AHSA2_HUMAN
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 03-AUG-2022, entry version 127.
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}.
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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 STRING; 9606.ENSP00000377970; -.
DR iPTMnet; Q719I0; -.
DR PhosphoSitePlus; Q719I0; -.
DR BioMuta; AHSA2; -.
DR DMDM; 166198353; -.
DR jPOST; Q719I0; -.
DR MassIVE; Q719I0; -.
DR PaxDb; Q719I0; -.
DR PeptideAtlas; Q719I0; -.
DR PRIDE; Q719I0; -.
DR ProteomicsDB; 68594; -. [Q719I0-1]
DR ProteomicsDB; 68595; -. [Q719I0-2]
DR ProteomicsDB; 68596; -. [Q719I0-3]
DR DNASU; 130872; -.
DR UCSC; uc002sbb.4; human. [Q719I0-1]
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; 14 hits in 1069 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 Genevisible; Q719I0; HS.
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; IPR036338; Aha1.
DR InterPro; IPR039981; AHSA-like.
DR InterPro; IPR015310; AHSA1_N.
DR InterPro; IPR023393; START-like_dom_sf.
DR PANTHER; PTHR13009; PTHR13009; 2.
DR Pfam; PF09229; Aha1_N; 1.
DR SMART; SM01000; Aha1_N; 1.
DR SUPFAM; SSF103111; SSF103111; 1.
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
