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P58462 (FOXP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Forkhead box protein P1
Alternative name(s):
Forkhead-related transcription factor 1
Gene names
Name:Foxp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length705 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional repressor that plays an important role in the specification and differentiation of lung epithelium. Can act with CTBP1 to synergistically repress transcription but CTPBP1 is not essential. Essential transcriptional regulator of B-cell development. Ref.5 Ref.6

Subunit structure

Forms homodimers and heterodimers with FOXP2 and FOXP4. Dimerization is required for DNA-binding. Interacts with CTBP1. Ref.5

Subcellular location

Nucleus Probable.

Tissue specificity

Highest expression in the lung, brain, and spleen. Lower expression in heart, skeletal muscle, kidney, small intestine (isoform 3 not present) and liver.

Developmental stage

Expressed in developing lung, neural, intestinal and cardiovascular tissues. Expressed in both the airway epithelium of the forming lung as well as in the surrounding mesenchyme. By 16.5 dpc, expressed throughout the conducting airway epithelium, with highest expression in the distal alveolar regions. Also expressed in the endotheial cells of the pulmonary vasculature. During intestinal development, expressed in the mucosal layer but absent from the epithelium at 12.5 dpc. By 16.5 dpc, expressed in both the inner circular and outer longitudinal muscular layers of the intestine as well as in the epithelium of the intestine and developing stomach. Ref.4

Domain

The leucine-zipper is required for dimerization and transcriptional repression. Ref.5

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 initiation
Alternative splicing
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionRepressor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac muscle cell differentiation

Inferred from mutant phenotype PubMed 15342473. Source: MGI

cardiovascular system development

Inferred from mutant phenotype PubMed 20457810. Source: MGI

heart development

Inferred from mutant phenotype PubMed 15342473PubMed 20457810. Source: MGI

immunoglobulin V(D)J recombination

Inferred from mutant phenotype Ref.6. Source: MGI

in utero embryonic development

Inferred from mutant phenotype PubMed 20457810. Source: MGI

lung development

Inferred from genetic interaction PubMed 17428829. Source: MGI

lung secretory cell differentiation

Inferred from genetic interaction PubMed 22675208. Source: MGI

motor neuron axon guidance

Inferred from mutant phenotype PubMed 20711475. Source: UniProtKB

negative regulation of lung goblet cell differentiation

Inferred from genetic interaction PubMed 22675208. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.5PubMed 17428829PubMed 20713518. Source: MGI

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.1. Source: MGI

pattern specification process

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of cardiac muscle cell differentiation

Inferred from mutant phenotype PubMed 20713518. Source: MGI

positive regulation of epithelial cell proliferation

Inferred from genetic interaction PubMed 17428829. Source: MGI

positive regulation of immunoglobulin production

Inferred from mutant phenotype Ref.6. Source: MGI

positive regulation of mesenchymal cell proliferation

Inferred from genetic interaction PubMed 17428829. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 20713518. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 20711475. Source: UniProtKB

pre-B cell differentiation

Inferred from mutant phenotype Ref.6. Source: MGI

regulation of cardiac muscle cell proliferation

Inferred from mutant phenotype PubMed 20713518. Source: MGI

regulation of lung goblet cell differentiation

Inferred from genetic interaction PubMed 22675208. Source: MGI

sarcomere organization

Inferred from genetic interaction PubMed 20457810. Source: MGI

skeletal muscle tissue development

Inferred from genetic interaction PubMed 17428829. Source: MGI

smooth muscle tissue development

Inferred from genetic interaction PubMed 17428829. Source: MGI

transcription from RNA polymerase II promoter

Inferred from direct assay Ref.6. Source: GOC

ventral spinal cord development

Inferred from expression pattern PubMed 20711475. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleus

Inferred from direct assay Ref.6PubMed 19797899PubMed 23610558. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay Ref.5. Source: MGI

DNA binding, bending

Inferred from Biological aspect of Ancestor. Source: RefGenome

RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.6. Source: MGI

chromatin binding

Inferred from direct assay PubMed 18347093. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.5. Source: UniProtKB

protein heterodimerization activity

Inferred from physical interaction Ref.5. Source: MGI

protein homodimerization activity

Inferred from physical interaction Ref.5. Source: MGI

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 17428829PubMed 19797899. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]
Isoform 1 (identifier: P58462-1)

Also known as: A;

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: P58462-2)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     539-602: Missing.
Isoform 3 (identifier: P58462-3)

Also known as: C;

The sequence of this isoform differs from the canonical sequence as follows:
     1-250: Missing.
Note: Produced by alternative initiation at Met-251 of isoform 1.
Isoform 4 (identifier: P58462-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-130: Missing.
Note: Produced by alternative splicing. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 705705Forkhead box protein P1
PRO_0000009336

Regions

Zinc finger334 – 35926C2H2-type
DNA binding493 – 58391Fork-head
Region376 – 39722Leucine-zipper
Region410 – 4145CTBP1-binding
Compositional bias55 – 258204Gln-rich

Natural variations

Alternative sequence1 – 250250Missing in isoform 3.
VSP_018732
Alternative sequence1 – 130130Missing in isoform 4.
VSP_026670
Alternative sequence539 – 60264Missing in isoform 2.
VSP_001557

Experimental info

Mutagenesis3881Missing: Loss of dimerization. Almost complete loss of DNA-binding. Reduced transcriptional repression activity. Ref.5
Mutagenesis410 – 4145PLNLV → AANAA: No significant effect on transcriptional repression activity. Ref.5
Sequence conflict61 – 9232Missing in AAH64764. Ref.3
Sequence conflict1991E → EQ in BAC28249. Ref.2
Sequence conflict1991E → EQ in BAC36586. Ref.2
Sequence conflict2811D → H in BAC28249. Ref.2
Sequence conflict3531K → T in BAC28249. Ref.2
Sequence conflict5971L → F in BAC28249. Ref.2

Sequences

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

Last modified December 5, 2001. Version 1.
Checksum: 92962B82917CC79D

FASTA70578,833
        10         20         30         40         50         60 
MMQESGSETK SNGSAIQNGS SGGNHLLECG ALRDTRSNGE APAVDLGAAD LAHVQQQQQQ 

        70         80         90        100        110        120 
ALQVARQLLL QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQVSG LKSPKRNDKQ 

       130        140        150        160        170        180 
PALQVPVSVA MMTPQVITPQ QMQQILQQQV LSPQQLQVLL QQQQALMLQQ QLQEFYKKQQ 

       190        200        210        220        230        240 
EQLQLQLLQQ QHAGKQPKEQ QVATQQLAFQ QQLLQMQQLQ QQHLLSLQRQ GLLTIQPGQP 

       250        260        270        280        290        300 
ALPLQPLAQG MIPTELQQLW KEVTSAHTAE ETTSSNHSSL DLTSTCVSSS APSKSSLIMN 

       310        320        330        340        350        360 
PHASTNGQLS VHTPKRESLS HEEHPHSHPL YGHGVCKWPG CEAVCDDFPA FLKHLNSEHA 

       370        380        390        400        410        420 
LDDRSTAQCR VQMQVVQQLE LQLAKDKERL QAMMTHLHVK STEPKAAPQP LNLVSSVTLS 

       430        440        450        460        470        480 
KSASEASPQS LPHTPTTPTA PLTPVTQGPS VITTTSMHTV GPIRRRYSDK YNVPISSADI 

       490        500        510        520        530        540 
AQNQEFYKNA EVRPPFTYAS LIRQAILESP EKQLTLNEIY NWFTRMFAYF RRNAATWKNA 

       550        560        570        580        590        600 
VRHNLSLHKC FVRVENVKGA VWTVDEVEFQ KRRPQKISGN PSLIKNMQSS HAYCTPLNAA 

       610        620        630        640        650        660 
LQASMAENSI PLYTTASMGN PTLGSLASAI REELNGAMEH TNSNESDSSP GRSPMQAVHP 

       670        680        690        700 
IHVKEEPLDP EEAEGPLSLV TTANHSPDFD HDRDYEDEPV NEDME 

« Hide

Isoform 2 (B) [UniParc].

Checksum: 8B898F9AC3BB917C
Show »

FASTA64171,591
Isoform 3 (C) [UniParc].

Checksum: EA5EC089D4DB8168
Show »

FASTA45550,493
Isoform 4 [UniParc].

Checksum: 381CAA8E3720A7F0
Show »

FASTA57564,422

References

« Hide 'large scale' references
[1]"Characterization of a new subfamily of winged-helix/forkhead (Fox) genes that are expressed in the lung and act as transcriptional repressors."
Shu W., Yang H., Zhang L., Lu M.M., Morrisey E.E.
J. Biol. Chem. 276:27488-27497(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
Strain: C57BL/6.
Tissue: Lung.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Strain: C57BL/6J.
Tissue: Lung and Testis.
[3]"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 1).
Strain: C57BL/6J.
Tissue: Embryo.
[4]"Foxp4: a novel member of the Foxp subfamily of winged-helix genes co-expressed with Foxp1 and Foxp2 in pulmonary and gut tissues."
Lu M.M., Li S., Yang H., Morrisey E.E.
Mech. Dev. 119:S197-S202(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[5]"Transcriptional and DNA binding activity of the Foxp1/2/4 family is modulated by heterotypic and homotypic protein interactions."
Li S., Weidenfeld J., Morrisey E.E.
Mol. Cell. Biol. 24:809-822(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DIMERIZATION, INTERACTION WITH CTBP1, DOMAIN, MUTAGENESIS OF GLU-388 AND 410-PRO--VAL-414.
[6]"Foxp1 is an essential transcriptional regulator of B cell development."
Hu H., Wang B., Borde M., Nardone J., Maika S., Allred L., Tucker P.W., Rao A.
Nat. Immunol. 7:819-826(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF339103 mRNA. Translation: AAK69648.1.
AF339104 mRNA. Translation: AAK69649.1.
AF339105 mRNA. Translation: AAK69650.1.
AK033368 mRNA. Translation: BAC28249.1.
AK077062 mRNA. Translation: BAC36586.1.
BC064764 mRNA. Translation: AAH64764.1.
CCDSCCDS39578.1. [P58462-1]
RefSeqNP_001184250.1. NM_001197321.1.
NP_001184251.1. NM_001197322.1.
NP_444432.1. NM_053202.2. [P58462-1]
XP_006505385.1. XM_006505322.1.
XP_006505386.1. XM_006505323.1.
UniGeneMm.234965.
Mm.392884.
Mm.485266.

3D structure databases

ProteinModelPortalP58462.
SMRP58462. Positions 339-397, 490-576.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid224357. 9 interactions.

PTM databases

PhosphoSiteP58462.

Proteomic databases

MaxQBP58462.
PaxDbP58462.
PRIDEP58462.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000074346; ENSMUSP00000073953; ENSMUSG00000030067. [P58462-1]
ENSMUST00000113322; ENSMUSP00000108948; ENSMUSG00000030067. [P58462-1]
ENSMUST00000113326; ENSMUSP00000108952; ENSMUSG00000030067.
ENSMUST00000113329; ENSMUSP00000108955; ENSMUSG00000030067. [P58462-2]
ENSMUST00000177437; ENSMUSP00000135809; ENSMUSG00000030067.
GeneID108655.
KEGGmmu:108655.
UCSCuc009dbi.2. mouse. [P58462-1]
uc009dbl.2. mouse. [P58462-2]

Organism-specific databases

CTD27086.
MGIMGI:1914004. Foxp1.

Phylogenomic databases

eggNOGCOG5025.
GeneTreeENSGT00750000117475.
HOGENOMHOG000092089.
HOVERGENHBG051657.
KOK09409.
OrthoDBEOG7M6D7G.

Gene expression databases

ArrayExpressP58462.
BgeeP58462.
CleanExMM_FOXP1.
GenevestigatorP58462.

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

ChiTaRSFOXP1. mouse.
NextBio361173.
PROP58462.
SOURCESearch...

Entry information

Entry nameFOXP1_MOUSE
AccessionPrimary (citable) accession number: P58462
Secondary accession number(s): Q6P221, Q8C5V2, Q8CCD9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: December 5, 2001
Last modified: July 9, 2014
This is version 120 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot