UN45A_HUMAN
ID UN45A_HUMAN Reviewed; 944 AA.
AC Q9H3U1; A8K6F7; Q7L3Y6; Q9H3U8; Q9NSE8; Q9NSE9;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Protein unc-45 homolog A;
DE Short=Unc-45A;
DE AltName: Full=GCUNC-45;
DE AltName: Full=Smooth muscle cell-associated protein 1;
DE Short=SMAP-1;
GN Name=UNC45A; Synonyms=SMAP1;
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 [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Heart;
RA Nishimoto S., Toyoda H., Tawara J., Aoki T., Komurasaki T.;
RT "Molecular cloning and characterization of human smooth muscle cell
RT associated protein-1 (SMAP-1).";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 756-944.
RC TISSUE=Brain, and Fetus;
RG The European IMAGE consortium;
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta, and Testis;
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 [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=Colon, Lung, and Uterus;
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 FUNCTION, ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=12119110; DOI=10.1016/s0378-1119(02)00645-5;
RA Marcos I., Borrego S., Rodriguez de Cordoba S., Galan J.J., Antinolo G.;
RT "Cloning, characterization and chromosome mapping of the human SMAP1
RT gene.";
RL Gene 292:167-171(2002).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70 AND LYS-483, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15, 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 [11]
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 [12]
RP IDENTIFICATION BY 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP STRUCTURE BY NMR OF 1-135.
RG RIKEN structural genomics initiative (RSGI);
RT "The solution structure of the tetratricopeptide repeat of human smooth
RT muscle cell associated protein-1.";
RL Submitted (JUN-2006) to the PDB data bank.
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PGR; NR3C1 AND HSP90AB1,
RP AND MUTAGENESIS OF LYS-33; ALA-40; LYS-70 AND ALA-77.
RX PubMed=16478993; DOI=10.1128/mcb.26.5.1722-1730.2006;
RA Chadli A., Graham J.D., Abel M.G., Jackson T.A., Gordon D.F., Wood W.M.,
RA Felts S.J., Horwitz K.B., Toft D.;
RT "GCUNC-45 is a novel regulator for the progesterone receptor/hsp90
RT chaperoning pathway.";
RL Mol. Cell. Biol. 26:1722-1730(2006).
RN [17]
RP INVOLVEMENT IN OOHE, AND VARIANTS OOHE TRP-98; 277-ARG--GLU-944 DEL;
RP VAL-343; ASP-438; 876-GLN--GLU-944 DEL; LEU-893 AND GLY-927.
RX PubMed=29429573; DOI=10.1016/j.ajhg.2018.01.009;
RA Esteve C., Francescatto L., Tan P.L., Bourchany A., De Leusse C.,
RA Marinier E., Blanchard A., Bourgeois P., Brochier-Armanet C., Bruel A.L.,
RA Delarue A., Duffourd Y., Ecochard-Dugelay E., Hery G., Huet F., Gauchez P.,
RA Gonzales E., Guettier-Bouttier C., Komuta M., Lacoste C., Maudinas R.,
RA Mazodier K., Rimet Y., Riviere J.B., Roquelaure B., Sigaudy S.,
RA Stephenne X., Thauvin-Robinet C., Thevenon J., Sarles J., Levy N.,
RA Badens C., Goulet O., Hugot J.P., Katsanis N., Faivre L., Fabre A.;
RT "Loss-of-Function Mutations in UNC45A Cause a Syndrome Associating
RT Cholestasis, Diarrhea, Impaired Hearing, and Bone Fragility.";
RL Am. J. Hum. Genet. 102:364-374(2018).
CC -!- FUNCTION: Acts as co-chaperone for HSP90. Prevents the stimulation of
CC HSP90AB1 ATPase activity by AHSA1. Positive factor in promoting PGR
CC function in the cell. May be necessary for proper folding of myosin
CC (Potential). Necessary for normal cell proliferation. Necessary for
CC normal myotube formation and myosin accumulation during muscle cell
CC development. May play a role in erythropoiesis in stroma cells in the
CC spleen (By similarity). {ECO:0000250, ECO:0000269|PubMed:12119110,
CC ECO:0000269|PubMed:16478993, ECO:0000305}.
CC -!- SUBUNIT: Interacts with PGR isoforms A and B as well as with NR3C1 in
CC the absence of ligand, and with HSP90AB1. Binding to HSP90AB1 involves
CC 2 UNC45A monomers per HSP90AB1 dimer. {ECO:0000269|PubMed:16478993}.
CC -!- INTERACTION:
CC Q9H3U1; Q96HU8: DIRAS2; NbExp=3; IntAct=EBI-1048763, EBI-911391;
CC Q9H3U1; Q8NA82: MARCHF10; NbExp=7; IntAct=EBI-1048763, EBI-2341554;
CC Q9H3U1; P61244: MAX; NbExp=4; IntAct=EBI-1048763, EBI-751711;
CC Q9H3U1; P61244-2: MAX; NbExp=3; IntAct=EBI-1048763, EBI-10218525;
CC Q9H3U1; P50221: MEOX1; NbExp=3; IntAct=EBI-1048763, EBI-2864512;
CC Q9H3U1; P50222: MEOX2; NbExp=3; IntAct=EBI-1048763, EBI-748397;
CC Q9H3U1; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-1048763, EBI-16439278;
CC Q9H3U1; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-1048763, EBI-10172526;
CC Q9H3U1; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-1048763, EBI-14066006;
CC Q9H3U1; Q969V4: TEKT1; NbExp=3; IntAct=EBI-1048763, EBI-10180409;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16478993}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:16478993}. Nucleus
CC {ECO:0000269|PubMed:16478993}. Note=Predominant in the perinuclear
CC region. Little protein in the nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=2, SMAP-1b;
CC IsoId=Q9H3U1-1; Sequence=Displayed;
CC Name=2; Synonyms=3;
CC IsoId=Q9H3U1-2; Sequence=VSP_020585;
CC Name=3;
CC IsoId=Q9H3U1-3; Sequence=VSP_020584;
CC -!- TISSUE SPECIFICITY: Detected in peripheral blood leukocytes, bone
CC marrow, adrenal gland, trachea, spinal cord, thyroid, lymph node and
CC stomach. {ECO:0000269|PubMed:12119110}.
CC -!- DISEASE: Osteootohepatoenteric syndrome (OOHE) [MIM:619377]: An
CC autosomal recessive disorder characterized by cholestasis, congenital
CC diarrhea, impaired hearing, and bone fragility. Some patients also
CC display mild developmental delay and intellectual disability.
CC {ECO:0000269|PubMed:29429573}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
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DR EMBL; AB014729; BAB20266.1; -; mRNA.
DR EMBL; AB014736; BAB20273.1; -; mRNA.
DR EMBL; AL357537; CAB93428.1; -; mRNA.
DR EMBL; AL357538; CAB93429.1; -; mRNA.
DR EMBL; AK291622; BAF84311.1; -; mRNA.
DR EMBL; AK125721; BAG54239.1; -; mRNA.
DR EMBL; CH471101; EAX02127.1; -; Genomic_DNA.
DR EMBL; BC006214; AAH06214.1; -; mRNA.
DR EMBL; BC010995; AAH10995.2; -; mRNA.
DR EMBL; BC037992; AAH37992.1; -; mRNA.
DR EMBL; BC045635; AAH45635.1; -; mRNA.
DR CCDS; CCDS10367.1; -. [Q9H3U1-1]
DR CCDS; CCDS42082.1; -. [Q9H3U1-2]
DR RefSeq; NP_001034764.1; NM_001039675.1. [Q9H3U1-2]
DR RefSeq; NP_001310548.1; NM_001323619.1. [Q9H3U1-1]
DR RefSeq; NP_001310550.1; NM_001323621.1. [Q9H3U1-2]
DR RefSeq; NP_061141.2; NM_018671.4. [Q9H3U1-1]
DR RefSeq; XP_011520081.1; XM_011521779.2.
DR PDB; 2DBA; NMR; -; A=1-135.
DR PDBsum; 2DBA; -.
DR AlphaFoldDB; Q9H3U1; -.
DR BMRB; Q9H3U1; -.
DR SMR; Q9H3U1; -.
DR BioGRID; 120986; 173.
DR IntAct; Q9H3U1; 80.
DR MINT; Q9H3U1; -.
DR STRING; 9606.ENSP00000407487; -.
DR GlyGen; Q9H3U1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H3U1; -.
DR MetOSite; Q9H3U1; -.
DR PhosphoSitePlus; Q9H3U1; -.
DR SwissPalm; Q9H3U1; -.
DR BioMuta; UNC45A; -.
DR DMDM; 74761419; -.
DR EPD; Q9H3U1; -.
DR jPOST; Q9H3U1; -.
DR MassIVE; Q9H3U1; -.
DR MaxQB; Q9H3U1; -.
DR PaxDb; Q9H3U1; -.
DR PeptideAtlas; Q9H3U1; -.
DR PRIDE; Q9H3U1; -.
DR ProteomicsDB; 80756; -. [Q9H3U1-1]
DR ProteomicsDB; 80757; -. [Q9H3U1-2]
DR ProteomicsDB; 80758; -. [Q9H3U1-3]
DR Antibodypedia; 28924; 119 antibodies from 24 providers.
DR DNASU; 55898; -.
DR Ensembl; ENST00000394275.7; ENSP00000377816.2; ENSG00000140553.18. [Q9H3U1-2]
DR Ensembl; ENST00000418476.2; ENSP00000407487.2; ENSG00000140553.18. [Q9H3U1-1]
DR GeneID; 55898; -.
DR KEGG; hsa:55898; -.
DR MANE-Select; ENST00000418476.2; ENSP00000407487.2; NM_018671.5; NP_061141.2.
DR UCSC; uc002bqd.3; human. [Q9H3U1-1]
DR CTD; 55898; -.
DR DisGeNET; 55898; -.
DR GeneCards; UNC45A; -.
DR HGNC; HGNC:30594; UNC45A.
DR HPA; ENSG00000140553; Low tissue specificity.
DR MIM; 611219; gene.
DR MIM; 619377; phenotype.
DR neXtProt; NX_Q9H3U1; -.
DR OpenTargets; ENSG00000140553; -.
DR PharmGKB; PA142670638; -.
DR VEuPathDB; HostDB:ENSG00000140553; -.
DR eggNOG; KOG4151; Eukaryota.
DR GeneTree; ENSGT00940000159320; -.
DR HOGENOM; CLU_007331_0_0_1; -.
DR InParanoid; Q9H3U1; -.
DR OMA; DHLYLTR; -.
DR OrthoDB; 1059433at2759; -.
DR PhylomeDB; Q9H3U1; -.
DR TreeFam; TF314096; -.
DR PathwayCommons; Q9H3U1; -.
DR SignaLink; Q9H3U1; -.
DR BioGRID-ORCS; 55898; 224 hits in 1081 CRISPR screens.
DR ChiTaRS; UNC45A; human.
DR EvolutionaryTrace; Q9H3U1; -.
DR GeneWiki; UNC45A; -.
DR GenomeRNAi; 55898; -.
DR Pharos; Q9H3U1; Tbio.
DR PRO; PR:Q9H3U1; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9H3U1; protein.
DR Bgee; ENSG00000140553; Expressed in esophagogastric junction muscularis propria and 181 other tissues.
DR ExpressionAtlas; Q9H3U1; baseline and differential.
DR Genevisible; Q9H3U1; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0051879; F:Hsp90 protein binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.10; -; 2.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR024660; UCS_central_dom.
DR Pfam; PF13181; TPR_8; 1.
DR Pfam; PF11701; UNC45-central; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48371; SSF48371; 2.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chaperone; Cytoplasm;
KW Deafness; Developmental protein; Differentiation; Myogenesis; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..944
FT /note="Protein unc-45 homolog A"
FT /id="PRO_0000249888"
FT REPEAT 21..54
FT /note="TPR 1"
FT REPEAT 58..91
FT /note="TPR 2"
FT REPEAT 92..125
FT /note="TPR 3"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 70
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 483
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..722
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_020584"
FT VAR_SEQ 1..17
FT /note="MTVSGPGTPEPRPATPG -> MT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1,
FT ECO:0000303|Ref.2"
FT /id="VSP_020585"
FT VARIANT 98
FT /note="R -> W (in OOHE; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:29429573"
FT /id="VAR_086010"
FT VARIANT 277..944
FT /note="Missing (in OOHE; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:29429573"
FT /id="VAR_086011"
FT VARIANT 343
FT /note="G -> V (in OOHE; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:29429573"
FT /id="VAR_086012"
FT VARIANT 438
FT /note="V -> D (in OOHE; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:29429573"
FT /id="VAR_086013"
FT VARIANT 796
FT /note="T -> M (in dbSNP:rs8041035)"
FT /id="VAR_052629"
FT VARIANT 876..944
FT /note="Missing (in OOHE; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:29429573"
FT /id="VAR_086014"
FT VARIANT 893
FT /note="S -> L (in OOHE; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:29429573"
FT /id="VAR_086015"
FT VARIANT 927
FT /note="C -> G (in OOHE; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:29429573"
FT /id="VAR_086016"
FT MUTAGEN 33
FT /note="K->E: Abolishes interaction with HSP90AB1; when
FT associated with D-40. No effect on interaction with PGR."
FT /evidence="ECO:0000269|PubMed:16478993"
FT MUTAGEN 40
FT /note="A->D: Abolishes interaction with HSP90AB1; when
FT associated with E-33. No effect on interaction with PGR."
FT /evidence="ECO:0000269|PubMed:16478993"
FT MUTAGEN 70
FT /note="K->E: Abolishes interaction with HSP90AB1; when
FT associated with D-77. No effect on interaction with PGR."
FT /evidence="ECO:0000269|PubMed:16478993"
FT MUTAGEN 77
FT /note="A->D: Abolishes interaction with HSP90AB1; when
FT associated with E-70. No effect on interaction with PGR."
FT /evidence="ECO:0000269|PubMed:16478993"
FT CONFLICT 921
FT /note="T -> R (in Ref. 2; CAB93429)"
FT /evidence="ECO:0000305"
FT HELIX 21..32
FT /evidence="ECO:0007829|PDB:2DBA"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:2DBA"
FT HELIX 37..48
FT /evidence="ECO:0007829|PDB:2DBA"
FT HELIX 54..70
FT /evidence="ECO:0007829|PDB:2DBA"
FT HELIX 74..87
FT /evidence="ECO:0007829|PDB:2DBA"
FT HELIX 92..105
FT /evidence="ECO:0007829|PDB:2DBA"
FT HELIX 108..121
FT /evidence="ECO:0007829|PDB:2DBA"
FT HELIX 126..135
FT /evidence="ECO:0007829|PDB:2DBA"
SQ SEQUENCE 944 AA; 103077 MW; 398707D0FF2A703D CRC64;
MTVSGPGTPE PRPATPGASS VEQLRKEGNE LFKCGDYGGA LAAYTQALGL DATPQDQAVL
HRNRAACHLK LEDYDKAETE ASKAIEKDGG DVKALYRRSQ ALEKLGRLDQ AVLDLQRCVS
LEPKNKVFQE ALRNIGGQIQ EKVRYMSSTD AKVEQMFQIL LDPEEKGTEK KQKASQNLVV
LAREDAGAEK IFRSNGVQLL QRLLDMGETD LMLAALRTLV GICSEHQSRT VATLSILGTR
RVVSILGVES QAVSLAACHL LQVMFDALKE GVKKGFRGKE GAIIVDPARE LKVLISNLLD
LLTEVGVSGQ GRDNALTLLI KAVPRKSLKD PNNSLTLWVI DQGLKKILEV GGSLQDPPGE
LAVTANSRMS ASILLSKLFD DLKCDAEREN FHRLCENYIK SWFEGQGLAG KLRAIQTVSC
LLQGPCDAGN RALELSGVME SVIALCASEQ EEEQLVAVEA LIHAAGKAKR ASFITANGVS
LLKDLYKCSE KDSIRIRALV GLCKLGSAGG TDFSMKQFAE GSTLKLAKQC RKWLCNDQID
AGTRRWAVEG LAYLTFDADV KEEFVEDAAA LKALFQLSRL EERSVLFAVA SALVNCTNSY
DYEEPDPKMV ELAKYAKQHV PEQHPKDKPS FVRARVKKLL AAGVVSAMVC MVKTESPVLT
SSCRELLSRV FLALVEEVED RGTVVAQGGG RALIPLALEG TDVGQTKAAQ ALAKLTITSN
PEMTFPGERI YEVVRPLVSL LHLNCSGLQN FEALMALTNL AGISERLRQK ILKEKAVPMI
EGYMFEEHEM IRRAATECMC NLAMSKEVQD LFEAQGNDRL KLLVLYSGED DELLQRAAAG
GLAMLTSMRP TLCSRIPQVT THWLEILQAL LLSSNQELQH RGAVVVLNMV EASREIASTL
MESEMMEILS VLAKGDHSPV TRAAAACLDK AVEYGLIQPN QDGE
