in the recruitment of HSP70-type molecular chaperone machinery to CC histone H3-H4 substrates, thereby maintaining the histone structural CC integrity (PubMed:33857403). Exhibits activity to assemble histones CC onto DNA in vitro (PubMed:33857403). {ECO:0000269|PubMed:17182002, CC ECO:0000269|PubMed:33857403}. CC -!- SUBUNIT: Forms a co-chaperone complex with MCM2 and histone H3.3-H4 CC heterodimers (PubMed:33857403). Within the complex, interacts (via C- CC terminus) with MCM2 (via N-terminus); the interaction is histone- CC dependent (PubMed:33857403). Within the complex, interacts (via C- CC terminus) with histone H3.3-H4 heterodimers; the interaction is direct CC (PubMed:33857403). Interacts with histones H4, H3.3, H3.2 and H3.1, but CC not with CENPA or the testis-specific histone H3.1t (PubMed:33857403). CC Interacts (via J domain) with HSPA1A, HSPA1B and HSPA8 CC (PubMed:17182002, PubMed:33857403). May interact with TONSL; the CC interaction seems to be histone-dependent (PubMed:33857403). May CC interact with HSPA8 and BAG2; the interactions seem to be histone- CC dependent (PubMed:33857403). {ECO:0000269|PubMed:17182002, CC ECO:0000269|PubMed:33857403}. CC -!- INTERACTION: CC Q8WXX5; Q6NXT2: H3-5; NbExp=3; IntAct=EBI-2349100, EBI-2868501; CC Q8WXX5; P68431: H3C12; NbExp=7; IntAct=EBI-2349100, EBI-79722; CC Q8WXX5; Q8NDC4: MORN4; NbExp=3; IntAct=EBI-2349100, EBI-10269566; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17182002}. Cytoplasm CC {ECO:0000269|PubMed:17182002}. Cell membrane CC {ECO:0000269|PubMed:17182002}. Note=Predominantly nuclear. Translocates CC to the cytoplasm and membrane after heat shock. CC {ECO:0000269|PubMed:17182002}. CC -!- TISSUE SPECIFICITY: Expressed in heart, placenta, liver, skeletal CC muscle, kidney, pancreas, thymus, ovary, colon and peripheral blood. CC {ECO:0000269|PubMed:17182002}. CC -!- INDUCTION: By heat shock, bacterial lipopolysaccharides (LPS), phorbol CC 12-myristate 13-acetate (PMA), and the cytokine TNF (at protein level). CC {ECO:0000269|PubMed:17182002}. CC -!- DOMAIN: The functional J domain is required for the release from CC histone-dependent chromatin-binding. {ECO:0000269|PubMed:33857403}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF327347; AAL56008.1; -; mRNA. DR EMBL; AK074420; BAB85076.1; -; mRNA. DR EMBL; AK094162; BAG52832.1; -; mRNA. DR EMBL; CH471083; EAW54483.1; -; Genomic_DNA. DR EMBL; BC136507; AAI36508.1; -; mRNA. DR CCDS; CCDS7322.1; -. DR RefSeq; NP_056005.1; NM_015190.4. DR PDB; 7CIZ; X-ray; 1.80 A; D/H/L=180-249. DR PDB; 7CJ0; X-ray; 2.50 A; A/D=171-249. DR PDBsum; 7CIZ; -. DR PDBsum; 7CJ0; -. DR AlphaFoldDB; Q8WXX5; -. DR SMR; Q8WXX5; -. DR BioGRID; 116839; 282. DR IntAct; Q8WXX5; 55. DR MINT; Q8WXX5; -. DR STRING; 9606.ENSP00000362041; -. DR GlyGen; Q8WXX5; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8WXX5; -. DR PhosphoSitePlus; Q8WXX5; -. DR SwissPalm; Q8WXX5; -. DR BioMuta; DNAJC9; -. DR DMDM; 52782787; -. DR EPD; Q8WXX5; -. DR jPOST; Q8WXX5; -. DR MassIVE; Q8WXX5; -. DR MaxQB; Q8WXX5; -. DR PaxDb; 9606-ENSP00000362041; -. DR PeptideAtlas; Q8WXX5; -. DR ProteomicsDB; 75112; -. DR Pumba; Q8WXX5; -. DR Antibodypedia; 29351; 158 antibodies from 26 providers. DR DNASU; 23234; -. DR Ensembl; ENST00000372950.6; ENSP00000362041.4; ENSG00000213551.7. DR GeneID; 23234; -. DR KEGG; hsa:23234; -. DR MANE-Select; ENST00000372950.6; ENSP00000362041.4; NM_015190.5; NP_056005.1. DR UCSC; uc010qkg.2; human. DR AGR; HGNC:19123; -. DR CTD; 23234; -. DR DisGeNET; 23234; -. DR GeneCards; DNAJC9; -. DR HGNC; HGNC:19123; DNAJC9. DR HPA; ENSG00000213551; Tissue enhanced (bone). DR MIM; 611206; gene. DR neXtProt; NX_Q8WXX5; -. DR OpenTargets; ENSG00000213551; -. DR PharmGKB; PA38797; -. DR VEuPathDB; HostDB:ENSG00000213551; -. DR eggNOG; KOG0719; Eukaryota. DR GeneTree; ENSGT00390000014549; -. DR HOGENOM; CLU_055868_1_0_1; -. DR InParanoid; Q8WXX5; -. DR OMA; DLWSKIF; -. DR OrthoDB; 149896at2759; -. DR PhylomeDB; Q8WXX5; -. DR TreeFam; TF105168; -. DR PathwayCommons; Q8WXX5; -. DR SignaLink; Q8WXX5; -. DR BioGRID-ORCS; 23234; 611 hits in 1153 CRISPR screens. DR ChiTaRS; DNAJC9; human. DR GenomeRNAi; 23234; -. DR Pharos; Q8WXX5; Tbio. DR PRO; PR:Q8WXX5; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q8WXX5; Protein. DR Bgee; ENSG00000213551; Expressed in secondary oocyte and 181 other cell types or tissues. DR ExpressionAtlas; Q8WXX5; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0101031; C:protein folding chaperone complex; IDA:UniProtKB. DR GO; GO:0031072; F:heat shock protein binding; IPI:UniProtKB. DR GO; GO:0042393; F:histone binding; IDA:UniProtKB. DR GO; GO:0051087; F:protein-folding chaperone binding; IDA:UniProtKB. DR GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB. DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IDA:UniProtKB. DR CDD; cd06257; DnaJ; 1. DR Gene3D; 1.10.287.110; DnaJ domain; 1. DR InterPro; IPR001623; DnaJ_domain. DR InterPro; IPR018253; DnaJ_domain_CS. DR InterPro; IPR036869; J_dom_sf. DR PANTHER; PTHR44144; DNAJ HOMOLOG SUBFAMILY C MEMBER 9; 1. DR PANTHER; PTHR44144:SF1; DNAJ HOMOLOG SUBFAMILY C MEMBER 9; 1. DR Pfam; PF00226; DnaJ; 1. DR PRINTS; PR00625; JDOMAIN. DR SMART; SM00271; DnaJ; 1. DR SUPFAM; SSF46565; Chaperone J-domain; 1. DR PROSITE; PS00636; DNAJ_1; 1. DR PROSITE; PS50076; DNAJ_2; 1. DR Genevisible; Q8WXX5; HS. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Chaperone; Cytoplasm; Membrane; Nucleus; KW Phosphoprotein; Reference proteome. FT CHAIN 1..260 FT /note="DnaJ homolog subfamily C member 9" FT /id="PRO_0000071063" FT DOMAIN 15..82 FT /note="J" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286" FT REGION 171..249 FT /note="Required for histone binding" FT /evidence="ECO:0000269|PubMed:33857403" FT REGION 185..208 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 188..208 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 109 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 215 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MUTAGEN 43..45 FT /note="HPD->QPN: Increased binding to histones H3 and H4. FT Less integration of histones H3 and H4 in chromatin. FT Increased recruitment of histone deposition factors to FT chromatin. Trapped on chromatin throughout the cell cycle FT in a manner depending on histone-binding. Released from FT chromatin trap; when associated with Ala-224; Ala-227; FT Ala-238 and Ala-242." FT /evidence="ECO:0000269|PubMed:33857403" FT MUTAGEN 195..200 FT /note="EEAKEA->AAAKAE: Reduces the co-chaperone complex FT formation with MCM2; histone H3.3 and H4." FT /evidence="ECO:0000269|PubMed:33857403" FT MUTAGEN 216..220 FT /note="LKAAI->AKAAA: Disrupts the formation of the FT co-chaperone complex with MCM2 and histones H3.3 and H4." FT /evidence="ECO:0000269|PubMed:33857403" FT MUTAGEN 224..242 FT /note="QKDRQKEMDNFLAQMEAKY->AKDAQKEMDNFLAQAEAKA: Abolishes FT the interaction with MCM2, TONSL and histones H3.3 and H4. FT Disrupts the formation of the co-chaperone complex with FT MCM2 and histones H3.3 and H4." FT /evidence="ECO:0000269|PubMed:33857403" FT MUTAGEN 224..227 FT /note="QKDR->AKDA: Partial loss of histone dimer H3-H4 FT interaction. Reduces the formation of the co-chaperone FT complex with MCM2 and histones H3.3 and H4." FT /evidence="ECO:0000269|PubMed:33857403" FT MUTAGEN 234..235 FT /note="FL->AA: Reduces the formation of the co-chaperone FT complex with MCM2 and histones H3.3 and H4." FT /evidence="ECO:0000269|PubMed:33857403" FT MUTAGEN 238..242 FT /note="MEAKY->AEAKA: Partial loss of histone dimer H3-H4 FT interaction. Reduces the co-chaperone complex formation FT with MCM2; histone H3.3 and H4." FT /evidence="ECO:0000269|PubMed:33857403" FT MUTAGEN 243 FT /note="C->S: Does not affect interaction with histones." FT /evidence="ECO:0000269|PubMed:33857403" FT HELIX 175..207 FT /evidence="ECO:0007829|PDB:7CJ0" FT HELIX 213..242 FT /evidence="ECO:0007829|PDB:7CIZ" FT HELIX 244..247 FT /evidence="ECO:0007829|PDB:7CJ0" SQ SEQUENCE 260 AA; 29910 MW; 6C5C34774217863F CRC64; MGLLDLCEEV FGTADLYRVL GVRREASDGE VRRGYHKVSL QVHPDRVGEG DKEDATRRFQ ILGKVYSVLS DREQRAVYDE QGTVDEDSPV LTQDRDWEAY WRLLFKKISL EDIQAFEKTY KGSEEELADI KQAYLDFKGD MDQIMESVLC VQYTEEPRIR NIIQQAIDAG EVPSYNAFVK ESKQKMNARK RRAQEEAKEA EMSRKELGLD EGVDSLKAAI QSRQKDRQKE MDNFLAQMEA KYCKSSKGGG KKSALKKEKK //