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 28-JAN-2026, entry version 220. 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=5; IntAct=EBI-357552, EBI-355275; CC Q99615; O95429: BAG4; NbExp=3; IntAct=EBI-357552, EBI-2949658; CC Q99615; Q9NRI5: DISC1; NbExp=3; IntAct=EBI-357552, EBI-529989; CC Q99615; P34931: HSPA1L; NbExp=2; IntAct=EBI-357552, EBI-354912; CC Q99615; Q15773: MLF2; NbExp=2; IntAct=EBI-357552, EBI-1051875; 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_001144766.3. [Q99615-2] DR RefSeq; NP_003306.3; NM_003315.4. [Q99615-1] DR RefSeq; XP_011523469.1; XM_011525167.4. [Q99615-2] DR RefSeq; XP_011523471.1; XM_011525169.4. [Q99615-2] DR RefSeq; XP_016880483.1; XM_017024994.3. [Q99615-2] DR RefSeq; XP_054173014.1; XM_054317039.1. [Q99615-2] DR RefSeq; XP_054173015.1; XM_054317040.1. [Q99615-2] DR RefSeq; XP_054173016.1; XM_054317041.1. [Q99615-2] DR AlphaFoldDB; Q99615; -. DR SMR; Q99615; -. DR BioGRID; 113117; 495. DR CORUM; Q99615; -. DR FunCoup; Q99615; 3720. DR IntAct; Q99615; 233. 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 jPOST; Q99615; -. DR MassIVE; Q99615; -. DR PaxDb; 9606-ENSP00000406463; -. DR PeptideAtlas; Q99615; -. DR ProteomicsDB; 69491; -. DR ProteomicsDB; 78359; -. [Q99615-1] DR Pumba; Q99615; -. DR Antibodypedia; 8072; 225 antibodies from 28 providers. DR DNASU; 7266; -. DR Ensembl; ENST00000316603.12; ENSP00000313311.7; ENSG00000168259.18. [Q99615-2] DR Ensembl; ENST00000426588.7; ENSP00000394327.2; ENSG00000168259.18. [Q99615-2] DR Ensembl; ENST00000457167.9; ENSP00000406463.2; ENSG00000168259.18. [Q99615-1] DR Ensembl; ENST00000590774.6; ENSP00000465340.2; ENSG00000168259.18. [Q99615-2] DR Ensembl; ENST00000674166.1; ENSP00000501364.1; ENSG00000168259.18. [Q99615-2] DR Ensembl; ENST00000674252.1; ENSP00000501366.1; ENSG00000168259.18. [Q99615-2] DR Ensembl; ENST00000674287.1; ENSP00000501482.1; ENSG00000168259.18. [Q99615-2] DR Ensembl; ENST00000674303.1; ENSP00000501468.1; ENSG00000168259.18. [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 ClinPGx; PA27424; -. DR CTD; 7266; -. DR DisGeNET; 7266; -. DR GeneCards; DNAJC7; -. DR HGNC; HGNC:12392; DNAJC7. DR HPA; ENSG00000168259; Low tissue specificity. DR MalaCards; DNAJC7; -. DR MIM; 601964; gene. DR OpenTargets; ENSG00000168259; -. DR VEuPathDB; HostDB:ENSG00000168259; -. DR eggNOG; KOG0550; Eukaryota. DR GeneTree; ENSGT00940000155338; -. DR HOGENOM; CLU_015935_3_1_1; -. DR InParanoid; Q99615; -. DR OrthoDB; 765884at2759; -. DR PAN-GO; Q99615; 1 GO annotation based on evolutionary models. DR PhylomeDB; Q99615; -. DR PathwayCommons; Q99615; -. DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response. DR SignaLink; Q99615; -. DR Agora; ENSG00000168259; -. DR BioGRID-ORCS; 7266; 20 hits in 1153 CRISPR screens. DR CD-CODE; DEE660B4; Stress granule. 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 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:0006457; P:protein folding; IDA:UniProtKB. DR GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome. DR CDD; cd06257; DnaJ; 1. DR FunFam; 1.10.287.110:FF:000018; DnaJ (Hsp40) homolog, subfamily C, member 7; 1. DR FunFam; 1.25.40.10:FF:000097; DnaJ homolog subfamily C member 7 homolog; 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_rpt. DR PANTHER; PTHR45188:SF2; DNAJ HOMOLOG SUBFAMILY C MEMBER 7; 1. DR PANTHER; PTHR45188; DNAJ PROTEIN P58IPK HOMOLOG; 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; KW Proteomics identification; Reference proteome; 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 //