[1]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT 92-GLN--GLN-95 DEL. DOI=10.1038/346387a0; PubMed=2374612 [NCBI, ExPASy, EBI, Israel, Japan] Hoffmann A., Sinn E., Yamamoto T., Wang J., Roy A., Horikoshi M., Roeder R.G.; "Highly conserved core domain and unique N-terminus with presumptive regulatory motifs in a human TATA factor (TFIID)."; Nature 346:387-390(1990).
[2]	NUCLEOTIDE SEQUENCE [MRNA], AND DOMAINS. DOI=10.1126/science.2363050; PubMed=2363050 [NCBI, ExPASy, EBI, Israel, Japan] Peterson M.G., Tanese N., Pugh B.F., Tjian R.; "Functional domains and upstream activation properties of cloned human TATA binding protein."; Science 248:1625-1630(1990).
[3]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Fibroblast; DOI=10.1126/science.2194289; PubMed=2194289 [NCBI, ExPASy, EBI, Israel, Japan] Kao C.C., Lieberman P.M., Schmidt M.C., Zhou Q., Pei R., Berk A.J.; "Cloning of a transcriptionally active human TATA binding factor."; Science 248:1646-1650(1990).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."; Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]	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).
[6]	INTERACTION WITH HIV-1 TAT. DOI=10.1038/367295a0; PubMed=8121496 [NCBI, ExPASy, EBI, Israel, Japan] Kashanchi F., Piras G., Radonovich M.F., Duvall J.F., Fattaey A., Chiang C.M., Roeder R.G., Brady J.N.; "Direct interaction of human TFIID with the HIV-1 transactivator tat."; Nature 367:295-299(1994).
[7]	INTERACTION WITH TAF1A; TAF1B AND TAF1C. DOI=10.1126/science.7801123; PubMed=7801123 [NCBI, ExPASy, EBI, Israel, Japan] Comai L., Zomerdijk J.C.B.M., Beckmann H., Zhou S., Admon A., Tjian R.; "Reconstitution of transcription factor SL1: exclusive binding of TBP by SL1 or TFIID subunits."; Science 266:1966-1972(1994).
[8]	INTERACTION WITH HIV-1 TAT. DOI=10.1006/jmbi.1995.0368; PubMed=7608968 [NCBI, ExPASy, EBI, Israel, Japan] Veschambre P., Simard P., Jalinot P.; "Evidence for functional interaction between the HIV-1 Tat transactivator and the TATA box binding protein in vivo."; J. Mol. Biol. 250:169-180(1995).
[9]	INTERACTION WITH UTF1. DOI=10.1074/jbc.273.40.25840; PubMed=9748258 [NCBI, ExPASy, EBI, Israel, Japan] Fukushima A., Okuda A., Nishimoto M., Seki N., Hori T.A., Muramatsu M.; "Characterization of functional domains of an embryonic stem cell coactivator UTF1 which are conserved and essential for potentiation of ATF-2 activity."; J. Biol. Chem. 273:25840-25849(1998).
[10]	TISSUE SPECIFICITY. DOI=10.1089/dna.2006.0527; PubMed=17570761 [NCBI, ExPASy, EBI, Israel, Japan] Di Pietro C., Ragusa M., Duro L., Guglielmino M.R., Barbagallo D., Carnemolla A., Lagana A., Buffa P., Angelica R., Rinaldi A., Calafato M.S., Milicia I., Caserta C., Giugno R., Pulvirenti A., Giunta V., Rapisarda A., Di Pietro V., Grillo A., Messina A., Ferro A., Grzeschik K.H., Purrello M.; "Genomics, evolution, and expression of TBPL2, a member of the TBP family."; DNA Cell Biol. 26:369-385(2007).
[11]	INTERACTION WITH SPIB. DOI=10.1074/jbc.274.16.11115; PubMed=10196196 [NCBI, ExPASy, EBI, Israel, Japan] Rao S., Matsumura A., Yoon J., Simon M.C.; "SPI-B activates transcription via a unique proline, serine, and threonine domain and exhibits DNA binding affinity differences from PU.1."; J. Biol. Chem. 274:11115-11124(1999).
[12]	INTERACTION WITH NCOA6. DOI=10.1074/jbc.274.48.34283; PubMed=10567404 [NCBI, ExPASy, EBI, Israel, Japan] Lee S.-K., Anzick S.L., Choi J.-E., Bubendorf L., Guan X.-Y., Jung Y.-K., Kallioniemi O.-P., Kononen J., Trent J.M., Azorsa D., Jhun B.-H., Cheong J.H., Lee Y.C., Meltzer P.S., Lee J.W.; "A nuclear factor ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo."; J. Biol. Chem. 274:34283-34293(1999).
[13]	INTERACTION WITH ELF3. DOI=10.1038/sj.onc.1202674; PubMed=10391676 [NCBI, ExPASy, EBI, Israel, Japan] Chang C.-H., Scott G.K., Baldwin M.A., Benz C.C.; "Exon 4-encoded acidic domain in the epithelium-restricted Ets factor, ESX, confers potent transactivating capacity and binds to TATA-binding protein (TBP)."; Oncogene 18:3682-3695(1999).
[14]	INTERACTION WITH BRF2. DOI=10.1074/jbc.M108515200; PubMed=11564744 [NCBI, ExPASy, EBI, Israel, Japan] Cabart P., Murphy S.; "BRFU, a TFIIB-like factor, is directly recruited to the TATA-box of polymerase III small nuclear RNA gene promoters through its interaction with TATA-binding protein."; J. Biol. Chem. 276:43056-43064(2001).
[15]	INTERACTION WITH TAF3. DOI=10.1128/MCB.21.15.5109-5121.2001; PubMed=11438666 [NCBI, ExPASy, EBI, Israel, Japan] Gangloff Y.G., Pointud J.-C., Thuault S., Carre L., Romier C., Muratoglu S., Brand M., Tora L., Couderc J.-L., Davidson I.; "The TFIID components human TAFII140 and Drosophila BIP2 (TAFII155) are novel metazoan homologues of yeast TAFII47 containing a histone fold and a PHD finger."; Mol. Cell. Biol. 21:5109-5121(2001).
[16]	INTERACTION WITH TAF1L. DOI=10.1093/hmg/11.19.2341; PubMed=12217962 [NCBI, ExPASy, EBI, Israel, Japan] Wang P.J., Page D.C.; "Functional substitution for TAF(II)250 by a retroposed homolog that is expressed in human spermatogenesis."; Hum. Mol. Genet. 11:2341-2346(2002).
[17]	INTERACTION WITH SNAPC1; SNAPC2 AND SNAPC4. DOI=10.1074/jbc.M204247200; PubMed=12621023 [NCBI, ExPASy, EBI, Israel, Japan] Hinkley C.S., Hirsch H.A., Gu L., LaMere B., Henry R.W.; "The small nuclear RNA-activating protein 190 Myb DNA binding domain stimulates TATA box-binding protein-TATA box recognition."; J. Biol. Chem. 278:18649-18657(2003).
[18]	INTERACTION WITH HIV-1 TAT. DOI=10.1371/journal.pbio.0030044; PubMed=15719058 [NCBI, ExPASy, EBI, Israel, Japan] Raha T., Cheng S.W.G., Green M.R.; "HIV-1 Tat stimulates transcription complex assembly through recruitment of TBP in the absence of TAFs."; PLoS Biol. 3:221-230(2005).
[19]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.
[20]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 159-337 IN COMPLEX WITH DNA. DOI=10.1073/pnas.93.10.4862; PubMed=8643494 [NCBI, ExPASy, EBI, Israel, Japan] Nikolov D.B., Chen H., Halay E.D., Hoffmann A., Roeder R.G., Burley S.K.; "Crystal structure of a human TATA box-binding protein/TATA element complex."; Proc. Natl. Acad. Sci. U.S.A. 93:4862-4867(1996).
[21]	X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 159-339 IN COMPLEX WITH DNA. DOI=10.1006/jmbi.1996.0456; PubMed=8757291 [NCBI, ExPASy, EBI, Israel, Japan] Juo Z.S., Chiu T.K., Leiberman P.M., Baikalov I., Berk A.J., Dickerson R.E.; "How proteins recognize the TATA box."; J. Mol. Biol. 261:239-254(1996).
[22]	X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 159-337 IN COMPLEX WITH GTF2B AND DNA. DOI=10.1093/emboj/19.1.25; PubMed=10619841 [NCBI, ExPASy, EBI, Israel, Japan] Tsai F.T.F., Sigler P.B.; "Structural basis of preinitiation complex assembly on human pol II promoters."; EMBO J. 19:25-36(2000).
[23]	X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 159-339 IN COMPLEX WITH DR1; DRAP1 AND DNA. DOI=10.1016/S0092-8674(01)00417-2; PubMed=11461703 [NCBI, ExPASy, EBI, Israel, Japan] Kamada K., Shu F., Chen H., Malik S., Stelzer G., Roeder R.G., Meisterernst M., Burley S.K.; "Crystal structure of negative cofactor 2 recognizing the TBP-DNA transcription complex."; Cell 106:71-81(2001).
[24]	POLYMORPHISM OF POLY-GLN REGION. DOI=10.1093/hmg/8.11.2047; PubMed=10484774 [NCBI, ExPASy, EBI, Israel, Japan] Koide R., Kobayashi S., Shimohata T., Ikeuchi T., Maruyama M., Saito M., Yamada M., Takahashi H., Tsuji S.; "A neurological disease caused by an expanded CAG trinucleotide repeat in the TATA-binding protein gene: a new polyglutamine disease?"; Hum. Mol. Genet. 8:2047-2053(1999).
[25]	POLYMORPHISM OF POLY-GLN REGION, AND INVOLVEMENT IN SCA17. DOI=10.1038/sj.ejhg.5200617; PubMed=11313753 [NCBI, ExPASy, EBI, Israel, Japan] Zuhlke C., Hellenbroich Y., Dalski A., Kononowa N., Hagenah J., Vieregge P., Riess O., Klein C., Schwinger E.; "Different types of repeat expansion in the TATA-binding protein gene are associated with a new form of inherited ataxia."; Eur. J. Hum. Genet. 9:160-164(2001).
[26]	POLYMORPHISM OF POLY-GLN REGION, AND INVOLVEMENT IN SCA17. DOI=10.1093/hmg/10.14.1441; PubMed=11448935 [NCBI, ExPASy, EBI, Israel, Japan] Nakamura K., Jeong S.-Y., Uchihara T., Anno M., Nagashima K., Nagashima T., Ikeda S., Tsuji S., Kanazawa I.; "SCA17, a novel autosomal dominant cerebellar ataxia caused by an expanded polyglutamine in TATA-binding protein."; Hum. Mol. Genet. 10:1441-1448(2001).
[27]	POLYMORPHISM OF POLY-GLN REGION, AND INVOLVEMENT IN SCA17. DOI=10.1001/archneur.59.4.623; PubMed=11939898 [NCBI, ExPASy, EBI, Israel, Japan] Silveira I., Miranda C., Guimaraes L., Moreira M.-C., Alonso I., Mendonca P., Ferro A., Pinto-Basto J., Coelho J., Ferreirinha F., Poirier J., Parreira E., Vale J., Januario C., Barbot C., Tuna A., Barros J., Koide R., Tsuji S., Holmes S.E., Margolis R.L., Jardim L., Pandolfo M., Coutinho P., Sequeiros J.; "Trinucleotide repeats in 202 families with ataxia: a small expanded (CAG)n allele at the SCA17 locus."; Arch. Neurol. 59:623-629(2002).

Comments

FUNCTION: General transcription factor that functions at the core of the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA box is the initial transcriptional step of the pre-initiation complex (PIC), playing a role in the activation of eukaryotic genes transcribed by RNA polymerase II.
SUBUNIT: Belongs to the TFIID complex together with the TBP-associated factors (TAFs). Component of the transcription factor SL1/TIFIB complex, composed of TBP and at least TAF1A, TAF1B TAF1C, and TAF3. Binds DNA as monomer. Interacts with TAFs, TFIIB, NCOA6, DRAP1, DR1 and ELF3. Interacts with SPIB, SNAPC1, SNAPC2 and SNAPC4. Interacts with HIV-1 Tat. Interacts with UTF1 which acts as a coactivator of ATF2 transcriptional activity. Interacts with GPBP1 (By similarity). Interacts with BRF2.
INTERACTION:
O60869:EDF1; NbExp=1; IntAct=EBI-355371, EBI-781301;
O60869-1:EDF1; NbExp=1; IntAct=EBI-355371, EBI-781310;
O60869-2:EDF1; NbExp=1; IntAct=EBI-355371, EBI-781315;
P52655-1:GTF2A1; NbExp=1; IntAct=EBI-355371, EBI-1019093;
P52657:GTF2A2; NbExp=2; IntAct=EBI-355371, EBI-1045262;
Q00987:MDM2; NbExp=1; IntAct=EBI-355371, EBI-389668;
P20265:POU3F2; NbExp=1; IntAct=EBI-355371, EBI-1167176;
P21675:TAF1; NbExp=1; IntAct=EBI-355371, EBI-491289;
P04637:TP53; NbExp=1; IntAct=EBI-355371, EBI-366083;
SUBCELLULAR LOCATION: Nucleus.
TISSUE SPECIFICITY: Widely expressed, with levels highest in the testis and ovary.
POLYMORPHISM: The poly-Gln region of TBP is highly polymorphic (25 to 42 repeats) in normal individuals and is expanded to about 47-63 repeats in spinocerebellar ataxia 17 (SCA17) patients.
DISEASE: Defects in TBP are the cause of spinocerebellar ataxia type 17 (SCA17) [MIM:607136]. Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA17 is an autosomal dominant cerebellar ataxia (ADCA) characterized by widespread cerebral and cerebellar atrophy, dementia and extrapyramidal signs. The molecular defect in SCA17 is the expansion of a CAG repeat in the coding region of TBP. Longer expansions result in earlier onset and more severe clinical manifestations of the disease.
SIMILARITY: Belongs to the TBP family.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=TBP";.

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

X54993; CAA38736.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M55654; AAA36731.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M34960; AAC03409.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456776; CAG33057.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL031259; CAA20286.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00022831; -.

A34830; TWHU2D.

NP_003185.1; -.

3D structure databases

PDB

1C9B; X-ray; 2.65 A; B/F/J/N/R=159-337.	[ExPASy / RCSB / EBI]
1CDW; X-ray; 1.90 A; A=159-337.	[ExPASy / RCSB / EBI]
1JFI; X-ray; 2.62 A; C=159-339.	[ExPASy / RCSB / EBI]
1NVP; X-ray; 2.10 A; A=159-339.	[ExPASy / RCSB / EBI]
1TGH; X-ray; 2.90 A; A=159-339.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1C9B; -.
1CDW; -.
1JFI; -.
1NVP; -.
1TGH; -.

ModBase

P20226.

Protein-protein interaction databases

DIP

DIP:1078N; -.

IntAct

P20226; 39.

Enzyme and pathway databases

Reactome

REACT_1788; Transcription.
REACT_6185; HIV Infection.
REACT_71; Gene Expression.

Organism-specific databases

GC06P170705; -.

HIX0032941; -.

HGNC:11588; TBP.

TBP.

CAB009442; -.

600075; gene. [NCBI / EBI]
607136; phenotype. [NCBI / EBI]

Orphanet

98759; Ataxia, spinocerebellar, type 17.
99; Autosomal dominant cerebellar ataxia.

PharmGKB

PA31224; -.

Gene expression databases

P20226; -.

P20226; -.

HS_TBP; -.

ENSG00000112592; Homo sapiens.

Ontologies

GO:0005672;	Cellular component: transcription factor TFIIA complex (inferred from direct assay from UniProtKB).
GO:0005669;	Cellular component: transcription factor TFIID complex (inferred from direct assay from UniProtKB).
GO:0003677;	Molecular function: DNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0016251;	Molecular function: general RNA polymerase II transcription factor activity (inferred by curator from UniProtKB).
GO:0008134;	Molecular function: transcription factor binding (inferred from physical interaction from UniProtKB).
GO:0008219;	Biological process: cell death (inferred from electronic annotation from UniProtKB-KW).
GO:0032568;	Biological process: general transcription from RNA polymerase II promoter (inferred from direct assay from UniProtKB).
GO:0044419;	Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0006355;	Biological process: regulation of transcription, DNA-dependent (inferred from electronic annotation from UniProtKB-KW).
GO:0006368;	Biological process: RNA elongation from RNA polymerase II promoter (inferred from experiment from Reactome).
GO:0006367;	Biological process: transcription initiation from RNA polymerase II promoter (inferred by curator from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR012295; b_Adaptin_TBP_C.
IPR000814; TBP.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.310.10; b_Adaptin_TBP_C; 2.

PANTHER

PTHR10126; TBP; 1.

Pfam

PF00352; TBP; 2.
Pfam graphical view of domain structure.

PRINTS

PR00686; TIFACTORIID.

PROSITE

PS00351; TFIID; 2.

Proteomic databases

PRIDE

P20226; -.

Genome annotation databases

Ensembl

ENSG00000112592; Homo sapiens. [Contig view]

GeneID

6908; -.

KEGG

hsa:6908; -.

Phylogenomic databases

HOGENOM

P20226; -.

HOVERGEN

P20226; -.

OMA

P20226; PMMPYGT.

Other

27015; -.

TBP; Homo sapiens.

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

Keywords

3D-structure; Disease mutation; DNA-binding; Host-virus interaction; Neurodegeneration; Nucleus; Polymorphism; Repeat; Spinocerebellar ataxia; Transcription; Transcription regulation; Triplet repeat expansion.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 339`	`339`	`TATA-box-binding protein.`	`PRO_0000153956`
`REPEAT`	`165 241`	`77`	`1.`
`REPEAT`	`255 332`	`78`	`2.`
`COMPBIAS`	`55 95`	`41`	`Poly-Gln.`
`VARIANT`	`92 95`	`4`	`Missing.`	`VAR_016987`
`CONFLICT`	`187 187`		`A -> R (in Ref. 3; AAC03409).`
`STRAND`	`164 173`	`10`
`HELIX`	`180 186`	`7`
`STRAND`	`190 192`	`3`
`TURN`	`194 196`	`3`
`STRAND`	`198 204`	`7`
`TURN`	`205 208`	`4`
`STRAND`	`209 213`	`5`
`STRAND`	`217 222`	`6`
`HELIX`	`227 244`	`18`
`STRAND`	`251 263`	`13`
`HELIX`	`270 276`	`7`
`TURN`	`277 280`	`4`
`TURN`	`285 287`	`3`
`STRAND`	`289 295`	`7`
`TURN`	`296 299`	`4`
`STRAND`	`300 304`	`5`
`STRAND`	`308 313`	`6`
`HELIX`	`318 333`	`16`

Sequence information

Length: 339 AA [This is the length of the unprocessed precursor]

Molecular weight: 37698 Da [This is the MW of the unprocessed precursor]

CRC64: A61A578D972B970B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDQNNSLPPY AQGLASPQGA MTPGIPIFSP MMPYGTGLTP QPIQNTNSLS ILEEQQRQQQ 

        70         80         90        100        110        120 
QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQAVAAA AVQQSTSQQA TQGTSGQAPQ 

       130        140        150        160        170        180 
LFHSQTLTTA PLPGTTPLYP SPMTPMTPIT PATPASESSG IVPQLQNIVS TVNLGCKLDL 

       190        200        210        220        230        240 
KTIALRARNA EYNPKRFAAV IMRIREPRTT ALIFSSGKMV CTGAKSEEQS RLAARKYARV 

       250        260        270        280        290        300 
VQKLGFPAKF LDFKIQNMVG SCDVKFPIRL EGLVLTHQQF SSYEPELFPG LIYRMIKPRI 

       310        320        330 
VLLIFVSGKV VLTGAKVRAE IYEAFENIYP ILKGFRKTT

P20226 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