ID DNJC7_HUMAN Reviewed; 494 AA.
AC Q99615; Q7Z784;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 27-MAR-2024, entry version 212.
DE RecName: Full=DnaJ homolog subfamily C member 7;
DE AltName: Full=Tetratricopeptide repeat protein 2;
DE Short=TPR repeat protein 2;
GN Name=DNAJC7; Synonyms=TPR2, TTC2;
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] (ISOFORM 2).
RC TISSUE=Salivary gland;
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] (ISOFORM 1).
RC TISSUE=Salivary gland;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, and Skin;
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 [6]
RP PROTEIN SEQUENCE OF 2-26; 69-77; 80-90; 138-156; 192-238; 274-291 AND
RP 430-442 (ISOFORM 1), CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-494 (ISOFORM 1).
RX PubMed=8836031; DOI=10.1089/dna.1996.15.727;
RA Murthy A.E., Bernards A., Church D., Wasmuth J., Gusella J.F.;
RT "Identification and characterization of two novel tetratricopeptide repeat-
RT containing genes.";
RL DNA Cell Biol. 15:727-735(1996).
RN [8]
RP INTERACTION WITH HSPA8.
RX PubMed=10567422; DOI=10.1074/jbc.274.48.34425;
RA Liu F.H., Wu S.J., Hu S.M., Hsiao C.D., Wang C.;
RT "Specific interaction of the 70-kDa heat shock cognate protein with the
RT tetratricopeptide repeats.";
RL J. Biol. Chem. 274:34425-34432(1999).
RN [9]
RP INTERACTION WITH RAD9A; HUS1 AND RAD1, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF HIS-409.
RX PubMed=11573955; DOI=10.1006/bbrc.2001.5685;
RA Xiang S.L., Kumano T., Iwasaki S.I., Sun X., Yoshioka K., Yamamoto K.C.;
RT "The J domain of Tpr2 regulates its interaction with the proapoptotic and
RT cell-cycle checkpoint protein, Rad9.";
RL Biochem. Biophys. Res. Commun. 287:932-940(2001).
RN [10]
RP FUNCTION, INTERACTION WITH HSP90AA1 AND HSPA1A/B, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ARG-101; ARG-333 AND HIS-409.
RX PubMed=12853476; DOI=10.1093/emboj/cdg362;
RA Brychzy A., Rein T., Winklhofer K.F., Hartl F.U., Young J.C.,
RA Obermann W.M.;
RT "Cofactor Tpr2 combines two TPR domains and a J domain to regulate the
RT Hsp70/Hsp90 chaperone system.";
RL EMBO J. 22:3613-3623(2003).
RN [11]
RP INTERACTION WITH NR1I3.
RX PubMed=14573755; DOI=10.1124/mol.64.5.1069;
RA Kobayashi K., Sueyoshi T., Inoue K., Moore R., Negishi M.;
RT "Cytoplasmic accumulation of the nuclear receptor CAR by a
RT tetratricopeptide repeat protein in HepG2 cells.";
RL Mol. Pharmacol. 64:1069-1075(2003).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [13]
RP FUNCTION, AND INTERACTION WITH HSP90AB1; HSPA1A/B AND PGR.
RX PubMed=18620420; DOI=10.1021/bi800770g;
RA Moffatt N.S., Bruinsma E., Uhl C., Obermann W.M., Toft D.;
RT "Role of the cochaperone Tpr2 in Hsp90 chaperoning.";
RL Biochemistry 47:8203-8213(2008).
RN [14]
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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, 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).
CC -!- FUNCTION: Acts as a co-chaperone regulating the molecular chaperones
CC HSP70 and HSP90 in folding of steroid receptors, such as the
CC glucocorticoid receptor and the progesterone receptor. Proposed to act
CC as a recycling chaperone by facilitating the return of chaperone
CC substrates to early stages of chaperoning if further folding is
CC required. In vitro, induces ATP-independent dissociation of HSP90 but
CC not of HSP70 from the chaperone-substrate complexes. Recruits NR1I3 to
CC the cytoplasm (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:12853476, ECO:0000269|PubMed:18620420}.
CC -!- SUBUNIT: Associates with complexes containing chaperones HSP70 and
CC HSP90. Interacts with the GAP domain of NF1. Interacts with HSP90AA1.
CC Interacts with HSPA1A/B; the interaction is enhanced by ATP. Interacts
CC with HSP90AB1. Interacts with PGR. Interacts with RAD9A; the
CC interaction is interrupted by UV and heat shock treatments. Interacts
CC with HUS1 and RAD1. Interacts with NR1I3. The DNAJC7-NR1I3 complex may
CC also include HSP90 (By similarity). Interacts with HSPA8. {ECO:0000250,
CC ECO:0000269|PubMed:10567422, ECO:0000269|PubMed:11573955,
CC ECO:0000269|PubMed:12853476, ECO:0000269|PubMed:14573755,
CC ECO:0000269|PubMed:18620420}.
CC -!- INTERACTION:
CC Q99615; O95816: BAG2; NbExp=2; IntAct=EBI-357552, EBI-355275;
CC Q99615; O95429: BAG4; NbExp=2; IntAct=EBI-357552, EBI-2949658;
CC Q99615; Q9NRI5: DISC1; NbExp=3; IntAct=EBI-357552, EBI-529989;
CC Q99615; P12504: vif; Xeno; NbExp=3; IntAct=EBI-357552, EBI-779991;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11573955,
CC ECO:0000269|PubMed:12853476}. Nucleus {ECO:0000269|PubMed:11573955}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9QYI3}.
CC Note=Colocalizes with NR1I3 to microtubules.
CC {ECO:0000250|UniProtKB:Q9QYI3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99615-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99615-2; Sequence=VSP_044279;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB36872.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH33772.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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; AK298860; BAG60982.1; -; mRNA.
DR EMBL; BX647209; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC105024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC125257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471152; EAW60788.1; -; Genomic_DNA.
DR EMBL; BC003601; AAH03601.1; -; mRNA.
DR EMBL; BC011837; AAH11837.2; -; mRNA.
DR EMBL; BC033772; AAH33772.1; ALT_INIT; mRNA.
DR EMBL; U46571; AAB36872.1; ALT_INIT; mRNA.
DR CCDS; CCDS45677.1; -. [Q99615-1]
DR CCDS; CCDS45678.1; -. [Q99615-2]
DR RefSeq; NP_001138238.1; NM_001144766.2. [Q99615-2]
DR RefSeq; NP_003306.3; NM_003315.3. [Q99615-1]
DR RefSeq; XP_011523469.1; XM_011525167.2. [Q99615-2]
DR RefSeq; XP_011523470.1; XM_011525168.2.
DR RefSeq; XP_011523471.1; XM_011525169.2. [Q99615-2]
DR RefSeq; XP_016880483.1; XM_017024994.1. [Q99615-2]
DR AlphaFoldDB; Q99615; -.
DR SMR; Q99615; -.
DR BioGRID; 113117; 446.
DR CORUM; Q99615; -.
DR IntAct; Q99615; 143.
DR MINT; Q99615; -.
DR STRING; 9606.ENSP00000406463; -.
DR GlyGen; Q99615; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99615; -.
DR MetOSite; Q99615; -.
DR PhosphoSitePlus; Q99615; -.
DR SwissPalm; Q99615; -.
DR BioMuta; DNAJC7; -.
DR DMDM; 46397879; -.
DR EPD; Q99615; -.
DR jPOST; Q99615; -.
DR MassIVE; Q99615; -.
DR MaxQB; Q99615; -.
DR PaxDb; 9606-ENSP00000406463; -.
DR PeptideAtlas; Q99615; -.
DR ProteomicsDB; 69491; -.
DR ProteomicsDB; 78359; -. [Q99615-1]
DR Pumba; Q99615; -.
DR Antibodypedia; 8072; 252 antibodies from 28 providers.
DR DNASU; 7266; -.
DR Ensembl; ENST00000316603.12; ENSP00000313311.7; ENSG00000168259.17. [Q99615-2]
DR Ensembl; ENST00000426588.7; ENSP00000394327.2; ENSG00000168259.17. [Q99615-2]
DR Ensembl; ENST00000457167.9; ENSP00000406463.2; ENSG00000168259.17. [Q99615-1]
DR Ensembl; ENST00000590774.6; ENSP00000465340.2; ENSG00000168259.17. [Q99615-2]
DR Ensembl; ENST00000674166.1; ENSP00000501364.1; ENSG00000168259.17. [Q99615-2]
DR Ensembl; ENST00000674252.1; ENSP00000501366.1; ENSG00000168259.17. [Q99615-2]
DR Ensembl; ENST00000674287.1; ENSP00000501482.1; ENSG00000168259.17. [Q99615-2]
DR Ensembl; ENST00000674303.1; ENSP00000501468.1; ENSG00000168259.17. [Q99615-2]
DR GeneID; 7266; -.
DR KEGG; hsa:7266; -.
DR MANE-Select; ENST00000457167.9; ENSP00000406463.2; NM_003315.4; NP_003306.3.
DR UCSC; uc002hyo.4; human. [Q99615-1]
DR AGR; HGNC:12392; -.
DR CTD; 7266; -.
DR DisGeNET; 7266; -.
DR GeneCards; DNAJC7; -.
DR HGNC; HGNC:12392; DNAJC7.
DR HPA; ENSG00000168259; Low tissue specificity.
DR MIM; 601964; gene.
DR neXtProt; NX_Q99615; -.
DR OpenTargets; ENSG00000168259; -.
DR PharmGKB; PA27424; -.
DR VEuPathDB; HostDB:ENSG00000168259; -.
DR eggNOG; KOG0550; Eukaryota.
DR GeneTree; ENSGT00940000155338; -.
DR HOGENOM; CLU_015935_3_1_1; -.
DR InParanoid; Q99615; -.
DR OrthoDB; 5473367at2759; -.
DR PhylomeDB; Q99615; -.
DR TreeFam; TF105166; -.
DR PathwayCommons; Q99615; -.
DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR SignaLink; Q99615; -.
DR BioGRID-ORCS; 7266; 20 hits in 1153 CRISPR screens.
DR ChiTaRS; DNAJC7; human.
DR GeneWiki; DNAJC7; -.
DR GenomeRNAi; 7266; -.
DR Pharos; Q99615; Tbio.
DR PRO; PR:Q99615; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q99615; Protein.
DR Bgee; ENSG00000168259; Expressed in nucleus accumbens and 206 other cell types or tissues.
DR ExpressionAtlas; Q99615; baseline and differential.
DR Genevisible; Q99615; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0001671; F:ATPase activator activity; TAS:Reactome.
DR GO; GO:0031072; F:heat shock protein binding; IPI:UniProtKB.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IDA:UniProtKB.
DR GO; GO:0006457; P:protein folding; TAS:ProtInc.
DR GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR44200; DNAJ HOMOLOG SUBFAMILY C MEMBER 7; 1.
DR PANTHER; PTHR44200:SF1; DNAJ HOMOLOG SUBFAMILY C MEMBER 7; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF13414; TPR_11; 1.
DR Pfam; PF13432; TPR_16; 1.
DR Pfam; PF13181; TPR_8; 2.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00028; TPR; 8.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF48452; TPR-like; 3.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS50005; TPR; 8.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chaperone; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; TPR repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:22814378"
FT CHAIN 2..494
FT /note="DnaJ homolog subfamily C member 7"
FT /id="PRO_0000071058"
FT REPEAT 28..61
FT /note="TPR 1"
FT REPEAT 62..95
FT /note="TPR 2"
FT REPEAT 96..129
FT /note="TPR 3"
FT REPEAT 142..175
FT /note="TPR 4"
FT REPEAT 177..209
FT /note="TPR 5"
FT REPEAT 210..243
FT /note="TPR 6"
FT REPEAT 256..289
FT /note="TPR 7"
FT REPEAT 294..327
FT /note="TPR 8"
FT REPEAT 328..361
FT /note="TPR 9"
FT DOMAIN 381..451
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:22814378"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..56
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_044279"
FT MUTAGEN 101
FT /note="R->A: Impairs interaction with HSP90AA1 and
FT HSPA1A/B. Abolishes interaction with HSP90AA1 and HSPA1A/B;
FT when associated with A-333 and A-409."
FT /evidence="ECO:0000269|PubMed:12853476"
FT MUTAGEN 333
FT /note="R->A: Impairs interaction with HSP90AA1 and
FT HSPA1A/B. Abolishes interaction with HSP90AA1 and HSPA1A/B;
FT when associated with A-101 and A-409."
FT /evidence="ECO:0000269|PubMed:12853476"
FT MUTAGEN 409
FT /note="H->A: Predominantly nuclear localization. Abolishes
FT interaction with HSP90AA1 and HSPA1A/B; when associated
FT with A-101 and A-333."
FT /evidence="ECO:0000269|PubMed:11573955,
FT ECO:0000269|PubMed:12853476"
FT CONFLICT 375
FT /note="K -> R (in Ref. 1; BX647209)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 56441 MW; 81C60CF71BFE951D CRC64;
MAAAAECDVV MAATEPELLD DQEAKREAET FKEQGNAYYA KKDYNEAYNY YTKAIDMCPK
NASYYGNRAA TLMMLGRFRE ALGDAQQSVR LDDSFVRGHL REGKCHLSLG NAMAACRSFQ
RALELDHKNA QAQQEFKNAN AVMEYEKIAE TDFEKRDFRK VVFCMDRALE FAPACHRFKI
LKAECLAMLG RYPEAQSVAS DILRMDSTNA DALYVRGLCL YYEDCIEKAV QFFVQALRMA
PDHEKACIAC RNAKALKAKK EDGNKAFKEG NYKLAYELYT EALGIDPNNI KTNAKLYCNR
GTVNSKLRKL DDAIEDCTNA VKLDDTYIKA YLRRAQCYMD TEQYEEAVRD YEKVYQTEKT
KEHKQLLKNA QLELKKSKRK DYYKILGVDK NASEDEIKKA YRKRALMHHP DRHSGASAEV
QKEEEKKFKE VGEAFTILSD PKKKTRYDSG QDLDEEGMNM GDFDPNNIFK AFFGGPGGFS
FEASGPGNFF FQFG
//
