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   28-JAN-2026, entry version 186.
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; Q15029: EFTUD2; NbExp=2; IntAct=EBI-12260682, EBI-357897;
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}.
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DR   EMBL; AK001496; BAA91724.1; -; mRNA.
DR   EMBL; BC000048; AAH00048.1; -; mRNA.
DR   CCDS; CCDS10065.1; -.
DR   RefSeq; NP_060633.1; NM_018163.3.
DR   PDB; 2D9O; NMR; -; A=168-254.
DR   PDBsum; 2D9O; -.
DR   AlphaFoldDB; Q9NVM6; -.
DR   SMR; Q9NVM6; -.
DR   BioGRID; 120489; 141.
DR   FunCoup; Q9NVM6; 1760.
DR   IntAct; Q9NVM6; 41.
DR   MINT; Q9NVM6; -.
DR   STRING; 9606.ENSP00000220496; -.
DR   iPTMnet; Q9NVM6; -.
DR   PhosphoSitePlus; Q9NVM6; -.
DR   BioMuta; DNAJC17; -.
DR   DMDM; 74761740; -.
DR   jPOST; Q9NVM6; -.
DR   MassIVE; Q9NVM6; -.
DR   PaxDb; 9606-ENSP00000220496; -.
DR   PeptideAtlas; Q9NVM6; -.
DR   ProteomicsDB; 82830; -.
DR   Pumba; Q9NVM6; -.
DR   Antibodypedia; 49787; 169 antibodies from 24 providers.
DR   DNASU; 55192; -.
DR   Ensembl; ENST00000220496.9; ENSP00000220496.4; ENSG00000104129.11.
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   AGR; HGNC:25556; -.
DR   ClinPGx; PA142671965; -.
DR   CTD; 55192; -.
DR   DisGeNET; 55192; -.
DR   GeneCards; DNAJC17; -.
DR   HGNC; HGNC:25556; DNAJC17.
DR   HPA; ENSG00000104129; Low tissue specificity.
DR   MalaCards; DNAJC17; -.
DR   MIM; 616844; gene.
DR   OpenTargets; ENSG00000104129; -.
DR   VEuPathDB; HostDB:ENSG00000104129; -.
DR   eggNOG; KOG0691; Eukaryota.
DR   GeneTree; ENSGT00940000155132; -.
DR   HOGENOM; CLU_045732_1_0_1; -.
DR   InParanoid; Q9NVM6; -.
DR   OMA; NPLHFQW; -.
DR   OrthoDB; 259708at2759; -.
DR   PAN-GO; Q9NVM6; 2 GO annotations based on evolutionary models.
DR   PhylomeDB; Q9NVM6; -.
DR   PathwayCommons; Q9NVM6; -.
DR   SignaLink; Q9NVM6; -.
DR   Agora; ENSG00000104129; -.
DR   BioGRID-ORCS; 55192; 752 hits in 1175 CRISPR screens.
DR   CD-CODE; 804901D1; Nuclear speckle.
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 114 other cell types or tissues.
DR   ExpressionAtlas; Q9NVM6; baseline and differential.
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   CDD; cd06257; DnaJ; 1.
DR   CDD; cd12429; RRM_DNAJC17; 1.
DR   FunFam; 1.10.287.110:FF:000059; dnaJ homolog subfamily C member 17; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 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; IPR052094; Pre-mRNA-splicing_ERAD.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   PANTHER; PTHR44313; DNAJ HOMOLOG SUBFAMILY C MEMBER 17; 1.
DR   PANTHER; PTHR44313:SF1; DNAJ HOMOLOG SUBFAMILY C MEMBER 17; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chaperone; Cytoplasm; Methylation; Nucleus; Phosphoprotein;
KW   Proteomics identification; Reference proteome; RNA-binding; Transcription;
KW   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   COMPBIAS        79..106
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..145
FT                   /note="Basic and acidic residues"
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
//