ID AHSA2_HUMAN Reviewed; 299 AA. AC Q719I0; B3KS51; D6W5E0; Q8NDU5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 2. DT 24-JAN-2024, entry version 133. DE RecName: Full=Putative activator of 90 kDa heat shock protein ATPase homolog 2 {ECO:0000305}; DE AltName: Full=Activator of HSP90 ATPase homolog 2 pseudogene {ECO:0000312|HGNC:HGNC:20437}; GN Name=AHSA2P {ECO:0000312|HGNC:HGNC:20437}; GN Synonyms=AHSA2 {ECO:0000312|HGNC:HGNC:20437}; 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 2). RA Zhang D.L., Cai J.J., Ma D.L.; RT "Cloning and characterization of a novel human gene with heat shock hsp90 RT proteins family signature and phytochrome chromophore attachment site."; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Small intestine; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). 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 IDENTIFICATION. 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 [8] RP VARIANT [LARGE SCALE ANALYSIS] THR-248. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Co-chaperone that stimulates HSP90 ATPase activity. CC {ECO:0000250|UniProtKB:Q12449}. CC -!- INTERACTION: CC Q719I0; P50222: MEOX2; NbExp=3; IntAct=EBI-9361704, EBI-748397; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q719I0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q719I0-2; Sequence=VSP_030570, VSP_030571; CC Name=3; CC IsoId=Q719I0-3; Sequence=VSP_030569; CC -!- SIMILARITY: Belongs to the AHA1 family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. {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; AF542548; AAQ09531.1; -; mRNA. DR EMBL; AK092817; BAG52613.1; -; mRNA. DR EMBL; AL833813; CAD38676.1; -; mRNA. DR EMBL; AC016747; AAY14686.1; -; Genomic_DNA. DR EMBL; CH471053; EAX00003.1; -; Genomic_DNA. DR EMBL; CH471053; EAX00006.1; -; Genomic_DNA. DR EMBL; CH471053; EAX00008.1; -; Genomic_DNA. DR EMBL; BC113671; AAI13672.1; -; mRNA. DR EMBL; BC117278; AAI17279.1; -; mRNA. DR RefSeq; NP_001308229.1; NM_001321300.1. DR RefSeq; NP_689605.1; NM_152392.4. DR AlphaFoldDB; Q719I0; -. DR SMR; Q719I0; -. DR BioGRID; 126261; 5. DR IntAct; Q719I0; 3. DR iPTMnet; Q719I0; -. DR PhosphoSitePlus; Q719I0; -. DR BioMuta; AHSA2; -. DR DMDM; 166198353; -. DR jPOST; Q719I0; -. DR MassIVE; Q719I0; -. DR PaxDb; 9606-ENSP00000377970; -. DR PeptideAtlas; Q719I0; -. DR DNASU; 130872; -. DR UCSC; uc002sbb.4; human. [Q719I0-1] DR AGR; HGNC:20437; -. DR GeneCards; AHSA2P; -. DR HGNC; HGNC:20437; AHSA2P. DR neXtProt; NX_Q719I0; -. DR eggNOG; KOG2936; Eukaryota. DR InParanoid; Q719I0; -. DR PhylomeDB; Q719I0; -. DR PathwayCommons; Q719I0; -. DR SignaLink; Q719I0; -. DR BioGRID-ORCS; 130872; 21 hits in 1143 CRISPR screens. DR ChiTaRS; AHSA2; human. DR GenomeRNAi; 130872; -. DR Pharos; Q719I0; Tdark. DR PRO; PR:Q719I0; -. DR Proteomes; UP000005640; Unplaced. DR RNAct; Q719I0; Protein. 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:protein-folding chaperone binding; IEA:InterPro. DR GO; GO:0006457; P:protein folding; IBA:GO_Central. DR Gene3D; 3.30.530.20; -; 1. DR Gene3D; 3.15.10.20; Activator of Hsp90 ATPase Aha1, N-terminal domain; 1. DR InterPro; IPR036338; Aha1. DR InterPro; IPR015310; AHSA1-like_N. DR InterPro; IPR023393; START-like_dom_sf. DR PANTHER; PTHR13009:SF4; ACTIVATOR OF 90 KDA HEAT SHOCK PROTEIN ATPASE HOMOLOG 2-RELATED; 1. DR PANTHER; PTHR13009; HEAT SHOCK PROTEIN 90 HSP90 CO-CHAPERONE AHA-1; 1. DR Pfam; PF09229; Aha1_N; 1. DR SMART; SM01000; Aha1_N; 1. DR SUPFAM; SSF103111; Activator of Hsp90 ATPase, Aha1; 1. DR SUPFAM; SSF55961; Bet v1-like; 1. DR Genevisible; Q719I0; HS. PE 5: Uncertain; KW Alternative splicing; Chaperone; Reference proteome; Stress response. FT CHAIN 1..299 FT /note="Putative activator of 90 kDa heat shock protein FT ATPase homolog 2" FT /id="PRO_0000315605" FT VAR_SEQ 1..162 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005" FT /id="VSP_030569" FT VAR_SEQ 1..153 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_030570" FT VAR_SEQ 154..157 FT /note="ALKT -> MTLP (in isoform 2)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_030571" FT VARIANT 248 FT /note="M -> T (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_038256" SQ SEQUENCE 299 AA; 33806 MW; B34F66CAA76CF13F CRC64; MAKWGQGNPH WIVEEREDGT NVNNWRWTER DATSLSKGKF QELLVGIVVE NDAGRGEINE LKQVEGEASC SSRKGKLIFF YEWNIKLGWK GIVKESGVKH KGLIEIPNLS EENEVDDTEV SLSKKKGDGV ILKDLMKTAG TAKVREALGD YLKALKTEFT TGMILPTKAM ATQELTVKRK LSGNTLQVQA SSPVALGVRI PTVALHMMEL FDTTVEQLYS IFTVKELTNK KIIMKWRCGN WPEEHYAMVA LNFVPTLGQT ELQLKEFLSI CKEENMKFCW QKQHFEEIKG SLQLTPLNG //