Full text data of DNAJC17
DNAJC17
[Confidence: low (only semi-automatic identification from reviews)]
DnaJ homolog subfamily C member 17
Note: presumably soluble (membrane word is not in UniProt keywords or features)
DnaJ homolog subfamily C member 17
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9NVM6
ID DJC17_HUMAN Reviewed; 304 AA.
AC Q9NVM6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 110.
DE RecName: Full=DnaJ homolog subfamily C member 17;
GN Name=DNAJC17;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASS
RP SPECTROMETRY.
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
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
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 -!- SIMILARITY: Contains 1 J domain.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK001496; BAA91724.1; -; mRNA.
DR EMBL; BC000048; AAH00048.1; -; mRNA.
DR RefSeq; NP_060633.1; NM_018163.2.
DR UniGene; Hs.511069; -.
DR PDB; 2D9O; NMR; -; A=167-254.
DR PDBsum; 2D9O; -.
DR ProteinModelPortal; Q9NVM6; -.
DR SMR; Q9NVM6; 13-74, 170-258.
DR MINT; MINT-4650891; -.
DR STRING; 9606.ENSP00000220496; -.
DR PhosphoSite; Q9NVM6; -.
DR DMDM; 74761740; -.
DR PaxDb; Q9NVM6; -.
DR PeptideAtlas; Q9NVM6; -.
DR PRIDE; Q9NVM6; -.
DR Ensembl; ENST00000220496; ENSP00000220496; ENSG00000104129.
DR GeneID; 55192; -.
DR KEGG; hsa:55192; -.
DR UCSC; uc001zms.2; human.
DR CTD; 55192; -.
DR GeneCards; GC15M041060; -.
DR HGNC; HGNC:25556; DNAJC17.
DR HPA; HPA040914; -.
DR HPA; HPA041187; -.
DR neXtProt; NX_Q9NVM6; -.
DR PharmGKB; PA142671965; -.
DR eggNOG; COG2214; -.
DR HOGENOM; HOG000239711; -.
DR HOVERGEN; HBG062744; -.
DR InParanoid; Q9NVM6; -.
DR KO; K09537; -.
DR OMA; LQMDLYG; -.
DR OrthoDB; EOG7RRF89; -.
DR PhylomeDB; Q9NVM6; -.
DR EvolutionaryTrace; Q9NVM6; -.
DR GenomeRNAi; 55192; -.
DR NextBio; 59047; -.
DR PRO; PR:Q9NVM6; -.
DR ArrayExpress; Q9NVM6; -.
DR Bgee; Q9NVM6; -.
DR CleanEx; HS_DNAJC17; -.
DR Genevestigator; Q9NVM6; -.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR Pfam; PF00226; DnaJ; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR PROSITE; PS00636; DNAJ_1; FALSE_NEG.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS50102; RRM; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Complete proteome; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT CHAIN 1 304 DnaJ homolog subfamily C member 17.
FT /FTId=PRO_0000247118.
FT DOMAIN 11 76 J.
FT DOMAIN 178 249 RRM.
FT COMPBIAS 111 117 Poly-Glu.
FT MOD_RES 112 112 Phosphoserine.
FT STRAND 172 176
FT HELIX 191 199
FT STRAND 204 222
FT HELIX 224 232
FT STRAND 238 241
FT STRAND 243 245
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
//
ID DJC17_HUMAN Reviewed; 304 AA.
AC Q9NVM6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 110.
DE RecName: Full=DnaJ homolog subfamily C member 17;
GN Name=DNAJC17;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASS
RP SPECTROMETRY.
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
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
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 -!- SIMILARITY: Contains 1 J domain.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK001496; BAA91724.1; -; mRNA.
DR EMBL; BC000048; AAH00048.1; -; mRNA.
DR RefSeq; NP_060633.1; NM_018163.2.
DR UniGene; Hs.511069; -.
DR PDB; 2D9O; NMR; -; A=167-254.
DR PDBsum; 2D9O; -.
DR ProteinModelPortal; Q9NVM6; -.
DR SMR; Q9NVM6; 13-74, 170-258.
DR MINT; MINT-4650891; -.
DR STRING; 9606.ENSP00000220496; -.
DR PhosphoSite; Q9NVM6; -.
DR DMDM; 74761740; -.
DR PaxDb; Q9NVM6; -.
DR PeptideAtlas; Q9NVM6; -.
DR PRIDE; Q9NVM6; -.
DR Ensembl; ENST00000220496; ENSP00000220496; ENSG00000104129.
DR GeneID; 55192; -.
DR KEGG; hsa:55192; -.
DR UCSC; uc001zms.2; human.
DR CTD; 55192; -.
DR GeneCards; GC15M041060; -.
DR HGNC; HGNC:25556; DNAJC17.
DR HPA; HPA040914; -.
DR HPA; HPA041187; -.
DR neXtProt; NX_Q9NVM6; -.
DR PharmGKB; PA142671965; -.
DR eggNOG; COG2214; -.
DR HOGENOM; HOG000239711; -.
DR HOVERGEN; HBG062744; -.
DR InParanoid; Q9NVM6; -.
DR KO; K09537; -.
DR OMA; LQMDLYG; -.
DR OrthoDB; EOG7RRF89; -.
DR PhylomeDB; Q9NVM6; -.
DR EvolutionaryTrace; Q9NVM6; -.
DR GenomeRNAi; 55192; -.
DR NextBio; 59047; -.
DR PRO; PR:Q9NVM6; -.
DR ArrayExpress; Q9NVM6; -.
DR Bgee; Q9NVM6; -.
DR CleanEx; HS_DNAJC17; -.
DR Genevestigator; Q9NVM6; -.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR Pfam; PF00226; DnaJ; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR PROSITE; PS00636; DNAJ_1; FALSE_NEG.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS50102; RRM; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Complete proteome; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT CHAIN 1 304 DnaJ homolog subfamily C member 17.
FT /FTId=PRO_0000247118.
FT DOMAIN 11 76 J.
FT DOMAIN 178 249 RRM.
FT COMPBIAS 111 117 Poly-Glu.
FT MOD_RES 112 112 Phosphoserine.
FT STRAND 172 176
FT HELIX 191 199
FT STRAND 204 222
FT HELIX 224 232
FT STRAND 238 241
FT STRAND 243 245
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
//