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Retinoic acid receptor gamma

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From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens

RARG

Available structures

PDB

Ortholog search:H3BMH6 PDBe H3BMH6 RCSB

List of PDB id codes
1EXA,1EXX,1FCX,1FCY,1FCZ,1FD0,2LBD,3LBD,4LBD

Identifiers

Aliases

RARG, NR1B3, RARC, retinoic acid receptor gamma, RARgamma

External IDs

OMIM:180190;MGI:97858;HomoloGene:20263;GeneCards:RARG;OMA:RARG - orthologs

Gene location (Human)

Chr.	Chromosome 12 (human)^[1]

Band	12q13.13	Start	53,210,567bp^[1]
Band	12q13.13	End	53,232,980bp^[1]

Gene location (Mouse)

Chr.	Chromosome 15 (mouse)^[2]

Band	15 F2\|15 57.4 cM	Start	102,143,373bp^[2]
Band	15 F2\|15 57.4 cM	End	102,165,952bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

skin of leg

skin of abdomen

stromal cell of endometrium

ectocervix

canal of the cervix

right coronary artery

vagina

right uterine tube

apex of heart

tibial nerve

Top expressed in

axial skeleton

human vertebral column

bones of pectoral girdle

sacrum

shoulder

cervical vertebral column

tail of embryo

ankle

vertebra

More reference expression data

BioGPS

n/a

Gene ontology
Molecular function	sequence-specific DNA binding RNA polymerase II transcription regulatory region sequence-specific DNA binding zinc ion binding metal ion binding steroid hormone receptor activity protein binding DNA-binding transcription factor activity DNA binding retinoid X receptor binding DNA-binding transcription factor activity, RNA polymerase II-specific transcription cis-regulatory region binding transcription factor binding nuclear receptor coactivator activity signaling receptor activity nuclear receptor activity
Cellular component	integral component of membrane nucleoplasm nucleus transcription regulator complex RNA polymerase II transcription regulator complex
Biological process	regulation of cell size growth plate cartilage development cellular response to retinoic acid gland development regulation of transcription, DNA-templated negative regulation of cartilage development response to retinoic acid multicellular organism growth negative regulation of cell differentiation bone morphogenesis chondrocyte development negative regulation of apoptotic process retinal pigment epithelium development transcription, DNA-templated epithelium development embryonic camera-type eye development reproductive structure development limb development face development neural tube closure negative regulation of chondrocyte differentiation Harderian gland development prostate gland epithelium morphogenesis regulation of myelination positive regulation of gene expression retina development in camera-type eye positive regulation of cell population proliferation growth plate cartilage chondrocyte growth canonical Wnt signaling pathway regulation of gene expression camera-type eye development transcription initiation from RNA polymerase II promoter regulation of myeloid cell differentiation bone development trachea cartilage development anterior/posterior pattern specification glandular epithelial cell development steroid hormone mediated signaling pathway negative regulation of transcription by RNA polymerase II positive regulation of transcription by RNA polymerase II embryonic hindlimb morphogenesis retinoic acid receptor signaling pathway negative regulation of cell population proliferation embryonic eye morphogenesis positive regulation of apoptotic process positive regulation of programmed cell death cellular response to leukemia inhibitory factor multicellular organism development hormone-mediated signaling pathway cell differentiation response to lipid
Sources:Amigo /QuickGO

Orthologs

Species

Human

Mouse

Entrez


5916


19411

Ensembl


ENSG00000172819


ENSMUSG00000001288

UniProt


P13631


P18911

RefSeq (mRNA)


NM_000966 NM_001042728 NM_001243730 NM_001243731 NM_001243732


NM_001042727 NM_011244

RefSeq (protein)


NP_000957 NP_001036193 NP_001230659 NP_001230660 NP_001230661


NP_001036192 NP_035374

Location (UCSC)

Chr 12: 53.21 – 53.23 Mb

Chr 15: 102.14 – 102.17 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Retinoic acid receptor gamma (RAR-γ), also known asNR1B3 (nuclear receptor subfamily 1, group B, member 3) is anuclear receptor encoded by theRARGgene.^[5]^[6]Adapalene selectively targetsretinoic acid receptor beta and retinoic acid receptor gamma^[7] and its agonism of the gamma subtype is largely responsible for adapalene's observed effects.^[8]

Interactions

[edit]

Retinoic acid receptor gamma has been shown tointeract withNCOR1.^[9]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000172819 –Ensembl, May 2017
^^a ^b ^cGRCm38: Ensembl release 89: ENSMUSG00000001288 –Ensembl, May 2017
^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Entrez Gene: RARG retinoic acid receptor, gamma".
^Lehmann JM, Hoffmann B, Pfahl M (Feb 1991)."Genomic organization of the retinoic acid receptor gamma gene".Nucleic Acids Research.19 (3):573–8.doi:10.1093/nar/19.3.573.PMC 333650.PMID 1849262.
^Mukherjee S, Date A, Patravale V, Korting HC, Roeder A, Weindl G (2006)."Retinoids in the treatment of skin aging: an overview of clinical efficacy and safety".Clinical Interventions in Aging.1 (4):327–48.doi:10.2147/ciia.2006.1.4.327.PMC 2699641.PMID 18046911.
^Michel S, Jomard A, Démarchez M (October 1998). "Pharmacology of adapalene".The British Journal of Dermatology.139 (Suppl 52):3–7.doi:10.1046/j.1365-2133.1998.1390s2003.x.PMID 9990413.S2CID 23084886.
^Dowell P, Ishmael JE, Avram D, Peterson VJ, Nevrivy DJ, Leid M (May 1999)."Identification of nuclear receptor corepressor as a peroxisome proliferator-activated receptor alpha interacting protein".The Journal of Biological Chemistry.274 (22):15901–7.doi:10.1074/jbc.274.22.15901.PMID 10336495.

Leid M, Kastner P, Lyons R, Nakshatri H, Saunders M, Zacharewski T, Chen JY, Staub A, Garnier JM, Mader S (Jan 1992). "Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficiently".Cell.68 (2):377–95.doi:10.1016/0092-8674(92)90478-U.PMID 1310259.S2CID 40617478.
Vollberg TM, Nervi C, George MD, Fujimoto W, Krust A, Jetten AM (May 1992)."Retinoic acid receptors as regulators of human epidermal keratinocyte differentiation".Molecular Endocrinology.6 (5):667–76.doi:10.1210/mend.6.5.1318502.PMID 1318502.S2CID 35884680.
Lehmann JM, Zhang XK, Pfahl M (Jul 1992)."RAR gamma 2 expression is regulated through a retinoic acid response element embedded in Sp1 sites".Molecular and Cellular Biology.12 (7):2976–85.doi:10.1128/mcb.12.7.2976.PMC 364511.PMID 1320193.
Mattei MG, Rivière M, Krust A, Ingvarsson S, Vennström B, Islam MQ, Levan G, Kautner P, Zelent A, Chambon P (Aug 1991)."Chromosomal assignment of retinoic acid receptor (RAR) genes in the human, mouse, and rat genomes"(PDF).Genomics.10 (4):1061–9.doi:10.1016/0888-7543(91)90199-O.hdl:1946/20678.PMID 1655630.
Kastner P, Krust A, Mendelsohn C, Garnier JM, Zelent A, Leroy P, Staub A, Chambon P (Apr 1990)."Murine isoforms of retinoic acid receptor gamma with specific patterns of expression".Proceedings of the National Academy of Sciences of the United States of America.87 (7):2700–4.Bibcode:1990PNAS...87.2700K.doi:10.1073/pnas.87.7.2700.PMC 53758.PMID 2157210.
Giguère V, Shago M, Zirngibl R, Tate P, Rossant J, Varmuza S (May 1990)."Identification of a novel isoform of the retinoic acid receptor gamma expressed in the mouse embryo".Molecular and Cellular Biology.10 (5):2335–40.doi:10.1128/mcb.10.5.2335.PMC 360581.PMID 2157970.
Ishikawa T, Umesono K, Mangelsdorf DJ, Aburatani H, Stanger BZ, Shibasaki Y, Imawari M, Evans RM, Takaku F (Jun 1990)."A functional retinoic acid receptor encoded by the gene on human chromosome 12".Molecular Endocrinology.4 (6):837–44.doi:10.1210/mend-4-6-837.PMID 2172793.
Krust A, Kastner P, Petkovich M, Zelent A, Chambon P (Jul 1989)."A third human retinoic acid receptor, hRAR-gamma".Proceedings of the National Academy of Sciences of the United States of America.86 (14):5310–4.Bibcode:1989PNAS...86.5310K.doi:10.1073/pnas.86.14.5310.PMC 297611.PMID 2546152.
Renaud JP, Rochel N, Ruff M, Vivat V, Chambon P, Gronemeyer H, Moras D (Dec 1995). "Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid".Nature.378 (6558):681–9.Bibcode:1995Natur.378..681R.doi:10.1038/378681a0.PMID 7501014.S2CID 4259376.
Zhou L, Pang J, Munroe DG, Lau C (May 1993)."A human retinoic acid receptor gamma isoform is homologous to the murine retinoic acid receptor gamma 7".Nucleic Acids Research.21 (10): 2520.doi:10.1093/nar/21.10.2520.PMC 309563.PMID 7685085.
Zitnik RJ, Kotloff RM, Latifpour J, Zheng T, Whiting NL, Schwalb J, Elias JA (Feb 1994)."Retinoic acid inhibition of IL-1-induced IL-6 production by human lung fibroblasts".Journal of Immunology.152 (3):1419–27.doi:10.4049/jimmunol.152.3.1419.PMID 8301142.S2CID 20598143.
Botling J, Castro DS, Oberg F, Nilsson K, Perlmann T (Apr 1997)."Retinoic acid receptor/retinoid X receptor heterodimers can be activated through both subunits providing a basis for synergistic transactivation and cellular differentiation".The Journal of Biological Chemistry.272 (14):9443–9.doi:10.1074/jbc.272.14.9443.PMID 9083083.
Lømo J, Smeland EB, Ulven S, Natarajan V, Blomhoff R, Gandhi U, Dawson MI, Blomhoff HK (Apr 1998). "RAR-, not RXR, ligands inhibit cell activation and prevent apoptosis in B-lymphocytes".Journal of Cellular Physiology.175 (1):68–77.doi:10.1002/(SICI)1097-4652(199804)175:1<68::AID-JCP8>3.0.CO;2-A.PMID 9491782.S2CID 21489004.
Klaholz BP, Renaud JP, Mitschler A, Zusi C, Chambon P, Gronemeyer H, Moras D (Mar 1998). "Conformational adaptation of agonists to the human nuclear receptor RAR gamma".Nature Structural Biology.5 (3):199–202.doi:10.1038/nsb0398-199.PMID 9501913.S2CID 30471226.
Zhang ZP, Gambone CJ, Gabriel JL, Wolfgang CL, Soprano KJ, Soprano DR (Dec 1998)."Arg278, but not Lys229 or Lys236, plays an important role in the binding of retinoic acid by retinoic acid receptor gamma".The Journal of Biological Chemistry.273 (51):34016–21.doi:10.1074/jbc.273.51.34016.PMID 9852056.
Yang C, Zhou D, Chen S (Dec 1998). "Modulation of aromatase expression in the breast tissue by ERR alpha-1 orphan receptor".Cancer Research.58 (24):5695–700.PMID 9865725.
Nagpal S, Ghosn C, DiSepio D, Molina Y, Sutter M, Klein ES, Chandraratna RA (Aug 1999)."Retinoid-dependent recruitment of a histone H1 displacement activity by retinoic acid receptor".The Journal of Biological Chemistry.274 (32):22563–8.doi:10.1074/jbc.274.32.22563.PMID 10428834.
Egea PF, Mitschler A, Rochel N, Ruff M, Chambon P, Moras D (Jun 2000)."Crystal structure of the human RXRalpha ligand-binding domain bound to its natural ligand: 9-cis retinoic acid".The EMBO Journal.19 (11):2592–601.doi:10.1093/emboj/19.11.2592.PMC 212755.PMID 10835357.
Boudjelal M, Voorhees JJ, Fisher GJ (Mar 2002). "Retinoid signaling is attenuated by proteasome-mediated degradation of retinoid receptors in human keratinocyte HaCaT cells".Experimental Cell Research.274 (1):130–7.doi:10.1006/excr.2001.5450.PMID 11855864.

This article on agene on humanchromosome 12 is astub. You can help Wikipedia byexpanding it.

v t e PDB gallery
1dsz: STRUCTURE OF THE RXR/RAR DNA-BINDING DOMAIN HETERODIMER IN COMPLEX WITH THE RETINOIC ACID RESPONSE ELEMENT DR1 1exa: ENANTIOMER DISCRIMINATION ILLUSTRATED BY CRYSTAL STRUCTURES OF THE HUMAN RETINOIC ACID RECEPTOR HRARGAMMA LIGAND BINDING DOMAIN: THE COMPLEX WITH THE ACTIVE R-ENANTIOMER BMS270394. 1exx: ENANTIOMER DISCRIMINATION ILLUSTRATED BY CRYSTAL STRUCTURES OF THE HUMAN RETINOIC ACID RECEPTOR HRARGAMMA LIGAND BINDING DOMAIN: THE COMPLEX WITH THE INACTIVE S-ENANTIOMER BMS270395. 1fcx: ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE RARGAMMA-SELECTIVE RETINOID BMS184394 1fcy: ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE RARBETA/GAMMA-SELECTIVE RETINOID CD564 1fcz: ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE PANAGONIST RETINOID BMS181156 1fd0: ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE RARGAMMA-SELECTIVE RETINOID SR11254 1hra: THE SOLUTION STRUCTURE OF THE HUMAN RETINOIC ACID RECEPTOR-BETA DNA-BINDING DOMAIN 2lbd: LIGAND-BINDING DOMAIN OF THE HUMAN RETINOIC ACID RECEPTOR GAMMA BOUND TO ALL-TRANS RETINOIC ACID 3lbd: LIGAND-BINDING DOMAIN OF THE HUMAN RETINOIC ACID RECEPTOR GAMMA BOUND TO 9-CIS RETINOIC ACID 4lbd: LIGAND-BINDING DOMAIN OF THE HUMAN RETINOIC ACID RECEPTOR GAMMA BOUND TO THE SYNTHETIC AGONIST BMS961

PDB gallery

1dsz: STRUCTURE OF THE RXR/RAR DNA-BINDING DOMAIN HETERODIMER IN COMPLEX WITH THE RETINOIC ACID RESPONSE ELEMENT DR1
1exa: ENANTIOMER DISCRIMINATION ILLUSTRATED BY CRYSTAL STRUCTURES OF THE HUMAN RETINOIC ACID RECEPTOR HRARGAMMA LIGAND BINDING DOMAIN: THE COMPLEX WITH THE ACTIVE R-ENANTIOMER BMS270394.
1exx: ENANTIOMER DISCRIMINATION ILLUSTRATED BY CRYSTAL STRUCTURES OF THE HUMAN RETINOIC ACID RECEPTOR HRARGAMMA LIGAND BINDING DOMAIN: THE COMPLEX WITH THE INACTIVE S-ENANTIOMER BMS270395.
1fcx: ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE RARGAMMA-SELECTIVE RETINOID BMS184394
1fcy: ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE RARBETA/GAMMA-SELECTIVE RETINOID CD564
1fcz: ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE PANAGONIST RETINOID BMS181156
1fd0: ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE RARGAMMA-SELECTIVE RETINOID SR11254
1hra: THE SOLUTION STRUCTURE OF THE HUMAN RETINOIC ACID RECEPTOR-BETA DNA-BINDING DOMAIN
2lbd: LIGAND-BINDING DOMAIN OF THE HUMAN RETINOIC ACID RECEPTOR GAMMA BOUND TO ALL-TRANS RETINOIC ACID
3lbd: LIGAND-BINDING DOMAIN OF THE HUMAN RETINOIC ACID RECEPTOR GAMMA BOUND TO 9-CIS RETINOIC ACID
4lbd: LIGAND-BINDING DOMAIN OF THE HUMAN RETINOIC ACID RECEPTOR GAMMA BOUND TO THE SYNTHETIC AGONIST BMS961

Transcription factors andintracellular receptors

(1) Basic domains

(1.1) Basicleucine 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
- sMaf
  - F
  - G
  - K
NFE
- 2
- L1
- L2
- L3
NFIL3
NRL
NRF
- 1
- 2
- 3
XBP1

(1.2) Basic helix-loop-helix (bHLH)

Group A	AS-C ASCL1 ASCL2 ATOH1 HAND 1 2 MESP2 Myogenic regulatory factors MyoD Myogenin MYF5 MYF6 NeuroD 1 2 Neurogenins 1 2 3 OLIG 1 2 Paraxis TCF15 Scleraxis SLC LYL1 TAL 1 2 Twist
Group B	FIGLA Myc c-Myc l-Myc n-Myc MXD4 TCF4
Group C bHLH-PAS	AhR AHRR ARNT ARNTL ARNTL2 CLOCK HIF 1A EPAS1 3A NPAS 1 2 3 PER 1 2 3 Period SIM 1 2
Group D	BHLH 2 3 9 Pho4 ID 1 2 3 4
Group E	HES 1 2 3 4 5 6 7 HEY 1 2 L
Group F bHLH-COE	EBF1

(1.3)bHLH-ZIP

(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 family
- 1
- 2
- 3
- REST
- S1
- S2
- YY1
HIC
- 1
- 2
HIVEP
- 1
- 2
- 3
IKZF
- 1
- 2
- 3
ILF
- 2
- 3
Sp/KLF family
- KLF
  - 1
  - 2
  - 3
  - 4
  - 5
  - 6
  - 7
  - 8
  - 9
  - 10
  - 11
  - 12
  - 13
  - 14
  - 15
  - 17
- SP
  - 1
  - 2
  - 4
  - 7
  - 8
MTF1
MYT1
OSR1
PRDM9
SALL
- 1
- 2
- 3
- 4
TSHZ3
WT1
Zbtb7
- 7A
- 7B
ZBTB
- 11
- 16
- 17
- 20
- 21
- 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
- 300
- 318
- 330
- 346
- 350
- 365
- 366
- 384
- 423
- 451
- 452
- 471
- 593
- 638
- 644
- 649
- 655
- 804A

(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-helixdomains

(3.1)Homeodomain

Antennapedia
ANTP class

protoHOX Hox-like	ParaHox Gsx 1 2 Xlox PDX1 Cdx 1 2 4 extended Hox:Evx1 Evx2 MEOX1 MEOX2 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 GBX1 GBX2 MNX1
metaHOX NK-like	BARHL1 BARHL2 BARX1 BARX2 BSX DBX 1 2 DLX 1 2 3 4 5 6 EMX 1 2 EN 1 2 HHEX HLX LBX1 LBX2 MSX 1 2 NANOG NKX 2-1 2-2 2-3 2-5 3-1 3-2 HMX1 HMX2 HMX3 6-1 6-2 NOTO TLX1 TLX2 TLX3 VAX1 VAX2

other

ARX
CRX
CUTL1
FHL
- 1
- 2
- 3
HESX1
HOPX
LMX
- 1A
- 1B
NOBOX
TALE
- IRX
  - 1
  - 2
  - 3
  - 4
  - 5
  - 6
  - MKX
- MEIS
  - 1
  - 2
- PBX
  - 1
  - 2
  - 3
- PKNOX
  - 1
  - 2
- SIX
  - 1
  - 2
  - 3
  - 4
  - 5
PHF
- 1
- 3
- 6
- 8
- 10
- 16
- 17
- 20
- 21A
POU domain
- PIT-1
- BRN-3:A
- B
- C
- Octamer transcription factor:1
- 2
- 3/4
- 6
- 7
- 11
SATB2
ZEB
- 1
- 2

(3.2) Paired box

PAX
- 1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 9
PRRX
- 1
- 2
PROP1
PHOX
- 2A
- 2B
RAX
SHOX
SHOX2
VSX1
VSX2
Bicoid
- GSC
- BICD2
- OTX
  - 1
  - 2
- PITX
  - 1
  - 2
  - 3

(3.3)Fork head /winged helix

E2F
- 1
- 2
- 3
- 4
- 5
FOX proteins
- A1
- A2
- A3
- B1
- B2
- C1
- C2
- D1
- D2
- D3
- D4
- D4L1
- D4L3
- D4L4
- D4L5
- D4L6
- E1
- E3
- F1
- F2
- G1
- H1
- I1
- I2
- I3
- J1
- J2
- J3
- K1
- K2
- L1
- L2
- M1
- N1
- N2
- N3
- N4
- O1
- O3
- O4
- O6
- P1
- P2
- P3
- P4
- Q1
- R1
- R2
- S1

(3.4)Heat shock factors

HSF
- 1
- 2
- 4

(3.5) Tryptophan clusters

ELF
- 2
- 4
- 5
EHF
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-like	p53 p63 p73 family p53 TP63 p73 TBX 1 2 3 5 19 21 22 TBR1 TBR2 TFT MYRF
(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 SOX 1 2 3 4 5 6 8 9 10 11 12 13 14 15 17 18 21 SRY SSRP1 TCF/LEF TCF 1 3 4 LEF1 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 alsotranscription factor/coregulator deficiencies

v t e Retinoid receptor modulators
RARTooltip Retinoic acid receptor	Agonists:9CDHRA 9-cis-Retinoic acid (alitretinoin) AC-261066 AC-55649 Acitretin Adapalene Arotinoid acid all-trans-Retinoic acid (tretinoin) AM-580 BMS-493 BMS-753 BMS-961 CD-1530 CD-2314 CD-437 Ch-55 EC 23 Etretinate Fenretinide Isotretinoin Palovarotene Retinoic acid Retinol (vitamin A) Tamibarotene Tazarotene Tazarotenic acid Trifarotene Antagonists:BMS-195614 BMS-493 CD-2665 ER-50891 LE-135 MM-11253 Retinoic acid metabolism inhibitors:Liarozole Talarozole
RXRTooltip Retinoid X receptor	Agonists:9CDHRA 9-cis-Retinoic acid (alitretinoin) all-trans-Retinoic acid (tretinoin) Bexarotene CD 3254 Docosahexaenoic acid Fluorobexarotene Isotretinoin LG-100268 LG-101506 LG-100754 Retinoic acid Retinol (vitamin A) SR-11237 Antagonists:HX-531 HX-630 LG-100754 PA-452 UVI-3003 HX-603 LE135 (RAR beta selective) LE-540 CD3254 PA-451 PA-452 Rhein HX-711 6-(N-ethyl-N-(5-isobutoxy-4-isopropyl-2-(E)-styrylphenyl)amino)nicotinic acid
See also Receptor/signaling modulators

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