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Q8MJA0 (FOXP2_PANTR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Forkhead box protein P2
Gene names
Name:FOXP2
OrganismPan troglodytes (Chimpanzee) [Reference proteome]
Taxonomic identifier9598 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePan

Protein attributes

Sequence length716 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

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.

Domain

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

Sequence similarities

Contains 1 C2H2-type zinc finger.

Contains 1 fork-head DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionRepressor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcamera-type eye development

Inferred from Biological aspect of Ancestor. Source: RefGenome

caudate nucleus development

Inferred from sequence or structural similarity. Source: UniProtKB

cerebellum development

Inferred from Biological aspect of Ancestor. Source: RefGenome

cerebral cortex development

Inferred from Biological aspect of Ancestor. Source: RefGenome

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 electronic annotation. Source: Ensembl

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 sequence or structural similarity. 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 sequence or structural similarity. 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 sequence or structural similarity. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 716716Forkhead box protein P2
PRO_0000091884

Regions

Zinc finger347 – 37226C2H2-type
DNA binding505 – 59591Fork-head
Region389 – 41022Leucine-zipper
Region423 – 4275CTBP1-binding By similarity
Compositional bias53 – 269217Gln-rich

Sequences

Sequence LengthMass (Da)Tools
Q8MJA0 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 3169A2786B42F79F

FASTA71680,061
        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 QQHPGKQAKE QQQQQQQQQQ LAAQQLVFQQ QLLQMQQLQQ QQHLLSLQRQ 

       250        260        270        280        290        300 
GLISIPPGQA ALPVQSLPQA GLSPAEIQQL WKEVTGVHSM EDNGIKHGGL DLTTNNSSST 

       310        320        330        340        350        360 
TSSTTSKASP PITHHSIVNG QSSVLNARRD SSSHEETGAS HTLYGHGVCK WPGCESICED 

       370        380        390        400        410        420 
FGQFLKHLNN EHALDDRSTA QCRVQMQVVQ QLEIQLSKER ERLQAMMTHL HMRPSEPKPS 

       430        440        450        460        470        480 
PKPLNLVSSV TMSKNMLETS PQSLPQTPTT PTAPVTPITQ GPSVITPASV PNVGAIRRRH 

       490        500        510        520        530        540 
SDKYNIPMSS EIAPNYEFYK NADVRPPFTY ATLIRQAIME SSDRQLTLNE IYSWFTRTFA 

       550        560        570        580        590        600 
YFRRNAATWK NAVRHNLSLH KCFVRVENVK GAVWTVDEVE YQKRRSQKIT GSPTLVKNIP 

       610        620        630        640        650        660 
TSLGYGAALN ASLQAALAES SLPLLSNPGL INNASSGLLQ AVHEDLNGSL DHIDSNGNSS 

       670        680        690        700        710 
PGCSPQPHIH SIHVKEEPVI AEDEDCPMSL VTTANHSPEL EDDREIEEEP LSEDLE 

« Hide

References

[1]"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 / MRNA].
[2]"Accelerated protein evolution and origins of human-specific features: Foxp2 as an example."
Zhang J., Webb D.M., Podlaha O.
Genetics 162:1825-1835(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The FOXP2 gene, implicated in language development, is conserved in mammalian evolution."
Walter N.A.R., Thompson J., McGoldrick D.J., Messier W.
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Tissue: Blood.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF512947 mRNA. Translation: AAN03385.1.
AF515051 Genomic DNA. Translation: AAN03409.1.
AF515052 Genomic DNA. Translation: AAN03410.1.
AY143178 mRNA. Translation: AAN60056.1.
AY064549 mRNA. Translation: AAL57735.1.
AY064565 expand/collapse EMBL AC list , AY064551, AY064552, AY064553, AY064554, AY064555, AY064556, AY064557, AY064558, AY064559, AY064560, AY064561, AY064562, AY064563, AY064564 Genomic DNA. Translation: AAL57731.1.
RefSeqNP_001009020.1. NM_001009020.2.
UniGenePtr.6303.

3D structure databases

ProteinModelPortalQ8MJA0.
SMRQ8MJA0. Positions 504-585.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSPTRT00000036314; ENSPTRP00000033573; ENSPTRG00000019608.
GeneID449627.
KEGGptr:449627.

Organism-specific databases

CTD93986.

Phylogenomic databases

eggNOGCOG5025.
GeneTreeENSGT00750000117475.
HOGENOMHOG000092089.
HOVERGENHBG051657.
KOK09409.
OMAPETKLCV.
OrthoDBEOG7M6D7G.
TreeFamTF326978.

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

NextBio20832734.

Entry information

Entry nameFOXP2_PANTR
AccessionPrimary (citable) accession number: Q8MJA0
Secondary accession number(s): Q8MHX3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 21, 2003
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families