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UniProtKB/Swiss-Prot entry O15409


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FOXP2_HUMAN
Primary accession number O15409
Secondary accession numbers Q6ZND1 Q75MJ3 Q8IZE0 Q8N0W2 Q8N6B7 Q8N6B8 Q8NFQ1 Q8NFQ2 Q8NFQ3 Q8NFQ4 Q8TD74
Integrated into Swiss-Prot on December 5, 2001
Sequence was last modified on December 5, 2001 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 81)
Name and origin of the protein
Protein name Forkhead box protein P2
Synonyms CAG repeat protein 44
Trinucleotide repeat-containing gene 10 protein
Gene name
Name: FOXP2
Synonyms: CAGH44, TNRC10
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] (ISOFORM 1), ALTERNATIVE SPLICING, AND VARIANT SPCH1 HIS-553.
DOI=10.1038/35097076; PubMed=11586359 [NCBI, ExPASy, EBI, Israel, Japan]
Lai C.S.L., Fisher S.E., Hurst J.A., Vargha-Khadem F., Monaco A.P.;
"A forkhead-domain gene is mutated in a severe speech and language disorder.";
Nature 413:519-523(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), NUCLEOTIDE SEQUENCE [MRNA] OF 1-415 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 259-715 (ISOFORM 6), AND TISSUE SPECIFICITY.
TISSUE=Brain, Corpus striatum, Fetal brain, and Frontal cortex;
DOI=10.1007/s00439-002-0768-5; PubMed=12189486 [NCBI, ExPASy, EBI, Israel, Japan]
Bruce H.A., Margolis R.L.;
"FOXP2: novel exons, splice variants, and CAG repeat length stability.";
Hum. Genet. 111:136-144(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
Vincent J.B., Scherer S.W.;
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Brain;
Guo J.H., Chen L., Yu L.;
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
TISSUE=Tongue;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature01782; PubMed=12853948 [NCBI, ExPASy, EBI, Israel, Japan]
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-304 (ISOFORM 1).
TISSUE=Brain cortex;
DOI=10.1007/s004390050476; PubMed=9225980 [NCBI, ExPASy, EBI, Israel, Japan]
Margolis R.L., Abraham M.R., Gatchell S.B., Li S.-H., Kidwai A.S., Breschel T.S., Stine O.C., Callahan C., McInnis M.G., Ross C.A.;
"cDNAs with long CAG trinucleotide repeats from human brain.";
Hum. Genet. 100:114-122(1997).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-329.
DOI=10.1038/nature01025; PubMed=12192408 [NCBI, ExPASy, EBI, Israel, Japan]
Enard W., Przeworski M., Fisher S.E., Lai C.S.L., Wiebe V., Kitano T., Monaco A.P., Paeaebo S.;
"Molecular evolution of FOXP2, a gene involved in speech and language.";
Nature 418:869-872(2002).
[9]
DEVELOPMENTAL STAGE.
DOI=10.1523/JNEUROSCI.5589-03.2004; PubMed=15056695 [NCBI, ExPASy, EBI, Israel, Japan]
Teramitsu I., Kudo L.C., London S.E., Geschwind D.H., White S.A.;
"Parallel FoxP1 and FoxP2 expression in songbird and human brain predicts functional interaction.";
J. Neurosci. 24:3152-3163(2004).
Comments
  • FUNCTION: Transcriptional repressor that may play a role in the specification and differentiation of lung epithelium. May also play a role in developing neural, gastrointestinal and cardiovascular tissues. Can act with CTBP1 to synergistically repress transcription but CTPBP1 is not essential. Involved in neural mechanisms mediating the development of speech and language.
  • SUBUNIT: Forms homodimers and heterodimers with FOXP1 and FOXP4. Dimerization is required for DNA-binding. Interacts with CTBP1 (By similarity).
  • SUBCELLULAR LOCATION: Nucleus (Probable).
  • ALTERNATIVE PRODUCTS: 8 named isoforms [FASTA] produced by alternative splicing.
    Name1
    SynonymsI
    Isoform IDO15409-1
    This is the isoform sequence displayed in this entry.
    Name2
    SynonymsII
    Isoform IDO15409-3
    The sequence of this isoform is not described.
    Name3
    SynonymsIII, IV
    Isoform IDO15409-2
    Features which should be applied to build the isoform sequence: VSP_001558.
    Name4
    Isoform IDO15409-4
    Features which should be applied to build the isoform sequence: VSP_011532.
    Name5
    Isoform IDO15409-5
    Features which should be applied to build the isoform sequence: VSP_011532, VSP_011535, VSP_011536.
    Name6
    SynonymsFOXP2-S
    Isoform IDO15409-6
    Features which should be applied to build the isoform sequence: VSP_011538, VSP_011539.
    Name7
    Isoform IDO15409-7
    Features which should be applied to build the isoform sequence: VSP_011537.
    Name8
    Isoform IDO15409-8
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_011533, VSP_011534.
  • TISSUE SPECIFICITY: Isoform 1 and isoform 6 are expressed in adult and fetal brain, caudate nucleus and lung.
  • DEVELOPMENTAL STAGE: Expressed in the brain at 15 and 22 weeks of gestation, with a pattern of strong cortical, basal ganglia, thalamic and cerebellar expression. Highly expressed in the head and tail of nucleus caudatus and putamen. Restricted expression within the globus pallidus, with high levels in the pars interna, which provides the principal source of output from the basal ganglia to the nucleus centrum medianum thalami (CM) and the major motor relay nuclei of the thalamus. In the thalamus, present in the CM and nucleus medialis dorsalis thalami. Lower levels are observed in the nuclei anterior thalami, dorsal and ventral, and the nucleus parafascicularis thalami. Expressed in the ventrobasal complex comprising the nucleus ventralis posterior lateralis/medialis. The ventral tier of the thalamus exhibits strong expression, including nuclei ventralis anterior, lateralis and posterior lateralis pars oralis. Also expressed in the nucleus subthalamicus bilaterally and in the nucleus ruber.
  • DOMAIN: The leucine-zipper is required for dimerization and transcriptional repression (By similarity).
  • DISEASE: Defects in FOXP2 are the cause of speech-language disorder 1 (SPCH1) [MIM:602081]; also known as autosomal dominant speech and language disorder with orofacial dyspraxia. Affected individuals have a severe impairment in the selection and sequencing of fine orofacial movements, which are necessary for articulation. They also show deficits in several facets of language processing (such as the ability to break up words into their constituent phonemes) and grammatical skills.
  • DISEASE: A chromosomal aberration disrupting FOXP2 is a cause of severe speech and language impairment. Translocation t(5;7)(q22;q31.2).
  • SIMILARITY: Contains 1 C2H2-type zinc finger.
  • SIMILARITY: Contains 1 fork-head DNA-binding domain.
  • WEB RESOURCE: Name=Protein Spotlight; Note=Talking heads - Issue 51 of October 2004; URL="http://www.expasy.org/spotlight/back_issues/sptlt051.shtml";.
  • WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=FOXP2";.
  • WEB RESOURCE: Name=Wikipedia; Note=FOXP2 entry; URL="http://en.wikipedia.org/wiki/FOXP2";.
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
AF337817; AAL10762.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF467252; AAM60762.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF467253; AAM60763.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF467254; AAM60764.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF467255; AAM60765.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF467256; AAM60766.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF467257; AAM60767.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF493430; AAM13672.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY144615; AAN60016.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK131266; BAD18444.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC003992; AAS07399.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC020606; AAS07502.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U80741; AAB91439.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF515031; AAN03389.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF515032; AAN03390.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF515033; AAN03391.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF515034; AAN03392.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF515035; AAN03393.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF515036; AAN03394.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF515037; AAN03395.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF515038; AAN03396.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF515039; AAN03397.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF515040; AAN03398.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF515041; AAN03399.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF515042; AAN03400.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF515043; AAN03401.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF515044; AAN03402.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF515045; AAN03403.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF515046; AAN03404.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF515047; AAN03405.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF515048; AAN03406.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF515049; AAN03407.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF515050; AAN03408.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_055306.1; -.
UniGene Hs.656280
3D structure databases
PDB
2A07; X-ray; 1.90 A; F/G/H/I=503-594, J/K=502-594.[ExPASy / RCSB / EBI]
2AS5; X-ray; 2.70 A; F/G=503-594.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2A07; -.
2AS5; -.
ModBase O15409.
Protein-protein interaction databases
DIP DIP:29004N; -.
IntAct O15409; -.
Organism-specific databases
H-InvDB HIX0033530; -.
HGNC HGNC:13875; FOXP2.
GenAtlas FOXP2.
HPA CAB011488; -.
HPA000382; -.
HPA000383; -.
MIM 602081; phenotype. [NCBI / EBI]
605317; gene. [NCBI / EBI]
PharmGKB PA28242; -.
GeneCards O15409.
Gene expression databases
ArrayExpress O15409; -.
GermOnline ENSG00000128573; Homo sapiens.
Ontologies
GO
GO:0003677; Molecular function: DNA binding (inferred from direct assay from UniProtKB).
GO:0042803; Molecular function: protein homodimerization activity (inferred from direct assay from UniProtKB).
GO:0021757; Biological process: caudate nucleus development (inferred from mutant phenotype from UniProtKB).
GO:0021758; Biological process: putamen development (inferred from mutant phenotype from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR001766; TF_Fork_head.
IPR011991; Wing_hlx_DNA_bd.
IPR007087; Znf_C2H2.
IPR015880; Znf_C2H2-like.
Graphical view of domain structure.
Gene3D G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
PANTHER PTHR11829; Fork_box_protein; 1.
Pfam PF00250; Fork_head; 1.
Pfam graphical view of domain structure.
PRINTS PR00053; FORKHEAD.
ProDom PD000425; TF_Fork_head; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00339; FH; 1.
SM00355; ZnF_C2H2; 1.
SMART graphical view of domain structure.
PROSITE PS00657; FORK_HEAD_1; FALSE_NEG.
PS00658; FORK_HEAD_2; 1.
PS50039; FORK_HEAD_3; 1.
PS00028; ZINC_FINGER_C2H2_1; 1.
PS50157; ZINC_FINGER_C2H2_2; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).
BLOCKS O15409.
Genome annotation databases
Ensembl ENSG00000128573; Homo sapiens. [Contig view]
GeneID 93986; -.
KEGG hsa:93986; -.
Phylogenomic databases
HOVERGEN O15409; -.
Other
SOURCE FOXP2; Homo sapiens.
ProtoNet O15409.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Chromosomal rearrangement; Coiled coil; Disease mutation; DNA-binding; Metal-binding; Nucleus; Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   715  715     Forkhead box protein P2. PRO_0000091879
DOMAIN   388   409  22     Leucine-zipper. 
ZN_FING   346   371  26     C2H2-type. 
DNA_BIND   504   594  91     Fork-head. 
REGION   422   426  5     CTBP1-binding (By similarity). 
COILED   117   231  115     Potential. 
COILED   376   409  34     Potential. 
COMPBIAS   53    56  4     Poly-Gln. 
COMPBIAS   123   126  4     Poly-Gln. 
COMPBIAS   131   136  6     Poly-Gln. 
COMPBIAS   152   191  40     Poly-Gln. 
COMPBIAS   200   209  10     Poly-Gln. 
COMPBIAS   223   231  9     Poly-Gln. 
VAR_SEQ   1    92        Missing (in isoform 3). VSP_001558
VAR_SEQ   86    86        Q -> QELLPETKLCICGHSSGDGHPHNTFA (in isoform 4 and isoform 5). VSP_011532
VAR_SEQ   87    87        V -> P (in isoform 8). VSP_011533
VAR_SEQ   88   715        Missing (in isoform 8). VSP_011534
VAR_SEQ   133   143        QQLQEFYKKQQ -> VMWVTCFGVLA (in isoform 5). VSP_011535
VAR_SEQ   144   715        Missing (in isoform 5). VSP_011536
VAR_SEQ   366   715        Missing (in isoform 7). VSP_011537
VAR_SEQ   423   432        LNLVSSVTMS -> VSAYCFINSK (in isoform 6). VSP_011538
VAR_SEQ   433   715        Missing (in isoform 6). VSP_011539
VARIANT   553   553  1     R -> H (in SPCH1). VAR_012278 [3D]
CONFLICT   29    29        A -> V (in Ref. 2; AAM60762). 
CONFLICT   134   134        Q -> H (in Ref. 7). 
CONFLICT   290   304        DLTTNNSSSTTSSNT -> EEFPVQGPAAVCAGL (in Ref. 7). 
CONFLICT   414   414        S -> L (in Ref. 2; AAM60766). 
HELIX   509   518  10      
HELIX   527   543  17      
TURN   544   547  4      
HELIX   548   558  11      
STRAND   562   566  5      
STRAND   568   575  8      
HELIX   577   580  4      
Sequence information
Length: 715 AA [This is the length of the unprocessed precursor] Molecular weight: 79919 Da [This is the MW of the unprocessed precursor] CRC64: 4F9FBDB6D90516E0 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MMQESATETI SNSSMNQNGM STLSSQLDAG SRDGRSSGDT SSEVSTVELL HLQQQQALQA 

        70         80         90        100        110        120 
ARQLLLQQQT SGLKSPKSSD KQRPLQVPVS VAMMTPQVIT PQQMQQILQQ QVLSPQQLQA 

       130        140        150        160        170        180 
LLQQQQAVML QQQQLQEFYK KQQEQLHLQL LQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ 

       190        200        210        220        230        240 
QQQQQQQQQQ QHPGKQAKEQ QQQQQQQQQL AAQQLVFQQQ LLQMQQLQQQ QHLLSLQRQG 

       250        260        270        280        290        300 
LISIPPGQAA LPVQSLPQAG LSPAEIQQLW KEVTGVHSME DNGIKHGGLD LTTNNSSSTT 

       310        320        330        340        350        360 
SSNTSKASPP ITHHSIVNGQ SSVLSARRDS SSHEETGASH TLYGHGVCKW PGCESICEDF 

       370        380        390        400        410        420 
GQFLKHLNNE HALDDRSTAQ CRVQMQVVQQ LEIQLSKERE RLQAMMTHLH MRPSEPKPSP 

       430        440        450        460        470        480 
KPLNLVSSVT MSKNMLETSP QSLPQTPTTP TAPVTPITQG PSVITPASVP NVGAIRRRHS 

       490        500        510        520        530        540 
DKYNIPMSSE IAPNYEFYKN ADVRPPFTYA TLIRQAIMES SDRQLTLNEI YSWFTRTFAY 

       550        560        570        580        590        600 
FRRNAATWKN AVRHNLSLHK CFVRVENVKG AVWTVDEVEY QKRRSQKITG SPTLVKNIPT 

       610        620        630        640        650        660 
SLGYGAALNA SLQAALAESS LPLLSNPGLI NNASSGLLQA VHEDLNGSLD HIDSNGNSSP 

       670        680        690        700        710 
GCSPQPHIHS IHVKEEPVIA EDEDCPMSLV TTANHSPELE DDREIEEEPL SEDLE 

O15409 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

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