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Q9H334 (FOXP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 P1
Gene names
Name:FOXP1
ORF Names:HSPC215
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length677 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional repressor. It 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 By similarity. Ref.10

Subunit structure

Forms homodimers and heterodimers with FOXP2 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.

Involvement in disease

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 features (MRLIAF) [MIM:613670]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10

Sequence similarities

Contains 1 C2H2-type zinc finger.

Contains 1 fork-head DNA-binding domain.

Sequence caution

The sequence AAF36135.1 differs from that shown. Reason: Frameshift at positions 531 and 545.

The sequence ABI33105.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB55005.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseMental retardation
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionRepressor
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac muscle cell differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

embryo development

Inferred from Biological aspect of Ancestor. Source: RefGenome

immunoglobulin V(D)J recombination

Inferred from Biological aspect of Ancestor. Source: RefGenome

lung development

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.10. Source: UniProtKB

pattern specification process

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of epithelial cell proliferation

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of immunoglobulin production

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of mesenchymal cell proliferation

Inferred from Biological aspect of Ancestor. Source: RefGenome

pre-B cell differentiation

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

   Cellular_componentcytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionDNA 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 Biological aspect of Ancestor. Source: RefGenome

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q9H334-1)

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: Q9H334-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-100: Missing.
     140-227: Missing.
Isoform 3 (identifier: Q9H334-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: MMQESGTETK...LAHAQQQQQQ → CRSTLVDPKN...APFAKLFIFS
     95-170: Missing.
Note: Incomplete sequence.
Isoform 4 (identifier: Q9H334-4)

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.
Isoform 5 (identifier: Q9H334-5)

The sequence of this isoform differs from the canonical sequence as follows:
     61-114: ALQVARQLLL...QVITPQQMQQ → WHLINHQPSR...PVCQPNPSPF
     115-677: Missing.
Isoform 6 (identifier: Q9H334-6)

The sequence of this isoform differs from the canonical sequence as follows:
     95-170: Missing.
Isoform 7 (identifier: Q9H334-7)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 677677Forkhead box protein P1
PRO_0000091877

Regions

Zinc finger306 – 33126C2H2-type
DNA binding465 – 55591Fork-head
Region348 – 36922Leucine-zipper
Region382 – 3865CTBP1-binding By similarity
Compositional bias55 – 230176Gln-rich

Sites

Site59 – 602Breakpoint for translocation to form PAX5-FOXP1

Natural variations

Alternative sequence1 – 100100Missing in isoform 2.
VSP_001553
Alternative sequence1 – 6060MMQES…QQQQQ → CRSTLVDPKNSARASQKQPE PIYSKKTEIQRQTVRAPFAK LFIFS in isoform 3 and isoform 4.
VSP_001555
Alternative sequence61 – 11454ALQVA…QQMQQ → WHLINHQPSRSPSSWLKRLI SSPWELEVLQVPLWGAVAET KMSGPVCQPNPSPF in isoform 5.
VSP_043462
Alternative sequence95 – 17076Missing in isoform 3 and isoform 6.
VSP_001556
Alternative sequence115 – 677563Missing in isoform 5.
VSP_043463
Alternative sequence140 – 22788Missing in isoform 2.
VSP_001554
Alternative sequence4501Missing in isoform 7.
VSP_046930
Natural variant51S → P. Ref.12
VAR_065067
Natural variant1011M → V. Ref.12
VAR_065068
Natural variant2151P → A. Ref.10 Ref.11 Ref.12
Corresponds to variant rs146606219 [ dbSNP | Ensembl ].
VAR_065069
Natural variant2611S → P. Ref.12
VAR_065070
Natural variant3901T → S. Ref.12
VAR_065071
Natural variant4451V → M. Ref.10
Corresponds to variant rs147756430 [ dbSNP | Ensembl ].
VAR_065072
Natural variant5701N → S. Ref.10 Ref.12
VAR_065073
Natural variant5971N → T. Ref.12
VAR_065074
Natural variant6131T → N. Ref.10
VAR_065075

Experimental info

Sequence conflict1381L → P in BAG53682. Ref.3
Sequence conflict1731Q → R in BAB55005. Ref.3
Sequence conflict2051L → V in BAB55005. Ref.3
Sequence conflict210 – 2123GQP → ARA in AAK69408. Ref.1

Secondary structure

................. 677
Helix Strand Turn

Details...

Sequences

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

Last modified March 1, 2001. Version 1.
Checksum: AEE92D47BB20964B

FASTA67775,317
        10         20         30         40         50         60 
MMQESGTETK SNGSAIQNGS GGSNHLLECG GLREGRSNGE TPAVDIGAAD LAHAQQQQQQ 

        70         80         90        100        110        120 
ALQVARQLLL QQQQQQQVSG LKSPKRNDKQ PALQVPVSVA MMTPQVITPQ QMQQILQQQV 

       130        140        150        160        170        180 
LSPQQLQVLL QQQQALMLQQ QQLQEFYKKQ QEQLQLQLLQ QQHAGKQPKE QQQVATQQLA 

       190        200        210        220        230        240 
FQQQLLQMQQ LQQQHLLSLQ RQGLLTIQPG QPALPLQPLA QGMIPTELQQ LWKEVTSAHT 

       250        260        270        280        290        300 
AEETTGNNHS SLDLTTTCVS SSAPSKTSLI MNPHASTNGQ LSVHTPKRES LSHEEHPHSH 

       310        320        330        340        350        360 
PLYGHGVCKW PGCEAVCEDF QSFLKHLNSE HALDDRSTAQ CRVQMQVVQQ LELQLAKDKE 

       370        380        390        400        410        420 
RLQAMMTHLH VKSTEPKAAP QPLNLVSSVT LSKSASEASP QSLPHTPTTP TAPLTPVTQG 

       430        440        450        460        470        480 
PSVITTTSMH TVGPIRRRYS DKYNVPISSA DIAQNQEFYK NAEVRPPFTY ASLIRQAILE 

       490        500        510        520        530        540 
SPEKQLTLNE IYNWFTRMFA YFRRNAATWK NAVRHNLSLH KCFVRVENVK GAVWTVDEVE 

       550        560        570        580        590        600 
FQKRRPQKIS GNPSLIKNMQ SSHAYCTPLN AALQASMAEN SIPLYTTASM GNPTLGNLAS 

       610        620        630        640        650        660 
AIREELNGAM EHTNSNESDS SPGRSPMQAV HPVHVKEEPL DPEEAEGPLS LVTTANHSPD 

       670 
FDHDRDYEDE PVNEDME 

« Hide

Isoform 2 [UniParc].

Checksum: 63DDAAD1B033BAF0
Show »

FASTA48954,563
Isoform 3 [UniParc].

Checksum: 099643CD5B363BDF
Show »

FASTA58665,431
Isoform 4 [UniParc].

Checksum: 168D2B3165278F9E
Show »

FASTA66274,330
Isoform 5 [UniParc].

Checksum: A1CC32BD8BBC4EA5
Show »

FASTA11412,256
Isoform 6 [UniParc].

Checksum: 599FC834381D194C
Show »

FASTA60166,417
Isoform 7 [UniParc].

Checksum: F70967CCDB289929
Show »

FASTA67675,246

References

« Hide 'large scale' references
[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. 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 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Genome-wide analysis of genetic alterations in acute lymphoblastic leukaemia."
Mullighan C.G., Goorha S., Radtke I., Miller C.B., Coustan-Smith E., Dalton J.D., Girtman K., Mathew S., Ma J., Pounds S.B., Su X., Pui C.-H., Relling M.V., Evans W.E., Shurtleff S.A., Downing J.R.
Nature 446:758-764(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"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.
[10]"De novo mutations in FOXP1 in cases with intellectual disability, autism, and language impairment."
Hamdan F.F., Daoud H., Rochefort D., Piton A., Gauthier J., Langlois M., Foomani G., Dobrzeniecka S., Krebs M.O., Joober R., Lafreniere R.G., Lacaille J.C., Mottron L., Drapeau P., Beauchamp M.H., Phillips M.S., Fombonne E., Rouleau G.A., Michaud J.L.
Am. J. Hum. Genet. 87:671-678(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INVOLVEMENT IN MRLIAF, VARIANTS ALA-215; MET-445; SER-570 AND ASN-613.
[11]"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.
[12]"Identification of FOXP1 deletions in three unrelated patients with mental retardation and significant speech and language deficits."
Horn D., Kapeller J., Rivera-Brugues N., Moog U., Lorenz-Depiereux B., Eck S., Hempel M., Wagenstaller J., Gawthrope A., Monaco A.P., Bonin M., Riess O., Wohlleber E., Illig T., Bezzina C.R., Franke A., Spranger S., Villavicencio-Lorini P. expand/collapse author list , Seifert W., Rosenfeld J., Klopocki E., Rappold G.A., Strom T.M.
Hum. Mutat. 31:E1851-E1860(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PRO-5; VAL-101; ALA-215; PRO-261; SER-390; SER-570 AND THR-597.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001012523.1. NM_001012505.1.
NP_001231737.1. NM_001244808.1.
NP_001231739.1. NM_001244810.1.
NP_001231741.1. NM_001244812.1.
NP_001231743.1. NM_001244814.1.
NP_001231744.1. NM_001244815.1.
NP_001231745.1. NM_001244816.1.
NP_116071.2. NM_032682.5.
XP_005264795.1. XM_005264738.2.
UniGeneHs.59368.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KIUNMR-A462-548[»]
ProteinModelPortalQ9H334.
SMRQ9H334. Positions 311-369, 462-548.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117989. 11 interactions.
DIPDIP-36585N.
IntActQ9H334. 9 interactions.
STRING9606.ENSP00000318902.

PTM databases

PhosphoSiteQ9H334.

Polymorphism databases

DMDM14548062.

Proteomic databases

PaxDbQ9H334.
PRIDEQ9H334.

Protocols and materials databases

DNASU27086.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000318779; 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]
GeneID27086.
KEGGhsa:27086.
UCSCuc003doi.3. human. [Q9H334-1]
uc003dom.3. human.
uc003dos.3. human. [Q9H334-5]

Organism-specific databases

CTD27086.
GeneCardsGC03M071088.
HGNCHGNC:3823. FOXP1.
HPACAB011501.
HPA003876.
MIM605515. gene.
613670. phenotype.
neXtProtNX_Q9H334.
Orphanet52417. MALT lymphoma.
99860. Precursor B-cell acute lymphoblastic leukemia.
PharmGKBPA28241.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5025.
HOGENOMHOG000092089.
HOVERGENHBG051657.
InParanoidQ9H334.
OrthoDBEOG7M6D7G.
PhylomeDBQ9H334.
TreeFamTF326978.

Enzyme and pathway databases

SignaLinkQ9H334.

Gene expression databases

ArrayExpressQ9H334.
BgeeQ9H334.
CleanExHS_FOXP1.
GenevestigatorQ9H334.

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. human.
GeneWikiFOXP1.
GenomeRNAi27086.
NextBio49693.
PROQ9H334.
SOURCESearch...

Entry information

Entry nameFOXP1_HUMAN
AccessionPrimary (citable) accession number: Q9H334
Secondary accession number(s): A3QVP8 expand/collapse secondary AC list , B3KV70, G5E9V8, Q8NAN6, Q9BSG9, Q9H332, Q9H333, Q9P0R1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 135 of the entry and version 1 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

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 3

Human chromosome 3: entries, gene names and cross-references to MIM