DJC17_HUMAN
ID DJC17_HUMAN Reviewed; 304 AA.
AC Q9NVM6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=DnaJ homolog subfamily C member 17;
GN Name=DNAJC17;
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 [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 [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND IDENTIFICATION BY
RP 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-112, 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-112, 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-112, AND IDENTIFICATION BY
RP 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 METHYLATION [LARGE SCALE ANALYSIS] AT LYS-264, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [11]
RP STRUCTURE BY NMR OF 162-258.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RNA binding domain in hypothetical protein
RT FLJ10634.";
RL Submitted (JUN-2006) to the PDB data bank.
CC -!- FUNCTION: May negatively affect PAX8-induced thyroglobulin/TG
CC transcription. {ECO:0000250|UniProtKB:Q91WT4}.
CC -!- INTERACTION:
CC Q9NVM6; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12260682, EBI-16439278;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:D3ZSC8}. Nucleus
CC {ECO:0000250|UniProtKB:D3ZSC8}. Note=Predominantly nuclear.
CC {ECO:0000250|UniProtKB:D3ZSC8}.
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; AK001496; BAA91724.1; -; mRNA.
DR EMBL; BC000048; AAH00048.1; -; mRNA.
DR CCDS; CCDS10065.1; -.
DR RefSeq; NP_060633.1; NM_018163.2.
DR PDB; 2D9O; NMR; -; A=168-254.
DR PDBsum; 2D9O; -.
DR AlphaFoldDB; Q9NVM6; -.
DR SMR; Q9NVM6; -.
DR BioGRID; 120489; 111.
DR IntAct; Q9NVM6; 7.
DR MINT; Q9NVM6; -.
DR STRING; 9606.ENSP00000220496; -.
DR iPTMnet; Q9NVM6; -.
DR PhosphoSitePlus; Q9NVM6; -.
DR BioMuta; DNAJC17; -.
DR DMDM; 74761740; -.
DR EPD; Q9NVM6; -.
DR jPOST; Q9NVM6; -.
DR MassIVE; Q9NVM6; -.
DR MaxQB; Q9NVM6; -.
DR PaxDb; Q9NVM6; -.
DR PeptideAtlas; Q9NVM6; -.
DR PRIDE; Q9NVM6; -.
DR ProteomicsDB; 82830; -.
DR Antibodypedia; 49787; 179 antibodies from 24 providers.
DR DNASU; 55192; -.
DR Ensembl; ENST00000220496.9; ENSP00000220496.4; ENSG00000104129.10.
DR GeneID; 55192; -.
DR KEGG; hsa:55192; -.
DR MANE-Select; ENST00000220496.9; ENSP00000220496.4; NM_018163.3; NP_060633.1.
DR UCSC; uc001zms.3; human.
DR CTD; 55192; -.
DR DisGeNET; 55192; -.
DR GeneCards; DNAJC17; -.
DR HGNC; HGNC:25556; DNAJC17.
DR HPA; ENSG00000104129; Low tissue specificity.
DR MIM; 616844; gene.
DR neXtProt; NX_Q9NVM6; -.
DR OpenTargets; ENSG00000104129; -.
DR PharmGKB; PA142671965; -.
DR VEuPathDB; HostDB:ENSG00000104129; -.
DR eggNOG; KOG0691; Eukaryota.
DR GeneTree; ENSGT00940000155132; -.
DR HOGENOM; CLU_045732_1_0_1; -.
DR InParanoid; Q9NVM6; -.
DR OMA; KPLHFEW; -.
DR OrthoDB; 1405648at2759; -.
DR PhylomeDB; Q9NVM6; -.
DR TreeFam; TF321770; -.
DR PathwayCommons; Q9NVM6; -.
DR SignaLink; Q9NVM6; -.
DR BioGRID-ORCS; 55192; 714 hits in 1088 CRISPR screens.
DR ChiTaRS; DNAJC17; human.
DR EvolutionaryTrace; Q9NVM6; -.
DR GenomeRNAi; 55192; -.
DR Pharos; Q9NVM6; Tbio.
DR PRO; PR:Q9NVM6; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9NVM6; protein.
DR Bgee; ENSG00000104129; Expressed in sural nerve and 112 other tissues.
DR ExpressionAtlas; Q9NVM6; baseline and differential.
DR Genevisible; Q9NVM6; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0000390; P:spliceosomal complex disassembly; IBA:GO_Central.
DR GO; GO:1901998; P:toxin transport; IEA:Ensembl.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd12429; RRM_DNAJC17; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR034254; DNAJC17_RRM.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..304
FT /note="DnaJ homolog subfamily C member 17"
FT /id="PRO_0000247118"
FT DOMAIN 11..76
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT DOMAIN 178..249
FT /note="RRM"
FT REGION 79..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19367720,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 264
FT /note="N6-methyllysine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:2D9O"
FT HELIX 191..199
FT /evidence="ECO:0007829|PDB:2D9O"
FT STRAND 204..222
FT /evidence="ECO:0007829|PDB:2D9O"
FT HELIX 224..232
FT /evidence="ECO:0007829|PDB:2D9O"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:2D9O"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:2D9O"
SQ SEQUENCE 304 AA; 34687 MW; 98A1BA8ABFF4120E CRC64;
MAVTKELLQM DLYALLGIEE KAADKEVKKA YRQKALSCHP DKNPDNPRAA ELFHQLSQAL
EVLTDAAARA AYDKVRKAKK QAAERTQKLD EKRKKVKLDL EARERQAQAQ ESEEEEESRS
TRTLEQEIER LREEGSRQLE EQQRLIREQI RQERDQRLRG KAENTEGQGT PKLKLKWKCK
KEDESKGGYS KDVLLRLLQK YGEVLNLVLS SKKPGTAVVE FATVKAAELA VQNEVGLVDN
PLKISWLEGQ PQDAVGRSHS GLSKGSVLSE RDYESLVMMR MRQAAERQQL IARMQQEDQE
GPPT
