POU2F1

Protein-coding gene in the species Homo sapiens
POU2F1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1CQT, 1E3O, 1GT0, 1HF0, 1O4X, 1OCT, 1POG

Identifiers
AliasesPOU2F1, OCT1, OTF1, oct-1B, POU class 2 homeobox 1, Oct1Z
External IDsOMIM: 164175; MGI: 101898; HomoloGene: 37658; GeneCards: POU2F1; OMA:POU2F1 - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for POU2F1
Genomic location for POU2F1
Band1q24.2Start167,220,876 bp[1]
End167,427,345 bp[1]
Gene location (Mouse)
Chromosome 1 (mouse)
Chr.Chromosome 1 (mouse)[2]
Chromosome 1 (mouse)
Genomic location for POU2F1
Genomic location for POU2F1
Band1 H2.3|1 73.21 cMStart165,692,723 bp[2]
End165,830,247 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • buccal mucosa cell

  • secondary oocyte

  • sural nerve

  • gonad

  • testicle

  • Achilles tendon

  • cerebellar vermis

  • Skeletal muscle tissue of rectus abdominis

  • tendon of biceps brachii

  • epithelium of colon
Top expressed in
  • secondary oocyte

  • primitive streak

  • renal corpuscle

  • ciliary body

  • ascending aorta

  • internal carotid artery

  • external carotid artery

  • ankle joint

  • retina

  • pineal gland
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • sequence-specific DNA binding
  • protein binding
  • RNA polymerase II core promoter sequence-specific DNA binding
  • RNA polymerase II general transcription initiation factor activity
  • DNA binding
  • DNA-binding transcription factor activity
  • DNA-binding transcription factor activity, RNA polymerase II-specific
  • RNA polymerase II cis-regulatory region sequence-specific DNA binding
Cellular component
  • endoplasmic reticulum
  • nucleus
  • intracellular membrane-bounded organelle
  • nucleoplasm
  • RNA polymerase II transcription regulator complex
Biological process
  • negative regulation of transcription, DNA-templated
  • regulation of transcription, DNA-templated
  • transcription, DNA-templated
  • snRNA transcription by RNA polymerase II
  • positive regulation of transcription by RNA polymerase II
  • cytokine-mediated signaling pathway
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5451

18986

Ensembl

ENSG00000143190

ENSMUSG00000026565

UniProt

P14859

P25425

RefSeq (mRNA)

NM_001198783
NM_001198786
NM_002697
NM_001365848
NM_001365849

NM_011137
NM_198932
NM_198933
NM_198934
NM_001368808

RefSeq (protein)

NP_001185712
NP_001185715
NP_002688
NP_001352777
NP_001352778

NP_035267
NP_945150
NP_945151
NP_945152
NP_001355737

Location (UCSC)Chr 1: 167.22 – 167.43 MbChr 1: 165.69 – 165.83 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

POU domain, class 2, transcription factor 1 is a protein that in humans is encoded by the POU2F1 gene.[5][6]

Interactions

POU2F1 has been shown to interact with:

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000143190 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026565 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Roberts SB, Segil N, Heintz N (October 1991). "Differential phosphorylation of the transcription factor Oct1 during the cell cycle". Science. 253 (5023): 1022–6. doi:10.1126/science.1887216. PMID 1887216. S2CID 23291453.
  6. ^ "Entrez Gene: POU2F1 POU domain, class 2, transcription factor 1".
  7. ^ Nie J, Sakamoto S, Song D, Qu Z, Ota K, Taniguchi T (March 1998). "Interaction of Oct-1 and automodification domain of poly(ADP-ribose) synthetase". FEBS Lett. 424 (1–2): 27–32. doi:10.1016/s0014-5793(98)00131-8. PMID 9537509. S2CID 872132.
  8. ^ a b Préfontaine GG, Walther R, Giffin W, Lemieux ME, Pope L, Haché RJ (September 1999). "Selective binding of steroid hormone receptors to octamer transcription factors determines transcriptional synergism at the mouse mammary tumor virus promoter". J. Biol. Chem. 274 (38): 26713–9. doi:10.1074/jbc.274.38.26713. PMID 10480874.
  9. ^ Wang JM, Préfontaine GG, Lemieux ME, Pope L, Akimenko MA, Haché RJ (October 1999). "Developmental effects of ectopic expression of the glucocorticoid receptor DNA binding domain are alleviated by an amino acid substitution that interferes with homeodomain binding". Mol. Cell. Biol. 19 (10): 7106–22. doi:10.1128/mcb.19.10.7106. PMC 84705. PMID 10490647.
  10. ^ Préfontaine GG, Lemieux ME, Giffin W, Schild-Poulter C, Pope L, LaCasse E, Walker P, Haché RJ (June 1998). "Recruitment of octamer transcription factors to DNA by glucocorticoid receptor". Mol. Cell. Biol. 18 (6): 3416–30. doi:10.1128/mcb.18.6.3416. PMC 108923. PMID 9584182.
  11. ^ a b McKnight S (July 2003). "Gene switching by metabolic enzymes--how did you get on the invitation list?". Cell. 114 (2): 150–2. doi:10.1016/s0092-8674(03)00563-4. PMID 12887915. S2CID 895360.
  12. ^ La Boissière S, Hughes T, O'Hare P (January 1999). "HCF-dependent nuclear import of VP16". EMBO J. 18 (2): 480–9. doi:10.1093/emboj/18.2.480. PMC 1171141. PMID 9889203.
  13. ^ Kristie TM, Sharp PA (March 1993). "Purification of the cellular C1 factor required for the stable recognition of the Oct-1 homeodomain by the herpes simplex virus alpha-trans-induction factor (VP16)". J. Biol. Chem. 268 (9): 6525–34. doi:10.1016/S0021-9258(18)53282-8. PMID 8454622.
  14. ^ Schild-Poulter C, Pope L, Giffin W, Kochan JC, Ngsee JK, Traykova-Andonova M, Haché RJ (May 2001). "The binding of Ku antigen to homeodomain proteins promotes their phosphorylation by DNA-dependent protein kinase". J. Biol. Chem. 276 (20): 16848–56. doi:10.1074/jbc.M100768200. PMID 11279128.
  15. ^ Matheos D, Ruiz MT, Price GB, Zannis-Hadjopoulos M (October 2002). "Ku antigen, an origin-specific binding protein that associates with replication proteins, is required for mammalian DNA replication". Biochim. Biophys. Acta. 1578 (1–3): 59–72. doi:10.1016/s0167-4781(02)00497-9. PMID 12393188.
  16. ^ Inamoto S, Segil N, Pan ZQ, Kimura M, Roeder RG (November 1997). "The cyclin-dependent kinase-activating kinase (CAK) assembly factor, MAT1, targets and enhances CAK activity on the POU domains of octamer transcription factors". J. Biol. Chem. 272 (47): 29852–8. doi:10.1074/jbc.272.47.29852. PMID 9368058.
  17. ^ Kakizawa T, Miyamoto T, Ichikawa K, Takeda T, Suzuki S, Mori J, Kumagai M, Yamashita K, Hashizume K (March 2001). "Silencing mediator for retinoid and thyroid hormone receptors interacts with octamer transcription factor-1 and acts as a transcriptional repressor". J. Biol. Chem. 276 (13): 9720–5. doi:10.1074/jbc.M008531200. PMID 11134019.
  18. ^ a b Wong MW, Henry RW, Ma B, Kobayashi R, Klages N, Matthias P, Strubin M, Hernandez N (January 1998). "The large subunit of basal transcription factor SNAPc is a Myb domain protein that interacts with Oct-1". Mol. Cell. Biol. 18 (1): 368–77. doi:10.1128/mcb.18.1.368. PMC 121507. PMID 9418884.
  19. ^ Chasman D, Cepek K, Sharp PA, Pabo CO (October 1999). "Crystal structure of an OCA-B peptide bound to an Oct-1 POU domain/octamer DNA complex: specific recognition of a protein-DNA interface". Genes Dev. 13 (20): 2650–7. doi:10.1101/gad.13.20.2650. PMC 317104. PMID 10541551.
  20. ^ Lee L, Stollar E, Chang J, Grossmann JG, O'Brien R, Ladbury J, Carpenter B, Roberts S, Luisi B (June 2001). "Expression of the Oct-1 transcription factor and characterization of its interactions with the Bob1 coactivator". Biochemistry. 40 (22): 6580–8. doi:10.1021/bi010095x. PMID 11380252.
  21. ^ van Heel DA, Udalova IA, De Silva AP, McGovern DP, Kinouchi Y, Hull J, Lench NJ, Cardon LR, Carey AH, Jewell DP, Kwiatkowski D (May 2002). "Inflammatory bowel disease is associated with a TNF polymorphism that affects an interaction between the OCT1 and NF(-kappa)B transcription factors". Hum. Mol. Genet. 11 (11): 1281–9. doi:10.1093/hmg/11.11.1281. PMID 12019209.
  22. ^ Kakizawa T, Miyamoto T, Ichikawa K, Kaneko A, Suzuki S, Hara M, Nagasawa T, Takeda T, Mori Ji, Kumagai M, Hashizume K (July 1999). "Functional interaction between Oct-1 and retinoid X receptor". J. Biol. Chem. 274 (27): 19103–8. doi:10.1074/jbc.274.27.19103. PMID 10383413.
  23. ^ Hovde S, Brooks A, Strong K, Geiger JH (March 2002). "Crystallization of the Oct-1/SNAP190 peptide/DNA complex". Acta Crystallogr. D. 58 (Pt 3): 511–2. doi:10.1107/s0907444901021461. PMID 11856838.
  24. ^ Ström AC, Forsberg M, Lillhager P, Westin G (June 1996). "The transcription factors Sp1 and Oct-1 interact physically to regulate human U2 snRNA gene expression". Nucleic Acids Res. 24 (11): 1981–6. doi:10.1093/nar/24.11.1981. PMC 145891. PMID 8668525.
  25. ^ Gunther M, Laithier M, Brison O (July 2000). "A set of proteins interacting with transcription factor Sp1 identified in a two-hybrid screening". Mol. Cell. Biochem. 210 (1–2): 131–42. doi:10.1023/A:1007177623283. PMID 10976766. S2CID 1339642.
  26. ^ Zwilling S, Annweiler A, Wirth T (May 1994). "The POU domains of the Oct1 and Oct2 transcription factors mediate specific interaction with TBP". Nucleic Acids Res. 22 (9): 1655–62. doi:10.1093/nar/22.9.1655. PMC 308045. PMID 8202368.

Further reading

  • Hsieh CL, Sturm R, Herr W, Francke U (1990). "The gene for the ubiquitous octamer-binding protein Oct–1 is on human chromosome 1, region cen-q32, and near Ly-22 and Ltw-4 on mouse chromosome 1". Genomics. 6 (4): 666–72. doi:10.1016/0888-7543(90)90502-L. PMID 2341156.
  • Sturm RA, Das G, Herr W (1989). "The ubiquitous octamer-binding protein Oct–1 contains a POU domain with a homeo box subdomain". Genes Dev. 2 (12A): 1582–99. doi:10.1101/gad.2.12a.1582. PMID 2905684.
  • Nakshatri H, Nakshatri P, Currie RA (1995). "Interaction of Oct–1 with TFIIB. Implications for a novel response elicited through the proximal octamer site of the lipoprotein lipase promoter". J. Biol. Chem. 270 (33): 19613–23. doi:10.1074/jbc.270.33.19613. hdl:1805/18867. PMID 7642649.
  • Cox M, van Tilborg PJ, de Laat W, Boelens R, van Leeuwen HC, van der Vliet PC, Kaptein R (1995). "Solution structure of the Oct–1 POU homeodomain determined by NMR and restrained molecular dynamics". J. Biomol. NMR. 6 (1): 23–32. doi:10.1007/BF00417488. PMID 7663141. S2CID 26063646.
  • Jeang KT, Chun R, Lin NH, Gatignol A, Glabe CG, Fan H (1993). "In vitro and in vivo binding of human immunodeficiency virus type 1 Tat protein and Sp1 transcription factor". J. Virol. 67 (10): 6224–33. doi:10.1128/JVI.67.10.6224-6233.1993. PMC 238044. PMID 7690421.
  • Zwilling S, König H, Wirth T (1995). "High mobility group protein 2 functionally interacts with the POU domains of octamer transcription factors". EMBO J. 14 (6): 1198–208. doi:10.1002/j.1460-2075.1995.tb07103.x. PMC 398197. PMID 7720710.
  • Sturm RA, Eyre HJ, Baker E, Sutherland GR (1995). "The human OTF1 locus which overlaps the CD3Z gene is located at 1q22→q23". Cytogenet. Cell Genet. 68 (3–4): 231–2. doi:10.1159/000133919. PMID 7842742.
  • Klemm JD, Rould MA, Aurora R, Herr W, Pabo CO (1994). "Crystal structure of the Oct–1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules". Cell. 77 (1): 21–32. doi:10.1016/0092-8674(94)90231-3. PMID 8156594. S2CID 36371069.
  • Zwilling S, Annweiler A, Wirth T (1994). "The POU domains of the Oct1 and Oct2 transcription factors mediate specific interaction with TBP". Nucleic Acids Res. 22 (9): 1655–62. doi:10.1093/nar/22.9.1655. PMC 308045. PMID 8202368.
  • Kristie TM, Sharp PA (1993). "Purification of the cellular C1 factor required for the stable recognition of the Oct–1 homeodomain by the herpes simplex virus alpha-trans-induction factor (VP16)". J. Biol. Chem. 268 (9): 6525–34. doi:10.1016/S0021-9258(18)53282-8. PMID 8454622.
  • Assa-Munt N, Mortishire-Smith RJ, Aurora R, Herr W, Wright PE (1993). "The solution structure of the Oct–1 POU-specific domain reveals a striking similarity to the bacteriophage lambda repressor DNA-binding domain". Cell. 73 (1): 193–205. doi:10.1016/0092-8674(93)90171-L. PMID 8462099. S2CID 24276357.
  • Dekker N, Cox M, Boelens R, Verrijzer CP, van der Vliet PC, Kaptein R (1993). "Solution structure of the POU-specific DNA-binding domain of Oct–1". Nature. 362 (6423): 852–5. Bibcode:1993Natur.362..852D. doi:10.1038/362852a0. PMID 8479524. S2CID 21540451.
  • Ström AC, Forsberg M, Lillhager P, Westin G (1996). "The transcription factors Sp1 and Oct–1 interact physically to regulate human U2 snRNA gene expression". Nucleic Acids Res. 24 (11): 1981–6. doi:10.1093/nar/24.11.1981. PMC 145891. PMID 8668525.
  • Inamoto S, Segil N, Pan ZQ, Kimura M, Roeder RG (1997). "The cyclin-dependent kinase-activating kinase (CAK) assembly factor, MAT1, targets and enhances CAK activity on the POU domains of octamer transcription factors". J. Biol. Chem. 272 (47): 29852–8. doi:10.1074/jbc.272.47.29852. PMID 9368058.
  • Wong MW, Henry RW, Ma B, Kobayashi R, Klages N, Matthias P, Strubin M, Hernandez N (1998). "The Large Subunit of Basal Transcription Factor SNAPc Is a Myb Domain Protein That Interacts with Oct–1". Mol. Cell. Biol. 18 (1): 368–77. doi:10.1128/mcb.18.1.368. PMC 121507. PMID 9418884.
  • Nie J, Sakamoto S, Song D, Qu Z, Ota K, Taniguchi T (1998). "Interaction of Oct–1 and automodification domain of poly(ADP-ribose) synthetase". FEBS Lett. 424 (1–2): 27–32. doi:10.1016/S0014-5793(98)00131-8. PMID 9537509. S2CID 872132.
  • Préfontaine GG, Lemieux ME, Giffin W, Schild-Poulter C, Pope L, LaCasse E, Walker P, Haché RJ (1998). "Recruitment of Octamer Transcription Factors to DNA by Glucocorticoid Receptor". Mol. Cell. Biol. 18 (6): 3416–30. doi:10.1128/MCB.18.6.3416. PMC 108923. PMID 9584182.
  • La Boissière S, Hughes T, O'Hare P (1999). "HCF-dependent nuclear import of VP16". EMBO J. 18 (2): 480–9. doi:10.1093/emboj/18.2.480. PMC 1171141. PMID 9889203.

External links

  • v
  • t
  • e
  • 1cqt: CRYSTAL STRUCTURE OF A TERNARY COMPLEX CONTAINING AN OCA-B PEPTIDE, THE OCT-1 POU DOMAIN, AND AN OCTAMER ELEMENT
    1cqt: CRYSTAL STRUCTURE OF A TERNARY COMPLEX CONTAINING AN OCA-B PEPTIDE, THE OCT-1 POU DOMAIN, AND AN OCTAMER ELEMENT
  • 1e3o: CRYSTAL STRUCTURE OF OCT-1 POU DIMER BOUND TO MORE
    1e3o: CRYSTAL STRUCTURE OF OCT-1 POU DIMER BOUND TO MORE
  • 1gt0: CRYSTAL STRUCTURE OF A POU/HMG/DNA TERNARY COMPLEX
    1gt0: CRYSTAL STRUCTURE OF A POU/HMG/DNA TERNARY COMPLEX
  • 1hf0: CRYSTAL STRUCTURE OF THE DNA-BINDING DOMAIN OF OCT-1 BOUND TO DNA AS A DIMER
    1hf0: CRYSTAL STRUCTURE OF THE DNA-BINDING DOMAIN OF OCT-1 BOUND TO DNA AS A DIMER
  • 1o4x: TERNARY COMPLEX OF THE DNA BINDING DOMAINS OF THE OCT1 AND SOX2 TRANSCRIPTION FACTORS WITH A 19MER OLIGONUCLEOTIDE FROM THE HOXB1 REGULATORY ELEMENT
    1o4x: TERNARY COMPLEX OF THE DNA BINDING DOMAINS OF THE OCT1 AND SOX2 TRANSCRIPTION FACTORS WITH A 19MER OLIGONUCLEOTIDE FROM THE HOXB1 REGULATORY ELEMENT
  • 1oct: CRYSTAL STRUCTURE OF THE OCT-1 POU DOMAIN BOUND TO AN OCTAMER SITE: DNA RECOGNITION WITH TETHERED DNA-BINDING MODULES
    1oct: CRYSTAL STRUCTURE OF THE OCT-1 POU DOMAIN BOUND TO AN OCTAMER SITE: DNA RECOGNITION WITH TETHERED DNA-BINDING MODULES
  • 1pog: SOLUTION STRUCTURE OF THE OCT-1 POU-HOMEO DOMAIN DETERMINED BY NMR AND RESTRAINED MOLECULAR DYNAMICS
    1pog: SOLUTION STRUCTURE OF THE OCT-1 POU-HOMEO DOMAIN DETERMINED BY NMR AND RESTRAINED MOLECULAR DYNAMICS
  • 1pou: THE SOLUTION STRUCTURE OF THE OCT-1 POU-SPECIFIC DOMAIN REVEALS A STRIKING SIMILARITY TO THE BACTERIOPHAGE LAMBDA REPRESSOR DNA-BINDING DOMAIN
    1pou: THE SOLUTION STRUCTURE OF THE OCT-1 POU-SPECIFIC DOMAIN REVEALS A STRIKING SIMILARITY TO THE BACTERIOPHAGE LAMBDA REPRESSOR DNA-BINDING DOMAIN
  • v
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  • e
(1) Basic domains
(1.1) Basic leucine zipper (bZIP)
(1.2) Basic helix-loop-helix (bHLH)
Group A
Group B
Group C
bHLH-PAS
Group D
Group E
Group F
bHLH-COE
(1.3) bHLH-ZIP
(1.4) NF-1
(1.5) RF-X
(1.6) Basic helix-span-helix (bHSH)
(2) Zinc finger DNA-binding domains
(2.1) Nuclear receptor (Cys4)
subfamily 1
subfamily 2
subfamily 3
subfamily 4
subfamily 5
subfamily 6
subfamily 0
(2.2) Other Cys4
(2.3) Cys2His2
(2.4) Cys6
(2.5) Alternating composition
(2.6) WRKY
(3) Helix-turn-helix domains
(3.1) Homeodomain
Antennapedia
ANTP class
protoHOX
Hox-like
metaHOX
NK-like
other
(3.2) Paired box
(3.3) Fork head / winged helix
(3.4) Heat shock factors
(3.5) Tryptophan clusters
(3.6) TEA domain
  • transcriptional enhancer factor
(4) β-Scaffold factors with minor groove contacts
(4.1) Rel homology region
(4.2) STAT
(4.3) p53-like
(4.4) MADS box
(4.6) TATA-binding proteins
(4.7) High-mobility group
(4.9) Grainyhead
(4.10) Cold-shock domain
(4.11) Runt
(0) Other transcription factors
(0.2) HMGI(Y)
(0.3) Pocket domain
(0.5) AP-2/EREBP-related factors
(0.6) Miscellaneous
see also transcription factor/coregulator deficiencies