Pbx1

Pre-B-cell leukemia homeobox 1

Cartoon diagram of a HOXB1–PBX1 heterodimer (violet) binding a DNA fragment (blue). Rendering based on PDB 1b72.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1B72, 1PUF

Identifiers

Symbols

PBX1; DKFZp686B09108; MGC126627

External IDs

OMIM: 176310 MGI: 97495 HomoloGene: 20574 ChEMBL: 4587 GeneCards: PBX1 Gene

Gene Ontology
Molecular function	• DNA binding • sequence-specific DNA binding transcription factor activity • protein binding • transcription factor binding • sequence-specific DNA binding • protein heterodimerization activity
Cellular component	• nucleus • transcription factor complex • nucleolus • cytoplasm
Biological process	• urogenital system development • branching involved in ureteric bud morphogenesis • regulation of transcription, DNA-dependent • steroid biosynthetic process • sex differentiation • positive regulation of cell proliferation • organ morphogenesis • anterior/posterior pattern specification • proximal/distal pattern formation • cell differentiation • regulation of ossification • adrenal gland development • embryonic limb morphogenesis • embryonic hemopoiesis • negative regulation of sequence-specific DNA binding transcription factor activity • negative regulation of neuron differentiation • positive regulation of transcription from RNA polymerase II promoter • spleen development • thymus development • embryonic skeletal system development
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
164.52 – 164.87 Mb

Chr 1:
170.05 – 170.36 Mb

PubMed search

[1]

[2]

Pre-B-cell leukemia transcription factor 1 is a protein that in humans is encoded by the PBX1 gene.^[1]

1 Interactions
2 References
3 Further reading
4 External links

Interactions [link]

PBX1 has been shown to interact with HOXB1,^[2]^[3] MEIS1^[4]^[5]^[6] and HOXB7.^[7]

References [link]

^ "Entrez Gene: PBX1 Pre-B-cell leukemia homeobox 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5087.
^ Berthelsen, J; Zappavigna V, Ferretti E, Mavilio F, Blasi F (Mar. 1998). "The novel homeoprotein Prep1 modulates Pbx-Hox protein cooperativity". EMBO J. (ENGLAND) 17 (5): 1434–45. DOI:10.1093/emboj/17.5.1434. ISSN 0261-4189. PMC 1170491. PMID 9482740. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1170491.
^ Piper, D E; Batchelor A H, Chang C P, Cleary M L, Wolberger C (Feb. 1999). "Structure of a HoxB1-Pbx1 heterodimer bound to DNA: role of the hexapeptide and a fourth homeodomain helix in complex formation". Cell (UNITED STATES) 96 (4): 587–97. DOI:10.1016/S0092-8674(00)80662-5. ISSN 0092-8674. PMID 10052460.
^ Shen, W F; Rozenfeld S, Kwong A, Köm ves L G, Lawrence H J, Largman C (Apr. 1999). "HOXA9 Forms Triple Complexes with PBX2 and MEIS1 in Myeloid Cells". Mol. Cell. Biol. (UNITED STATES) 19 (4): 3051–61. ISSN 0270-7306. PMC 84099. PMID 10082572. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=84099.
^ Shanmugam, K; Green N C, Rambaldi I, Saragovi H U, Featherstone M S (Nov. 1999). "PBX and MEIS as Non-DNA-Binding Partners in Trimeric Complexes with HOX Proteins". Mol. Cell. Biol. (UNITED STATES) 19 (11): 7577–88. ISSN 0270-7306. PMC 84774. PMID 10523646. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=84774.
^ Jacobs, Y; Schnabel C A, Cleary M L (Jul. 1999). "Trimeric Association of Hox and TALE Homeodomain Proteins Mediates Hoxb2 Hindbrain Enhancer Activity". Mol. Cell. Biol. (UNITED STATES) 19 (7): 5134–42. ISSN 0270-7306. PMC 84356. PMID 10373562. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=84356.
^ Chang, C P; Shen W F, Rozenfeld S, Lawrence H J, Largman C, Cleary M L (Mar. 1995). "Pbx proteins display hexapeptide-dependent cooperative DNA binding with a subset of Hox proteins". Genes Dev. (UNITED STATES) 9 (6): 663–74. DOI:10.1101/gad.9.6.663. ISSN 0890-9369. PMID 7729685.

Further reading [link]

Sanyal M, Tung JW (2007). "B-cell development fails in the absence of the Pbx1 proto-oncogene". Blood. 109 (10): 4191–9. DOI:10.1182/blood-2006-10-054213. PMC 1885499. PMID 17244677. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1885499.
Hui H, Perfetti R (2002). "Pancreas duodenum homeobox-1 regulates pancreas development during embryogenesis and islet cell function in adulthood". Eur. J. Endocrinol. 146 (2): 129–41. DOI:10.1530/eje.0.1460129. PMID 11834421.
Hunger SP, Galili N, Carroll AJ, et al. (1991). "The t(1;19)(q23;p13) results in consistent fusion of E2A and PBX1 coding sequences in acute lymphoblastic leukemias". Blood 77 (4): 687–93. PMID 1671560.
Monica K, Galili N, Nourse J, et al. (1991). "PBX2 and PBX3, new homeobox genes with extensive homology to the human proto-oncogene PBX1". Mol. Cell. Biol. 11 (12): 6149–57. PMC 361792. PMID 1682799. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=361792.
Nourse J, Mellentin JD, Galili N, et al. (1990). "Chromosomal translocation t(1;19) results in synthesis of a homeobox fusion mRNA that codes for a potential chimeric transcription factor". Cell 60 (4): 535–45. DOI:10.1016/0092-8674(90)90657-Z. PMID 1967982.
Kamps MP, Murre C, Sun XH, Baltimore D (1990). "A new homeobox gene contributes the DNA binding domain of the t(1;19) translocation protein in pre-B ALL". Cell 60 (4): 547–55. DOI:10.1016/0092-8674(90)90658-2. PMID 1967983.
Lu Q, Wright DD, Kamps MP (1994). "Fusion with E2A converts the Pbx1 homeodomain protein into a constitutive transcriptional activator in human leukemias carrying the t(1;19) translocation". Mol. Cell. Biol. 14 (6): 3938–48. PMC 358760. PMID 7910944. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=358760.
Van Dijk MA, Voorhoeve PM, Murre C (1993). "Pbx1 is converted into a transcriptional activator upon acquiring the N-terminal region of E2A in pre-B-cell acute lymphoblastoid leukemia". Proc. Natl. Acad. Sci. U.S.A. 90 (13): 6061–5. DOI:10.1073/pnas.90.13.6061. PMC 46867. PMID 8327485. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=46867.
Lu Q, Kamps MP (1996). "Structural determinants within Pbx1 that mediate cooperative DNA binding with pentapeptide-containing Hox proteins: proposal for a model of a Pbx1-Hox-DNA complex". Mol. Cell. Biol. 16 (4): 1632–40. PMC 231149. PMID 8657138. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=231149.
Berthelsen J, Zappavigna V, Mavilio F, Blasi F (1998). "Prep1, a novel functional partner of Pbx proteins". EMBO J. 17 (5): 1423–33. DOI:10.1093/emboj/17.5.1423. PMC 1170490. PMID 9482739. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1170490.
Berthelsen J, Zappavigna V, Ferretti E, et al. (1998). "The novel homeoprotein Prep1 modulates Pbx-Hox protein cooperativity". EMBO J. 17 (5): 1434–45. DOI:10.1093/emboj/17.5.1434. PMC 1170491. PMID 9482740. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1170491.
Piper DE, Batchelor AH, Chang CP, et al. (1999). "Structure of a HoxB1-Pbx1 heterodimer bound to DNA: role of the hexapeptide and a fourth homeodomain helix in complex formation". Cell 96 (4): 587–97. DOI:10.1016/S0092-8674(00)80662-5. PMID 10052460.
Shen WF, Rozenfeld S, Kwong A, et al. (1999). "HOXA9 Forms Triple Complexes with PBX2 and MEIS1 in Myeloid Cells". Mol. Cell. Biol. 19 (4): 3051–61. PMC 84099. PMID 10082572. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=84099.
Jacobs Y, Schnabel CA, Cleary ML (1999). "Trimeric Association of Hox and TALE Homeodomain Proteins Mediates Hoxb2 Hindbrain Enhancer Activity". Mol. Cell. Biol. 19 (7): 5134–42. PMC 84356. PMID 10373562. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=84356.
Knoepfler PS, Bergstrom DA, Uetsuki T, et al. (1999). "A conserved motif N-terminal to the DNA-binding domains of myogenic bHLH transcription factors mediates cooperative DNA binding with pbx-Meis1/Prep1". Nucleic Acids Res. 27 (18): 3752–61. DOI:10.1093/nar/27.18.3752. PMC 148632. PMID 10471746. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=148632.
McWhirter JR, Neuteboom ST, Wancewicz EV, et al. (1999). "Oncogenic homeodomain transcription factor E2A-Pbx1 activates a novel WNT gene in pre-B acute lymphoblastoid leukemia". Proc. Natl. Acad. Sci. U.S.A. 96 (20): 11464–9. DOI:10.1073/pnas.96.20.11464. PMC 18056. PMID 10500199. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=18056.
Shanmugam K, Green NC, Rambaldi I, et al. (1999). "PBX and MEIS as Non-DNA-Binding Partners in Trimeric Complexes with HOX Proteins". Mol. Cell. Biol. 19 (11): 7577–88. PMC 84774. PMID 10523646. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=84774.
Mikkola I, Bruun JA, Holm T, Johansen T (2001). "Superactivation of Pax6-mediated transactivation from paired domain-binding sites by dna-independent recruitment of different homeodomain proteins". J. Biol. Chem. 276 (6): 4109–18. DOI:10.1074/jbc.M008882200. PMID 11069920.
Thameem F, Wolford JK, Bogardus C, Prochazka M (2001). "Analysis of PBX1 as a candidate gene for type 2 diabetes mellitus in Pima Indians". Biochim. Biophys. Acta 1518 (1–2): 215–20. PMID 11267683.
Liu Y, MacDonald RJ, Swift GH (2001). "DNA binding and transcriptional activation by a PDX1.PBX1b.MEIS2b trimer and cooperation with a pancreas-specific basic helix-loop-helix complex". J. Biol. Chem. 276 (21): 17985–93. DOI:10.1074/jbc.M100678200. PMID 11279116.
Mal A, Sturniolo M, Schiltz RL, et al. (2001). "A role for histone deacetylase HDAC1 in modulating the transcriptional activity of MyoD: inhibition of the myogenic program". EMBO J. 20 (7): 1739–53. DOI:10.1093/emboj/20.7.1739. PMC 145490. PMID 11285237. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=145490.

PDB gallery

1b72: PBX1, HOMEOBOX PROTEIN HOX-B1/DNA TERNARY COMPLEX

1b8i: STRUCTURE OF THE HOMEOTIC UBX/EXD/DNA TERNARY COMPLEX

1du6: SOLUTION STRUCTURE OF THE TRUNCATED PBX HOMEODOMAIN

1lfu: NMR Solution Stucture of the Extended PBX Homeodomain Bound to DNA

1puf: Crystal Structure of HoxA9 and Pbx1 homeodomains bound to DNA

External links [link]

PBX1+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)

This article on a gene on chromosome 1 is a stub. You can help Wikipedia by expanding it.

Transcription factors and intracellular receptors

(1) Basic domains

(1.1) Basic leucine zipper (bZIP)	Activating transcription factor (AATF, 1, 2, 3, 4, 5, 6, 7) · AP-1 (c-Fos, FOSB, FOSL1, FOSL2, JDP2, c-Jun, JUNB, JUND) · BACH (1, 2) · BATF · BLZF1 · C/EBP (α, β, γ, δ, ε, ζ) · CREB (1, 3, L1) · CREM · DBP · DDIT3 · GABPA · HLF · MAF (B, F, G, K) · NFE (2, L1, L2, L3) · NFIL3 · NRL · NRF (1, 2, 3) · XBP1

(1.2) Basic helix-loop-helix (bHLH)	ATOH1 · AhR · AHRR · ARNT · ASCL1 · BHLH (2, 9) · BMAL (ARNTL, ARNTL2) · CLOCK · EPAS1 · FIGLA · HAND (1, 2) · HES (5, 6) · HEY (1, 2, L) · HES1 · HIF (1A, 3A) · ID (1, 2, 3, 4) · LYL1 · MESP2 · MXD4 · MYCL1 · MYCN · Myogenic regulatory factors (MyoD, Myogenin, MYF5, MYF6) · Neurogenins (1, 2, 3) · NeuroD (1, 2) · NPAS (1, 2, 3) · OLIG (1, 2) · Pho4 · Scleraxis · SIM (1, 2) · TAL (1, 2) · Twist · USF1

(1.3) bHLH-ZIP	AP-4 · MAX · MITF · MNT · MLX · MXI1 · Myc · SREBP (1, 2)

(1.4) NF-1	NFI (A, B, C, X) · SMAD (R-SMAD (1, 2, 3, 5, 9) - I-SMAD (6, 7) - 4)

(1.5) RF-X	RFX (1, 2, 3, 4, 5, 6, ANK)

(1.6) Basic helix-span-helix (bHSH)	AP-2 (α, β, γ, δ, ε)

(2) Zinc finger DNA-binding domains

(2.1) Nuclear receptor (Cys₄)	subfamily 1 (Thyroid hormone (α, β), CAR, FXR, LXR (α, β), PPAR (α, β/δ, γ), PXR, RAR (α, β, γ), ROR (α, β, γ), Rev-ErbA (α, β), VDR) subfamily 2 (COUP-TF (I, II), Ear-2, HNF4 (α, γ), PNR, RXR (α, β, γ), Testicular receptor (2, 4), TLX) subfamily 3 (Steroid hormone (Androgen, Estrogen (α, β), Glucocorticoid, Mineralocorticoid, Progesterone), Estrogen related (α, β, γ)) subfamily 4 NUR (NGFIB, NOR1, NURR1) · subfamily 5 (LRH-1, SF1) · subfamily 6 (GCNF) · subfamily 0 (DAX1, SHP)

(2.2) Other Cys₄	GATA (1, 2, 3, 4, 5, 6) · MTA (1, 2, 3) · TRPS1

(2.3) Cys₂His₂	General transcription factors (TFIIA, TFIIB, TFIID, TFIIE (1, 2), TFIIF (1, 2), TFIIH (1, 2, 4, 2I, 3A, 3C1, 3C2)) ATBF1 · BCL (6, 11A, 11B) · CTCF · E4F1 · EGR (1, 2, 3, 4) · ERV3 · GFI1 · GLI-Krüppel family (1, 2, 3, REST, S2, YY1) · HIC (1, 2) · HIVEP (1, 2, 3) · IKZF (1, 2, 3) · ILF (2, 3) · KLF (2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 17) · MTF1 · MYT1 · OSR1 · PRDM9 · SALL (1, 2, 3, 4) · SP (1, 2, 4, 7, 8) · TSHZ3 · WT1 · Zbtb7 (7A, 7B) · ZBTB (11, 16, 17, 20, 32, 33, 40) · zinc finger (3, 7, 9, 10, 19, 22, 24, 33B, 34, 35, 41, 43, 44, 51, 74, 143, 146, 148, 165, 202, 217, 219, 238, 239, 259, 267, 268, 281, 295, 300, 318, 330, 346, 350, 365, 366, 384, 423, 451, 452, 471, 593, 638, 644, 649, 655)

(2.4) Cys₆	HIVEP1

(2.5) Alternating composition	AIRE · DIDO1 · GRLF1 · ING (1, 2, 4) · JARID (1A, 1B, 1C, 1D, 2) · JMJD1B

(3) Helix-turn-helix domains

(3.1) Homeodomain	ARX · CDX (1, 2) · CRX · CUTL1 · DBX (1, 2) · DLX (3, 4, 5) · EMX (1, 2) · EN (1, 2) · FHL (1, 2, 3) · HESX1 · HHEX · HLX · Homeobox (A1, A2, A3, A4, A5, A7, A9, A10, A11, A13, B1, B2, B3, B4, B5, B6, B7, B8, B9, B13, C4, C5, C6, C8, C9, C10, C11, C12, C13, D1, D3, D4, D8, D9, D10, D11, D12, D13) · HOPX · IRX (1, 2, 3, 4, 5, 6, MKX) · LMX (1A, 1B) · MEIS (1, 2) · MEOX2 · MNX1 · MSX (1, 2) · NANOG · NKX (2-1, 2-2, 2-3, 2-5, 3-1, 3-2, 6-1, 6-2) · NOBOX · PBX (1, 2, 3) · PHF (1, 3, 6, 8, 10, 16, 17, 20, 21A) · PHOX (2A, 2B) · PITX (1, 2, 3) · POU domain (PIT-1, BRN-3: A, B, C, Octamer transcription factor: 1, 2, 3/4, 6, 7, 11) · OTX (1, 2) · PDX1 · SATB2 · SHOX2 · SIX (1, 2, 3, 4, 5) · VAX1 · ZEB (1, 2)

(3.2) Paired box	PAX (1, 2, 3, 4, 5, 6, 7, 8, 9)

(3.3) Fork head / winged helix	E2F (1, 2, 3, 4, 5) · FOX proteins (A1, A2, A3, C1, C2, D3, D4, E1, E3, F1, G1, H1, I1, J1, J2, K1, K2, L2, M1, N1, N3, O1, O3, O4, P1, P2, P3, P4)

(3.4) Heat Shock Factors	HSF (1, 2, 4)

(3.5) Tryptophan clusters	ELF (2, 4, 5) · EGF · ELK (1, 3, 4) · ERF · ETS (1, 2, ERG, SPIB) · ETV (1, 4, 5, 6) · FLI1 · Interferon regulatory factors (1, 2, 3, 4, 5, 6, 7, 8) · MYB · MYBL2

(3.6) TEA domain	transcriptional enhancer factor (1, 2, 3, 4)

(4) β-Scaffold factors with minor groove contacts

(4.1) Rel homology region	NF-κB (NFKB1, NFKB2, REL, RELA, RELB) · NFAT (C1, C2, C3, C4, 5)

(4.2) STAT	STAT (1, 2, 3, 4, 5, 6)

(4.3) p53	p53 · TBX (1, 2, 3, 5, 19, 21, 22, Brachyury, TBR1, TBR2) · TP63

(4.4) MADS box	Mef2 (A, B, C, D) · SRF

(4.6) TATA binding proteins	TBP · TBPL1

(4.7) High-mobility group	BBX · HMGB (1, 2, 3, 4) · HMGN (1, 2, 3, 4) · HNF (1A, 1B) · LEF1 · SOX (1, 2, 3, 4, 5, 6, 8, 9, 10, 11, 12, 13, 14, 15, 18, 21) · SRY · SSRP1 · TCF (3, 4) · TOX (1, 2, 3, 4)

(4.9) Grainyhead	TFCP2

(4.10) Cold-shock domain	CSDA, YBX1

(4.11) Runt	CBF (CBFA2T2, CBFA2T3, RUNX1, RUNX2, RUNX3, RUNX1T1)

(0) Other transcription factors

(0.2) HMGI(Y)	HMGA (1, 2) · HBP1

(0.3) Pocket domain	Rb · RBL1 · RBL2

(0.5) AP-2/EREBP-related factors	Apetala 2 · EREBP · B3

(0.6) Miscellaneous	ARID (1A, 1B, 2, 3A, 3B, 4A) · CAP · IFI (16, 35) · MLL (2, 3, T1) · MNDA · NFY (A, B, C) · Rho/Sigma

see also transcription factor/coregulator deficiencies
B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)

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