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P40424

- PBX1_HUMAN

UniProt

P40424 - PBX1_HUMAN

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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

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. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  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 transcription factor activity Source: ProtInc
  5. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP40424.
CleanExiHS_PBX1.
HS_PRL.
ExpressionAtlasiP40424. baseline and differential.
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. 34 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.
GeneTreeiENSGT00390000016426.
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

        10         20         30         40         50
MDEQPRLMHS HAGVGMAGHP GLSQHLQDGA GGTEGEGGRK QDIGDILQQI
60 70 80 90 100
MTITDQSLDE AQARKHALNC HRMKPALFNV LCEIKEKTVL SIRGAQEEEP
110 120 130 140 150
TDPQLMRLDN MLLAEGVAGP EKGGGSAAAA AAAAASGGAG SDNSVEHSDY
160 170 180 190 200
RAKLSQIRQI YHTELEKYEQ ACNEFTTHVM NLLREQSRTR PISPKEIERM
210 220 230 240 250
VSIIHRKFSS IQMQLKQSTC EAVMILRSRF LDARRKRRNF NKQATEILNE
260 270 280 290 300
YFYSHLSNPY PSEEAKEELA KKCGITVSQV SNWFGNKRIR YKKNIGKFQE
310 320 330 340 350
EANIYAAKTA VTATNVSAHG SQANSPSTPN SAGSSSSFNM SNSGDLFMSV
360 370 380 390 400
QSLNGDSYQG AQVGANVQSQ VDTLRHVISQ TGGYSDGLAA SQMYSPQGIS
410 420 430
ANGGWQDATT PSSVTSPTEG PGSVHSDTSN
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]
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]
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 ]
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. 34 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 ]
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.
GeneTreei ENSGT00390000016426.
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

Bgeei P40424.
CleanExi HS_PBX1.
HS_PRL.
ExpressionAtlasi P40424. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 157 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