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Activator of 90 kDa heat shock protein ATPase homolog 1 (AHA1) (p38)

 AHSA1_HUMAN             Reviewed;         338 AA.
O95433; B2R9L2; B4DUR9; Q96IL6; Q9P060;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
28-MAR-2018, entry version 166.
RecName: Full=Activator of 90 kDa heat shock protein ATPase homolog 1;
Short=AHA1;
AltName: Full=p38;
Name=AHSA1; Synonyms=C14orf3; ORFNames=HSPC322;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Michaud J., Chrast R., Rossier C., Papassavas M.P., Antonarakis S.E.,
Scott H.S.;
"Isolation of a novel gene underexpressed in Down syndrome.";
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Adrenal gland;
PubMed=10931946; DOI=10.1073/pnas.160270997;
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
"Gene expression profiling in the human hypothalamus-pituitary-adrenal
axis and full-length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, and Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 67-338 (ISOFORM 1).
TISSUE=Umbilical cord blood;
PubMed=11042152; DOI=10.1101/gr.140200;
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for
300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[8]
INTERACTION WITH VSV G, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=11554768; DOI=10.1006/bbrc.2001.5621;
Sevier C.S., Machamer C.E.;
"p38: a novel protein that associates with the vesicular stomatitis
virus glycoprotein.";
Biochem. Biophys. Res. Commun. 287:574-582(2001).
[9]
INTERACTION WITH HSPCA, IDENTIFICATION BY MASS SPECTROMETRY, AND
INDUCTION.
PubMed=12504007; DOI=10.1016/S1097-2765(02)00785-2;
Panaretou B., Siligardi G., Meyer P., Maloney A., Sullivan J.K.,
Singh S., Millson S.H., Clarke P.A., Naaby-Hansen S., Stein R.,
Cramer R., Mollapour M., Workman P., Piper P.W., Pearl L.H.,
Prodromou C.;
"Activation of the ATPase activity of hsp90 by the stress-regulated
cochaperone aha1.";
Mol. Cell 10:1307-1318(2002).
[10]
INTERACTION WITH HSPCA.
PubMed=12604615; DOI=10.1074/jbc.M212761200;
Lotz G.P., Lin H., Harst A., Obermann W.M.J.;
"Aha1 binds to the middle domain of Hsp90, contributes to client
protein activation, and stimulates the ATPase activity of the
molecular chaperone.";
J. Biol. Chem. 278:17228-17235(2003).
[11]
INTERACTION WITH GCH1.
PubMed=16696853; DOI=10.1111/j.1471-4159.2006.03836.x;
Swick L., Kapatos G.;
"A yeast 2-hybrid analysis of human GTP cyclohydrolase I protein
interactions.";
J. Neurochem. 97:1447-1455(2006).
[12]
INTERACTION WITH SRPK1.
PubMed=19240134; DOI=10.1101/gad.1752109;
Zhong X.Y., Ding J.H., Adams J.A., Ghosh G., Fu X.D.;
"Regulation of SR protein phosphorylation and alternative splicing by
modulating kinetic interactions of SRPK1 with molecular chaperones.";
Genes Dev. 23:482-495(2009).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3 AND LYS-212, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-182, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[20]
FUNCTION, AND INTERACTION WITH FLCN AND HSP90AA1.
PubMed=27353360; DOI=10.1038/ncomms12037;
Woodford M.R., Dunn D.M., Blanden A.R., Capriotti D., Loiselle D.,
Prodromou C., Panaretou B., Hughes P.F., Smith A., Ackerman W.,
Haystead T.A., Loh S.N., Bourboulia D., Schmidt L.S.,
Marston Linehan W., Bratslavsky G., Mollapour M.;
"The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and
enhance drug binding.";
Nat. Commun. 7:12037-12037(2016).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-203, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[22]
STRUCTURE BY NMR OF 204-335.
RIKEN structural genomics initiative (RSGI);
"The solution structure of the C-terminal domain of human activator of
90 kDa heat shock protein ATPase homolog 1.";
Submitted (NOV-2005) to the PDB data bank.
-!- FUNCTION: Acts as a co-chaperone of HSP90AA1. Activates the ATPase
activity of HSP90AA1 leading to increase in its chaperone
activity. Competes with the inhibitory co-chaperone FNIP1 for
binding to HSP90AA1, thereby providing a reciprocal regulatory
mechanism for chaperoning of client proteins (PubMed:27353360).
{ECO:0000269|PubMed:27353360}.
-!- SUBUNIT: Interacts with HSPCA/HSP90 and with the cytoplasmic tail
of the vesicular stomatitis virus glycoprotein (VSV G). Interacts
with GCH1. Interacts with SRPK1. Interacts with FLCN
(PubMed:27353360). Interacts with HSP90AA1; the interaction
activates HSP90AA1 ATPase activity (PubMed:27353360). Interacts
with HSP90AB1 (By similarity). {ECO:0000250|UniProtKB:Q8BK64,
ECO:0000269|PubMed:11554768, ECO:0000269|PubMed:12504007,
ECO:0000269|PubMed:12604615, ECO:0000269|PubMed:16696853,
ECO:0000269|PubMed:19240134, ECO:0000269|PubMed:27353360}.
-!- INTERACTION:
P30793:GCH1; NbExp=3; IntAct=EBI-448610, EBI-958183;
P07900:HSP90AA1; NbExp=4; IntAct=EBI-448610, EBI-296047;
P08238:HSP90AB1; NbExp=3; IntAct=EBI-448610, EBI-352572;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:11554768}. Endoplasmic reticulum
{ECO:0000269|PubMed:11554768}. Note=May transiently interact with
the endoplasmic reticulum.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O95433-1; Sequence=Displayed;
Name=2;
IsoId=O95433-2; Sequence=VSP_055797;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in numerous tissues, including
brain, heart, skeletal muscle and kidney and, at lower levels,
liver and placenta. {ECO:0000269|PubMed:11554768}.
-!- INDUCTION: By heat shock and treatment with the HSP90 inhibitor
17-demethoxygeldanamycin (17AAG). {ECO:0000269|PubMed:12504007}.
-!- SIMILARITY: Belongs to the AHA1 family. {ECO:0000305}.
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EMBL; AJ243310; CAB45684.1; -; mRNA.
EMBL; AF164791; AAF80755.1; -; mRNA.
EMBL; AK300766; BAG62431.1; -; mRNA.
EMBL; AK313824; BAG36559.1; -; mRNA.
EMBL; AF111168; AAD09623.1; -; Genomic_DNA.
EMBL; CH471061; EAW81291.1; -; Genomic_DNA.
EMBL; BC000321; AAH00321.1; -; mRNA.
EMBL; BC007398; AAH07398.2; -; mRNA.
EMBL; AF161440; AAF29000.1; -; mRNA.
CCDS; CCDS9863.1; -. [O95433-1]
PIR; JC7769; JC7769.
RefSeq; NP_001308370.1; NM_001321441.1.
RefSeq; NP_036243.1; NM_012111.2. [O95433-1]
UniGene; Hs.204041; -.
PDB; 1X53; NMR; -; A=204-335.
PDBsum; 1X53; -.
ProteinModelPortal; O95433; -.
SMR; O95433; -.
BioGrid; 115846; 175.
IntAct; O95433; 38.
MINT; O95433; -.
STRING; 9606.ENSP00000216479; -.
ChEMBL; CHEMBL3309113; -.
iPTMnet; O95433; -.
PhosphoSitePlus; O95433; -.
SwissPalm; O95433; -.
BioMuta; AHSA1; -.
REPRODUCTION-2DPAGE; IPI00030706; -.
EPD; O95433; -.
MaxQB; O95433; -.
PaxDb; O95433; -.
PeptideAtlas; O95433; -.
PRIDE; O95433; -.
Ensembl; ENST00000216479; ENSP00000216479; ENSG00000100591. [O95433-1]
Ensembl; ENST00000535854; ENSP00000440108; ENSG00000100591. [O95433-2]
GeneID; 10598; -.
KEGG; hsa:10598; -.
UCSC; uc001xtw.4; human. [O95433-1]
CTD; 10598; -.
DisGeNET; 10598; -.
EuPathDB; HostDB:ENSG00000100591.7; -.
GeneCards; AHSA1; -.
HGNC; HGNC:1189; AHSA1.
HPA; CAB006244; -.
HPA; HPA000903; -.
MIM; 608466; gene.
neXtProt; NX_O95433; -.
OpenTargets; ENSG00000100591; -.
PharmGKB; PA25515; -.
eggNOG; KOG2936; Eukaryota.
eggNOG; COG5580; LUCA.
GeneTree; ENSGT00390000006429; -.
HOGENOM; HOG000242852; -.
HOVERGEN; HBG065806; -.
InParanoid; O95433; -.
OMA; EYYVRSI; -.
OrthoDB; EOG091G0BRP; -.
PhylomeDB; O95433; -.
TreeFam; TF313680; -.
SIGNOR; O95433; -.
ChiTaRS; AHSA1; human.
EvolutionaryTrace; O95433; -.
GeneWiki; AHSA1; -.
GenomeRNAi; 10598; -.
PRO; PR:O95433; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000100591; -.
CleanEx; HS_AHSA1; -.
ExpressionAtlas; O95433; baseline and differential.
Genevisible; O95433; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0001671; F:ATPase activator activity; IDA:UniProtKB.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0051087; F:chaperone binding; IDA:UniProtKB.
GO; GO:0006950; P:response to stress; IEA:InterPro.
Gene3D; 3.15.10.20; -; 1.
Gene3D; 3.30.530.20; -; 1.
InterPro; IPR013538; Activator_of_Hsp90_ATPase.
InterPro; IPR036338; Aha1.
InterPro; IPR015310; AHSA1_N.
InterPro; IPR023393; START-like_dom_sf.
Pfam; PF09229; Aha1_N; 1.
Pfam; PF08327; AHSA1; 1.
SMART; SM01000; Aha1_N; 1.
SUPFAM; SSF103111; SSF103111; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Chaperone;
Complete proteome; Cytoplasm; Endoplasmic reticulum; Isopeptide bond;
Phosphoprotein; Reference proteome; Stress response; Ubl conjugation.
CHAIN 1 338 Activator of 90 kDa heat shock protein
ATPase homolog 1.
/FTId=PRO_0000215820.
MOD_RES 3 3 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 193 193 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 212 212 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 258 258 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 182 182 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 203 203 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 283 338 HFATITLTFIDKNGETELCMEGRGIPAPEEERTRQGWQRYY
FEGIKQTFGYGARLF -> SHCHSG (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055797.
CONFLICT 67 68 EA -> CL (in Ref. 7; AAF29000).
{ECO:0000305}.
STRAND 206 217 {ECO:0000244|PDB:1X53}.
HELIX 219 225 {ECO:0000244|PDB:1X53}.
HELIX 229 235 {ECO:0000244|PDB:1X53}.
TURN 253 256 {ECO:0000244|PDB:1X53}.
STRAND 261 265 {ECO:0000244|PDB:1X53}.
TURN 266 268 {ECO:0000244|PDB:1X53}.
STRAND 269 276 {ECO:0000244|PDB:1X53}.
STRAND 285 290 {ECO:0000244|PDB:1X53}.
STRAND 298 308 {ECO:0000244|PDB:1X53}.
HELIX 309 317 {ECO:0000244|PDB:1X53}.
TURN 318 323 {ECO:0000244|PDB:1X53}.
HELIX 324 330 {ECO:0000244|PDB:1X53}.
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


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AHSA1-322H Protein: Recombinant Human AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (yeast) 20ug
CSB-EL001483HU Human AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (yeast) (AHSA1) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL001484BO Bovine AHA1, activator of heat shock 90kDa protein ATPase homolog 2 (yeast) (AHSA2) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
CSB-EL001484HU Human AHA1, activator of heat shock 90kDa protein ATPase homolog 2 (yeast) (AHSA2) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL001483MO Mouse AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (yeast) (AHSA1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL001484MO Mouse AHA1, activator of heat shock 90kDa protein ATPase homolog 2 (yeast) (AHSA2) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-PA001483GA01HU Rabbit anti-human AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (yeast) polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
CSB-PA001483GA01HU Rabbit anti-human AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (yeast) polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul
AHA0701 Heat shock proteins (Chaperonins): Activator of Hsp90 ATPase-1 (AHA1, 19-337), Human, E.coli 100ug
AHA0701 Heat shock proteins (Chaperonins): Activator of Hsp90 ATPase-1 (AHA1, 19-337), Human, E.coli 0.5mg
CSB-RP054544h Recombinant human Activator of 90 kDa heat shock protein ATPase homolog 1 500ug
CSB-RP054554h Recombinant human Activator of 90 kDa heat shock protein ATPase homolog 1 500ug
CSB-EL001484HU Human Activator of 90 kDa heat shock protein ATPase homolog 2(AHSA2) ELISA kit 96T
15-1060-1 Polyclonal antibody Anti-Activator of 90 kDa heat shock protein ATPase homolog 1 100
CSB-EL001483MO Mouse Activator of 90 kDa heat shock protein ATPase homolog 1(AHSA1) ELISA kit 96T
CSB-EL001484BO Bovine Activator of 90 kDa heat shock protein ATPase homolog 2(AHSA2) ELISA kit 96T
CSB-EL001483HU Human Activator of 90 kDa heat shock protein ATPase homolog 1(AHSA1) ELISA kit 96T
CSB-EL001484MO Mouse Activator of 90 kDa heat shock protein ATPase homolog 2(AHSA2) ELISA kit 96T
CSB-RP054554h Recombinant human Activator of 90 kDa heat shock protein ATPase homolog 1 Source: E.coli 200ug
CSB-EL001484MO Mouse Activator of 90 kDa heat shock protein ATPase homolog 2(AHSA2) ELISA kit SpeciesMouse 96T
CSB-RP054544h Recombinant human Activator of 90 kDa heat shock protein ATPase homolog 1 Source: E.coli 1mg


 

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