[1]	NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. TISSUE=Testis; DOI=10.1006/bbrc.1999.0897; PubMed=10381378 [NCBI, ExPASy, EBI, Israel, Japan] Frye R.A.; "Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity."; Biochem. Biophys. Res. Commun. 260:273-279(1999).
[2]	NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH HES1 AND HEY2, AND MUTAGENESIS OF HIS-363. DOI=10.1016/S0006-291X(02)03020-6; PubMed=12535671 [NCBI, ExPASy, EBI, Israel, Japan] Takata T., Ishikawa F.; "Human Sir2-related protein SIRT1 associates with the bHLH repressors HES1 and HEY2 and is involved in HES1- and HEY2-mediated transcriptional repression."; Biochem. Biophys. Res. Commun. 301:250-257(2003).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-3. NIEHS SNPs program; Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1038/nature02462; PubMed=15164054 [NCBI, ExPASy, EBI, Israel, Japan] Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; "The DNA sequence and comparative analysis of human chromosome 10."; Nature 429:375-381(2004).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 124-747. TISSUE=Prostate; 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).
[6]	FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TP53, AND MUTAGENESIS OF HIS-363. DOI=10.1016/S0092-8674(01)00527-X; PubMed=11672523 [NCBI, ExPASy, EBI, Israel, Japan] Vaziri H., Dessain S.K., Ng Eaton E., Imai S., Frye R.A., Pandita T.K., Guarente L., Weinberg R.A.; "hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase."; Cell 107:149-159(2001).
[7]	FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH PML, AND MUTAGENESIS OF HIS-363. DOI=10.1093/emboj/21.10.2383; PubMed=12006491 [NCBI, ExPASy, EBI, Israel, Japan] Langley E., Pearson M., Faretta M., Bauer U.-M., Frye R.A., Minucci S., Pelicci P.G., Kouzarides T.; "Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence."; EMBO J. 21:2383-2396(2002).
[8]	ENZYME REGULATION. DOI=10.1074/jbc.M205670200; PubMed=12297502 [NCBI, ExPASy, EBI, Israel, Japan] Bitterman K.J., Anderson R.M., Cohen H.Y., Latorre-Esteves M., Sinclair D.A.; "Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1."; J. Biol. Chem. 277:45099-45107(2002).
[9]	ENZYME REGULATION. DOI=10.1038/nature01960; PubMed=12939617 [NCBI, ExPASy, EBI, Israel, Japan] Howitz K.T., Bitterman K.J., Cohen H.Y., Lamming D.W., Lavu S., Wood J.G., Zipkin R.E., Chung P., Kisielewski A., Zhang L.-L., Scherer B., Sinclair D.A.; "Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan."; Nature 425:191-196(2003).
[10]	INTERACTION WITH MLLT7. DOI=10.1074/jbc.M401138200; PubMed=15126506 [NCBI, ExPASy, EBI, Israel, Japan] van der Horst A., Tertoolen L.G.J., de Vries-Smits L.M.M., Frye R.A., Medema R.H., Burgering B.M.T.; "FOXO4 is acetylated upon peroxide stress and deacetylated by the longevity protein hSir2(SIRT1)."; J. Biol. Chem. 279:28873-28879(2004).
[11]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-47, 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).
[12]	INTERACTION WITH HIV-1 TAT. DOI=10.1371/journal.pbio.0030041; PubMed=15719057 [NCBI, ExPASy, EBI, Israel, Japan] Pagans S., Pedal A., North B.J., Kaehlcke K., Marshall B.L., Dorr A., Hetzer-Egger C., Henklein P., Frye R., McBurney M.W., Hruby H., Jung M., Verdin E., Ott M.; "SIRT1 regulates HIV transcription via Tat deacetylation."; PLoS Biol. 3:210-220(2005).
[13]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, 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).
[14]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, 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).
[15]	INTERACTION WITH RPS19BP1. DOI=10.1016/j.molcel.2007.08.030; PubMed=17964266 [NCBI, ExPASy, EBI, Israel, Japan] Kim E.-J., Kho J.-H., Kang M.-R., Um S.-J.; "Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppression of p53 activity."; Mol. Cell 28:277-290(2007).
[16]	ERRATUM. Kim E.-J., Kho J.-H., Kang M.-R., Um S.-J.; Mol. Cell 28:513-513(2007).
[17]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan] Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; J. Proteome Res. 6:4150-4162(2007).
[18]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASS SPECTROMETRY. DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan] Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; "Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Anal. Sci. 24:161-166(2008).
[19]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND THR-719, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan] Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.; "A quantitative atlas of mitotic phosphorylation."; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[20]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.

Comments

FUNCTION: NAD-dependent deacetylase, which regulates processes such as apoptosis and muscle differentiation by deacetylating key proteins. Deacetylates 'Lys-382' of p53/TP53 and impairs its ability to induce proapoptotic program and modulate cell senescence. Deacetylates TAF1B and thereby represses rDNA transcription by the RNA polymerase I. Involved in HES1- and HEY2-mediated transcriptional repression. Inhibits skeletal muscle differentiation by deacetylating PCAF and MYOD1. May serve as a sensor of the cytosolic ratio of NAD(+)/NADH, which is essential in skeletal muscle cell differentiation. Despite some ability to deacetylate histones in vitro, such activity is either weak or inexistent in vivo. In case of HIV-1 infection, interacts with and deacetylates the viral Tat protein.
CATALYTIC ACTIVITY: NAD⁺ + an acetylprotein = nicotinamide + O-acetyl-ADP-ribose + a protein.
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
ENZYME REGULATION: Inhibited by nicotinamide. Activated by resveratrol (3,5,4'-trihydroxy-trans-stilbene), butein (3,4,2',4'-tetrahydroxychalcone), piceatannol (3,5,3',4'-tetrahydroxy-trans-stilbene), Isoliquiritigenin (4,2',4'-trihydroxychalcone), fisetin (3,7,3',4'-tetrahydroxyflavone) and quercetin (3,5,7,3',4'-pentahydroxyflavone). RPS19BP1/AROS acts as a positive regulator of deacetylation activity.
SUBUNIT: Interacts with TAF1B. Found in a complex with PCAF and MYOD1 (By similarity). Interacts with MLLT7/FOXO4, HES1, HEY2, p53/TP53 and PML. Interacts with RPS19BP1/AROS.
INTERACTION:
Q9WTL8-2:Arntl (xeno); NbExp=1; IntAct=EBI-1802965, EBI-644559;
O43159:KIAA0409; NbExp=1; IntAct=EBI-1802965, EBI-2008793;
O54943:Per2 (xeno); NbExp=1; IntAct=EBI-1802965, EBI-1266779;
SUBCELLULAR LOCATION: Nucleus. Note=Recruited to the nuclear bodies via its interaction with PML.
TISSUE SPECIFICITY: Widely expressed.
MISCELLANEOUS: Red wine, which contains resveratrol, may participate in activation of sirtuin proteins, and may therefore participate in an extended lifespan as it has been observed in yeast.
SIMILARITY: Belongs to the sirtuin family.
SIMILARITY: Contains 1 deacetylase sirtuin-type domain.
WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/sirt1/";.

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

AF083106; AAD40849.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF235040; AAG38486.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ278604; ABB72675.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133551; CAI16036.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012499; AAH12499.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00016802; -.

NP_036370.2; -.

3D structure databases

HSSP

Q8IXJ6; 1J8F. [HSSP ENTRY / PDB]

ModBase

Q96EB6.

Protein-protein interaction databases

IntAct

Q96EB6; 4.

PTM databases

PhosphoSite

Q96EB6; -.

Enzyme and pathway databases

Pathway_Interaction_DB

foxopathway; FoxO family signaling.
ar_tf_pathway; Regulation of Androgen receptor activity.
hdac_classi_pathway; Signaling events mediated by HDAC Class I.
hdac_classiii_pathway; Signaling events mediated by HDAC Class III.

Organism-specific databases

GC10P069314; -.

HIX0008867; -.

HGNC:14929; SIRT1.

CAB003855; -.
HPA006295; -.

MIM

604479; gene. [NCBI / EBI]

PharmGKB

PA37935; -.

Gene expression databases

Q96EB6; -.

Q96EB6; -.

HS_SIRT1; -.

ENSG00000096717; Homo sapiens.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from HPA).
GO:0005635;	Cellular component: nuclear envelope (inferred from direct assay from UniProtKB).
GO:0005730;	Cellular component: nucleolus (inferred from direct assay from UniProtKB).
GO:0016605;	Cellular component: PML body (inferred from direct assay from UniProtKB).
GO:0042393;	Molecular function: histone binding (inferred from physical interaction from UniProtKB).
GO:0042802;	Molecular function: identical protein binding (inferred from physical interaction from UniProtKB).
GO:0070403;	Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0017136;	Molecular function: NAD-dependent histone deacetylase activity (inferred from direct assay from UniProtKB).
GO:0002039;	Molecular function: p53 binding (inferred from physical interaction from UniProtKB).
GO:0008022;	Molecular function: protein C-terminus binding (inferred from physical interaction from UniProtKB).
GO:0019904;	Molecular function: protein domain specific binding (inferred from sequence or structural similarity from UniProtKB).
GO:0003714;	Molecular function: transcription corepressor activity (inferred from sequence or structural similarity from UniProtKB).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006915;	Biological process: apoptosis (inferred from electronic annotation from UniProtKB-KW).
GO:0007569;	Biological process: cell aging (traceable author statement from UniProtKB).
GO:0009267;	Biological process: cellular response to starvation (inferred from sequence or structural similarity from UniProtKB).
GO:0006281;	Biological process: DNA repair (traceable author statement from UniProtKB).
GO:0006260;	Biological process: DNA replication (traceable author statement from UniProtKB).
GO:0006343;	Biological process: establishment of chromatin silencing (inferred from direct assay from UniProtKB).
GO:0016575;	Biological process: histone deacetylation (inferred from direct assay from UniProtKB).
GO:0044419;	Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0006344;	Biological process: maintenance of chromatin silencing (inferred from mutant phenotype from UniProtKB).
GO:0007517;	Biological process: muscle organ development (inferred from electronic annotation from UniProtKB-KW).
GO:0043518;	Biological process: negative regulation of DNA damage response, signal transduction by p53 class mediator (inferred from direct assay from UniProtKB).
GO:0045599;	Biological process: negative regulation of fat cell differentiation (inferred from sequence or structural similarity from UniProtKB).
GO:0051097;	Biological process: negative regulation of helicase activity (inferred from direct assay from UniProtKB).
GO:0043433;	Biological process: negative regulation of transcription factor activity (inferred from direct assay from UniProtKB).
GO:0034983;	Biological process: peptidyl-lysine deacetylation (inferred from direct assay from UniProtKB).
GO:0045768;	Biological process: positive regulation of anti-apoptosis (traceable author statement from UniProtKB).
GO:0031937;	Biological process: positive regulation of chromatin silencing (inferred from mutant phenotype from UniProtKB).
GO:0042981;	Biological process: regulation of apoptosis (inferred from sequence or structural similarity from UniProtKB).
GO:0042127;	Biological process: regulation of cell proliferation (inferred from mutant phenotype from UniProtKB).
GO:0033158;	Biological process: regulation of protein import into nucleus, translocation (inferred from mutant phenotype from UniProtKB).
GO:0034339;	Biological process: regulation of transcription from RNA polymerase II promoter by nuclear hormone receptor (inferred from sequence or structural similarity from UniProtKB).
GO:0006350;	Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
GO:0006642;	Biological process: triglyceride mobilization (inferred from sequence or structural similarity from UniProtKB).
GO:0050872;	Biological process: white fat cell differentiation (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR003000; NAD-dep_histone_deAcase_SIR2.
Graphical view of domain structure.

PANTHER

PTHR11085; SIR2; 1.

Pfam

PF02146; SIR2; 1.
Pfam graphical view of domain structure.

PROSITE

PS50305; SIRTUIN; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PeptideAtlas

Q96EB6; -.

PRIDE

Q96EB6; -.

Genome annotation databases

Ensembl

ENSG00000096717; Homo sapiens. [Contig view]

GeneID

23411; -.

KEGG

hsa:23411; -.

NMPDR

fig|9606.3.peg.4026; -.

Phylogenomic databases

HOGENOM

Q96EB6; -.

HOVERGEN

Q96EB6; -.

OMA

Q96EB6; AGEPLRK.

Other

45603; -.

SIRT1; Homo sapiens.

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

Keywords

Apoptosis; Developmental protein; Differentiation; Host-virus interaction; Hydrolase; Metal-binding; Myogenesis; NAD; Nucleus; Phosphoprotein; Polymorphism; Transcription; Transcription regulation; Zinc.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 747`	`747`	`NAD-dependent deacetylase sirtuin-1.`	`PRO_0000110256`
`DOMAIN`	`244 498`	`255`	`Deacetylase sirtuin-type.`
`NP_BIND`	`261 280`	`20`	`NAD (By similarity).`
`NP_BIND`	`345 349`	`5`	`NAD (By similarity).`
`COMPBIAS`	`54 98`	`45`	`Ala-rich.`
`COMPBIAS`	`122 127`	`6`	`Poly-Asp.`
`COMPBIAS`	`128 134`	`7`	`Poly-Glu.`
`ACT_SITE`	`363 363`		`Proton acceptor.`
`METAL`	`371 371`		`Zinc (By similarity).`
`METAL`	`374 374`		`Zinc (By similarity).`
`METAL`	`395 395`		`Zinc (By similarity).`
`METAL`	`398 398`		`Zinc (By similarity).`
`MOD_RES`	`27 27`		`Phosphoserine.`
`MOD_RES`	`47 47`		`Phosphoserine.`
`MOD_RES`	`719 719`		`Phosphothreonine.`
`VARIANT`	`3 3`	`1`	`D -> E.`	`VAR_025148`
`VARIANT`	`484 484`	`1`	`V -> D (in dbSNP:rs1063111 [NCBI]).`	`VAR_051976`
`MUTAGEN`	`363 363`		`H->Y: Loss of function.`
`CONFLICT`	`386 389`		`DIFN -> ALFS (in Ref. 5; AAH12499).`

Sequence information

Length: 747 AA [This is the length of the unprocessed precursor]

Molecular weight: 81681 Da [This is the MW of the unprocessed precursor]

CRC64: 2D3BEA6D73DA229F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MADEAALALQ PGGSPSAAGA DREAASSPAG EPLRKRPRRD GPGLERSPGE PGGAAPEREV 

        70         80         90        100        110        120 
PAAARGCPGA AAAALWREAE AEAAAAGGEQ EAQATAAAGE GDNGPGLQGP SREPPLADNL 

       130        140        150        160        170        180 
YDEDDDDEGE EEEEAAAAAI GYRDNLLFGD EIITNGFHSC ESDEEDRASH ASSSDWTPRP 

       190        200        210        220        230        240 
RIGPYTFVQQ HLMIGTDPRT ILKDLLPETI PPPELDDMTL WQIVINILSE PPKRKKRKDI 

       250        260        270        280        290        300 
NTIEDAVKLL QECKKIIVLT GAGVSVSCGI PDFRSRDGIY ARLAVDFPDL PDPQAMFDIE 

       310        320        330        340        350        360 
YFRKDPRPFF KFAKEIYPGQ FQPSLCHKFI ALSDKEGKLL RNYTQNIDTL EQVAGIQRII 

       370        380        390        400        410        420 
QCHGSFATAS CLICKYKVDC EAVRGDIFNQ VVPRCPRCPA DEPLAIMKPE IVFFGENLPE 

       430        440        450        460        470        480 
QFHRAMKYDK DEVDLLIVIG SSLKVRPVAL IPSSIPHEVP QILINREPLP HLHFDVELLG 

       490        500        510        520        530        540 
DCDVIINELC HRLGGEYAKL CCNPVKLSEI TEKPPRTQKE LAYLSELPPT PLHVSEDSSS 

       550        560        570        580        590        600 
PERTSPPDSS VIVTLLDQAA KSNDDLDVSE SKGCMEEKPQ EVQTSRNVES IAEQMENPDL 

       610        620        630        640        650        660 
KNVGSSTGEK NERTSVAGTV RKCWPNRVAK EQISRRLDGN QYLFLPPNRY IFHGAEVYSD 

       670        680        690        700        710        720 
SEDDVLSSSS CGSNSDSGTC QSPSLEEPME DESEIEEFYN GLEDEPDVPE RAGGAGFGTD 

       730        740 
GDDQEAINEA ISVKQEVTDM NYPSNKS

Q96EB6 in FASTA 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