Angiotensin-1
     (Angiotensin I)
     (Ang I)
Angiotensin-2
     (Angiotensin II)
     (Ang II)
Angiotensin-3
     (Angiotensin III)
     (Ang III)
     (Des-Asp[1]-angiotensin II)

Gene name

	Name:	AGT
	Synonyms:	SERPINA8

From

Homo sapiens (Human)

[TaxID: 9606]

Taxonomy

Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1021/bi00311a006; PubMed=6089875 [NCBI, ExPASy, EBI, Israel, Japan] Kageyama R., Ohkubo H., Nakanishi S.; "Primary structure of human preangiotensinogen deduced from the cloned cDNA sequence."; Biochemistry 23:3603-3609(1984).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2924688 [NCBI, ExPASy, EBI, Israel, Japan] Gaillard I., Clauser E., Corvol P.; "Structure of human angiotensinogen gene."; DNA 8:87-99(1989).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=1692023 [NCBI, ExPASy, EBI, Israel, Japan] Fukamizu A., Takahashi S., Seo M.S., Tada M., Tanimoto K., Uehara S., Murakami K.; "Structure and expression of the human angiotensinogen gene. Identification of a unique and highly active promoter."; J. Biol. Chem. 265:7576-7582(1990).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-335. TISSUE=Brain; 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).
[5]	NUCLEOTIDE SEQUENCE [MRNA] OF 1-338. PubMed=2885106 [NCBI, ExPASy, EBI, Israel, Japan] Kunapuli S.P., Kumar A.; "Molecular cloning of human angiotensinogen cDNA and evidence for the presence of its mRNA in rat heart."; Circ. Res. 60:786-790(1987).
[6]	NUCLEOTIDE SEQUENCE [MRNA] OF 32-184. DOI=10.1016/0003-9861(87)90148-2; PubMed=3579322 [NCBI, ExPASy, EBI, Israel, Japan] Kunapuli S.P., Benedict C.R., Kumar A.; "Tissue specific hormonal regulation of the rat angiotensinogen gene expression."; Arch. Biochem. Biophys. 254:642-646(1987).
[7]	PROTEIN SEQUENCE OF 34-58. DOI=10.1016/0006-291X(81)90762-2; PubMed=7259779 [NCBI, ExPASy, EBI, Israel, Japan] Tewksbury D.A., Dart R.A., Travis J.; "The amino terminal amino acid sequence of human angiotensinogen."; Biochem. Biophys. Res. Commun. 99:1311-1315(1981).
[8]	PROTEIN SEQUENCE OF 34-45, AND SUBUNIT. TISSUE=Serum; DOI=10.1074/jbc.270.23.13645; PubMed=7539791 [NCBI, ExPASy, EBI, Israel, Japan] Oxvig C., Haaning J., Kristensen L., Wagner J.M., Rubin I., Stigbrand T., Gleich G.J., Sottrup-Jensen L.; "Identification of angiotensinogen and complement C3dg as novel proteins binding the proform of eosinophil major basic protein in human pregnancy serum and plasma."; J. Biol. Chem. 270:13645-13651(1995).
[9]	PROTEIN SEQUENCE OF 34-43. PubMed=4300938 [NCBI, ExPASy, EBI, Israel, Japan] Arakawa K., Minohara A., Yamada J., Nakamura M.; "Enzymatic degradation and electrophoresis of human angiotensin I."; Biochim. Biophys. Acta 168:106-112(1968).
[10]	GLYCOSYLATION AT ASN-47; ASN-170; ASN-304 AND ASN-328. DOI=10.1016/0303-7207(85)90039-5; PubMed=3934016 [NCBI, ExPASy, EBI, Israel, Japan] Campbell D.J., Bouhnik J., Coezy E., Menard J., Corvol P.; "Processing of rat and human angiotensinogen precursors by microsomal membranes."; Mol. Cell. Endocrinol. 43:31-40(1985).
[11]	FUNCTION OF ANGIOTENSIN-3. PubMed=1132082 [NCBI, ExPASy, EBI, Israel, Japan] Goodfriend T.L., Peach M.J.; "Angiotensin III: (DES-Aspartic Acid-1)-Angiotensin II. Evidence and speculation for its role as an important agonist in the renin - angiotensin system."; Circ. Res. 36:38-48(1975).
[12]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-47, AND MASS SPECTROMETRY. TISSUE=Plasma; DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan] Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.; "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."; J. Proteome Res. 4:2070-2080(2005).
[13]	DECARBOXYLATION AT ASP-34, FUNCTION, AND MASS SPECTROMETRY. DOI=10.1161/01.ATV.0000253889.09765.5f; PubMed=17138938 [NCBI, ExPASy, EBI, Israel, Japan] Jankowski V., Vanholder R., van der Giet M., Tolle M., Karadogan S., Gobom J., Furkert J., Oksche A., Krause E., Tran T.N., Tepel M., Schuchardt M., Schluter H., Wiedon A., Beyermann M., Bader M., Todiras M., Zidek W., Jankowski J.; "Mass-spectrometric identification of a novel angiotensin peptide in human plasma."; Arterioscler. Thromb. Vasc. Biol. 27:297-302(2007).
[14]	STRUCTURE BY NMR OF ANGIOTENSIN-2. DOI=10.1046/j.1432-1327.1998.2510448.x; PubMed=9492317 [NCBI, ExPASy, EBI, Israel, Japan] Carpenter K.A., Wilkes B.C., Schiller P.W.; "The octapeptide angiotensin II adopts a well-defined structure in a phospholipid environment."; Eur. J. Biochem. 251:448-453(1998).
[15]	VARIANTS MET-207; THR-268 AND CYS-281. DOI=10.1016/0092-8674(92)90275-H; PubMed=1394429 [NCBI, ExPASy, EBI, Israel, Japan] Jeunemaitre X., Soubrier F., Kotelevtsev Y.V., Lifton R.P., Williams C.S., Charru A., Hunt S.C., Hopkins P.N., Williams R.R., Lalouel J.-M., Corvol P.; "Molecular basis of human hypertension: role of angiotensinogen."; Cell 71:169-180(1992).
[16]	VARIANT THR-268. DOI=10.1038/ng0593-59; PubMed=8513325 [NCBI, ExPASy, EBI, Israel, Japan] Ward K., Hata A., Jeunemaitre X., Helin C., Nelson L., Namikawa C., Farrington P.F., Ogasawara M., Suzumori K., Tomoda S., Berrebi S., Sasaki M., Corvol P., Lifton R.P., Lalouel J.-M.; "A molecular variant of angiotensinogen associated with preeclampsia."; Nat. Genet. 4:59-61(1993).
[17]	VARIANTS ILE-242; ARG-244 AND CYS-281. DOI=10.1007/BF00214197; PubMed=7607642 [NCBI, ExPASy, EBI, Israel, Japan] Hixson J.E., Powers P.K.; "Detection and characterization of new mutations in the human angiotensinogen gene (AGT)."; Hum. Genet. 96:110-112(1995).
[18]	VARIANT PRE-ECLAMPSIA PHE-43. DOI=10.1074/jbc.270.19.11430; PubMed=7744780 [NCBI, ExPASy, EBI, Israel, Japan] Inoue I., Rohrwasser A., Helin C., Jeunemaitre X., Crain P., Bohlender J., Lifton R.P., Corvol P., Ward K., Lalouel J.-M.; "A mutation of angiotensinogen in a patient with preeclampsia leads to altered kinetics of the renin-angiotensin system."; J. Biol. Chem. 270:11430-11436(1995).
[19]	CHARACTERIZATION OF VARIANT CYS-281. DOI=10.1074/jbc.271.16.9838; PubMed=8621667 [NCBI, ExPASy, EBI, Israel, Japan] Gimenez-Roqueplo A.P., Leconte I., Cohen P., Simon D., Guyene T.T., Celerier J., Pau B., Corvol P., Clauser E., Jeunemaitre X.; "The natural mutation Y248C of human angiotensinogen leads to abnormal glycosylation and altered immunological recognition of the protein."; J. Biol. Chem. 271:9838-9844(1996).
[20]	VARIANT RTD GLN-375. DOI=10.1038/ng1623; PubMed=16116425 [NCBI, ExPASy, EBI, Israel, Japan] Gribouval O., Gonzales M., Neuhaus T., Aziza J., Bieth E., Laurent N., Bouton J.M., Feuillet F., Makni S., Ben Amar H., Laube G., Delezoide A.-L., Bouvier R., Dijoud F., Ollagnon-Roman E., Roume J., Joubert M., Antignac C., Gubler M.-C.; "Mutations in genes in the renin-angiotensin system are associated with autosomal recessive renal tubular dysgenesis."; Nat. Genet. 37:964-968(2005).

Comments

FUNCTION: In response to lowered blood pressure, the enzyme renin cleaves angiotensin-1, from angiotensinogen. ACE (angiotensin converting enzyme) then removes a dipeptide to yield the physiologically active peptide angiotensin-2, the most potent pressor substance known, which helps regulate volume and mineral balance of body fluids.
FUNCTION: Angiotensin-3 stimulates aldosterone release.
SUBUNIT: During pregnancy, exists as a disulfide-linked 2:2 heterotetramer with the proform of PRG2 and as a complex (probably a 2:2:2 heterohexamer) with pro-PRG2 and C3dg.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
PTM: Beta-decarboxylation of Asp-34 in angiotensin-2, by mononuclear leukocytes produces alanine. The resulting peptide form, angiotensin-A, has the same affinity for the AT1 receptor as angiotensin-2, but a higher affinity for the AT2 receptor.
DISEASE: Defects in AGT are associated with susceptibility to essential hypertension [MIM:145500]. Hypertension also occurs in 5-7% of all pregnancies where it is a leading cause of maternal, fetal and neonatal morbidity and mortality. Among pregnancy-induced hypertension cases, severe pre-eclampsia [MIM:189800] is characterized by the development of hypertension and proteinuria after the 20th week of pregnancy and is the most distinctive, life-threatening form.
DISEASE: Defects in AGT are a cause of renal tubular dysgenesis (RTD) [MIM:267430]. RTD is an autosomal recessive severe disorder of renal tubular development characterized by persistent fetal anuria and perinatal death, probably due to pulmonary hypoplasia from early-onset oligohydramnios (the Potter phenotype).
SIMILARITY: Belongs to the serpin family.
CAUTION: It is uncertain whether Met-1 or Met-10 is the initiator.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=AGT";.
WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and polymorphism database; URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=AGT";.
WEB RESOURCE: Name=Wikipedia; Note=Angiotensin entry; URL="http://en.wikipedia.org/wiki/Angiotensin";.

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

K02215; AAA51731.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M24689; AAA51679.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M24686; AAA51679.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M24687; AAA51679.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M24688; AAA51679.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X15324; CAA33385.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X15325; CAA33385.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X15326; CAA33385.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X15327; CAA33385.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011519; AAH11519.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M69110; AAA52282.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S78529; AAD14287.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S78530; AAD14288.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A35203; ANHU.

NP_000020.1; -.

3D structure databases

PDB

1N9U; NMR; -; A=34-43.	[ExPASy / RCSB / EBI]
1N9V; NMR; -; A=34-41.	[ExPASy / RCSB / EBI]
2JP8; NMR; -; P=34-40.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1N9U; -.
1N9V; -.
2JP8; -.

ModBase

P01019.

Protein-protein interaction databases

DIP

DIP:309N; -.

IntAct

P01019; -.

Protein family/group databases

MEROPS

I04.953; -.

2D gel databases

SWISS-2DPAGE

P01019; -.

Organism-specific databases

HIX0001686; -.

HGNC:333; AGT.

AGT.

HPA001557; -.

106150; gene. [NCBI / EBI]
145500; phenotype. [NCBI / EBI]
267430; phenotype. [NCBI / EBI]

Orphanet

3033; Renal tubular dysgenesis.

PharmGKB

PA42; -.

GeneCards

P01019.

Gene expression databases

ArrayExpress

P01019; -.

CleanEx

HS_AGT; -.

GermOnline

ENSG00000135744; Homo sapiens.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from HPA).
GO:0005615;	Cellular component: extracellular space (inferred by curator from UniProtKB).
GO:0005625;	Cellular component: soluble fraction (traceable author statement from ProtInc).
GO:0008083;	Molecular function: growth factor activity (traceable author statement from UniProtKB).
GO:0005179;	Molecular function: hormone activity (inferred by curator from UniProtKB).
GO:0004867;	Molecular function: serine-type endopeptidase inhibitor activity (traceable author statement from ProtInc).
GO:0031702;	Molecular function: type 1 angiotensin receptor binding (inferred from physical interaction from UniProtKB).
GO:0031703;	Molecular function: type 2 angiotensin receptor binding (inferred from physical interaction from UniProtKB).
GO:0001974;	Biological process: blood vessel remodeling (traceable author statement from UniProtKB).
GO:0007267;	Biological process: cell-cell signaling (traceable author statement from ProtInc).
GO:0007199;	Biological process: G-protein signaling, coupled to cGMP nucleotide second messenger (traceable author statement from UniProtKB).
GO:0007200;	Biological process: G-protein signaling, coupled to IP3 second messenger (phospholipase C activating) (non-traceable author statement from UniProtKB).
GO:0001822;	Biological process: kidney development (inferred from mutant phenotype from UniProtKB).
GO:0051387;	Biological process: negative regulation of nerve growth factor receptor signaling pathway (inferred from direct assay from UniProtKB).
GO:0007263;	Biological process: nitric oxide mediated signal transduction (traceable author statement from UniProtKB).
GO:0006800;	Biological process: oxygen and reactive oxygen species metabolic process (traceable author statement from UniProtKB).
GO:0043065;	Biological process: positive regulation of apoptosis (inferred from direct assay from UniProtKB).
GO:0010613;	Biological process: positive regulation of cardiac muscle hypertrophy (inferred from sequence or structural similarity from UniProtKB).
GO:0001819;	Biological process: positive regulation of cytokine production (traceable author statement from UniProtKB).
GO:0010595;	Biological process: positive regulation of endothelial cell migration (inferred from direct assay from UniProtKB).
GO:0045742;	Biological process: positive regulation of epidermal growth factor receptor signaling pathway (inferred from direct assay from UniProtKB).
GO:0048146;	Biological process: positive regulation of fibroblast proliferation (inferred from sequence or structural similarity from UniProtKB).
GO:0050729;	Biological process: positive regulation of inflammatory response (traceable author statement from UniProtKB).
GO:0033864;	Biological process: positive regulation of NAD(P)H oxidase activity (traceable author statement from UniProtKB).
GO:0051092;	Biological process: positive regulation of NF-kappaB transcription factor activity (traceable author statement from UniProtKB).
GO:0050731;	Biological process: positive regulation of peptidyl-tyrosine phosphorylation (inferred from direct assay from UniProtKB).
GO:0014068;	Biological process: positive regulation of phosphoinositide 3-kinase cascade (inferred from direct assay from UniProtKB).
GO:0002034;	Biological process: regulation of blood vessel size by renin-angiotensin (traceable author statement from UniProtKB).
GO:0001558;	Biological process: regulation of cell growth (non-traceable author statement from UniProtKB).
GO:0003078;	Biological process: regulation of natriuresis (non-traceable author statement from UniProtKB).
GO:0002019;	Biological process: regulation of renal output by angiotensin (non-traceable author statement from UniProtKB).
GO:0019229;	Biological process: regulation of vasoconstriction (non-traceable author statement from UniProtKB).
GO:0002018;	Biological process: renin-angiotensin regulation of aldosterone production (non-traceable author statement from UniProtKB).
GO:0014873;	Biological process: response to muscle activity involved in regulation of muscle adaptation (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR000227; Angiotensngn.
IPR000215; Protease_inhib_I4_serpin.
Graphical view of domain structure.

PANTHER

PTHR11461; Prot_inh_serpin; 1.

Pfam

PF00079; Serpin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00654; ANGIOTENSNGN.

SMART

SM00093; SERPIN; 1.
SMART graphical view of domain structure.

PS00284; SERPIN; 1.

Proteomic databases

P01019; -.

Genome annotation databases

Ensembl

ENSG00000135744; Homo sapiens. [Contig view]

GeneID

183; -.

KEGG

hsa:183; -.

Phylogenomic databases

HOVERGEN

P01019; -.

Other

DrugBank

DB01258; Aliskiren.
DB01076; Atorvastatin.
DB01340; Cilazapril.
DB01029; Irbesartan.
DB00722; Lisinopril.
DB01092; Ouabain.
DB00641; Simvastatin.

NextBio

748; -.

SOURCE

AGT; Homo sapiens.

UniRef

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

Keywords

3D-structure; Direct protein sequencing; Disease mutation; Glycoprotein; Polymorphism; Secreted; Signal; Vasoactive; Vasoconstrictor.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 33`	`33`
`CHAIN`	`34 485`	`452`	`Angiotensinogen.`	`PRO_0000032456`
`PEPTIDE`	`34 43`	`10`	`Angiotensin-1.`	`PRO_0000032457`
`PEPTIDE`	`34 41`	`8`	`Angiotensin-2.`	`PRO_0000032458`
`PEPTIDE`	`35 41`	`7`	`Angiotensin-3.`	`PRO_0000032459`
`MOD_RES`	`34 34`		`Beta-decarboxylated aspartate; in form angiotensin-A.`
`CARBOHYD`	`47 47`		`N-linked (GlcNAc...).`
`CARBOHYD`	`170 170`		`N-linked (GlcNAc...).`
`CARBOHYD`	`304 304`		`N-linked (GlcNAc...).`
`CARBOHYD`	`328 328`		`N-linked (GlcNAc...).`
`VARIANT`	`43 43`	`1`	`L -> F (in pre-eclampsia; alters the reactions with renin and angiotensin-converting enzyme; dbSNP:rs41271499 [NCBI]).`	`VAR_022933`
`VARIANT`	`98 98`	`1`	`E -> K (in dbSNP:rs11568032 [NCBI]).`	`VAR_029166`
`VARIANT`	`137 137`	`1`	`T -> M (in dbSNP:rs34829218 [NCBI]).`	`VAR_035431`
`VARIANT`	`207 207`	`1`	`T -> M (associated with hypertension; dbSNP:rs4762 [NCBI]).`	`VAR_007093`
`VARIANT`	`242 242`	`1`	`T -> I (in hypertension).`	`VAR_007094`
`VARIANT`	`244 244`	`1`	`L -> R (in hypertension; dbSNP:rs5041 [NCBI]).`	`VAR_007095`
`VARIANT`	`268 268`	`1`	`M -> I (in dbSNP:rs11568053 [NCBI]).`	`VAR_029167`
`VARIANT`	`268 268`	`1`	`M -> T (associated with essential hypertension and pre-eclampsia; dbSNP:rs699 [NCBI]).`	`VAR_007096`
`VARIANT`	`281 281`	`1`	`Y -> C (in hypertension; alters the structure, glycosylation and secretion of angiotensinogen).`	`VAR_007097`
`VARIANT`	`335 335`	`1`	`P -> S (in dbSNP:rs17856352 [NCBI]).`	`VAR_035432`
`VARIANT`	`375 375`	`1`	`R -> Q (in RTD).`	`VAR_035433`
`VARIANT`	`392 392`	`1`	`L -> M (in dbSNP:rs1805090 [NCBI]).`	`VAR_014573`
`CONFLICT`	`51 51`		`C -> S (in Ref. 7; AA sequence).`
`CONFLICT`	`58 58`		`N -> D (in Ref. 7; AA sequence).`
`CONFLICT`	`333 333`		`Q -> E (in Ref. 2; AAA51679).`

Sequence information

Length: 485 AA [This is the length of the unprocessed precursor]

Molecular weight: 53154 Da [This is the MW of the unprocessed precursor]

CRC64: 5026C2DFB2DD236E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRKRAPQSEM APAGVSLRAT ILCLLAWAGL AAGDRVYIHP FHLVIHNEST CEQLAKANAG 

        70         80         90        100        110        120 
KPKDPTFIPA PIQAKTSPVD EKALQDQLVL VAAKLDTEDK LRAAMVGMLA NFLGFRIYGM 

       130        140        150        160        170        180 
HSELWGVVHG ATVLSPTAVF GTLASLYLGA LDHTADRLQA ILGVPWKDKN CTSRLDAHKV 

       190        200        210        220        230        240 
LSALQAVQGL LVAQGRADSQ AQLLLSTVVG VFTAPGLHLK QPFVQGLALY TPVVLPRSLD 

       250        260        270        280        290        300 
FTELDVAAEK IDRFMQAVTG WKTGCSLMGA SVDSTLAFNT YVHFQGKMKG FSLLAEPQEF 

       310        320        330        340        350        360 
WVDNSTSVSV PMLSGMGTFQ HWSDIQDNFS VTQVPFTESA CLLLIQPHYA SDLDKVEGLT 

       370        380        390        400        410        420 
FQQNSLNWMK KLSPRTIHLT MPQLVLQGSY DLQDLLAQAE LPAILHTELN LQKLSNDRIR 

       430        440        450        460        470        480 
VGEVLNSIFF ELEADEREPT ESTQQLNKPE VLEVTLNRPF LFAVYDQSAT ALHFLGRVAN 


PLSTA

P01019 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