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Protein

Forkhead box protein P1

Gene

FOXP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcriptional repressor (PubMed:18347093). Can act with CTBP1 to synergistically repress transcription but CTPBP1 is not essential (By similarity). Plays an important role in the specification and differentiation of lung epithelium. Acts cooperatively with FOXP4 to regulate lung secretory epithelial cell fate and regeneration by restricting the goblet cell lineage program; the function may involve regulation of AGR2. Essential transcriptional regulator of B-cell development. Involved in regulation of cardiac muscle cell proliferation. Involved in the columnar organization of spinal motor neurons. Promotes the formation of the lateral motor neuron column (LMC) and the preganglionic motor column (PGC) and is required for respective appropriate motor axon projections. The segment-appropriate generation of spinal chord motor columns requires cooperation with other Hox proteins. Can regulate PITX3 promoter activity; may promote midbrain identity in embryonic stem cell-derived dopamine neurons by regulating PITX3. Negatively regulates the differentiation of T follicular helper cells T(FH)s. Involved in maintainance of hair follicle stem cell quiescence; the function probably involves regulation of FGF18 (By similarity). Represses transcription of various pro-apoptotic genes and cooperates with NF-kappa B-signaling in promoting B-cell expansion by inhibition of caspase-dependent apoptosis (PubMed:25267198). Binds to CSF1R promoter elements and is involved in regulation of monocyte differentiation and macrophage functions; repression of CSF1R in monocytes seems to involve NCOR2 as corepressor (PubMed:15286807, PubMed:18799727, PubMed:18347093). Involved in endothelial cell proliferation, tube formation and migration indicative for a role in angiogenesis; the role in neovascularization seems to implicate suppression of SEMA5B (PubMed:24023716). Can negatively regulate androgen receptor signaling (PubMed:18640093).By similarity2 Publications5 Publications
Isoform 8: Involved in transcriptional regulation in embryonic stem cells (ESCs). Stimulates expression of transcription factors that are required for pluripotency and decreases expression of differentiation-associated genes. Has distinct DNA-binding specifities as compared to the canonical form and preferentially binds DNA with the sequence 5'-CGATACAA-3' (or closely related sequences) (PubMed:21924763). Promotes ESC self-renewal and pluripotency (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei59 – 602Breakpoint for translocation to form PAX5-FOXP1

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri306 – 33126C2H2-typeAdd
BLAST
DNA bindingi465 – 55591Fork-headPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. androgen receptor binding Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW
  3. sequence-specific DNA binding Source: InterPro
  4. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: GO_Central

GO - Biological processi

  1. chemokine (C-C motif) ligand 2 secretion Source: UniProtKB
  2. endothelial cell activation Source: UniProtKB
  3. interleukin-21 secretion Source: UniProtKB
  4. macrophage activation Source: UniProtKB
  5. monocyte activation Source: UniProtKB
  6. negative regulation of androgen receptor signaling pathway Source: UniProtKB
  7. negative regulation of B cell apoptotic process Source: UniProtKB
  8. negative regulation of transcription, DNA-templated Source: UniProtKB
  9. osteoclast development Source: UniProtKB
  10. osteoclast differentiation Source: UniProtKB
  11. positive regulation of endothelial cell migration Source: UniProtKB
  12. positive regulation of smooth muscle cell proliferation Source: UniProtKB
  13. regulation of defense response to bacterium Source: UniProtKB
  14. regulation of endothelial tube morphogenesis Source: UniProtKB
  15. regulation of inflammatory response Source: UniProtKB
  16. regulation of interleukin-12 secretion Source: UniProtKB
  17. regulation of interleukin-1 beta secretion Source: UniProtKB
  18. regulation of macrophage colony-stimulating factor production Source: UniProtKB
  19. regulation of monocyte differentiation Source: UniProtKB
  20. regulation of transcription from RNA polymerase II promoter Source: GO_Central
  21. regulation of tumor necrosis factor production Source: UniProtKB
  22. response to lipopolysaccharide Source: UniProtKB
  23. T follicular helper cell differentiation Source: UniProtKB
  24. transcription from RNA polymerase II promoter Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiQ9H334.

Names & Taxonomyi

Protein namesi
Recommended name:
Forkhead box protein P1
Alternative name(s):
Mac-1-regulated forkhead1 Publication
Short name:
MFH1 Publication
Gene namesi
Name:FOXP1
ORF Names:HSPC215
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:3823. FOXP1.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleoplasm Source: HPA
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving FOXP1 is found in acute lymphoblastic leukemia. Translocation t(9;3)(p13;p14.1) with PAX5.

Mental retardation with language impairment and autistic features1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA developmental disorder characterized by mild to moderate mental retardation, language impairment, and autistic features. Patients show global delay, delayed walking, severely delayed speech development, and behavioral abnormalities, including irritability, hyperactivity, aggression, and stereotypical rigid behaviors.

See also OMIM:613670

Keywords - Diseasei

Mental retardation

Organism-specific databases

MIMi613670. phenotype.
Orphaneti391372. Intellectual disability-severe speech delay-mild dysmorphism syndrome.
52417. MALT lymphoma.
99860. Precursor B-cell acute lymphoblastic leukemia.
PharmGKBiPA28241.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 677677Forkhead box protein P1PRO_0000091877Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei653 – 6531Phosphothreonine1 Publication
Modified residuei658 – 6581Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9H334.
PaxDbiQ9H334.
PRIDEiQ9H334.

PTM databases

PhosphoSiteiQ9H334.

Expressioni

Tissue specificityi

Isoform 8 is specifically expressed in embryonic stem cells.1 Publication

Inductioni

By androgen in an isoform-specific manner; expression of isoform 4 is greatly induced.1 Publication

Gene expression databases

BgeeiQ9H334.
CleanExiHS_FOXP1.
ExpressionAtlasiQ9H334. baseline and differential.
GenevestigatoriQ9H334.

Organism-specific databases

HPAiCAB011501.
HPA003876.

Interactioni

Subunit structurei

Forms homodimers and heterodimers with FOXP2 and FOXP4 (PubMed:25027557). Dimerization is required for DNA-binding. Interacts with CTBP1 (By similarity). Interacts with NCOR2, AR (PubMed:18347093, PubMed:18640093).By similarity3 Publications

Protein-protein interaction databases

BioGridi117989. 12 interactions.
DIPiDIP-36585N.
IntActiQ9H334. 10 interactions.
STRINGi9606.ENSP00000318902.

Structurei

Secondary structure

1
677
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi470 – 47910Combined sources
Beta strandi481 – 4866Combined sources
Helixi488 – 49811Combined sources
Helixi500 – 5023Combined sources
Helixi506 – 51914Combined sources
Beta strandi523 – 5264Combined sources
Beta strandi533 – 5364Combined sources
Helixi538 – 5436Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KIUNMR-A462-548[»]
ProteinModelPortaliQ9H334.
SMRiQ9H334. Positions 311-369, 462-548.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni348 – 36922Leucine-zipperAdd
BLAST
Regioni382 – 3865CTBP1-bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi55 – 230176Gln-richAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 C2H2-type zinc finger.Curated
Contains 1 fork-head DNA-binding domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri306 – 33126C2H2-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5025.
GeneTreeiENSGT00780000121840.
HOGENOMiHOG000092089.
HOVERGENiHBG051657.
InParanoidiQ9H334.
OrthoDBiEOG7M6D7G.
PhylomeDBiQ9H334.
TreeFamiTF326978.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR001766. TF_fork_head.
IPR018122. TF_fork_head_CS.
IPR011991. WHTH_DNA-bd_dom.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamiPF00250. Fork_head. 1 hit.
[Graphical view]
PRINTSiPR00053. FORKHEAD.
SMARTiSM00339. FH. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]
PROSITEiPS00658. FORK_HEAD_2. 1 hit.
PS50039. FORK_HEAD_3. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q9H334-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MMQESGTETK SNGSAIQNGS GGSNHLLECG GLREGRSNGE TPAVDIGAAD
60 70 80 90 100
LAHAQQQQQQ ALQVARQLLL QQQQQQQVSG LKSPKRNDKQ PALQVPVSVA
110 120 130 140 150
MMTPQVITPQ QMQQILQQQV LSPQQLQVLL QQQQALMLQQ QQLQEFYKKQ
160 170 180 190 200
QEQLQLQLLQ QQHAGKQPKE QQQVATQQLA FQQQLLQMQQ LQQQHLLSLQ
210 220 230 240 250
RQGLLTIQPG QPALPLQPLA QGMIPTELQQ LWKEVTSAHT AEETTGNNHS
260 270 280 290 300
SLDLTTTCVS SSAPSKTSLI MNPHASTNGQ LSVHTPKRES LSHEEHPHSH
310 320 330 340 350
PLYGHGVCKW PGCEAVCEDF QSFLKHLNSE HALDDRSTAQ CRVQMQVVQQ
360 370 380 390 400
LELQLAKDKE RLQAMMTHLH VKSTEPKAAP QPLNLVSSVT LSKSASEASP
410 420 430 440 450
QSLPHTPTTP TAPLTPVTQG PSVITTTSMH TVGPIRRRYS DKYNVPISSA
460 470 480 490 500
DIAQNQEFYK NAEVRPPFTY ASLIRQAILE SPEKQLTLNE IYNWFTRMFA
510 520 530 540 550
YFRRNAATWK NAVRHNLSLH KCFVRVENVK GAVWTVDEVE FQKRRPQKIS
560 570 580 590 600
GNPSLIKNMQ SSHAYCTPLN AALQASMAEN SIPLYTTASM GNPTLGNLAS
610 620 630 640 650
AIREELNGAM EHTNSNESDS SPGRSPMQAV HPVHVKEEPL DPEEAEGPLS
660 670
LVTTANHSPD FDHDRDYEDE PVNEDME
Length:677
Mass (Da):75,317
Last modified:March 1, 2001 - v1
Checksum:iAEE92D47BB20964B
GO
Isoform 2 (identifier: Q9H334-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-100: Missing.
     140-227: Missing.

Show »
Length:489
Mass (Da):54,563
Checksum:i63DDAAD1B033BAF0
GO
Isoform 3 (identifier: Q9H334-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: MMQESGTETK...LAHAQQQQQQ → CRSTLVDPKN...APFAKLFIFS
     95-170: Missing.

Note: Incomplete sequence.

Show »
Length:586
Mass (Da):65,431
Checksum:i099643CD5B363BDF
GO
Isoform 4 (identifier: Q9H334-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: MMQESGTETK...LAHAQQQQQQ → CRSTLVDPKN...APFAKLFIFS

Note: Incomplete sequence. No experimental confirmation available.

Show »
Length:662
Mass (Da):74,330
Checksum:i168D2B3165278F9E
GO
Isoform 5 (identifier: Q9H334-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     61-114: ALQVARQLLL...QVITPQQMQQ → WHLINHQPSR...PVCQPNPSPF
     115-677: Missing.

Show »
Length:114
Mass (Da):12,256
Checksum:iA1CC32BD8BBC4EA5
GO
Isoform 6 (identifier: Q9H334-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     95-170: Missing.

Show »
Length:601
Mass (Da):66,417
Checksum:i599FC834381D194C
GO
Isoform 7 (identifier: Q9H334-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     450-450: Missing.

Note: No experimental confirmation available. May be due to competing acceptor splice site.

Show »
Length:676
Mass (Da):75,246
Checksum:iF70967CCDB289929
GO
Isoform 8 (identifier: Q9H334-8) [UniParc]FASTAAdd to basket

Also known as: FOXP1-ES

The sequence of this isoform differs from the canonical sequence as follows:
     511-551: NAVRHNLSLH...QKRRPQKISG → GAIRTLSLHK...DENFDELVAH

Show »
Length:692
Mass (Da):77,249
Checksum:i54B850510CD39CB1
GO

Sequence cautioni

The sequence AAF36135.1 differs from that shown. Reason: Frameshift at positions 531 and 545. Curated
The sequence ABI33105.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB55005.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti138 – 1381L → P in BAG53682 (PubMed:14702039).Curated
Sequence conflicti173 – 1731Q → R in BAB55005 (PubMed:14702039).Curated
Sequence conflicti205 – 2051L → V in BAB55005 (PubMed:14702039).Curated
Sequence conflicti210 – 2123GQP → ARA in AAK69408 (PubMed:11751404).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 51S → P.1 Publication
VAR_065067
Natural varianti101 – 1011M → V.1 Publication
VAR_065068
Natural varianti215 – 2151P → A.3 Publications
Corresponds to variant rs146606219 [ dbSNP | Ensembl ].
VAR_065069
Natural varianti261 – 2611S → P.1 Publication
VAR_065070
Natural varianti390 – 3901T → S.1 Publication
VAR_065071
Natural varianti445 – 4451V → M.1 Publication
Corresponds to variant rs147756430 [ dbSNP | Ensembl ].
VAR_065072
Natural varianti570 – 5701N → S.2 Publications
VAR_065073
Natural varianti597 – 5971N → T.1 Publication
VAR_065074
Natural varianti613 – 6131T → N.1 Publication
VAR_065075

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 100100Missing in isoform 2. 1 PublicationVSP_001553Add
BLAST
Alternative sequencei1 – 6060MMQES…QQQQQ → CRSTLVDPKNSARASQKQPE PIYSKKTEIQRQTVRAPFAK LFIFS in isoform 3 and isoform 4. 1 PublicationVSP_001555Add
BLAST
Alternative sequencei61 – 11454ALQVA…QQMQQ → WHLINHQPSRSPSSWLKRLI SSPWELEVLQVPLWGAVAET KMSGPVCQPNPSPF in isoform 5. 2 PublicationsVSP_043462Add
BLAST
Alternative sequencei95 – 17076Missing in isoform 3 and isoform 6. 1 PublicationVSP_001556Add
BLAST
Alternative sequencei115 – 677563Missing in isoform 5. 2 PublicationsVSP_043463Add
BLAST
Alternative sequencei140 – 22788Missing in isoform 2. 1 PublicationVSP_001554Add
BLAST
Alternative sequencei450 – 4501Missing in isoform 7. 2 PublicationsVSP_046930
Alternative sequencei511 – 55141NAVRH…QKISG → GAIRTLSLHKCFIRVEDEFG SFWTVDDEEFKRGRHIQRGR PRKYCPDENFDELVAH in isoform 8. 1 PublicationVSP_057341Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF146696 mRNA. Translation: AAG47632.1.
AF146697 mRNA. Translation: AAG47633.1.
AF146698 mRNA. Translation: AAG47634.1.
AF275309 mRNA. Translation: AAK69408.1.
BT006643 mRNA. Translation: AAP35289.1.
AK092383 mRNA. Translation: BAC03875.1.
AK122710 mRNA. Translation: BAG53682.1.
AC097632 Genomic DNA. No translation available.
AC097634 Genomic DNA. No translation available.
AC103586 Genomic DNA. No translation available.
AC104442 Genomic DNA. No translation available.
AC104645 Genomic DNA. No translation available.
AC138058 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW65494.1.
CH471055 Genomic DNA. Translation: EAW65499.1.
BC005055 mRNA. Translation: AAH05055.1.
BC054815 mRNA. Translation: AAH54815.1.
BC071893 mRNA. Translation: AAH71893.1.
BC080521 mRNA. Translation: AAH80521.1.
DQ845346 mRNA. Translation: ABI33105.1. Different initiation.
AK027264 mRNA. Translation: BAB55005.1. Different initiation.
AF151049 mRNA. Translation: AAF36135.1. Frameshift.
CCDSiCCDS2914.1. [Q9H334-1]
CCDS33785.1. [Q9H334-5]
CCDS58838.1. [Q9H334-6]
CCDS58839.1. [Q9H334-7]
RefSeqiNP_001012523.1. NM_001012505.1. [Q9H334-5]
NP_001231737.1. NM_001244808.1. [Q9H334-7]
NP_001231739.1. NM_001244810.1.
NP_001231741.1. NM_001244812.1. [Q9H334-6]
NP_001231743.1. NM_001244814.1. [Q9H334-1]
NP_001231744.1. NM_001244815.1.
NP_001231745.1. NM_001244816.1. [Q9H334-1]
NP_116071.2. NM_032682.5. [Q9H334-1]
XP_005264795.1. XM_005264738.2. [Q9H334-7]
XP_006713165.1. XM_006713102.1. [Q9H334-1]
XP_006713166.1. XM_006713103.1. [Q9H334-1]
XP_006713167.1. XM_006713104.1. [Q9H334-1]
XP_006713170.1. XM_006713107.1. [Q9H334-5]
UniGeneiHs.59368.

Genome annotation databases

EnsembliENST00000318779; ENSP00000318721; ENSG00000114861. [Q9H334-5]
ENST00000318789; ENSP00000318902; ENSG00000114861. [Q9H334-1]
ENST00000475937; ENSP00000419393; ENSG00000114861. [Q9H334-1]
ENST00000484350; ENSP00000417857; ENSG00000114861. [Q9H334-6]
ENST00000493089; ENSP00000418524; ENSG00000114861. [Q9H334-7]
ENST00000498215; ENSP00000418102; ENSG00000114861. [Q9H334-1]
ENST00000622151; ENSP00000477918; ENSG00000114861. [Q9H334-5]
GeneIDi27086.
KEGGihsa:27086.
UCSCiuc003doi.3. human. [Q9H334-1]
uc003dom.3. human.
uc003doo.3. human.
uc003dos.3. human. [Q9H334-5]

Polymorphism databases

DMDMi14548062.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF146696 mRNA. Translation: AAG47632.1.
AF146697 mRNA. Translation: AAG47633.1.
AF146698 mRNA. Translation: AAG47634.1.
AF275309 mRNA. Translation: AAK69408.1.
BT006643 mRNA. Translation: AAP35289.1.
AK092383 mRNA. Translation: BAC03875.1.
AK122710 mRNA. Translation: BAG53682.1.
AC097632 Genomic DNA. No translation available.
AC097634 Genomic DNA. No translation available.
AC103586 Genomic DNA. No translation available.
AC104442 Genomic DNA. No translation available.
AC104645 Genomic DNA. No translation available.
AC138058 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW65494.1.
CH471055 Genomic DNA. Translation: EAW65499.1.
BC005055 mRNA. Translation: AAH05055.1.
BC054815 mRNA. Translation: AAH54815.1.
BC071893 mRNA. Translation: AAH71893.1.
BC080521 mRNA. Translation: AAH80521.1.
DQ845346 mRNA. Translation: ABI33105.1. Different initiation.
AK027264 mRNA. Translation: BAB55005.1. Different initiation.
AF151049 mRNA. Translation: AAF36135.1. Frameshift.
CCDSiCCDS2914.1. [Q9H334-1]
CCDS33785.1. [Q9H334-5]
CCDS58838.1. [Q9H334-6]
CCDS58839.1. [Q9H334-7]
RefSeqiNP_001012523.1. NM_001012505.1. [Q9H334-5]
NP_001231737.1. NM_001244808.1. [Q9H334-7]
NP_001231739.1. NM_001244810.1.
NP_001231741.1. NM_001244812.1. [Q9H334-6]
NP_001231743.1. NM_001244814.1. [Q9H334-1]
NP_001231744.1. NM_001244815.1.
NP_001231745.1. NM_001244816.1. [Q9H334-1]
NP_116071.2. NM_032682.5. [Q9H334-1]
XP_005264795.1. XM_005264738.2. [Q9H334-7]
XP_006713165.1. XM_006713102.1. [Q9H334-1]
XP_006713166.1. XM_006713103.1. [Q9H334-1]
XP_006713167.1. XM_006713104.1. [Q9H334-1]
XP_006713170.1. XM_006713107.1. [Q9H334-5]
UniGeneiHs.59368.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KIUNMR-A462-548[»]
ProteinModelPortaliQ9H334.
SMRiQ9H334. Positions 311-369, 462-548.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117989. 12 interactions.
DIPiDIP-36585N.
IntActiQ9H334. 10 interactions.
STRINGi9606.ENSP00000318902.

PTM databases

PhosphoSiteiQ9H334.

Polymorphism databases

DMDMi14548062.

Proteomic databases

MaxQBiQ9H334.
PaxDbiQ9H334.
PRIDEiQ9H334.

Protocols and materials databases

DNASUi27086.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000318779; ENSP00000318721; ENSG00000114861. [Q9H334-5]
ENST00000318789; ENSP00000318902; ENSG00000114861. [Q9H334-1]
ENST00000475937; ENSP00000419393; ENSG00000114861. [Q9H334-1]
ENST00000484350; ENSP00000417857; ENSG00000114861. [Q9H334-6]
ENST00000493089; ENSP00000418524; ENSG00000114861. [Q9H334-7]
ENST00000498215; ENSP00000418102; ENSG00000114861. [Q9H334-1]
ENST00000622151; ENSP00000477918; ENSG00000114861. [Q9H334-5]
GeneIDi27086.
KEGGihsa:27086.
UCSCiuc003doi.3. human. [Q9H334-1]
uc003dom.3. human.
uc003doo.3. human.
uc003dos.3. human. [Q9H334-5]

Organism-specific databases

CTDi27086.
GeneCardsiGC03M071088.
HGNCiHGNC:3823. FOXP1.
HPAiCAB011501.
HPA003876.
MIMi605515. gene.
613670. phenotype.
neXtProtiNX_Q9H334.
Orphaneti391372. Intellectual disability-severe speech delay-mild dysmorphism syndrome.
52417. MALT lymphoma.
99860. Precursor B-cell acute lymphoblastic leukemia.
PharmGKBiPA28241.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5025.
GeneTreeiENSGT00780000121840.
HOGENOMiHOG000092089.
HOVERGENiHBG051657.
InParanoidiQ9H334.
OrthoDBiEOG7M6D7G.
PhylomeDBiQ9H334.
TreeFamiTF326978.

Enzyme and pathway databases

SignaLinkiQ9H334.

Miscellaneous databases

ChiTaRSiFOXP1. human.
GeneWikiiFOXP1.
GenomeRNAii27086.
NextBioi49693.
PROiQ9H334.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H334.
CleanExiHS_FOXP1.
ExpressionAtlasiQ9H334. baseline and differential.
GenevestigatoriQ9H334.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR001766. TF_fork_head.
IPR018122. TF_fork_head_CS.
IPR011991. WHTH_DNA-bd_dom.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamiPF00250. Fork_head. 1 hit.
[Graphical view]
PRINTSiPR00053. FORKHEAD.
SMARTiSM00339. FH. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]
PROSITEiPS00658. FORK_HEAD_2. 1 hit.
PS50039. FORK_HEAD_3. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The FOXP1 winged helix transcription factor is a novel candidate tumor suppressor gene on chromosome 3p."
    Banham A.H., Beasley N., Campo E., Fernandez P.L., Fidler C., Gatter K., Jones M., Mason D.Y., Prime J.E., Trougouboff P., Wood K., Cordell J.L.
    Cancer Res. 61:8820-8829(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), NUCLEOTIDE SEQUENCE [MRNA] OF 210-677 (ISOFORM 7), PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Tissue: Testis.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
  3. "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.
    , 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 6 AND 7), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-677 (ISOFORM 4).
    Tissue: Embryonic head and Tongue.
  4. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 5).
    Tissue: Lung.
  7. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 60-677, CHROMOSOMAL TRANSLOCATION WITH PAX5.
  8. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 528-677.
    Tissue: Umbilical cord blood.
  9. "Integrin engagement regulates monocyte differentiation through the forkhead transcription factor Foxp1."
    Shi C., Zhang X., Chen Z., Sulaiman K., Feinberg M.W., Ballantyne C.M., Jain M.K., Simon D.I.
    J. Clin. Invest. 114:408-418(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "FOXP1 is an androgen-responsive transcription factor that negatively regulates androgen receptor signaling in prostate cancer cells."
    Takayama K., Horie-Inoue K., Ikeda K., Urano T., Murakami K., Hayashizaki Y., Ouchi Y., Inoue S.
    Biochem. Biophys. Res. Commun. 374:388-393(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AR, INDUCTION BY ANDROGEN.
  11. "Down-regulation of the forkhead transcription factor Foxp1 is required for monocyte differentiation and macrophage function."
    Shi C., Sakuma M., Mooroka T., Liscoe A., Gao H., Croce K.J., Sharma A., Kaplan D., Greaves D.R., Wang Y., Simon D.I.
    Blood 112:4699-4711(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Cooperative regulation in development by SMRT and FOXP1."
    Jepsen K., Gleiberman A.S., Shi C., Simon D.I., Rosenfeld M.G.
    Genes Dev. 22:740-745(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NCOR2.
  13. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: FUNCTION, INVOLVEMENT IN MRLIAF, VARIANTS ALA-215; MET-445; SER-570 AND ASN-613.
  15. Cited for: ALTERNATIVE SPLICING (ISOFORM 8), FUNCTION (ISOFORM 8), TISSUE SPECIFICITY (ISOFORM 8).
  16. "FoxP1 stimulates angiogenesis by repressing the inhibitory guidance protein semaphorin 5B in endothelial cells."
    Grundmann S., Lindmayer C., Hans F.P., Hoefer I., Helbing T., Pasterkamp G., Bode C., de Kleijn D., Moser M.
    PLoS ONE 8:E70873-E70873(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "FOXP1 directly represses transcription of pro-apoptotic genes and cooperates with NF-kappaB to promote survival of human B-cells."
    van Keimpema M., Grueneberg L.J., Mokry M., van Boxtel R., Koster J., Coffer P.J., Pals S.T., Spaargaren M.
    Blood 124:3431-3440(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "Transcriptional Regulation by FOXP1, FOXP2, and FOXP4 Dimerization."
    Sin C., Li H., Crawford D.A.
    J. Mol. Neurosci. 0:0-0(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FOXP2 AND FOXP4, SUBCELLULAR LOCATION.
  19. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-653 AND SER-658, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  20. "Solution structure and backbone dynamics of the DNA-binding domain of FOXP1: insight into its domain swapping and DNA binding."
    Chu Y.P., Chang C.H., Shiu J.H., Chang Y.T., Chen C.Y., Chuang W.J.
    Protein Sci. 20:908-924(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 462-548.
  21. "Assessing the impact of FOXP1 mutations on developmental verbal dyspraxia."
    Vernes S.C., MacDermot K.D., Monaco A.P., Fisher S.E.
    Eur. J. Hum. Genet. 17:1354-1358(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ALA-215.
  22. Cited for: VARIANTS PRO-5; VAL-101; ALA-215; PRO-261; SER-390; SER-570 AND THR-597.

Entry informationi

Entry nameiFOXP1_HUMAN
AccessioniPrimary (citable) accession number: Q9H334
Secondary accession number(s): A3QVP8
, B3KV70, G5E9V8, Q8NAN6, Q9BSG9, Q9H332, Q9H333, Q9P0R1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: March 1, 2001
Last modified: March 4, 2015
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.