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O15409 (FOXP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Forkhead box protein P2
Alternative name(s):
CAG repeat protein 44
Trinucleotide repeat-containing gene 10 protein
Gene names
Name:FOXP2
Synonyms:CAGH44, TNRC10
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length715 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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. Plays a role in synapse formation by regulating SRPX2 levels. Involved in neural mechanisms mediating the development of speech and language.

Subunit structure

Forms homodimers and heterodimers with FOXP1 and FOXP4. Dimerization is required for DNA-binding. Interacts with CTBP1 By similarity.

Subcellular location

Nucleus Probable.

Tissue specificity

Isoform 1 and isoform 6 are expressed in adult and fetal brain, caudate nucleus and lung. Ref.2

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. Ref.12

Domain

The leucine-zipper is required for dimerization and transcriptional repression By similarity.

Involvement in disease

Speech-language disorder 1 (SPCH1) [MIM:602081]: A disorder characterized by severe orofacial dyspraxia resulting in largely incomprehensible speech. Affected individuals have severe impairment in the selection and sequencing of fine orofacial movements which are necessary for articulation, and deficits in several facets of grammatical skills and language processing, such as the ability to break up words into their constituent phonemes.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1

A chromosomal aberration involving FOXP2 is a cause of severe speech and language impairment. Translocation t(5;7)(q22;q31.2).

Sequence similarities

Contains 1 C2H2-type zinc finger.

Contains 1 fork-head DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
   DiseaseDisease mutation
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionRepressor
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcamera-type eye development

Inferred from Biological aspect of Ancestor. Source: RefGenome

caudate nucleus development

Inferred from mutant phenotype PubMed 11872605. Source: UniProtKB

cerebellum development

Inferred from Biological aspect of Ancestor. Source: RefGenome

cerebral cortex development

Inferred from expression pattern PubMed 18987363. Source: BHF-UCL

embryo development

Inferred from Biological aspect of Ancestor. Source: RefGenome

growth

Inferred from Biological aspect of Ancestor. Source: RefGenome

lung alveolus development

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 18987363. Source: BHF-UCL

pattern specification process

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of epithelial cell proliferation involved in lung morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of mesenchymal cell proliferation

Inferred from Biological aspect of Ancestor. Source: RefGenome

post-embryonic development

Inferred from Biological aspect of Ancestor. Source: RefGenome

putamen development

Inferred from mutant phenotype PubMed 11872605. Source: UniProtKB

righting reflex

Inferred from Biological aspect of Ancestor. Source: RefGenome

skeletal muscle tissue development

Inferred from Biological aspect of Ancestor. Source: RefGenome

smooth muscle tissue development

Inferred from Biological aspect of Ancestor. Source: RefGenome

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

vocal learning

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentcytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from direct assay PubMed 16407075. Source: UniProtKB

DNA binding, bending

Inferred from Biological aspect of Ancestor. Source: RefGenome

chromatin binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein heterodimerization activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein homodimerization activity

Inferred from direct assay PubMed 16407075. Source: UniProtKB

sequence-specific DNA binding

Inferred from direct assay PubMed 18987363. Source: BHF-UCL

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 18987363. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O15409-1)

Also known as: I;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O15409-3)

Also known as: II;

The sequence of this isoform is not available.
Isoform 3 (identifier: O15409-2)

Also known as: III; IV;

The sequence of this isoform differs from the canonical sequence as follows:
     1-92: Missing.
Isoform 4 (identifier: O15409-4)

The sequence of this isoform differs from the canonical sequence as follows:
     86-86: Q → QELLPETKLCICGHSSGDGHPHNTFA
Isoform 5 (identifier: O15409-5)

The sequence of this isoform differs from the canonical sequence as follows:
     86-86: Q → QELLPETKLCICGHSSGDGHPHNTFA
     133-143: QQLQEFYKKQQ → VMWVTCFGVLA
     144-715: Missing.
Isoform 6 (identifier: O15409-6)

Also known as: FOXP2-S;

The sequence of this isoform differs from the canonical sequence as follows:
     423-432: LNLVSSVTMS → VSAYCFINSK
     433-715: Missing.
Isoform 7 (identifier: O15409-7)

The sequence of this isoform differs from the canonical sequence as follows:
     366-715: Missing.
Isoform 8 (identifier: O15409-8)

The sequence of this isoform differs from the canonical sequence as follows:
     87-87: V → P
     88-715: Missing.
Note: No experimental confirmation available.
Isoform 9 (identifier: O15409-9)

The sequence of this isoform differs from the canonical sequence as follows:
     132-132: Q → QDFLDSGLENFRAALEKN
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 715715Forkhead box protein P2
PRO_0000091879

Regions

Zinc finger346 – 37126C2H2-type
DNA binding504 – 59491Fork-head
Region388 – 40922Leucine-zipper
Region422 – 4265CTBP1-binding By similarity
Compositional bias53 – 268216Gln-rich

Natural variations

Alternative sequence1 – 9292Missing in isoform 3.
VSP_001558
Alternative sequence861Q → QELLPETKLCICGHSSGDGH PHNTFA in isoform 4 and isoform 5.
VSP_011532
Alternative sequence871V → P in isoform 8.
VSP_011533
Alternative sequence88 – 715628Missing in isoform 8.
VSP_011534
Alternative sequence1321Q → QDFLDSGLENFRAALEKN in isoform 9.
VSP_043464
Alternative sequence133 – 14311QQLQEFYKKQQ → VMWVTCFGVLA in isoform 5.
VSP_011535
Alternative sequence144 – 715572Missing in isoform 5.
VSP_011536
Alternative sequence366 – 715350Missing in isoform 7.
VSP_011537
Alternative sequence423 – 43210LNLVSSVTMS → VSAYCFINSK in isoform 6.
VSP_011538
Alternative sequence433 – 715283Missing in isoform 6.
VSP_011539
Natural variant5531R → H in SPCH1. Ref.1
VAR_012278

Experimental info

Sequence conflict291A → V in AAM60762. Ref.2
Sequence conflict1341Q → H in AAB91439. Ref.10
Sequence conflict290 – 30415DLTTN…TSSNT → EEFPVQGPAAVCAGL in AAB91439. Ref.10
Sequence conflict4141S → L in AAM60766. Ref.2

Secondary structure

............ 715
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (I) [UniParc].

Last modified December 5, 2001. Version 2.
Checksum: 4F9FBDB6D90516E0

FASTA71579,919
        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 

« Hide

Isoform 2 (II) (Sequence not available).
Isoform 3 (III) (IV) [UniParc].

Checksum: F78EA67F33A3AE05
Show »

FASTA62370,104
Isoform 4 [UniParc].

Checksum: 423EC421368FCD94
Show »

FASTA74082,565
Isoform 5 [UniParc].

Checksum: 61B297B4D64BC670
Show »

FASTA16818,315
Isoform 6 (FOXP2-S) [UniParc].

Checksum: 42BC7890ACAF498C
Show »

FASTA43248,764
Isoform 7 [UniParc].

Checksum: 0B052282E2E30771
Show »

FASTA36540,969
Isoform 8 [UniParc].

Checksum: 624274B876E062E4
Show »

FASTA879,377
Isoform 9 [UniParc].

Checksum: 8B72F946ABD821EE
Show »

FASTA73281,840

References

« Hide 'large scale' references
[1]"A forkhead-domain gene is mutated in a severe speech and language disorder."
Lai C.S.L., Fisher S.E., Hurst J.A., Vargha-Khadem F., Monaco A.P.
Nature 413:519-523(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, VARIANT SPCH1 HIS-553.
[2]"FOXP2: novel exons, splice variants, and CAG repeat length stability."
Bruce H.A., Margolis R.L.
Hum. Genet. 111:136-144(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), NUCLEOTIDE SEQUENCE [MRNA] OF 1-415 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 259-715 (ISOFORM 6), TISSUE SPECIFICITY.
Tissue: Brain, Corpus striatum, Fetal brain and Frontal cortex.
[3]Vincent J.B., Scherer S.W.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
[4]Guo J.H., Chen L., Yu L.
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Brain.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 8 AND 9).
Tissue: Tongue.
[6]"The DNA sequence of human chromosome 7."
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. expand/collapse author list , 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.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain.
[10]"cDNAs with long CAG trinucleotide repeats from human brain."
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.
Hum. Genet. 100:114-122(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-304 (ISOFORM 1).
Tissue: Brain cortex.
[11]"Molecular evolution of FOXP2, a gene involved in speech and language."
Enard W., Przeworski M., Fisher S.E., Lai C.S.L., Wiebe V., Kitano T., Monaco A.P., Paeaebo S.
Nature 418:869-872(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-329.
[12]"Parallel FoxP1 and FoxP2 expression in songbird and human brain predicts functional interaction."
Teramitsu I., Kudo L.C., London S.E., Geschwind D.H., White S.A.
J. Neurosci. 24:3152-3163(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Web resources

Protein Spotlight

Talking heads - Issue 51 of October 2004

GeneReviews
Wikipedia

FOXP2 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF337817 mRNA. Translation: AAL10762.1.
AF467252 mRNA. Translation: AAM60762.1.
AF467253 mRNA. Translation: AAM60763.1.
AF467254 mRNA. Translation: AAM60764.1.
AF467255 mRNA. Translation: AAM60765.1.
AF467256 mRNA. Translation: AAM60766.1.
AF467257 mRNA. Translation: AAM60767.1.
AF493430 mRNA. Translation: AAM13672.1.
AY144615 mRNA. Translation: AAN60016.1.
AK131266 mRNA. Translation: BAD18444.1. Sequence problems.
AK296957 mRNA. Translation: BAG59501.1.
AC003992 Genomic DNA. Translation: AAS07399.1.
AC020606 Genomic DNA. Translation: AAS07502.1.
AC073626 Genomic DNA. No translation available.
AC074000 Genomic DNA. No translation available.
AC092148 Genomic DNA. No translation available.
AC092606 Genomic DNA. No translation available.
CH236947 Genomic DNA. Translation: EAL24367.1.
CH236947 Genomic DNA. Translation: EAL24369.1.
CH471070 Genomic DNA. Translation: EAW83484.1.
CH471070 Genomic DNA. Translation: EAW83486.1.
BC126104 mRNA. Translation: AAI26105.1.
BC143866 mRNA. Translation: AAI43867.1.
U80741 mRNA. Translation: AAB91439.1.
AF515031 Genomic DNA. Translation: AAN03389.1.
AF515032 Genomic DNA. Translation: AAN03390.1.
AF515033 Genomic DNA. Translation: AAN03391.1.
AF515034 Genomic DNA. Translation: AAN03392.1.
AF515035 Genomic DNA. Translation: AAN03393.1.
AF515036 Genomic DNA. Translation: AAN03394.1.
AF515037 Genomic DNA. Translation: AAN03395.1.
AF515038 Genomic DNA. Translation: AAN03396.1.
AF515039 Genomic DNA. Translation: AAN03397.1.
AF515040 Genomic DNA. Translation: AAN03398.1.
AF515041 Genomic DNA. Translation: AAN03399.1.
AF515042 Genomic DNA. Translation: AAN03400.1.
AF515043 Genomic DNA. Translation: AAN03401.1.
AF515044 Genomic DNA. Translation: AAN03402.1.
AF515045 Genomic DNA. Translation: AAN03403.1.
AF515046 Genomic DNA. Translation: AAN03404.1.
AF515047 Genomic DNA. Translation: AAN03405.1.
AF515048 Genomic DNA. Translation: AAN03406.1.
AF515049 Genomic DNA. Translation: AAN03407.1.
AF515050 Genomic DNA. Translation: AAN03408.1.
RefSeqNP_001166237.1. NM_001172766.2.
NP_001166238.1. NM_001172767.2.
NP_055306.1. NM_014491.3.
NP_683696.2. NM_148898.3.
NP_683697.2. NM_148899.3.
NP_683698.2. NM_148900.3.
UniGeneHs.282787.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2A07X-ray1.90F/G/H/I/J/K503-594[»]
2AS5X-ray2.70F/G503-594[»]
ProteinModelPortalO15409.
SMRO15409. Positions 351-409, 503-584.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125073. 6 interactions.
DIPDIP-29004N.
IntActO15409. 1 interaction.

PTM databases

PhosphoSiteO15409.

Proteomic databases

PaxDbO15409.
PRIDEO15409.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000350908; ENSP00000265436; ENSG00000128573. [O15409-1]
ENST00000360232; ENSP00000353367; ENSG00000128573. [O15409-6]
ENST00000378237; ENSP00000367482; ENSG00000128573. [O15409-7]
ENST00000393489; ENSP00000377129; ENSG00000128573. [O15409-2]
ENST00000393494; ENSP00000377132; ENSG00000128573. [O15409-1]
ENST00000403559; ENSP00000385069; ENSG00000128573. [O15409-9]
ENST00000408937; ENSP00000386200; ENSG00000128573. [O15409-4]
ENST00000412402; ENSP00000405470; ENSG00000128573. [O15409-8]
ENST00000441290; ENSP00000416825; ENSG00000128573. [O15409-8]
GeneID93986.
KEGGhsa:93986.
UCSCuc003vgv.1. human. [O15409-7]
uc003vgw.3. human. [O15409-5]
uc003vgx.2. human. [O15409-1]
uc003vgz.3. human. [O15409-4]
uc003vhd.3. human. [O15409-6]
uc011kmu.2. human. [O15409-9]

Organism-specific databases

CTD93986.
GeneCardsGC07P113649.
HGNCHGNC:13875. FOXP2.
HPACAB011488.
HPA000382.
HPA000383.
MIM602081. phenotype.
605317. gene.
neXtProtNX_O15409.
Orphanet251061. 7q31 microdeletion syndrome.
209908. Childhood apraxia of speech.
PharmGKBPA28242.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5025.
HOGENOMHOG000092089.
HOVERGENHBG051657.
KOK09409.
OMAPETKLCV.
OrthoDBEOG7M6D7G.
PhylomeDBO15409.
TreeFamTF326978.

Gene expression databases

ArrayExpressO15409.
BgeeO15409.
GenevestigatorO15409.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR001766. TF_fork_head.
IPR018122. TF_fork_head_CS.
IPR011991. WHTH_DNA-bd_dom.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamPF00250. Fork_head. 1 hit.
[Graphical view]
PRINTSPR00053. FORKHEAD.
SMARTSM00339. FH. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]
PROSITEPS00658. FORK_HEAD_2. 1 hit.
PS50039. FORK_HEAD_3. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFOXP2. human.
EvolutionaryTraceO15409.
GeneWikiFOXP2.
GenomeRNAi93986.
NextBio78260.
PROO15409.
SOURCESearch...

Entry information

Entry nameFOXP2_HUMAN
AccessionPrimary (citable) accession number: O15409
Secondary accession number(s): A0AUV6 expand/collapse secondary AC list , A4D0U8, A6NNW4, B4DLD9, Q6ZND1, Q75MJ3, Q8IZE0, Q8N0W2, Q8N6B7, Q8N6B8, Q8NFQ1, Q8NFQ2, Q8NFQ3, Q8NFQ4, Q8TD74
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: December 5, 2001
Last modified: April 16, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM