[1]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-587. DOI=10.1126/science.277.5327.805; PubMed=9242607 [NCBI, ExPASy, EBI, Israel, Japan] van Slegtenhorst M.A., de Hoogt R., Hermans C., Nellist M., Janssen B., Verhoef S., Lindhout D., van den Ouweland A.M.W., Halley D.J.J., Young J., Burley M., Jeremiah S., Woodward K., Nahmias J., Fox M., Ekong R., Osborne J., Wolfe J., Povey S., Snell R.G., Cheadle J.P., Jones A.C., Tachataki M., Ravine D., Sampson J.R., Reeve M.P., Richardson P., Wilmer F., Munro C., Hawkins T.L., Sepp T., Ali J.B.M., Ward S., Green A.J., Yates J.R.W., Kwiatkowska J., Henske E.P., Short M.P., Haines J.H., Jozwiak S., Kwiatkowski D.J.; "Identification of the tuberous sclerosis gene TSC1 on chromosome 9q34."; Science 277:805-808(1997).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 466-1164. TISSUE=Bone marrow; DOI=10.1093/dnares/3.5.321; PubMed=9039502 [NCBI, ExPASy, EBI, Israel, Japan] Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.; "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."; DNA Res. 3:321-329(1996).
[3]	NUCLEOTIDE SEQUENCE OF 568-586. Fang L., Wang N., Murong S.X., Wu Z.Y., Lin M.T.; "A silent mutation 1947 T-->C in exon 15 of TSC1 in Chinese."; Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[4]	SUBCELLULAR LOCATION, AND INTERACTION WITH TSC2. PubMed=9809973 [NCBI, ExPASy, EBI, Israel, Japan] Plank T.L., Yeung R.S., Henske E.P.; "Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene, interacts with tuberin and appears to be localized to cytoplasmic vesicles."; Cancer Res. 58:4766-4770(1998).
[5]	INTERACTION WITH TSC2. DOI=10.1093/hmg/7.6.1053; PubMed=9580671 [NCBI, ExPASy, EBI, Israel, Japan] van Slegtenhorst M.A., Nellist M., Nagelkerken B., Cheadle J.P., Snell R.G., van den Ouweland A.M.W., Reuser A., Sampson J.R., Halley D.J.J., van der Sluijs P.; "Interaction between hamartin and tuberin, the TSC1 and TSC2 gene products."; Hum. Mol. Genet. 7:1053-1057(1998).
[6]	INTERACTION WITH TSC2. DOI=10.1074/jbc.274.50.35647; PubMed=10585443 [NCBI, ExPASy, EBI, Israel, Japan] Nellist M., van Slegtenhorst M.A., Goedbloed M., van den Ouweland A.M.W., Halley D.J.J., van der Sluijs P.; "Characterization of the cytosolic tuberin-hamartin complex. Tuberin is a cytosolic chaperone for hamartin."; J. Biol. Chem. 274:35647-35652(1999).
[7]	PHOSPHORYLATION AT SER-505, MASS SPECTROMETRY, AND INTERACTION WITH DOCK7 AND TSC2. DOI=10.1016/j.bbrc.2005.05.175; PubMed=15963462 [NCBI, ExPASy, EBI, Israel, Japan] Nellist M., Burgers P.C., van den Ouweland A.M.W., Halley D.J.J., Luider T.M.; "Phosphorylation and binding partner analysis of the TSC1-TSC2 complex."; Biochem. Biophys. Res. Commun. 333:818-826(2005).
[8]	INTERACTION WITH TSC2. DOI=10.1074/jbc.C500451200; PubMed=16464865 [NCBI, ExPASy, EBI, Israel, Japan] Chong-Kopera H., Inoki K., Li Y., Zhu T., Garcia-Gonzalo F.R., Rosa J.L., Guan K.-L.; "TSC1 stabilizes TSC2 by inhibiting the interaction between TSC2 and the HERC1 ubiquitin ligase."; J. Biol. Chem. 281:8313-8316(2006).
[9]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1102, 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).
[10]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505, 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).
[11]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505; SER-511 AND SER-598, 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).
[12]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.
[13]	VARIANT TSC GLU-726, AND VARIANTS THR-322; TYR-732 AND SER-1035. TISSUE=Peripheral blood; DOI=10.1093/hmg/6.12.2155; PubMed=9328481 [NCBI, ExPASy, EBI, Israel, Japan] Jones A.C., Daniells C.E., Snell R.G., Tachataki M., Idziaszczyk S.A., Krawczak M., Sampson J.R., Cheadle J.P.; "Molecular genetic and phenotypic analysis reveals differences between TSC1 and TSC2 associated familial and sporadic tuberous sclerosis."; Hum. Mol. Genet. 6:2155-2161(1997).
[14]	VARIANTS THR-322; ARG-587; TYR-732; SER-1035 AND SER-1108. TISSUE=Blood; DOI=10.1046/j.1469-1809.1998.6240277.x; PubMed=9924605 [NCBI, ExPASy, EBI, Israel, Japan] Kwiatkowska J., Jozwiak S., Hall F., Henske E.P., Haines J.L., McNamara P., Braiser J., Wigowska-Sowinska J., Kasprzyk-Obara J., Short M.P., Kwiatkowski D.J.; "Comprehensive mutational analysis of the TSC1 gene: observations on frequency of mutation, associated features, and nonpenetrance."; Ann. Hum. Genet. 62:277-285(1998).
[15]	VARIANT TSC PRO-72. DOI=10.1002/(SICI)1098-1004(199911)14:5<428::AID-HUMU9>3.0.CO;2-5; PubMed=10533069 [NCBI, ExPASy, EBI, Israel, Japan] Benit P., Kara-Mostefa A., Hadj-Rabia S., Munnich A., Bonnefont J.-P.; "Protein truncation test for screening hamartin gene mutations and report of new disease-causing mutations."; Hum. Mutat. 14:428-432(1999).
[16]	VARIANTS THR-322; TYR-732 AND GLN-809. TISSUE=Blood, and Lymphoblast; DOI=10.1002/(SICI)1098-1004(199911)14:5<412::AID-HUMU7>3.0.CO;2-K; PubMed=10533067 [NCBI, ExPASy, EBI, Israel, Japan] Niida Y., Lawrence-Smith N., Banwell A., Hammer E., Lewis J., Beauchamp R.L., Sims K., Ramesh V., Ozelius L.; "Analysis of both TSC1 and TSC2 for germline mutations in 126 unrelated patients with tuberous sclerosis."; Hum. Mutat. 14:412-422(1999).
[17]	VARIANTS TSC ILE-417; GLU-654 AND SER-899, AND VARIANT THR-322. TISSUE=Blood; DOI=10.1007/s100380050185; PubMed=10570911 [NCBI, ExPASy, EBI, Israel, Japan] Zhang H., Nanba E., Yamamoto T., Ninomiya H., Ohno K., Mizuguchi M., Takeshita K.; "Mutational analysis of TSC1 and TSC2 genes in Japanese patients with tuberous sclerosis complex."; J. Hum. Genet. 44:391-396(1999).
[18]	VARIANTS TSC, AND VARIANTS. TISSUE=Peripheral blood; PubMed=10227394 [NCBI, ExPASy, EBI, Israel, Japan] Van Slegtenhorst M.A., Verhoef S., Tempelaars A., Bakker L., Wang Q., Wessels M., Bakker R., Nellist M., Lindhout D., Halley D.J.J., van den Ouweland A.M.W.; "Mutational spectrum of the TSC1 gene in a cohort of 225 tuberous sclerosis complex patients: no evidence for genotype-phenotype correlation."; J. Med. Genet. 36:285-289(1999).
[19]	VARIANTS THR-322; ILE-417; ASP-577 AND ARG-829. TISSUE=Peripheral blood leukocyte; DOI=10.1002/(SICI)1096-8628(20000117)90:2<123::AID-AJMG7>3.3.CO;2-C; PubMed=10607950 [NCBI, ExPASy, EBI, Israel, Japan] Yamashita Y., Ono J., Okada S., Wataya-Kaneda M., Yoshikawa K., Nishizawa M., Hirayama Y., Kobayashi E., Seyama K., Hino O.; "Analysis of all exons of TSC1 and TSC2 genes for germline mutations in Japanese patients with tuberous sclerosis: report of 10 mutations."; Am. J. Med. Genet. 90:123-126(2000).
[20]	VARIANT TSC GLN-500. DOI=10.1002/1098-1004(200007)16:1<88::AID-HUMU15>3.3.CO;2-A; PubMed=10874311 [NCBI, ExPASy, EBI, Israel, Japan] Hass J., Mayer K., Rott H.-D.; "Tuberous sclerosis type 1: three novel mutations detected in exon 15 by a combination of HDA and TGGE."; Hum. Mutat. 16:88-88(2000).
[21]	VARIANT FCDBC TYR-732. DOI=10.1002/ana.10251; PubMed=12112044 [NCBI, ExPASy, EBI, Israel, Japan] Becker A.J., Urbach H., Scheffler B., Baden T., Normann S., Lahl R., Pannek H.W., Tuxhorn I., Elger C.E., Schramm J., Wiestler O.D., Bluemcke I.; "Focal cortical dysplasia of Taylor's balloon cell type: mutational analysis of the TSC1 gene indicates a pathogenic relationship to tuberous sclerosis."; Ann. Neurol. 52:29-37(2002).
[22]	VARIANTS ARG-68; CYS-158; ASP-206; LEU-216 AND ILE-417, AND CHARACTERIZATION OF VARIANTS ARG-68; CYS-158; ASP-206; LEU-216 AND ILE-417. DOI=10.1093/hmg/ddn098; PubMed=18397877 [NCBI, ExPASy, EBI, Israel, Japan] Pymar L.S., Platt F.M., Askham J.M., Morrison E.E., Knowles M.A.; "Bladder tumour-derived somatic TSC1 missense mutations cause loss of function via distinct mechanisms."; Hum. Mol. Genet. 17:2006-2017(2008).

Comments

FUNCTION: Implicated as a tumor suppressor. May have a function in vesicular transport. Interaction between TSC1 and TSC2 may facilitate vesicular docking.
SUBUNIT: Interacts with TSC2, leading to stabilize TSC2. In the absence of TSC2, TSC1 self-aggregates. Interacts with DOCK7.
INTERACTION:
O14920:IKBKB; NbExp=3; IntAct=EBI-1386638, EBI-81266;
Q00994:NGFRAP1; NbExp=4; IntAct=EBI-1386638, EBI-741753;
P49815:TSC2; NbExp=3; IntAct=EBI-1386638, EBI-396587;
SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Note=At steady state found in association with membranes.
TISSUE SPECIFICITY: Highly expressed in skeletal muscle, followed by heart, brain, placenta, pancreas, lung, liver and kidney. Also expressed in embryonic kidney cells.
DOMAIN: The C-terminal putative coiled-coil domain is necessary for interaction with TSC2.
PTM: Phosphorylation at Ser-505 does not affect interaction with TSC2.
PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
DISEASE: Defects in TSC1 are the cause of tuberous sclerosis complex (TSC) [MIM:191100]. The molecular basis of TSC is a functional impairement of the hamartin-tuberin complex. TSC is an autosomal dominant multi-system disorder that affects especially the brain, kidneys, heart, and skin. TSC is characterized by hamartomas (benign overgrowths predominantly of a cell or tissue type that occurs normally in the organ) and hamartias (developmental abnormalities of tissue combination). Clinical symptoms can range from benign hypopigmented macules of the skin to profound mental retardation with intractable seizures to premature death from a variety of disease-associated causes.
DISEASE: Defects in TSC1 may be a cause of focal cortical dysplasia of Taylor balloon cell type (FCDBC) [MIM:607341]. FCDBC is a subtype of cortical displasias linked to chronic intractable epilepsy. Cortical dysplasias display a broad spectrum of structural changes, which appear to result from changes in proliferation, migration, differentiation, and apoptosis of neuronal precursors and neurons during cortical development.
WEB RESOURCE: Name=TSC variation database; URL="http://zk.bwh.harvard.edu/ts/";.
WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/TSC1ID183.html";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=TSC1";.

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

AF013168; AAC51674.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AC002096; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
D87683; BAA13436.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF234185; AAF61948.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00022043; -.

T03814; T03814.

NP_000359.1; -.

3D structure databases

ModBase

Q92574.

Protein-protein interaction databases

IntAct

Q92574; 21.

PTM databases

PhosphoSite

Q92574; -.

Enzyme and pathway databases

Pathway_Interaction_DB

pi3kciaktpathway; Class I PI3K signaling events mediated by Akt.
mtor_4pathway; mTOR signaling pathway.

Reactome

REACT_498; Signaling by Insulin receptor.

Organism-specific databases

GC09M134756; -.

HIX0008496; -.

HGNC:12362; TSC1.

CAB011568; -.
CAB012481; -.

MIM

191100; phenotype. [NCBI / EBI]
605284; gene. [NCBI / EBI]
607341; phenotype. [NCBI / EBI]

Orphanet

65683; Focal cortical dysplasia.
538; Lymphangioleiomyomatosis.
805; Tuberous sclerosis.

PharmGKB

PA32845; -.

HUGE

KIAA0243.

Gene expression databases

Bgee

Q92574; -.

CleanEx

HS_TSC1; -.

GermOnline

ENSG00000165699; Homo sapiens.

Ontologies

GO:0005938;	Cellular component: cell cortex (inferred from direct assay from UniProtKB).
GO:0030027;	Cellular component: lamellipodium (inferred from direct assay from UniProtKB).
GO:0016020;	Cellular component: membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005624;	Cellular component: membrane fraction (inferred from direct assay from UniProtKB).
GO:0033596;	Cellular component: TSC1-TSC2 complex (inferred from direct assay from UniProtKB).
GO:0051087;	Molecular function: chaperone binding (inferred from physical interaction from UniProtKB).
GO:0047485;	Molecular function: protein N-terminus binding (inferred from physical interaction from UniProtKB).
GO:0032862;	Biological process: activation of Rho GTPase activity (inferred from direct assay from UniProtKB).
GO:0007049;	Biological process: cell cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0007160;	Biological process: cell-matrix adhesion (inferred from mutant phenotype from UniProtKB).
GO:0045786;	Biological process: negative regulation of cell cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0008285;	Biological process: negative regulation of cell proliferation (inferred from mutant phenotype from UniProtKB).
GO:0031397;	Biological process: negative regulation of protein ubiquitination (inferred from direct assay from UniProtKB).
GO:0032007;	Biological process: negative regulation of TOR signaling pathway (inferred from mutant phenotype from UniProtKB).
GO:0017148;	Biological process: negative regulation of translation (inferred from mutant phenotype from UniProtKB).
GO:0051894;	Biological process: positive regulation of focal adhesion formation (inferred from direct assay from UniProtKB).
GO:0043666;	Biological process: regulation of phosphoprotein phosphatase activity (inferred from mutant phenotype from UniProtKB).
GO:0051492;	Biological process: regulation of stress fiber formation (inferred from direct assay from UniProtKB).
GO:0032868;	Biological process: response to insulin stimulus (inferred from direct assay from UniProtKB).
GO:0006407;	Biological process: rRNA export from nucleus (inferred from mutant phenotype from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR007483; Hamartin.
Graphical view of domain structure.

PANTHER

PTHR15154; Hamartin; 1.

Pfam

PF04388; Hamartin; 1.
Pfam graphical view of domain structure.

Proteomic databases

PRIDE

Q92574; -.

Genome annotation databases

Ensembl

ENSG00000165699; Homo sapiens. [Contig view]

GeneID

7248; -.

KEGG

hsa:7248; -.

Phylogenomic databases

HOGENOM

Q92574; -.

HOVERGEN

Q92574; -.

OMA

Q92574; EHNAAMK.

Other

28341; -.

TSC1; Homo sapiens.

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

Keywords

Anti-oncogene; Cell cycle; Coiled coil; Cytoplasm; Disease mutation; Epilepsy; Membrane; Phosphoprotein; Polymorphism.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 1164`	`1164`	`Hamartin.`	`PRO_0000065651`
`COILED`	`721 997`	`277`	`Potential.`
`COMPBIAS`	`1034 1037`	`4`	`Poly-Gly.`
`COMPBIAS`	`1038 1043`	`6`	`Poly-Ser.`
`MOD_RES`	`505 505`		`Phosphoserine.`
`MOD_RES`	`511 511`		`Phosphoserine.`
`MOD_RES`	`598 598`		`Phosphoserine.`
`MOD_RES`	`1102 1102`		`Phosphoserine.`
`VARIANT`	`51 51`	`1`	`E -> D (in TSC; could be a polymorphism).`	`VAR_009397`
`VARIANT`	`68 68`	`1`	`H -> R (in a bladder tumor; somatic mutation; reduced stability; does not affect interaction with TSC2).`	`VAR_054386`
`VARIANT`	`72 72`	`1`	`L -> P (in TSC).`	`VAR_054387`
`VARIANT`	`158 158`	`1`	`F -> C (in a bladder tumor; somatic mutation; reduced stability; does not affect interaction with TSC2).`	`VAR_054388`
`VARIANT`	`190 190`	`1`	`R -> S.`	`VAR_009398`
`VARIANT`	`191 191`	`1`	`L -> H (in TSC; could be a polymorphism).`	`VAR_009399`
`VARIANT`	`198 199`	`2`	`NF -> I (in TSC).`	`VAR_009400`
`VARIANT`	`206 206`	`1`	`H -> D (in a bladder tumor; somatic mutation; reduced stability; does not affect interaction with TSC2).`	`VAR_054389`
`VARIANT`	`216 216`	`1`	`F -> L (in a bladder tumor; diffuse punctate cytoplasmic distribution in aminoacid-starved conditions; does not affect interaction with TSC2).`	`VAR_054390`
`VARIANT`	`224 224`	`1`	`M -> R (in TSC; could be a polymorphism).`	`VAR_009401`
`VARIANT`	`322 322`	`1`	`M -> T (in dbSNP:rs1073123 [NCBI]).`	`VAR_009402`
`VARIANT`	`417 417`	`1`	`T -> I (in TSC; could be a polymorphism; does not affect interaction with TSC2).`	`VAR_009403`
`VARIANT`	`500 500`	`1`	`R -> Q (in TSC).`	`VAR_054391`
`VARIANT`	`577 577`	`1`	`E -> D.`	`VAR_009404`
`VARIANT`	`586 589`	`4`	`CKIP -> S (in TSC).`	`VAR_009405`
`VARIANT`	`587 587`	`1`	`K -> R (in TSC; could be a polymorphism).`	`VAR_009406`
`VARIANT`	`654 654`	`1`	`Q -> E (in TSC).`	`VAR_009407`
`VARIANT`	`726 726`	`1`	`A -> E (in TSC).`	`VAR_009408`
`VARIANT`	`732 732`	`1`	`H -> Y (in FCDBC; could be a polymorphism).`	`VAR_009409`
`VARIANT`	`809 809`	`1`	`E -> Q.`	`VAR_009410`
`VARIANT`	`829 829`	`1`	`S -> R.`	`VAR_009411`
`VARIANT`	`899 899`	`1`	`T -> S (in TSC).`	`VAR_009412`
`VARIANT`	`1035 1035`	`1`	`G -> S.`	`VAR_009413`
`VARIANT`	`1108 1108`	`1`	`G -> S.`	`VAR_009414`

Sequence information

Length: 1164 AA [This is the length of the unprocessed precursor]

Molecular weight: 129767 Da [This is the MW of the unprocessed precursor]

CRC64: EF15509385C7AACC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAQQANVGEL LAMLDSPMLG VRDDVTAVFK ENLNSDRGPM LVNTLVDYYL ETSSQPALHI 

        70         80         90        100        110        120 
LTTLQEPHDK HLLDRINEYV GKAATRLSIL SLLGHVIRLQ PSWKHKLSQA PLLPSLLKCL 

       130        140        150        160        170        180 
KMDTDVVVLT TGVLVLITML PMIPQSGKQH LLDFFDIFGR LSSWCLKKPG HVAEVYLVHL 

       190        200        210        220        230        240 
HASVYALFHR LYGMYPCNFV SFLRSHYSMK ENLETFEEVV KPMMEHVRIH PELVTGSKDH 

       250        260        270        280        290        300 
ELDPRRWKRL ETHDVVIECA KISLDPTEAS YEDGYSVSHQ ISARFPHRSA DVTTSPYADT 

       310        320        330        340        350        360 
QNSYGCATST PYSTSRLMLL NMPGQLPQTL SSPSTRLITE PPQATLWSPS MVCGMTTPPT 

       370        380        390        400        410        420 
SPGNVPPDLS HPYSKVFGTT AGGKGTPLGT PATSPPPAPL CHSDDYVHIS LPQATVTPPR 

       430        440        450        460        470        480 
KEERMDSARP CLHRQHHLLN DRGSEEPPGS KGSVTLSDLP GFLGDLASEE DSIEKDKEEA 

       490        500        510        520        530        540 
AISRELSEIT TAEAEPVVPR GGFDSPFYRD SLPGSQRKTH SAASSSQGAS VNPEPLHSSL 

       550        560        570        580        590        600 
DKLGPDTPKQ AFTPIDLPCG SADESPAGDR ECQTSLETSI FTPSPCKIPP PTRVGFGSGQ 

       610        620        630        640        650        660 
PPPYDHLFEV ALPKTAHHFV IRKTEELLKK AKGNTEEDGV PSTSPMEVLD RLIQQGADAH 

       670        680        690        700        710        720 
SKELNKLPLP SKSVDWTHFG GSPPSDEIRT LRDQLLLLHN QLLYERFKRQ QHALRNRRLL 

       730        740        750        760        770        780 
RKVIKAAALE EHNAAMKDQL KLQEKDIQMW KVSLQKEQAR YNQLQEQRDT MVTKLHSQIR 

       790        800        810        820        830        840 
QLQHDREEFY NQSQELQTKL EDCRNMIAEL RIELKKANNK VCHTELLLSQ VSQKLSNSES 

       850        860        870        880        890        900 
VQQQMEFLNR QLLVLGEVNE LYLEQLQNKH SDTTKEVEMM KAAYRKELEK NRSHVLQQTQ 

       910        920        930        940        950        960 
RLDTSQKRIL ELESHLAKKD HLLLEQKKYL EDVKLQARGQ LQAAESRYEA QKRITQVFEL 

       970        980        990       1000       1010       1020 
EILDLYGRLE KDGLLKKLEE EKAEAAEAAE ERLDCCNDGC SDSMVGHNEE ASGHNGETKT 

      1030       1040       1050       1060       1070       1080 
PRPSSARGSS GSRGGGGSSS SSSELSTPEK PPHQRAGPFS SRWETTMGEA SASIPTTVGS 

      1090       1100       1110       1120       1130       1140 
LPSSKSFLGM KARELFRNKS ESQCDEDGMT SSLSESLKTE LGKDLGVEAK IPLNLDGPHP 

      1150       1160 
SPPTPDSVGQ LHIMDYNETH HEHS

Q92574 in FASTA format

View entry in raw text format (no links)
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	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