[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0378-1119(87)90012-6; PubMed=3301534 [NCBI, ExPASy, EBI, Israel, Japan] Rebbe N.F., Ware J., Bertina R.M., Modrich P., Stafford D.W.; "Nucleotide sequence of a cDNA for a member of the human 90-kDa heat-shock protein family."; Gene 53:235-245(1987).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2768249 [NCBI, ExPASy, EBI, Israel, Japan] Rebbe N.F., Hickman W.S., Ley T.J., Stafford D.W., Hickman S.; "Nucleotide sequence and regulation of a human 90-kDa heat shock protein gene."; J. Biol. Chem. 264:15006-15011(1989).
[3]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0378-1119(88)90182-5; PubMed=2469626 [NCBI, ExPASy, EBI, Israel, Japan] Hoffmann T., Hovemann B.; "Heat-shock proteins, Hsp84 and Hsp86, of mice and men: two related genes encode formerly identified tumour-specific transplantation antigens."; Gene 74:491-501(1988).
[4]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Testis; Lu L., Huang X.Y., Yin L.L., Xu M., Li J.M., Zhou Z.M., Sha J.H.; "Cloning a new isoform of heat shock 90kDa in testis."; Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Amygdala; DOI=10.1101/gr.GR1547R; PubMed=11230166 [NCBI, ExPASy, EBI, Israel, Japan] Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.; "Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."; Genome Res. 11:422-435(2001).
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. NHLBI resequencing and genotyping service (RS&G); Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
[7]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan] Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; "The DNA sequence and analysis of human chromosome 6."; Nature 425:805-811(2003).
[8]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Colon, Lymph, Muscle, Skin, and Testis; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[9]	NUCLEOTIDE SEQUENCE [MRNA] OF 93-724. TISSUE=Pancreas; Mason A., O'Connor D., Greenhalf W.; "Novel sequence for human Hsp90 beta giving a substitution of R55T (R147 in original sequence) and M85R (M177 in original sequence)."; Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[10]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 51-118. DOI=10.1007/BF00292342; PubMed=8180474 [NCBI, ExPASy, EBI, Israel, Japan] Takahashi I., Tanuma R., Hirata M., Hashimoto K.; "A cosmid clone at the D6S182 locus on human chromosome 6p12 contains the 90-kDa heat shock protein beta gene (HSP90 beta)."; Mamm. Genome 5:121-122(1994).
[11]	PROTEIN SEQUENCE OF 2-21, AND PHOSPHORYLATION. PubMed=2492519 [NCBI, ExPASy, EBI, Israel, Japan] Lees-Miller S.P., Anderson C.W.; "Two human 90-kDa heat shock proteins are phosphorylated in vivo at conserved serines that are phosphorylated in vitro by casein kinase II."; J. Biol. Chem. 264:2431-2437(1989).
[12]	PROTEIN SEQUENCE OF 54-64 AND 187-199. TISSUE=Colon carcinoma; DOI=10.1002/elps.1150180344; PubMed=9150948 [NCBI, ExPASy, EBI, Israel, Japan] Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.; "A two-dimensional gel database of human colon carcinoma proteins."; Electrophoresis 18:605-613(1997).
[13]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 AND SER-261, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan] Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.; "Large-scale characterization of HeLa cell nuclear phosphoproteins."; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[14]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-484, AND MASS SPECTROMETRY. DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan] Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.; "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; Nat. Biotechnol. 23:94-101(2005).
[15]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND MASS SPECTROMETRY. TISSUE=Brain cortex; DOI=10.1021/pr0498436; PubMed=15822905 [NCBI, ExPASy, EBI, Israel, Japan] DeGiorgis J.A., Jaffe H., Moreira J.E., Carlotti C.G. Jr., Leite J.P., Pant H.C., Dosemeci A.; "Phosphoproteomic analysis of synaptosomes from human cerebral cortex."; J. Proteome Res. 4:306-315(2005).
[16]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND MASS SPECTROMETRY. TISSUE=T-cell; DOI=10.1038/nmeth776; PubMed=16094384 [NCBI, ExPASy, EBI, Israel, Japan] Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R.; "Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry."; Nat. Methods 2:591-598(2005).
[17]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-255, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."; Cell 127:635-648(2006).
[18]	SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. DOI=10.1021/pr060363j; PubMed=17081065 [NCBI, ExPASy, EBI, Israel, Japan] Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.; "Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."; J. Proteome Res. 5:3135-3144(2006).
[19]	ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-624, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.molcel.2006.06.026; PubMed=16916647 [NCBI, ExPASy, EBI, Israel, Japan] Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; "Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."; Mol. Cell 23:607-618(2006).
[20]	FUNCTION, AND INTERACTION WITH UNC45A. DOI=10.1128/MCB.26.5.1722-1730.2006; PubMed=16478993 [NCBI, ExPASy, EBI, Israel, Japan] Chadli A., Graham J.D., Abel M.G., Jackson T.A., Gordon D.F., Wood W.M., Felts S.J., Horwitz K.B., Toft D.; "GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway."; Mol. Cell. Biol. 26:1722-1730(2006).
[21]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-255 AND SER-261, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan] Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."; Nat. Biotechnol. 24:1285-1292(2006).
[22]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1073/pnas.0507066103; PubMed=16565220 [NCBI, ExPASy, EBI, Israel, Japan] Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; "Phosphoproteome analysis of the human mitotic spindle."; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
[23]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-484, AND MASS SPECTROMETRY. DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan] Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; "Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."; Cell 131:1190-1203(2007).
[24]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND MASS SPECTROMETRY. DOI=10.1002/elps.200600782; PubMed=17487921 [NCBI, ExPASy, EBI, Israel, Japan] Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."; Electrophoresis 28:2027-2034(2007).
[25]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-297, AND MASS SPECTROMETRY. DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan] Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."; Science 316:1160-1166(2007).
[26]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-255, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan] Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; "Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[27]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-255, AND MASS SPECTROMETRY. TISSUE=Platelet; DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan] Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.; "Phosphoproteome of resting human platelets."; J. Proteome Res. 7:526-534(2008).
[28]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-255, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1002/pmic.200700884; PubMed=18318008 [NCBI, ExPASy, EBI, Israel, Japan] Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.; "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."; Proteomics 8:1346-1361(2008).
[29]	X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1-221 IN COMPLEX WITH PURINE ANALOG. DOI=10.1016/j.chembiol.2004.03.033; PubMed=15217611 [NCBI, ExPASy, EBI, Israel, Japan] Wright L., Barril X., Dymock B., Sheridan L., Surgenor A., Beswick M., Drysdale M., Collier A., Massey A., Davies N., Fink A., Fromont C., Aherne W., Boxall K., Sharp S., Workman P., Hubbard R.E.; "Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms."; Chem. Biol. 11:775-785(2004).

Comments

FUNCTION: Molecular chaperone. Has ATPase activity.
SUBUNIT: Homodimer. Interacts with TP53/p53 (By similarity). Interacts with UNC45A. Binding to UNC45A involves 2 UNC45A monomers per HSP90AB1 dimer.
INTERACTION:
O14757:CHEK1; NbExp=1; IntAct=EBI-352572, EBI-974488;
P04049:RAF1; NbExp=1; IntAct=EBI-352572, EBI-365996;
SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
SIMILARITY: Belongs to the heat shock protein 90 family.
SEQUENCE CAUTION:
- Sequence=CAB66478.1; Type=Frameshift; Positions=709;

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M16660; AAA36025.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J04988; AAA36026.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY359878; AAQ63401.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136543; CAB66478.1; ALT_FRAME; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ314872; ABC40731.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL139392; CAI20095.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC004928; AAH04928.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC009206; AAH09206.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012807; AAH12807.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC014485; AAH14485.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC016753; AAH16753.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC068474; AAH68474.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF275719; AAF82792.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S70561; AAD14062.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A29461; HHHU84.
T46243; T46243.

RefSeq

NP_031381.2; -.

UniGene

Hs.509736

3D structure databases

PDB

1QZ2; X-ray; 3.00 A; G/H=720-724.	[ExPASy / RCSB / EBI]
1UYM; X-ray; 2.45 A; A=1-221.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1QZ2; -.
1UYM; -.

ModBase

P08238.

Protein-protein interaction databases

DIP

DIP:413N; -.

IntAct

P08238; -.

PTM databases

PhosphoSite

P08238; -.

2D gel databases

HSC-2DPAGE

P08238; -.

OGP

P08238; -.

Organism-specific databases

H-InvDB

HIX0005922; -.
HIX0059399; -.

HGNC:5258; HSP90AB1.

CAB005230; -.

140572; gene. [NCBI / EBI]

GeneCards

P08238.

Gene expression databases

CleanEx

HS_HSP90AB1; -.

GermOnline

ENSG00000096384; Homo sapiens.

Ontologies

GO:0005737;	Cellular component: cytoplasm (non-traceable author statement from UniProtKB).
GO:0030235;	Molecular function: nitric-oxide synthase regulator activity (inferred from sequence or structural similarity from UniProtKB).
GO:0030911;	Molecular function: TPR domain binding (inferred from sequence or structural similarity from UniProtKB).
GO:0045429;	Biological process: positive regulation of nitric oxide biosynthetic process (inferred from sequence or structural similarity from UniProtKB).
GO:0006986;	Biological process: response to unfolded protein (non-traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR003594; ATP_bd_ATPase.
IPR001404; Hsp90.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.565.10; ATP_bd_ATPase; 1.

PANTHER

PTHR11528; Hsp90; 1.

Pfam

PF02518; HATPase_c; 1.
PF00183; HSP90; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF002583; Hsp90; 1.

PRINTS

PR00775; HEATSHOCK90.

SMART

SM00387; HATPase_c; 1.
SMART graphical view of domain structure.

PS00298; HSP90; 1.

Proteomic databases

P08238; -.

Genome annotation databases

Ensembl

ENSG00000096384; Homo sapiens. [Contig view]

GeneID

3326; -.

KEGG

hsa:3326; -.

NMPDR

fig|9606.3.peg.27233; -.

Phylogenomic databases

HOVERGEN

P08238; -.

Other

LinkHub

P08238; -.

NextBio

13182; -.

SOURCE

HSP90AB1; Homo sapiens.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing; Nucleotide-binding; Phosphoprotein; Stress response.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 724`	`723`	`Heat shock protein HSP 90-beta.`	`PRO_0000062917`
`MOD_RES`	`226 226`		`Phosphoserine.`
`MOD_RES`	`255 255`		`Phosphoserine.`
`MOD_RES`	`261 261`		`Phosphoserine.`
`MOD_RES`	`297 297`		`Phosphothreonine.`
`MOD_RES`	`305 305`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`484 484`		`Phosphotyrosine.`
`MOD_RES`	`624 624`		`N6-acetyllysine.`
`CONFLICT`	`147 147`		`T -> R (in Ref. 1; AAA36025).`
`CONFLICT`	`177 177`		`R -> M (in Ref. 1; AAA36025).`
`CONFLICT`	`403 403`		`V -> A (in Ref. 5; CAB66478).`
`STRAND`	`13 16`	`4`
`HELIX`	`19 30`	`12`
`HELIX`	`38 57`	`20`
`TURN`	`58 60`	`3`
`HELIX`	`62 65`	`4`
`STRAND`	`73 78`	`6`
`TURN`	`79 82`	`4`
`STRAND`	`83 88`	`6`
`HELIX`	`95 99`	`5`
`HELIX`	`101 117`	`17`
`TURN`	`118 120`	`3`
`HELIX`	`123 129`	`7`
`HELIX`	`132 138`	`7`
`STRAND`	`140 148`	`9`
`STRAND`	`155 159`	`5`
`STRAND`	`164 169`	`6`
`STRAND`	`176 185`	`10`
`HELIX`	`187 193`	`7`
`HELIX`	`195 205`	`11`
`STRAND`	`213 215`	`3`

Sequence information

Length: 724 AA [This is the length of the unprocessed precursor]

Molecular weight: 83264 Da [This is the MW of the unprocessed precursor]

CRC64: A93118C214D03810 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPEEVHHGEE EVETFAFQAE IAQLMSLIIN TFYSNKEIFL RELISNASDA LDKIRYESLT 

        70         80         90        100        110        120 
DPSKLDSGKE LKIDIIPNPQ ERTLTLVDTG IGMTKADLIN NLGTIAKSGT KAFMEALQAG 

       130        140        150        160        170        180 
ADISMIGQFG VGFYSAYLVA EKVVVITKHN DDEQYAWESS AGGSFTVRAD HGEPIGRGTK 

       190        200        210        220        230        240 
VILHLKEDQT EYLEERRVKE VVKKHSQFIG YPITLYLEKE REKEISDDEA EEEKGEKEEE 

       250        260        270        280        290        300 
DKDDEEKPKI EDVGSDEEDD SGKDKKKKTK KIKEKYIDQE ELNKTKPIWT RNPDDITQEE 

       310        320        330        340        350        360 
YGEFYKSLTN DWEDHLAVKH FSVEGQLEFR ALLFIPRRAP FDLFENKKKK NNIKLYVRRV 

       370        380        390        400        410        420 
FIMDSCDELI PEYLNFIRGV VDSEDLPLNI SREMLQQSKI LKVIRKNIVK KCLELFSELA 

       430        440        450        460        470        480 
EDKENYKKFY EAFSKNLKLG IHEDSTNRRR LSELLRYHTS QSGDEMTSLS EYVSRMKETQ 

       490        500        510        520        530        540 
KSIYYITGES KEQVANSAFV ERVRKRGFEV VYMTEPIDEY CVQQLKEFDG KSLVSVTKEG 

       550        560        570        580        590        600 
LELPEDEEEK KKMEESKAKF ENLCKLMKEI LDKKVEKVTI SNRLVSSPCC IVTSTYGWTA 

       610        620        630        640        650        660 
NMERIMKAQA LRDNSTMGYM MAKKHLEINP DHPIVETLRQ KAEADKNDKA VKDLVVLLFE 

       670        680        690        700        710        720 
TALLSSGFSL EDPQTHSNRI YRMIKLGLGI DEDEVAAEEP NAAVPDEIPP LEGDEDASRM 


EEVD

P08238 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools

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