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P40424

- PBX1_HUMAN

UniProt

P40424 - PBX1_HUMAN

Protein

Pre-B-cell leukemia transcription factor 1

Gene

PBX1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Binds the sequence 5'-ATCAATCAA-3'. Acts as a transcriptional activator of PF4 in complex with MEIS1. Converted into a potent transcriptional activator by the (1;19) translocation. May have a role in steroidogenesis and, subsequently, sexual development and differentiation. Isoform PBX1b as part of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar cells is involved in the transcriptional activation of the ELA1 enhancer; the complex binds to the enhancer B element and cooperates with the transcription factor 1 complex (PTF1) bound to the enhancer A element. Probably in complex with MEIS2, is involved in transcriptional regulation by KLF4. Acts as a transcriptional activator of NKX2-5 and a transcriptional repressor of CDKN2B. Together with NKX2-5, it is required for spleen development through a mechanism that involves CDKN2B repression By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei88 – 892Breakpoint for translocation to form TCF3-PBX1 oncogene

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi233 – 29563Homeobox; TALE-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
    4. sequence-specific DNA binding Source: Ensembl
    5. sequence-specific DNA binding transcription factor activity Source: ProtInc
    6. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. adrenal gland development Source: Ensembl
    2. anterior/posterior pattern specification Source: Ensembl
    3. branching involved in ureteric bud morphogenesis Source: Ensembl
    4. embryonic hemopoiesis Source: Ensembl
    5. embryonic limb morphogenesis Source: Ensembl
    6. embryonic skeletal system development Source: Ensembl
    7. negative regulation of neuron differentiation Source: Ensembl
    8. negative regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
    9. organ morphogenesis Source: Ensembl
    10. positive regulation of cell proliferation Source: Ensembl
    11. positive regulation of G2/M transition of mitotic cell cycle Source: Ensembl
    12. proximal/distal pattern formation Source: Ensembl
    13. regulation of ossification Source: Ensembl
    14. sex differentiation Source: UniProtKB-KW
    15. spleen development Source: Ensembl
    16. steroid biosynthetic process Source: UniProtKB-KW
    17. thymus development Source: Ensembl

    Keywords - Molecular functioni

    Activator, Developmental protein, Repressor

    Keywords - Biological processi

    Differentiation, Sexual differentiation, Steroidogenesis, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_200812. Transcriptional regulation of pluripotent stem cells.
    SignaLinkiP40424.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pre-B-cell leukemia transcription factor 1
    Alternative name(s):
    Homeobox protein PBX1
    Homeobox protein PRL
    Gene namesi
    Name:PBX1
    Synonyms:PRL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:8632. PBX1.

    Subcellular locationi

    Nucleus PROSITE-ProRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProtKB
    3. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving PBX1 is a cause of pre-B-cell acute lymphoblastic leukemia (B-ALL). Translocation t(1;19)(q23;p13.3) with TCF3. TCF3-PBX1 transforms cells by constitutively activating transcription of genes regulated by PBX1 or by other members of the PBX protein family.

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    Orphaneti99860. Precursor B-cell acute lymphoblastic leukemia.
    PharmGKBiPA32970.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 430430Pre-B-cell leukemia transcription factor 1PRO_0000049235Add
    BLAST

    Proteomic databases

    MaxQBiP40424.
    PaxDbiP40424.
    PRIDEiP40424.

    PTM databases

    PhosphoSiteiP40424.

    Expressioni

    Tissue specificityi

    Expressed in all tissues except in cells of the B and T lineage.

    Gene expression databases

    ArrayExpressiP40424.
    BgeeiP40424.
    CleanExiHS_PBX1.
    HS_PRL.
    GenevestigatoriP40424.

    Organism-specific databases

    HPAiCAB018768.
    HPA003505.
    HPA003881.

    Interactioni

    Subunit structurei

    Forms a heterodimer with MEIS1 which binds DNA including a cAMP-responsive sequence in CYP17. Also forms heterotrimers with MEIS1 and a number of HOX proteins including HOXA9, HOXD4, HOXD9 and HOXD10. Interacts with PBXIP1 and TLX1. Isoform PBX1a interacts with MEIS2 isoform 4, SP1, SP3 and KLF4. Isoform PBX1b is part of a PDX1:PBX1b:MEIS2b complex; PBX1b recruits Meis2B to the complex.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FOXC1Q129484EBI-301611,EBI-1175253
    MEIS2O14770-46EBI-301611,EBI-8025850
    TLX1P313142EBI-6390251,EBI-2820655

    Protein-protein interaction databases

    BioGridi111120. 30 interactions.
    IntActiP40424. 7 interactions.
    MINTiMINT-1532549.
    STRINGi9606.ENSP00000405890.

    Structurei

    Secondary structure

    1
    430
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi242 – 25413
    Turni255 – 2573
    Helixi263 – 27311
    Helixi277 – 29317
    Turni295 – 3006
    Helixi301 – 3044

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B72X-ray2.35B233-319[»]
    1PUFX-ray1.90B233-305[»]
    ProteinModelPortaliP40424.
    SMRiP40424. Positions 233-305.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP40424.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi127 – 1359Poly-Ala

    Sequence similaritiesi

    Belongs to the TALE/PBX homeobox family.Curated
    Contains 1 homeobox DNA-binding domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Homeobox

    Phylogenomic databases

    eggNOGiNOG248144.
    HOGENOMiHOG000266972.
    HOVERGENiHBG000122.
    InParanoidiP40424.
    KOiK09355.
    OMAiNIQSQVD.
    PhylomeDBiP40424.
    TreeFamiTF314340.

    Family and domain databases

    Gene3Di1.10.10.60. 1 hit.
    InterProiIPR017970. Homeobox_CS.
    IPR001356. Homeobox_dom.
    IPR009057. Homeodomain-like.
    IPR005542. PBX.
    [Graphical view]
    PfamiPF00046. Homeobox. 1 hit.
    PF03792. PBC. 1 hit.
    [Graphical view]
    SMARTiSM00389. HOX. 1 hit.
    [Graphical view]
    SUPFAMiSSF46689. SSF46689. 1 hit.
    PROSITEiPS00027. HOMEOBOX_1. 1 hit.
    PS50071. HOMEOBOX_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform PBX1a (identifier: P40424-1) [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

    MDEQPRLMHS HAGVGMAGHP GLSQHLQDGA GGTEGEGGRK QDIGDILQQI    50
    MTITDQSLDE AQARKHALNC HRMKPALFNV LCEIKEKTVL SIRGAQEEEP 100
    TDPQLMRLDN MLLAEGVAGP EKGGGSAAAA AAAAASGGAG SDNSVEHSDY 150
    RAKLSQIRQI YHTELEKYEQ ACNEFTTHVM NLLREQSRTR PISPKEIERM 200
    VSIIHRKFSS IQMQLKQSTC EAVMILRSRF LDARRKRRNF NKQATEILNE 250
    YFYSHLSNPY PSEEAKEELA KKCGITVSQV SNWFGNKRIR YKKNIGKFQE 300
    EANIYAAKTA VTATNVSAHG SQANSPSTPN SAGSSSSFNM SNSGDLFMSV 350
    QSLNGDSYQG AQVGANVQSQ VDTLRHVISQ TGGYSDGLAA SQMYSPQGIS 400
    ANGGWQDATT PSSVTSPTEG PGSVHSDTSN 430
    Length:430
    Mass (Da):46,626
    Last modified:February 1, 1995 - v1
    Checksum:iAD3FFACBC5A9E715
    GO
    Isoform PBX1b (identifier: P40424-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         334-347: SSSSFNMSNSGDLF → GYPSPCYQPDRRIQ
         348-430: Missing.

    Show »
    Length:347
    Mass (Da):38,427
    Checksum:iC4A2BDDD4A410C20
    GO
    Isoform 3 (identifier: P40424-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         401-430: ANGGWQDATTPSSVTSPTEGPGSVHSDTSN → HLPRHPRQAHYHFRLPTWHP

    Note: No experimental confirmation available.

    Show »
    Length:420
    Mass (Da):46,265
    Checksum:i1CC4B8B2EA51E509
    GO

    Sequence cautioni

    The sequence AAA36764.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti351 – 3511Q → H in BAG61583. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti31 – 311G → S.1 Publication
    Corresponds to variant rs2275558 [ dbSNP | Ensembl ].
    VAR_068904

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei334 – 34714SSSSF…SGDLF → GYPSPCYQPDRRIQ in isoform PBX1b. CuratedVSP_002271Add
    BLAST
    Alternative sequencei348 – 43083Missing in isoform PBX1b. CuratedVSP_002272Add
    BLAST
    Alternative sequencei401 – 43030ANGGW…SDTSN → HLPRHPRQAHYHFRLPTWHP in isoform 3. 1 PublicationVSP_044499Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M86546 mRNA. Translation: AAA60031.1.
    AF313404
    , AF313396, AF313397, AF313398, AF313399, AF313400, AF313401, AF313402, AF313403 Genomic DNA. Translation: AAG30941.1.
    AK299673 mRNA. Translation: BAG61583.1.
    AL359255, AL357568, AL390119 Genomic DNA. Translation: CAI14854.1.
    AL390119, AL359255, AL357568 Genomic DNA. Translation: CAH73499.1.
    AL357568, AL390119, AL359255 Genomic DNA. Translation: CAI14908.1.
    AL391001 Genomic DNA. No translation available.
    BC101578 mRNA. Translation: AAI01579.1.
    M31522 mRNA. Translation: AAA36764.1. Different initiation.
    CCDSiCCDS1246.1. [P40424-1]
    CCDS55653.1. [P40424-3]
    CCDS55654.1. [P40424-2]
    PIRiB34734.
    RefSeqiNP_001191892.1. NM_001204963.1. [P40424-3]
    NP_002576.1. NM_002585.3. [P40424-1]
    XP_005245286.1. XM_005245229.1. [P40424-1]
    UniGeneiHs.557097.

    Genome annotation databases

    EnsembliENST00000367897; ENSP00000356872; ENSG00000185630. [P40424-2]
    ENST00000420696; ENSP00000405890; ENSG00000185630. [P40424-1]
    ENST00000540236; ENSP00000439943; ENSG00000185630. [P40424-3]
    GeneIDi5087.
    KEGGihsa:5087.
    UCSCiuc001gct.3. human. [P40424-1]
    uc010pku.2. human. [P40424-3]

    Polymorphism databases

    DMDMi730279.

    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M86546 mRNA. Translation: AAA60031.1 .
    AF313404
    , AF313396 , AF313397 , AF313398 , AF313399 , AF313400 , AF313401 , AF313402 , AF313403 Genomic DNA. Translation: AAG30941.1 .
    AK299673 mRNA. Translation: BAG61583.1 .
    AL359255 , AL357568 , AL390119 Genomic DNA. Translation: CAI14854.1 .
    AL390119 , AL359255 , AL357568 Genomic DNA. Translation: CAH73499.1 .
    AL357568 , AL390119 , AL359255 Genomic DNA. Translation: CAI14908.1 .
    AL391001 Genomic DNA. No translation available.
    BC101578 mRNA. Translation: AAI01579.1 .
    M31522 mRNA. Translation: AAA36764.1 . Different initiation.
    CCDSi CCDS1246.1. [P40424-1 ]
    CCDS55653.1. [P40424-3 ]
    CCDS55654.1. [P40424-2 ]
    PIRi B34734.
    RefSeqi NP_001191892.1. NM_001204963.1. [P40424-3 ]
    NP_002576.1. NM_002585.3. [P40424-1 ]
    XP_005245286.1. XM_005245229.1. [P40424-1 ]
    UniGenei Hs.557097.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B72 X-ray 2.35 B 233-319 [» ]
    1PUF X-ray 1.90 B 233-305 [» ]
    ProteinModelPortali P40424.
    SMRi P40424. Positions 233-305.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111120. 30 interactions.
    IntActi P40424. 7 interactions.
    MINTi MINT-1532549.
    STRINGi 9606.ENSP00000405890.

    Chemistry

    BindingDBi P40424.

    PTM databases

    PhosphoSitei P40424.

    Polymorphism databases

    DMDMi 730279.

    Proteomic databases

    MaxQBi P40424.
    PaxDbi P40424.
    PRIDEi P40424.

    Protocols and materials databases

    DNASUi 5087.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367897 ; ENSP00000356872 ; ENSG00000185630 . [P40424-2 ]
    ENST00000420696 ; ENSP00000405890 ; ENSG00000185630 . [P40424-1 ]
    ENST00000540236 ; ENSP00000439943 ; ENSG00000185630 . [P40424-3 ]
    GeneIDi 5087.
    KEGGi hsa:5087.
    UCSCi uc001gct.3. human. [P40424-1 ]
    uc010pku.2. human. [P40424-3 ]

    Organism-specific databases

    CTDi 5087.
    GeneCardsi GC01P164524.
    HGNCi HGNC:8632. PBX1.
    HPAi CAB018768.
    HPA003505.
    HPA003881.
    MIMi 176310. gene.
    neXtProti NX_P40424.
    Orphaneti 99860. Precursor B-cell acute lymphoblastic leukemia.
    PharmGKBi PA32970.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG248144.
    HOGENOMi HOG000266972.
    HOVERGENi HBG000122.
    InParanoidi P40424.
    KOi K09355.
    OMAi NIQSQVD.
    PhylomeDBi P40424.
    TreeFami TF314340.

    Enzyme and pathway databases

    Reactomei REACT_200812. Transcriptional regulation of pluripotent stem cells.
    SignaLinki P40424.

    Miscellaneous databases

    ChiTaRSi PBX1. human.
    EvolutionaryTracei P40424.
    GeneWikii PBX1.
    GenomeRNAii 5087.
    NextBioi 19618.
    PROi P40424.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P40424.
    Bgeei P40424.
    CleanExi HS_PBX1.
    HS_PRL.
    Genevestigatori P40424.

    Family and domain databases

    Gene3Di 1.10.10.60. 1 hit.
    InterProi IPR017970. Homeobox_CS.
    IPR001356. Homeobox_dom.
    IPR009057. Homeodomain-like.
    IPR005542. PBX.
    [Graphical view ]
    Pfami PF00046. Homeobox. 1 hit.
    PF03792. PBC. 1 hit.
    [Graphical view ]
    SMARTi SM00389. HOX. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46689. SSF46689. 1 hit.
    PROSITEi PS00027. HOMEOBOX_1. 1 hit.
    PS50071. HOMEOBOX_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "PBX2 and PBX3, new homeobox genes with extensive homology to the human proto-oncogene PBX1."
      Monica K., Galili N., Nourse J., Saltman D., Cleary M.L.
      Mol. Cell. Biol. 11:6149-6157(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PBX1A).
    2. "Analysis of PBX1 as a candidate gene for type 2 diabetes mellitus in Pima Indians."
      Thameem F., Wolford J.K., Bogardus C., Prochazka M.
      Biochim. Biophys. Acta 1518:215-220(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM PBX1A).
    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] (ISOFORM 3), VARIANT SER-31.
      Tissue: Brain.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 PBX1A).
      Tissue: Brain.
    6. "A new homeobox gene contributes the DNA binding domain of the t(1;19) translocation protein in pre-B ALL."
      Kamps M.P., Murre C., Sun X.-H., Baltimore D.
      Cell 60:547-555(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 89-430, CHROMOSOMAL TRANSLOCATION WITH TCF3.
    7. "The t(1;19)(q23;p13) results in consistent fusion of E2A and PBX1 coding sequences in acute lymphoblastic leukemias."
      Hunger S.P., Galili N., Carroll A.J., Crist W.M., Link M.P., Cleary M.L.
      Blood 77:687-693(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH TCF3.
    8. "Pbx1 is converted into a transcriptional activator upon acquiring the N-terminal region of E2A in pre-B-cell acute lymphoblastoid leukemia."
      van Dijk M.A., Voorhoeve P.M., Murre C.
      Proc. Natl. Acad. Sci. U.S.A. 90:6061-6065(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    9. "Fusion with E2A converts the Pbx1 homeodomain protein into a constitutive transcriptional activator in human leukemias carrying the t(1;19) translocation."
      Lu Q., Wright D.D., Kamps M.P.
      Mol. Cell. Biol. 14:3938-3948(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    10. "Functional cloning and characterization of a novel nonhomeodomain protein that inhibits the binding of PBX1-HOX complexes to DNA."
      Abramovich C., Shen W.-F., Pineault N., Imren S., Montpetit B., Largman C., Humphries R.K.
      J. Biol. Chem. 275:26172-26177(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PBXIP1.
    11. "Homeodomain proteins MEIS1 and PBXs regulate the lineage-specific transcription of the platelet factor 4 gene."
      Okada Y., Nagai R., Sato T., Matsuura E., Minami T., Morita I., Doi T.
      Blood 101:4748-4756(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MEIS1.
    12. "An autoinhibitory effect of the homothorax domain of Meis2."
      Hyman-Walsh C., Bjerke G.A., Wotton D.
      FEBS J. 277:2584-2597(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MEIS2.
    13. Cited for: INTERACTION WITH TLX1.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Cooperative transcriptional activation by Klf4, Meis2, and Pbx1."
      Bjerke G.A., Hyman-Walsh C., Wotton D.
      Mol. Cell. Biol. 31:3723-3733(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SP1; SP3 AND KLF4.
    16. "Structure of a HoxB1-Pbx1 heterodimer bound to DNA: role of the hexapeptide and a fourth homeodomain helix in complex formation."
      Piper D.E., Batchelor A.H., Chang C.-P., Cleary M.L., Wolberger C.
      Cell 96:587-597(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 233-319 IN COMPLEX WITH HOXB1.

    Entry informationi

    Entry nameiPBX1_HUMAN
    AccessioniPrimary (citable) accession number: P40424
    Secondary accession number(s): B4DSC1, F5H4U9, Q5T488
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 156 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 1
      Human chromosome 1: 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