AHSA2_MOUSE
ID AHSA2_MOUSE Reviewed; 331 AA.
AC Q8N9S3; Q0P626; Q6P3F2; Q7TMW7; Q8CBI4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Activator of 90 kDa heat shock protein ATPase homolog 2;
GN Name=Ahsa2;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, and Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6NCr, and Czech II;
RC TISSUE=Hematopoietic stem cell, Jaw, Limb, and Mammary tumor;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, and Spleen;
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).
CC -!- FUNCTION: Co-chaperone that stimulates HSP90 ATPase activity.
CC {ECO:0000250|UniProtKB:Q12449}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8N9S3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N9S3-2; Sequence=VSP_030572;
CC Name=3;
CC IsoId=Q8N9S3-3; Sequence=VSP_030573;
CC -!- SIMILARITY: Belongs to the AHA1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH38397.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK093945; BAC04256.1; -; mRNA.
DR EMBL; AK035941; BAC29251.1; -; mRNA.
DR EMBL; AK137116; BAE23240.1; -; mRNA.
DR EMBL; AK154196; BAE32431.1; -; mRNA.
DR EMBL; AK155265; BAE33153.1; -; mRNA.
DR EMBL; AL672049; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC038397; AAH38397.2; ALT_INIT; mRNA.
DR EMBL; BC052829; AAH52829.1; -; mRNA.
DR EMBL; BC064012; AAH64012.1; -; mRNA.
DR CCDS; CCDS24476.1; -. [Q8N9S3-1]
DR CCDS; CCDS70149.1; -. [Q8N9S3-2]
DR RefSeq; NP_001277583.1; NM_001290654.1. [Q8N9S3-2]
DR RefSeq; NP_001277584.1; NM_001290655.1. [Q8N9S3-3]
DR RefSeq; NP_765979.3; NM_172391.4. [Q8N9S3-1]
DR AlphaFoldDB; Q8N9S3; -.
DR SMR; Q8N9S3; -.
DR BioGRID; 234490; 1.
DR STRING; 10090.ENSMUSP00000020529; -.
DR iPTMnet; Q8N9S3; -.
DR PhosphoSitePlus; Q8N9S3; -.
DR EPD; Q8N9S3; -.
DR MaxQB; Q8N9S3; -.
DR PaxDb; Q8N9S3; -.
DR PRIDE; Q8N9S3; -.
DR ProteomicsDB; 296087; -. [Q8N9S3-1]
DR ProteomicsDB; 296088; -. [Q8N9S3-2]
DR ProteomicsDB; 296089; -. [Q8N9S3-3]
DR DNASU; 268390; -.
DR Ensembl; ENSMUST00000020529; ENSMUSP00000020529; ENSMUSG00000020288. [Q8N9S3-1]
DR Ensembl; ENSMUST00000109539; ENSMUSP00000105166; ENSMUSG00000020288. [Q8N9S3-2]
DR GeneID; 268390; -.
DR KEGG; mmu:268390; -.
DR UCSC; uc007ifb.2; mouse. [Q8N9S3-1]
DR UCSC; uc056ykb.1; mouse. [Q8N9S3-3]
DR CTD; 268390; -.
DR MGI; MGI:1916133; Ahsa2.
DR VEuPathDB; HostDB:ENSMUSG00000020288; -.
DR eggNOG; KOG2936; Eukaryota.
DR GeneTree; ENSGT00940000157344; -.
DR HOGENOM; CLU_049046_0_0_1; -.
DR InParanoid; Q8N9S3; -.
DR OMA; CEVNQRK; -.
DR OrthoDB; 1548191at2759; -.
DR PhylomeDB; Q8N9S3; -.
DR TreeFam; TF313680; -.
DR BioGRID-ORCS; 268390; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Ahsa2; mouse.
DR PRO; PR:Q8N9S3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8N9S3; protein.
DR Bgee; ENSMUSG00000020288; Expressed in cortical plate and 257 other tissues.
DR ExpressionAtlas; Q8N9S3; baseline and differential.
DR Genevisible; Q8N9S3; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0001671; F:ATPase activator activity; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR GO; GO:0051879; F:Hsp90 protein binding; IEA:InterPro.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IBA:GO_Central.
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 Alternative splicing; Chaperone; Reference proteome; Stress response.
FT CHAIN 1..331
FT /note="Activator of 90 kDa heat shock protein ATPase
FT homolog 2"
FT /id="PRO_0000315606"
FT VAR_SEQ 1..48
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_030572"
FT VAR_SEQ 275..331
FT /note="EHYATVELNFVPAPGQTELQLDCKGVPVCKEENMKFCWQKQHFEEIKGLLEL
FT TAQNA -> ALGFFPRTLCNS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030573"
FT CONFLICT 14
FT /note="E -> A (in Ref. 4; AAH52829)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="E -> A (in Ref. 4; AAH52829)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="E -> G (in Ref. 1; BAC04256)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="T -> A (in Ref. 4; AAH38397)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 331 AA; 37648 MW; 94C560599937A951 CRC64;
MAKWGQGDPR WIVEEREDGT NVNNWHWTER DATIWSKGKL RELLVGIAME NEAGRCEISE
LKQVEGEASC NSRKGKLIFF YEWNIKLAWK GTVKESGAKH KGLIEIPSLS EENEINDTEV
NVSKKKGDGE ILKDLMRTTG TAKVREALGE YLKALKTEFT TGMILPTKAV ATQELTLQRK
LNENKLQASP VALGVRIPTV ALHLTELFDT TVEQLYSIFT VKELVQKFSK SPAVLEAERG
GKFQMFDGNI SGEYVELVTN RKIIMKWRCR NWPEEHYATV ELNFVPAPGQ TELQLDCKGV
PVCKEENMKF CWQKQHFEEI KGLLELTAQN A
