USF1

For the failed Formula One team, see US F1 Team.

VALUE_ERROR (nil)

Identifiers
Aliases|
External IDs| GeneCards: [1]
Orthologs
Species| Human| Mouse
Entrez| |

n/a

n/a

Ensembl| |

n/a

n/a

UniProt| |

n/a

n/a

RefSeq (mRNA)| |

n/a

n/a

RefSeq (protein)| |

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Location (UCSC)| n/a| n/a
PubMed search| n/a| n/a
Wikidata
| View/Edit Human|

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Upstream stimulatory factor 1 is a protein that in humans is encoded by the USF1 gene.[1][2]

## Contents

* 1 Function
* 2 Interactions
* 3 References
* 4 Further reading
* 5 External links

## Function[edit | edit source]

This gene encodes a member of the basic helix-loop-helix leucine zipper family and can function as a cellular transcription factor. The encoded protein can activate transcription through pyrimidine-rich initiator (Inr) elements and E-box motifs. This gene has been linked to familial combined hyperlipidemia (FCHL). Two transcript variants encoding distinct isoforms have been identified for this gene.[2]

A study of mice suggested reduced USF1 levels increases metabolism in brown fat.[3]

## Interactions[edit | edit source]

USF1 (human gene) has been shown to interact with USF2,[4][5] FOSL1[6] and GTF2I.[7][8]

## References[edit | edit source]

1. ↑ Shieh BH, Sparkes RS, Gaynor RB, Lusis AJ (Apr 1993). "Localization of the gene-encoding upstream stimulatory factor (USF) to human chromosome 1q22-q23". Genomics. 16 (1): 266–8. doi:10.1006/geno.1993.1174. PMID 8486371.
2. ↑ 2.0 2.1 "Entrez Gene: USF1 upstream transcription factor 1".
3. ↑ Laurila PP, Soronen J, Kooijman S, Forsström S, Boon MR, Surakka I, et al. (2016). "USF1 deficiency activates brown adipose tissue and improves cardiometabolic health". Science Translational Medicine. 8 (323): 323ra13. doi:10.1126/scitranslmed.aad0015. PMID 26819196.
4. ↑ Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
5. ↑ Viollet B, Lefrançois-Martinez AM, Henrion A, Kahn A, Raymondjean M, Martinez A (Jan 1996). "Immunochemical characterization and transacting properties of upstream stimulatory factor isoforms". The Journal of Biological Chemistry. 271 (3): 1405–15. doi:10.1074/jbc.271.3.1405. PMID 8576131.
6. ↑ Pognonec P, Boulukos KE, Aperlo C, Fujimoto M, Ariga H, Nomoto A, Kato H (May 1997). "Cross-family interaction between the bHLHZip USF and bZip Fra1 proteins results in down-regulation of AP1 activity". Oncogene. 14 (17): 2091–8. doi:10.1038/sj.onc.1201046. PMID 9160889.
7. ↑ Roy AL, Du H, Gregor PD, Novina CD, Martinez E, Roeder RG (Dec 1997). "Cloning of an inr- and E-box-binding protein, TFII-I, that interacts physically and functionally with USF1". The EMBO Journal. 16 (23): 7091–104. doi:10.1093/emboj/16.23.7091. PMC 1170311. PMID 9384587.
8. ↑ Roy AL, Meisterernst M, Pognonec P, Roeder RG (Nov 1991). "Cooperative interaction of an initiator-binding transcription initiation factor and the helix-loop-helix activator USF". Nature. 354 (6350): 245–8. doi:10.1038/354245a0. PMID 1961251.

## Further reading[edit | edit source]

* Corre S, Galibert MD (Jan 2006). "[USF as a key regulatory element of gene expression]" (PDF). Médecine Sciences. 22 (1): 62–7. doi:10.1051/medsci/200622162. PMID 16386222.
* Lee JC, Lusis AJ, Pajukanta P (Apr 2006). "Familial combined hyperlipidemia: upstream transcription factor 1 and beyond". Current Opinion in Lipidology. 17 (2): 101–9. doi:10.1097/01.mol.0000217890.54875.13. PMID 16531745.
* Roy AL, Meisterernst M, Pognonec P, Roeder RG (Nov 1991). "Cooperative interaction of an initiator-binding transcription initiation factor and the helix-loop-helix activator USF". Nature. 354 (6350): 245–8. doi:10.1038/354245a0. PMID 1961251.
* Gregor PD, Sawadogo M, Roeder RG (Oct 1990). "The adenovirus major late transcription factor USF is a member of the helix-loop-helix group of regulatory proteins and binds to DNA as a dimer". Genes & Development. 4 (10): 1730–40. doi:10.1101/gad.4.10.1730. PMID 2249772.
* Henrion AA, Martinez A, Mattei MG, Kahn A, Raymondjean M (Jan 1995). "Structure, sequence, and chromosomal location of the gene for USF2 transcription factors in mouse". Genomics. 25 (1): 36–43. doi:10.1016/0888-7543(95)80107-W. PMID 7774954.
* Ferré-D'Amaré AR, Pognonec P, Roeder RG, Burley SK (Jan 1994). "Structure and function of the b/HLH/Z domain of USF". The EMBO Journal. 13 (1): 180–9. PMC 394791. PMID 8306960.
* Viollet B, Lefrançois-Martinez AM, Henrion A, Kahn A, Raymondjean M, Martinez A (Jan 1996). "Immunochemical characterization and transacting properties of upstream stimulatory factor isoforms". The Journal of Biological Chemistry. 271 (3): 1405–15. doi:10.1074/jbc.271.3.1405. PMID 8576131.
* Ghosh AK, Datta PK, Jacob ST (Feb 1997). "The dual role of helix-loop--helix-zipper protein USF in ribosomal RNA gene transcription in vivo". Oncogene. 14 (5): 589–94. doi:10.1038/sj.onc.1200866. PMID 9053857.
* Pognonec P, Boulukos KE, Aperlo C, Fujimoto M, Ariga H, Nomoto A, Kato H (May 1997). "Cross-family interaction between the bHLHZip USF and bZip Fra1 proteins results in down-regulation of AP1 activity". Oncogene. 14 (17): 2091–8. doi:10.1038/sj.onc.1201046. PMID 9160889.
* Roy AL, Du H, Gregor PD, Novina CD, Martinez E, Roeder RG (Dec 1997). "Cloning of an inr- and E-box-binding protein, TFII-I, that interacts physically and functionally with USF1". The EMBO Journal. 16 (23): 7091–104. doi:10.1093/emboj/16.23.7091. PMC 1170311. PMID 9384587.
* Pajukanta P, Nuotio I, Terwilliger JD, Porkka KV, Ylitalo K, Pihlajamäki J, Suomalainen AJ, Syvänen AC, Lehtimäki T, Viikari JS, Laakso M, Taskinen MR, Ehnholm C, Peltonen L (Apr 1998). "Linkage of familial combined hyperlipidaemia to chromosome 1q21-q23". Nature Genetics. 18 (4): 369–73. doi:10.1038/ng0498-369. PMID 9537421.
* Hartley JL, Temple GF, Brasch MA (Nov 2000). "DNA cloning using in vitro site-specific recombination". Genome Research. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
* Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A (Mar 2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Research. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
* Bengtsson SH, Madeyski-Bengtson K, Nilsson J, Bjursell G (Jul 2002). "Transcriptional regulation of the human carboxyl ester lipase gene in THP-1 monocytes: an E-box required for activation binds upstream stimulatory factors 1 and 2". The Biochemical Journal. 365 (Pt 2): 481–8. doi:10.1042/BJ20020223. PMC 1222691. PMID 11945176.
* Villavicencio EH, Yoon JW, Frank DJ, Füchtbauer EM, Walterhouse DO, Iannaccone PM (Apr 2002). "Cooperative E-box regulation of human GLI1 by TWIST and USF". Genesis. 32 (4): 247–58. doi:10.1002/gene.10078. PMID 11948912.
* Coulson JM, Edgson JL, Marshall-Jones ZV, Mulgrew R, Quinn JP, Woll PJ (Feb 2003). "Upstream stimulatory factor activates the vasopressin promoter via multiple motifs, including a non-canonical E-box". The Biochemical Journal. 369 (Pt 3): 549–61. doi:10.1042/BJ20021176. PMC 1223122. PMID 12403649.
* Salero E, Giménez C, Zafra F (Mar 2003). "Identification of a non-canonical E-box motif as a regulatory element in the proximal promoter region of the apolipoprotein E gene". The Biochemical Journal. 370 (Pt 3): 979–86. doi:10.1042/BJ20021142. PMC 1223214. PMID 12444925.
* Pickwell GV, Shih H, Quattrochi LC (Apr 2003). "Interaction of upstream stimulatory factor proteins with an E-box located within the human CYP1A2 5'-flanking gene contributes to basal transcriptional gene activation". Biochemical Pharmacology. 65 (7): 1087–96. doi:10.1016/S0006-2952(03)00037-6. PMID 12663044.

## External links[edit | edit source]

* FactorBook USF1

* v
* t
* e

PDB gallery

* 1an4: STRUCTURE AND FUNCTION OF THE B/HLH/Z DOMAIN OF USF

1an4: STRUCTURE AND FUNCTION OF THE B/HLH/Z DOMAIN OF USF

* v
* t
* e

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
* GCN4
* 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
* 3
* 9
* ARNTL
* 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
* MXD3
* 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
* S1
* S2
* YY1
* HIC
* 1
* 2
* HIVEP
* 1
* 2
* 3
* IKZF
* 1
* 2
* 3
* ILF
* 2
* 3
* KLF
* 1
* 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

(2.6) WRKY|

* WRKY

(3) Helix-turn-helix domains

| (3.1) Homeodomain|

* ARX
* CDX
* 1
* 2
* CRX
* CUTL1
* DBX
* 1
* 2
* DLX
* 1
* 2
* 3
* 4
* 5
* 6
* 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
* PRRX
* 1
* 2
* RAX

(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
* TBR1
* TBR2
* TFT
* MYRF
* 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
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