AHSA1_HUMAN
ID AHSA1_HUMAN Reviewed; 338 AA.
AC O95433; B2R9L2; B4DUR9; Q96IL6; Q9P060;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Activator of 90 kDa heat shock protein ATPase homolog 1;
DE Short=AHA1;
DE AltName: Full=p38;
GN Name=AHSA1; Synonyms=C14orf3; ORFNames=HSPC322;
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] (ISOFORM 1).
RA Michaud J., Chrast R., Rossier C., Papassavas M.P., Antonarakis S.E.,
RA Scott H.S.;
RT "Isolation of a novel gene underexpressed in Down syndrome.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
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].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, and Ovary;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 67-338 (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [8]
RP INTERACTION WITH VSV G, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11554768; DOI=10.1006/bbrc.2001.5621;
RA Sevier C.S., Machamer C.E.;
RT "p38: a novel protein that associates with the vesicular stomatitis virus
RT glycoprotein.";
RL Biochem. Biophys. Res. Commun. 287:574-582(2001).
RN [9]
RP INTERACTION WITH HSPCA, IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RX PubMed=12504007; DOI=10.1016/s1097-2765(02)00785-2;
RA Panaretou B., Siligardi G., Meyer P., Maloney A., Sullivan J.K., Singh S.,
RA Millson S.H., Clarke P.A., Naaby-Hansen S., Stein R., Cramer R.,
RA Mollapour M., Workman P., Piper P.W., Pearl L.H., Prodromou C.;
RT "Activation of the ATPase activity of hsp90 by the stress-regulated
RT cochaperone aha1.";
RL Mol. Cell 10:1307-1318(2002).
RN [10]
RP INTERACTION WITH HSPCA.
RX PubMed=12604615; DOI=10.1074/jbc.m212761200;
RA Lotz G.P., Lin H., Harst A., Obermann W.M.J.;
RT "Aha1 binds to the middle domain of Hsp90, contributes to client protein
RT activation, and stimulates the ATPase activity of the molecular
RT chaperone.";
RL J. Biol. Chem. 278:17228-17235(2003).
RN [11]
RP INTERACTION WITH GCH1.
RX PubMed=16696853; DOI=10.1111/j.1471-4159.2006.03836.x;
RA Swick L., Kapatos G.;
RT "A yeast 2-hybrid analysis of human GTP cyclohydrolase I protein
RT interactions.";
RL J. Neurochem. 97:1447-1455(2006).
RN [12]
RP INTERACTION WITH SRPK1.
RX PubMed=19240134; DOI=10.1101/gad.1752109;
RA Zhong X.Y., Ding J.H., Adams J.A., Ghosh G., Fu X.D.;
RT "Regulation of SR protein phosphorylation and alternative splicing by
RT modulating kinetic interactions of SRPK1 with molecular chaperones.";
RL Genes Dev. 23:482-495(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3 AND LYS-212, AND IDENTIFICATION
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, 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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, 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 [18]
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 [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-182, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [20]
RP FUNCTION, AND INTERACTION WITH FLCN AND HSP90AA1.
RX PubMed=27353360; DOI=10.1038/ncomms12037;
RA Woodford M.R., Dunn D.M., Blanden A.R., Capriotti D., Loiselle D.,
RA Prodromou C., Panaretou B., Hughes P.F., Smith A., Ackerman W.,
RA Haystead T.A., Loh S.N., Bourboulia D., Schmidt L.S., Marston Linehan W.,
RA Bratslavsky G., Mollapour M.;
RT "The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance
RT drug binding.";
RL Nat. Commun. 7:12037-12037(2016).
RN [21]
RP FUNCTION, INTERACTION WITH HSP90AA1, PHOSPHORYLATION AT TYR-223, AND
RP MUTAGENESIS OF TYR-223.
RX PubMed=29127155; DOI=10.15252/embj.201796700;
RA Woodford M.R., Sager R.A., Marris E., Dunn D.M., Blanden A.R., Murphy R.L.,
RA Rensing N., Shapiro O., Panaretou B., Prodromou C., Loh S.N., Gutmann D.H.,
RA Bourboulia D., Bratslavsky G., Wong M., Mollapour M.;
RT "Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding
RT of kinase and non-kinase clients.";
RL EMBO J. 36:3650-3665(2017).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-203, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [23]
RP STRUCTURE BY NMR OF 204-335.
RG RIKEN structural genomics initiative (RSGI);
RT "The solution structure of the C-terminal domain of human activator of 90
RT kDa heat shock protein ATPase homolog 1.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Acts as a co-chaperone of HSP90AA1 (PubMed:29127155).
CC Activates the ATPase activity of HSP90AA1 leading to increase in its
CC chaperone activity (PubMed:29127155). Competes with the inhibitory co-
CC chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal
CC regulatory mechanism for chaperoning of client proteins
CC (PubMed:27353360). Competes with the inhibitory co-chaperone TSC1 for
CC binding to HSP90AA1, thereby providing a reciprocal regulatory
CC mechanism for chaperoning of client proteins (PubMed:29127155).
CC {ECO:0000269|PubMed:27353360, ECO:0000269|PubMed:29127155}.
CC -!- SUBUNIT: Interacts with HSPCA/HSP90 (PubMed:12504007, PubMed:12604615).
CC Interacts (phosphorylated on Tyr-223) with HSP90AA1; the interaction
CC activates HSP90AA1 ATPase activity (PubMed:27353360, PubMed:29127155).
CC Interacts with HSP90AB1 (By similarity). Interacts with GCH1
CC (PubMed:16696853). Interacts with SRPK1 (PubMed:19240134). Interacts
CC with FLCN (PubMed:27353360). {ECO:0000250|UniProtKB:Q8BK64,
CC ECO:0000269|PubMed:12504007, ECO:0000269|PubMed:12604615,
CC ECO:0000269|PubMed:16696853, ECO:0000269|PubMed:19240134,
CC ECO:0000269|PubMed:27353360, ECO:0000269|PubMed:29127155}.
CC -!- SUBUNIT: (Microbial infection) Interacts with vesicular stomatitis
CC virus glycoprotein (VSV G) (via cytoplasmic tail).
CC {ECO:0000269|PubMed:11554768}.
CC -!- INTERACTION:
CC O95433; P30793: GCH1; NbExp=3; IntAct=EBI-448610, EBI-958183;
CC O95433; P07900: HSP90AA1; NbExp=4; IntAct=EBI-448610, EBI-296047;
CC O95433; P08238: HSP90AB1; NbExp=4; IntAct=EBI-448610, EBI-352572;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11554768}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:11554768}. Note=May
CC transiently interact with the endoplasmic reticulum.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O95433-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95433-2; Sequence=VSP_055797;
CC -!- TISSUE SPECIFICITY: Expressed in numerous tissues, including brain,
CC heart, skeletal muscle and kidney and, at lower levels, liver and
CC placenta. {ECO:0000269|PubMed:11554768}.
CC -!- INDUCTION: By heat shock and treatment with the HSP90 inhibitor 17-
CC demethoxygeldanamycin (17AAG). {ECO:0000269|PubMed:12504007}.
CC -!- PTM: Phosphorylation at Tyr-223 enhances binding to chaperone HSP90AA1.
CC {ECO:0000269|PubMed:29127155}.
CC -!- SIMILARITY: Belongs to the AHA1 family. {ECO:0000305}.
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DR EMBL; AJ243310; CAB45684.1; -; mRNA.
DR EMBL; AF164791; AAF80755.1; -; mRNA.
DR EMBL; AK300766; BAG62431.1; -; mRNA.
DR EMBL; AK313824; BAG36559.1; -; mRNA.
DR EMBL; AF111168; AAD09623.1; -; Genomic_DNA.
DR EMBL; CH471061; EAW81291.1; -; Genomic_DNA.
DR EMBL; BC000321; AAH00321.1; -; mRNA.
DR EMBL; BC007398; AAH07398.2; -; mRNA.
DR EMBL; AF161440; AAF29000.1; -; mRNA.
DR CCDS; CCDS9863.1; -. [O95433-1]
DR PIR; JC7769; JC7769.
DR RefSeq; NP_001308370.1; NM_001321441.1.
DR RefSeq; NP_036243.1; NM_012111.2. [O95433-1]
DR PDB; 1X53; NMR; -; A=204-335.
DR PDB; 7DMD; NMR; -; A=28-162.
DR PDB; 7DME; NMR; -; A=28-335.
DR PDBsum; 1X53; -.
DR PDBsum; 7DMD; -.
DR PDBsum; 7DME; -.
DR AlphaFoldDB; O95433; -.
DR BMRB; O95433; -.
DR SMR; O95433; -.
DR BioGRID; 115846; 220.
DR IntAct; O95433; 53.
DR MINT; O95433; -.
DR STRING; 9606.ENSP00000216479; -.
DR ChEMBL; CHEMBL3309113; -.
DR TCDB; 8.A.163.1.1; the hsp90/cdc37 (hsp90/cdc37) family.
DR GlyGen; O95433; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95433; -.
DR MetOSite; O95433; -.
DR PhosphoSitePlus; O95433; -.
DR SwissPalm; O95433; -.
DR BioMuta; AHSA1; -.
DR REPRODUCTION-2DPAGE; IPI00030706; -.
DR EPD; O95433; -.
DR jPOST; O95433; -.
DR MassIVE; O95433; -.
DR MaxQB; O95433; -.
DR PaxDb; O95433; -.
DR PeptideAtlas; O95433; -.
DR PRIDE; O95433; -.
DR ProteomicsDB; 50878; -. [O95433-1]
DR ProteomicsDB; 5208; -.
DR Antibodypedia; 54; 888 antibodies from 36 providers.
DR DNASU; 10598; -.
DR Ensembl; ENST00000216479.8; ENSP00000216479.3; ENSG00000100591.8. [O95433-1]
DR Ensembl; ENST00000535854.6; ENSP00000440108.2; ENSG00000100591.8. [O95433-2]
DR GeneID; 10598; -.
DR KEGG; hsa:10598; -.
DR MANE-Select; ENST00000216479.8; ENSP00000216479.3; NM_012111.3; NP_036243.1.
DR UCSC; uc001xtw.4; human. [O95433-1]
DR CTD; 10598; -.
DR DisGeNET; 10598; -.
DR GeneCards; AHSA1; -.
DR HGNC; HGNC:1189; AHSA1.
DR HPA; ENSG00000100591; Low tissue specificity.
DR MIM; 608466; gene.
DR neXtProt; NX_O95433; -.
DR OpenTargets; ENSG00000100591; -.
DR PharmGKB; PA25515; -.
DR VEuPathDB; HostDB:ENSG00000100591; -.
DR eggNOG; KOG2936; Eukaryota.
DR GeneTree; ENSGT00940000155144; -.
DR HOGENOM; CLU_049046_0_0_1; -.
DR InParanoid; O95433; -.
DR OMA; WAIKLAW; -.
DR OrthoDB; 1548191at2759; -.
DR PhylomeDB; O95433; -.
DR TreeFam; TF313680; -.
DR PathwayCommons; O95433; -.
DR SignaLink; O95433; -.
DR SIGNOR; O95433; -.
DR BioGRID-ORCS; 10598; 29 hits in 1083 CRISPR screens.
DR ChiTaRS; AHSA1; human.
DR EvolutionaryTrace; O95433; -.
DR GeneWiki; AHSA1; -.
DR GenomeRNAi; 10598; -.
DR Pharos; O95433; Tbio.
DR PRO; PR:O95433; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; O95433; protein.
DR Bgee; ENSG00000100591; Expressed in oocyte and 208 other tissues.
DR ExpressionAtlas; O95433; baseline and differential.
DR Genevisible; O95433; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0001671; F:ATPase activator activity; IDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0051087; F:chaperone binding; IDA:UniProtKB.
DR GO; GO:0051879; F:Hsp90 protein binding; IPI:UniProtKB.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IDA:UniProtKB.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR Gene3D; 3.15.10.20; -; 1.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR013538; Activator_of_Hsp90_ATPase.
DR InterPro; IPR036338; Aha1.
DR InterPro; IPR039981; AHSA-like.
DR InterPro; IPR015310; AHSA1_N.
DR InterPro; IPR023393; START-like_dom_sf.
DR PANTHER; PTHR13009; PTHR13009; 1.
DR Pfam; PF09229; Aha1_N; 1.
DR Pfam; PF08327; AHSA1; 1.
DR SMART; SM01000; Aha1_N; 1.
DR SUPFAM; SSF103111; SSF103111; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chaperone; Cytoplasm;
KW Endoplasmic reticulum; Host-virus interaction; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Stress response; Ubl conjugation.
FT CHAIN 1..338
FT /note="Activator of 90 kDa heat shock protein ATPase
FT homolog 1"
FT /id="PRO_0000215820"
FT MOD_RES 3
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 212
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 223
FT /note="Phosphotyrosine; by ABL"
FT /evidence="ECO:0000305|PubMed:29127155"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 182
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 203
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 283..338
FT /note="HFATITLTFIDKNGETELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFGYG
FT ARLF -> SHCHSG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055797"
FT MUTAGEN 223
FT /note="Y->E: Phosphomimetic mutant. Increases the binding
FT to HSP90AA1 resulting in TSC1 dissociation from HSP90AA1."
FT /evidence="ECO:0000269|PubMed:29127155"
FT CONFLICT 67..68
FT /note="EA -> CL (in Ref. 7; AAF29000)"
FT /evidence="ECO:0000305"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:7DMD"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:7DME"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:7DMD"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:7DMD"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:7DME"
FT STRAND 78..93
FT /evidence="ECO:0007829|PDB:7DMD"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:7DMD"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:7DMD"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:7DMD"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:7DMD"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:7DMD"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:7DMD"
FT HELIX 131..159
FT /evidence="ECO:0007829|PDB:7DMD"
FT STRAND 206..217
FT /evidence="ECO:0007829|PDB:1X53"
FT HELIX 219..225
FT /evidence="ECO:0007829|PDB:1X53"
FT HELIX 229..235
FT /evidence="ECO:0007829|PDB:1X53"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:7DME"
FT TURN 253..256
FT /evidence="ECO:0007829|PDB:1X53"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:1X53"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:1X53"
FT STRAND 269..276
FT /evidence="ECO:0007829|PDB:1X53"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:1X53"
FT STRAND 298..308
FT /evidence="ECO:0007829|PDB:1X53"
FT HELIX 309..317
FT /evidence="ECO:0007829|PDB:1X53"
FT TURN 318..323
FT /evidence="ECO:0007829|PDB:1X53"
FT HELIX 324..330
FT /evidence="ECO:0007829|PDB:1X53"
SQ SEQUENCE 338 AA; 38274 MW; E6B686DDD8D7D729 CRC64;
MAKWGEGDPR WIVEERADAT NVNNWHWTER DASNWSTDKL KTLFLAVQVQ NEEGKCEVTE
VSKLDGEASI NNRKGKLIFF YEWSVKLNWT GTSKSGVQYK GHVEIPNLSD ENSVDEVEIS
VSLAKDEPDT NLVALMKEEG VKLLREAMGI YISTLKTEFT QGMILPTMNG ESVDPVGQPA
LKTEERKAKP APSKTQARPV GVKIPTCKIT LKETFLTSPE ELYRVFTTQE LVQAFTHAPA
TLEADRGGKF HMVDGNVSGE FTDLVPEKHI VMKWRFKSWP EGHFATITLT FIDKNGETEL
CMEGRGIPAP EEERTRQGWQ RYYFEGIKQT FGYGARLF
