AHSA1_MOUSE
ID AHSA1_MOUSE Reviewed; 338 AA.
AC Q8BK64; Q8R3E6;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Activator of 90 kDa heat shock protein ATPase homolog 1;
DE Short=AHA1;
GN Name=Ahsa1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|EMBL:BAC36160.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP INTERACTION WITH HSP90AB1.
RX PubMed=22022502; DOI=10.1371/journal.pone.0026044;
RA Echeverria P.C., Bernthaler A., Dupuis P., Mayer B., Picard D.;
RT "An interaction network predicted from public data as a discovery tool:
RT application to the Hsp90 molecular chaperone machine.";
RL PLoS ONE 6:E26044-E26044(2011).
RN [5]
RP FUNCTION, AND INTERACTION WITH HSP90AA1.
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).
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 (By
CC similarity). Competes with the inhibitory co-chaperone TSC1 for binding
CC to HSP90AA1, thereby providing a reciprocal regulatory mechanism for
CC chaperoning of client proteins (PubMed:29127155).
CC {ECO:0000250|UniProtKB:O95433, ECO:0000269|PubMed:29127155}.
CC -!- SUBUNIT: Interacts with HSPCA/HSP90 (By similarity). Interacts with
CC HSP90AA1; the interaction activates HSP90AA1 ATPase activity
CC (PubMed:29127155). Interacts with HSP90AB1 (PubMed:22022502). Interacts
CC with GCH1 (By similarity). Interacts with SRPK1 (By similarity).
CC Interacts with FLCN (By similarity). {ECO:0000250|UniProtKB:O95433,
CC ECO:0000269|PubMed:22022502, ECO:0000269|PubMed:29127155}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O95433}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:O95433}. Note=May transiently interact with the
CC endoplasmic reticulum. {ECO:0000250|UniProtKB:O95433}.
CC -!- INDUCTION: By heat shock and treatment with the HSP90 inhibitor 17-
CC demethoxygeldanamycin (17AAG).
CC -!- PTM: Phosphorylation at Tyr-223 enhances binding to chaperone HSP90AA1.
CC {ECO:0000305|PubMed:29127155}.
CC -!- SIMILARITY: Belongs to the AHA1 family. {ECO:0000305}.
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DR EMBL; AK076069; BAC36160.1; -; mRNA.
DR EMBL; BC023857; AAH23857.1; -; mRNA.
DR EMBL; BC025552; AAH25552.1; -; mRNA.
DR CCDS; CCDS26075.1; -.
DR RefSeq; NP_666148.1; NM_146036.1.
DR AlphaFoldDB; Q8BK64; -.
DR BMRB; Q8BK64; -.
DR SMR; Q8BK64; -.
DR BioGRID; 229959; 25.
DR IntAct; Q8BK64; 1.
DR STRING; 10090.ENSMUSP00000021425; -.
DR iPTMnet; Q8BK64; -.
DR PhosphoSitePlus; Q8BK64; -.
DR SwissPalm; Q8BK64; -.
DR REPRODUCTION-2DPAGE; Q8BK64; -.
DR EPD; Q8BK64; -.
DR jPOST; Q8BK64; -.
DR MaxQB; Q8BK64; -.
DR PaxDb; Q8BK64; -.
DR PRIDE; Q8BK64; -.
DR ProteomicsDB; 285569; -.
DR Antibodypedia; 54; 888 antibodies from 36 providers.
DR Ensembl; ENSMUST00000021425; ENSMUSP00000021425; ENSMUSG00000021037.
DR GeneID; 217737; -.
DR KEGG; mmu:217737; -.
DR UCSC; uc007oit.1; mouse.
DR CTD; 10598; -.
DR MGI; MGI:2387603; Ahsa1.
DR VEuPathDB; HostDB:ENSMUSG00000021037; -.
DR eggNOG; KOG2936; Eukaryota.
DR GeneTree; ENSGT00940000155144; -.
DR HOGENOM; CLU_049046_0_0_1; -.
DR InParanoid; Q8BK64; -.
DR OMA; WAIKLAW; -.
DR OrthoDB; 1548191at2759; -.
DR PhylomeDB; Q8BK64; -.
DR TreeFam; TF313680; -.
DR BioGRID-ORCS; 217737; 8 hits in 60 CRISPR screens.
DR ChiTaRS; Ahsa1; mouse.
DR PRO; PR:Q8BK64; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8BK64; protein.
DR Bgee; ENSMUSG00000021037; Expressed in ear vesicle and 246 other tissues.
DR ExpressionAtlas; Q8BK64; baseline and differential.
DR Genevisible; Q8BK64; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0001671; F:ATPase activator activity; ISS:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR GO; GO:0051879; F:Hsp90 protein binding; IPI:UniProtKB.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISO:MGI.
DR GO; GO:0006457; P:protein folding; ISS:UniProtKB.
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 Acetylation; Chaperone; Cytoplasm; Endoplasmic reticulum; 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_0000215821"
FT MOD_RES 3
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O95433"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95433"
FT MOD_RES 212
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O95433"
FT MOD_RES 223
FT /note="Phosphotyrosine; by ABL"
FT /evidence="ECO:0000250|UniProtKB:O95433"
FT CROSSLNK 182
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:O95433"
FT CROSSLNK 203
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95433"
FT CONFLICT 192
FT /note="P -> L (in Ref. 2; BAC36160)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 38117 MW; C4F0F94FF44F9FB3 CRC64;
MAKWGEGDPR WIVEERADAT NVNNWHWTER DASNWSTEKL KTLFLAVRVE NEEGKCEVTE
VNKLDGEASI NNRKGKLIFF YEWTIKLNWT GTSKSGVQYK GHVEIPNLSD ENSVDEVEIS
VSLAKDEPDT NLVALMKEDG VKLLREAVGI YISTLKTEFT QGMILPTVNG ESVDPVGQPA
LKTETCKAKS APSKSQAKPV GVKIPTCKIT LKETFLTSPE ELYRVFTTQE LVQAFTHAPA
ALEADRGGKF HMVDGNVTGE FTDLVPEKHI AMKWRFKSWP EGHFATITLT FIDKNGETEL
CMEGRGIPAP EEERTRQGWQ RYYFEGIKQT FGYGARLF
