Transcription initiation protein SPT3 homolog

Transcription initiation protein SPT3 homolog is a protein that in humans is encoded by the SUPT3H gene.[5][6][7]

SUPT3H
Identifiers
Aliases	SUPT3H, SPT3, SPT3L, SPT3 homolog, SAGA and STAGA complex component
External IDs	OMIM: 602947 MGI: 1923723 HomoloGene: 121570 GeneCards: SUPT3H
Gene location (Human) Chr. Chromosome 6 (human)[1] Band 6p21.1 Start 44,809,317 bp[1] End 45,377,953 bp[1]
Gene location (Mouse) Chr. Chromosome 17 (mouse)[2] Band 17|17 B3 Start 44,777,152 bp[2] End 45,119,290 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • protein heterodimerization activity • histone acetyltransferase activity • GO:0001105 transcription coactivator activity • DNA binding • GO:0001104 transcription coregulator activity Cellular component • transcription factor TFTC complex • STAGA complex • cell nucleus • nucleoplasm • SAGA complex • transcription factor TFIID complex Biological process • regulation of transcription from RNA polymerase II promoter • positive regulation of transcription, DNA-templated • histone deubiquitination • regulation of transcription, DNA-templated • transcription from RNA polymerase II promoter • histone H3 acetylation • transcription, DNA-templated Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	8464	109115
Ensembl	ENSG00000196284	ENSMUSG00000038954
UniProt	O75486	n/a
RefSeq (mRNA)	NM_001261823 NM_003599 NM_181356 NM_001350324 NM_001350325 NM_001350326 NM_001350327 NM_001350329	NM_178652 NM_001357320
RefSeq (protein)	NP_001248752 NP_003590 NP_852001 NP_001337253 NP_001337254 NP_001337255 NP_001337256 NP_001337258	n/a
Location (UCSC)	Chr 6: 44.81 – 45.38 Mb	Chr 17: 44.78 – 45.12 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Interactions

Transcription initiation protein SPT3 homolog has been shown to interact with GCN5L2,[8][9] TAF6L,[9] TADA3L,[9] TAF5L,[9] SF3B3,[9] SUPT7L,[9] Myc,[10] TAF9,[9] Transformation/transcription domain-associated protein,[9] TAF12,[9] TAF10,[8][9] TAF4[8] and DDB1.[9]

Model organisms

Model organisms have been used in the study of SUPT3H function. A conditional knockout mouse line called Supt3^{tm1a(EUCOMM)Hmgu} was generated at the Wellcome Trust Sanger Institute.[11] Male and female animals underwent a standardized phenotypic screen[12] to determine the effects of deletion.[13][14][15][16] Additional screens performed: - In-depth immunological phenotyping[17]

Supt3 knockout mouse phenotype

Characteristic	Phenotype
All data available at.[12][17]
Peripheral blood leukocytes 6 Weeks	Normal
Insulin	Normal
Haematology 6 Weeks	Normal
Homozygous viability at P14	Abnormal
Recessive lethal study	Abnormal
Body weight	Normal
Neurological assessment	Normal
Grip strength	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Eye morphology	Normal
Clinical chemistry	Normal
Haematology 16 Weeks	Normal
Peripheral blood leukocytes 16 Weeks	Normal
Heart weight	Normal
Salmonella infection	Normal
Cytotoxic T Cell Function	Normal
Spleen Immunophenotyping	Normal
Mesenteric Lymph Node Immunophenotyping	Normal
Bone Marrow Immunophenotyping	Normal
Epidermal Immune Composition	Normal
Trichuris Challenge	Normal

References

1. GRCh38: Ensembl release 89: ENSG00000196284 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000038954 - 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. Ogryzko VV, Kotani T, Zhang X, Schiltz RL, Howard T, Yang XJ, Howard BH, Qin J, Nakatani Y (Jul 1998). "Histone-like TAFs within the PCAF histone acetylase complex". Cell. 94 (1): 35–44. doi:10.1016/S0092-8674(00)81219-2. PMID 9674425. S2CID 18942972.
6. Martinez E, Kundu TK, Fu J, Roeder RG (Sep 1998). "A human SPT3-TAFII31-GCN5-L acetylase complex distinct from transcription factor IID". The Journal of Biological Chemistry. 273 (37): 23781–5. doi:10.1074/jbc.273.37.23781. PMID 9726987.
7. "Entrez Gene: SUPT3H suppressor of Ty 3 homolog (S. cerevisiae)".
8. Brand M, Moggs JG, Oulad-Abdelghani M, Lejeune F, Dilworth FJ, Stevenin J, Almouzni G, Tora L (Jun 2001). "UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation". The EMBO Journal. 20 (12): 3187–96. doi:10.1093/emboj/20.12.3187. PMC 150203. PMID 11406595.
9. Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG (Oct 2001). "Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo". Molecular and Cellular Biology. 21 (20): 6782–95. doi:10.1128/MCB.21.20.6782-6795.2001. PMC 99856. PMID 11564863.
10. Liu X, Tesfai J, Evrard YA, Dent SY, Martinez E (May 2003). "c-Myc transformation domain recruits the human STAGA complex and requires TRRAP and GCN5 acetylase activity for transcription activation". The Journal of Biological Chemistry. 278 (22): 20405–12. doi:10.1074/jbc.M211795200. PMC 4031917. PMID 12660246.
11. Gerdin AK (2010). "The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x. S2CID 85911512.
12. "International Mouse Phenotyping Consortium".
13. Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
14. Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
15. Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247. S2CID 18872015.
16. White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, Salisbury J, Clare S, Ingham NJ, Podrini C, Houghton R, Estabel J, Bottomley JR, Melvin DG, Sunter D, Adams NC, Tannahill D, Logan DW, Macarthur DG, Flint J, Mahajan VB, Tsang SH, Smyth I, Watt FM, Skarnes WC, Dougan G, Adams DJ, Ramirez-Solis R, Bradley A, Steel KP (Jul 2013). "Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes". Cell. 154 (2): 452–64. doi:10.1016/j.cell.2013.06.022. PMC 3717207. PMID 23870131.
17. "Infection and Immunity Immunophenotyping (3i) Consortium".

Further reading

• Yu J, Madison JM, Mundlos S, Winston F, Olsen BR (Oct 1998). "Characterization of a human homologue of the Saccharomyces cerevisiae transcription factor spt3 (SUPT3H)". Genomics. 53 (1): 90–6. doi:10.1006/geno.1998.5500. PMID 9787080.
• Vassilev A, Yamauchi J, Kotani T, Prives C, Avantaggiati ML, Qin J, Nakatani Y (Dec 1998). "The 400 kDa subunit of the PCAF histone acetylase complex belongs to the ATM superfamily". Molecular Cell. 2 (6): 869–75. doi:10.1016/S1097-2765(00)80301-9. PMID 9885574.
• Brand M, Yamamoto K, Staub A, Tora L (Jun 1999). "Identification of TATA-binding protein-free TAFII-containing complex subunits suggests a role in nucleosome acetylation and signal transduction". The Journal of Biological Chemistry. 274 (26): 18285–9. doi:10.1074/jbc.274.26.18285. PMID 10373431.
• Speek M (Mar 2001). "Antisense promoter of human L1 retrotransposon drives transcription of adjacent cellular genes". Molecular and Cellular Biology. 21 (6): 1973–85. doi:10.1128/MCB.21.6.1973-1985.2001. PMC 86790. PMID 11238933.
• Brand M, Moggs JG, Oulad-Abdelghani M, Lejeune F, Dilworth FJ, Stevenin J, Almouzni G, Tora L (Jun 2001). "UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation". The EMBO Journal. 20 (12): 3187–96. doi:10.1093/emboj/20.12.3187. PMC 150203. PMID 11406595.
• Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG (Oct 2001). "Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo". Molecular and Cellular Biology. 21 (20): 6782–95. doi:10.1128/MCB.21.20.6782-6795.2001. PMC 99856. PMID 11564863.
• Cavusoglu N, Brand M, Tora L, Van Dorsselaer A (Feb 2003). "Novel subunits of the TATA binding protein free TAFII-containing transcription complex identified by matrix-assisted laser desorption/ionization-time of flight mass spectrometry following one-dimensional gel electrophoresis". Proteomics. 3 (2): 217–23. doi:10.1002/pmic.200390030. PMID 12601814. S2CID 6035986.
• Liu X, Tesfai J, Evrard YA, Dent SY, Martinez E (May 2003). "c-Myc transformation domain recruits the human STAGA complex and requires TRRAP and GCN5 acetylase activity for transcription activation". The Journal of Biological Chemistry. 278 (22): 20405–12. doi:10.1074/jbc.M211795200. PMC 4031917. PMID 12660246.