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Homo sapiens heat shock protein 90kDa alpha (cytosolic), class A member 1 (HSP90AA1), transcript variant 1, mRNA.


RefSeq Accession Definition Sequence Price Select
NM_001017963 Homo sapiens heat shock protein 90kDa alpha (cytosolic), class A member 1 (HSP90AA1), transcript variant 1, mRNA. Full Lenth $1360.45
ORF Sequence $743.85


RefSeq Version NM_001017963.2, 153792589
Length 3887 bp
Structure linear
Update Date 10-APR-2011
Organism Homo sapiens (human)
Definition Homo sapiens heat shock protein 90kDa alpha (cytosolic), class A member 1 (HSP90AA1), transcript variant 1, mRNA.
Product heat shock protein HSP 90-alpha isoform 1
Comment

Summary: HSP90 proteins are highly conserved molecular chaperones that have key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90 proteins normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress. There are 2 major cytosolic HSP90 proteins, HSP90AA1, an inducible form, and HSP90AB1 (MIM 140572), a constitutive form. Other HSP90 proteins are found in endoplasmic reticulum (HSP90B1; MIM 191175) and mitochondria (TRAP1; MIM 606219) (Chen et al., 2005 [PubMed 16269234]).[supplied by OMIM].


Transcript Variant: This variant (1) represents the longer transcript and encodes the longer isoform (1).

RefSeq NP_001017963.2
CDS 346..2910
Exon (1)1..500
Exon (2)1..500
Exon (3)501..711
Exon (4)712..873
Exon (5)874..1240
Exon (6)1241..1374
Exon (7)1375..1692
Exon (8)1693..1858
Exon (9)1859..2049
Exon (10)2050..2197
Exon (11)2198..2466
Exon (12)2467..2800
Exon (13)2801..3884
Translation MPPCSGGDGSTPPGPSLRDRDCPAQSAEYPRDRLDPRPGSPSEASSPPFLRSRAPVNWYQ EKAQVFLWHLMVSGSTTLLCLWKQPFHVSAFPVTASLAFRQSQGAGQHLYKDLQPFILLR LLMPEETQTQDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDK IRYESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAF MEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGE PMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAEEK EDKEEEKEKEEKESEDKPEIEDVGSDEEEEKKDGDKKKKKKIKEKYIDQEELNKTKPIWT RNPDDITNEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENRKKK NNIKLYVRRVFIMDNCEELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNLVK KCLELFTELAEDKENYKKFYEQFSKNIKLGIHEDSQNRKKLSELLRYYTSASGDEMVSLK DYCTRMKENQKHIYYITGETKDQVANSAFVERLRKHGLEVIYMIEPIDEYCVQQLKEFEG KTLVSVTKEGLELPEDEEEKKKQEEKKTKFENLCKIMKDILEKKVEKVVVSNRLVTSPCC IVTSTYGWTANMERIMKAQALRDNSTMGYMAAKKHLEINPDHSIIETLRQKAEADKNDKS VKDLVILLYETALLSSGFSLEDPQTHANRIYRMIKLGLGIDEDDPTADDTSAAVTEEMPP LEGDDDTSRMEEVD
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Position Chain Variation Link
complement(63)-g, adbSNP:113602506
complement(175)-g, cdbSNP:116641992
179+c, tdbSNP:35538974
complement(287)-g, cdbSNP:78436885
complement(445)-g, adbSNP:41285492
complement(556)-t, adbSNP:8005905
complement(627)-g, adbSNP:10873531
complement(664)-g, adbSNP:61744640
665+a, gdbSNP:35446359
771+a, cdbSNP:11547538
792+a, cdbSNP:11547539
complement(836)-t, cdbSNP:56030286
complement(840)-g, adbSNP:116476189
844+c, tdbSNP:11547522
872+a, gdbSNP:11547527
complement(872)-t, cdbSNP:112990598
complement(888)-g, adbSNP:116285249
930+a, gdbSNP:11547540
966+a, gdbSNP:11547530
1101+g, tdbSNP:11547537
complement(1203)-g, adbSNP:115674612
complement(1229)-t, cdbSNP:115967466
complement(1248)-g, adbSNP:11547541
complement(1287)-t, gdbSNP:78712166
1289+a, cdbSNP:1801329
complement(1432..1434)-, tttdbSNP:3832931
1441+a, gdbSNP:3208444
1447+a, gdbSNP:3208445
complement(1448)-t, cdbSNP:55783428
1502+a, cdbSNP:11547519
complement(1547)-t, adbSNP:55793809
complement(1614)-g, adbSNP:112394273
complement(1627)-t, gdbSNP:115457506
complement(1638)-g, adbSNP:115513913
1645+c, tdbSNP:11547515
complement(1647)-g, adbSNP:115566847
complement(1686)-t, cdbSNP:115927657
1705+g, tdbSNP:11547514
1755+c, tdbSNP:11547518
1791+c, tdbSNP:4947
complement(1884)-t, cdbSNP:113508244
complement(1995)-t, cdbSNP:113261380
2090+c, tdbSNP:11547529
2097+a, gdbSNP:34913441
complement(2112)-t, cdbSNP:114259343
2273+a, tdbSNP:11547543
complement(2376)-t, adbSNP:75630701
2421+c, tdbSNP:36078484
complement(2468)-g, adbSNP:114789230
2545+a, cdbSNP:34644998
2561+a, tdbSNP:11547512
2586+a, gdbSNP:11547532
2622+a, cdbSNP:61733529
complement(2628)-g, adbSNP:113093780
2703+c, tdbSNP:35598057
2733+c, tdbSNP:11547513
complement(2740)-t, gdbSNP:112366202
2763+c, tdbSNP:36025350
2764+g, tdbSNP:11547536
complement(2778)-g, adbSNP:114622252
2790+a, gdbSNP:11547524
complement(2800)-t, cdbSNP:56205516
2808+c, tdbSNP:11547523
complement(2880)-g, adbSNP:61999351
complement(2951)-t, cdbSNP:112417493
2953+g, tdbSNP:35798224
complement(3032)-t, adbSNP:116145388
3050+c, tdbSNP:1802096
complement(3120)-g, adbSNP:55980776
3185..3186+, tgdbSNP:35997255
complement(3186..3187)-, cadbSNP:72520876
complement(3188..3189)-, acdbSNP:113020563
3189..3190+, tgdbSNP:3831488
3204+c, gdbSNP:11547511
3214+c, tdbSNP:2298878
complement(3247)-t, gdbSNP:115690563
complement(3311)-g, adbSNP:112268853
3311+c, tdbSNP:1058078
3357+c, tdbSNP:11547531
3471+a, gdbSNP:35754658
complement(3498)-g, adbSNP:11547545
3586+a, cdbSNP:34287031
3625..3628+, agttdbSNP:34767631
complement(3654)-t, cdbSNP:115514898
3741+c, tdbSNP:1059623
complement(3818)-g, adbSNP:114412854
3854+c, tdbSNP:1059629
Gene SymbolHSP90AA1
Gene SynonymFLJ31884; HSP86; Hsp89; HSP89A; Hsp90; HSP90A; HSP90N; HSPC1; HSPCA; HSPCAL1; HSPCAL4; HSPN; LAP2
Chromosome14
Locus Map14q32.33
All Transcripts NM_001017963 , NM_005348
Title HSP90 is crucial for regulation of LAT expression in activated T cells .
Author Hayashi,K. and Kamikawa,Y.
Journal Mol. Immunol. 48 (6-7), 941-946 (2011)
Title Heat shock protein 90 facilitates formation of the HBV capsid via interacting with the HBV core protein dimers .
Author Shim,H.Y., Quan,X., Yi,Y.S. and Jung,G.
Journal Virology 410 (1), 161-169 (2011)
Title N-terminal domain of human Hsp90 triggers binding to the cochaperone p23 .
Author Karagoz,G.E., Duarte,A.M., Ippel,H., Uetrecht,C., Sinnige,T., van Rosmalen,M., Hausmann,J., Heck,A.J., Boelens,R. and Rudiger,S.G.
Journal Proc. Natl. Acad. Sci. U.S.A. 108 (2), 580-585 (2011)
Title Gyrase B inhibitor impairs HIV-1 replication by targeting Hsp90 and the capsid protein .
Author Vozzolo,L., Loh,B., Gane,P.J., Tribak,M., Zhou,L., Anderson,I., Nyakatura,E., Jenner,R.G., Selwood,D. and Fassati,A.
Journal J. Biol. Chem. 285 (50), 39314-39328 (2010)
Title Activating transcription factor-3 (ATF3) functions as a tumor suppressor in colon cancer and is up-regulated upon heat-shock protein 90 (Hsp90) inhibition .
Author Hackl,C., Lang,S.A., Moser,C., Mori,A., Fichtner-Feigl,S., Hellerbrand,C., Dietmeier,W., Schlitt,H.J., Geissler,E.K. and Stoeltzing,O.
Journal BMC Cancer 10, 668 (2010)
Title Conformational activation of a basic helix-loop-helix protein (MyoD1) by the C-terminal region of murine HSP90 (HSP84) .
Author Shaknovich,R., Shue,G. and Kohtz,D.S.
Journal Mol. Cell. Biol. 12 (11), 5059-5068 (1992)
Title Association of the 90-kDa heat shock protein does not affect the ligand-binding ability of androgen receptor .
Author Nemoto,T., Ohara-Nemoto,Y. and Ota,M.
Journal J. Steroid Biochem. Mol. Biol. 42 (8), 803-812 (1992)
Title Reconstitution of the multiprotein complex of pp60src, hsp90, and p50 in a cell-free system .
Author Hutchison,K.A., Brott,B.K., De Leon,J.H., Perdew,G.H., Jove,R. and Pratt,W.B.
Journal J. Biol. Chem. 267 (5), 2902-2908 (1992)
Title Mapping of the gene family for human heat-shock protein 90 alpha to chromosomes 1, 4, 11, and 14 .
Author Ozawa,K., Murakami,Y., Eki,T., Soeda,E. and Yokoyama,K.
Journal Genomics 12 (2), 214-220 (1992)
Title Molecular cloning of cDNA encoding a human heat-shock protein whose expression is induced by adenovirus type 12 E1A in HeLa cells .
Author Yamazaki,M., Tashiro,H., Yokoyama,K. and Soeda,E.
Journal Agric. Biol. Chem. 54 (12), 3163-3170 (1990)

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