TRIM29

TRIM29
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2CSV
Identifiers
Aliases	TRIM29 , ATDC, tripartite motif containing 29
External IDs	OMIM: 610658 MGI: 1919419 HomoloGene: 8100 GeneCards: TRIM29
Gene location (Human)
Chr.	Chromosome 11 (human)
End	120,185,529 bp
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)
End	43,247,412 bp
RNA expression pattern
	Top expressed in
	gums; ; skin of abdomen; ; vulva; ; human penis; ; nipple; ; cavity of mouth; ; cervix epithelium; ; body of tongue; ; palpebral conjunctiva; ; hair follicle;
	Top expressed in
	lip; ; esophagus; ; epidermis; ; skin of abdomen; ; skin of back; ; hair follicle; ; conjunctival fornix; ; cornea; ; middle ear; ; Eustachian tube;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	DNA-binding transcription factor activity ; zinc ion binding ; p53 binding ; protein binding ; metal ion binding ; cadherin binding involved in cell-cell adhesion ; identical protein binding ;
Cellular component	intracellular anatomical structure ; cytoplasm ; lysosome ;
Biological process	negative regulation of protein localization to nucleus ; negative regulation of transcription by RNA polymerase II ; transcription by RNA polymerase II ; cell-cell adhesion ; immune system process ; innate immune response ;
	Sources:Amigo / QuickGO
Orthologs
	23650
	72169
	ENSG00000137699
	ENSMUSG00000032013
	Q14134
	Q8R2Q0
	NM_012101 ; NM_058193 ; NM_001330382
	NM_023655
	NP_001317311 ; NP_036233
	NP_076144
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated August 14, 2023

Tripartite motif-containing protein 29 is a protein that in humans is encoded by the TRIM29 gene.^[5]^[6]

Function

The protein encoded by this gene belongs to the TRIM protein family. It has multiple zinc finger motifs and a leucine zipper motif. It has been proposed to form homo- or heterodimers which are involved in nucleic acid binding. Thus, it may act as a transcriptional regulatory factor involved in carcinogenesis and/or differentiation. It may also function in the suppression of radiosensitivity since it is associated with ataxia–telangiectasia phenotype.^[6]

Interactions

TRIM29 has been shown to interact with TRIM23 ^[5] and GCC1.^[7]

Related Research Articles

Tripartite motif-containing 28 (TRIM28), also known as transcriptional intermediary factor 1β (TIF1β) and KAP1, is a protein that in humans is encoded by the TRIM28 gene.

Zinc finger protein RFP is a protein that in humans is encoded by the TRIM27 gene.

Tripartite motif-containing protein 37 is an E3 ubiquitin ligase in humans that is encoded by the TRIM37 gene.

RNA-binding protein with multiple splicing is a protein that in humans is encoded by the RBPMS gene.

Cleavage and polyadenylation specificity factor subunit 6 is a protein that in humans is encoded by the CPSF6 gene.

Midline-2 is a protein that in humans is encoded by the MID2 gene.

Tripartite motif-containing protein 32 is a protein that in humans is encoded by the TRIM32 gene. Since its discovery in 1995, TRIM32 has been shown to be implicated in a number of diverse biological pathways.

Tripartite motif-containing protein 31 is a protein that in humans is encoded by the TRIM31 gene.

DAZ-associated protein 2 is a protein that in humans is encoded by the DAZAP2 gene.

E3 ubiquitin-protein ligase TRIM33, also known as (ectodermin homolog and tripartite motif-containing 33) is a protein encoded in the human by the gene TRIM33, a member of the tripartite motif family.

THAP domain-containing protein 1 is a protein that in humans is encoded by the THAP1 gene. The synonyme is DYT6.

Tripartite motif-containing protein 9 is a protein that in humans is encoded by the TRIM9 gene.

Brain-enriched guanylate kinase-associated protein is an enzyme that in humans is encoded by the BEGAIN gene.

GRIP and coiled-coil domain-containing protein 1 is a protein that in humans is encoded by the GCC1 gene.

IST1 homolog is a protein that in humans is encoded by the KIAA0174 gene.

Putative RNA-binding protein 11 is a protein that is encoded by the RBM11 gene in humans.

Tripartite motif-containing protein 11 is a protein found in humans that is encoded by the TRIM11 gene.

Tripartite motif-containing protein 15 is a protein that in humans is encoded by the TRIM15 gene.

Tripartite motif-containing protein 41 is a protein that in humans is encoded by the TRIM41 gene.

Ataxia-telangiectasia group D complementing (ATDC) is a gene implicated in ataxia-telangiectasia.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000137699 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000032013 - 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.
1 2 Reymond A, Meroni G, Fantozzi A, Merla G, Cairo S, Luzi L, Riganelli D, Zanaria E, Messali S, Cainarca S, Guffanti A, Minucci S, Pelicci PG, Ballabio A (May 2001). "The tripartite motif family identifies cell compartments". EMBO J. 20 (9): 2140–51. doi:10.1093/emboj/20.9.2140. PMC 125245 . PMID 11331580.
1 2 "Entrez Gene: TRIM29 tripartite motif-containing 29".
↑ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

Kapp LN, Painter RB, Yu LC, van Loon N, Richard CW, James MR, Cox DR, Murnane JP (1992). "Cloning of a candidate gene for ataxia-telangiectasia group D". Am. J. Hum. Genet. 51 (1): 45–54. PMC 1682873 . PMID 1609804.
Hosoi Y, Kapp LN (1994). "Expression of a candidate ataxia-telangiectasia group D gene in cultured fibroblast cell lines and human tissues". Int. J. Radiat. Biol. 66 (6 Suppl): S71-6. doi:10.1080/09553009414551891. PMID 7530755.
Brzoska PM, Chen H, Zhu Y, Levin NA, Disatnik MH, Mochly-Rosen D, Murnane JP, Christman MF (1995). "The product of the ataxia-telangiectasia group D complementing gene, ATDC, interacts with a protein kinase C substrate and inhibitor". Proc. Natl. Acad. Sci. U.S.A. 92 (17): 7824–8. Bibcode:1995PNAS...92.7824B. doi: 10.1073/pnas.92.17.7824 . PMC 41238 . PMID 7644499.
Murnane JP, Zhu Y, Young BR, Christman MF (1994). "Expression of the candidate A-T gene ATDC is not detectable in a human cell line with a normal response to ionizing radiation". Int. J. Radiat. Biol. 66 (6 Suppl): S77-84. doi:10.1080/09553009414551901. PMID 7836856.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Leonhardt EA, Kapp LN, Young BR, Murnane JP (1994). "Nucleotide sequence analysis of a candidate gene for ataxia-telangiectasia group D (ATDC)". Genomics. 19 (1): 130–6. doi:10.1006/geno.1994.1022. PMID 8188213.
Richard CW, Cox DR, Kapp L, Murnane J, Cornelis F, Julier C, Lathrop GM, James MR (1993). "A radiation hybrid map of human chromosome 11q22-q23 containing the ataxia-telangiectasia disease locus". Genomics. 17 (1): 1–5. doi:10.1006/geno.1993.1275. PMID 8406440.
Laderoute KR, Knapp AM, Green CJ, Sutherland RM, Kapp LN (1996). "Expression of the ATDC (ataxia telangiectasia group D-complementing) gene in A431 human squamous carcinoma cells". Int. J. Cancer. 66 (6): 772–8. doi: 10.1002/(SICI)1097-0215(19960611)66:6<772::AID-IJC11>3.0.CO;2-5 . PMID 8647648. S2CID 29088136.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Tauchi H, Green C, Knapp M, Laderoute K, Kapp L (2000). "Altered splicing of the ATDC message in ataxia telangiectasia group D cells results in the absence of a functional protein". Mutagenesis. 15 (2): 105–8. doi: 10.1093/mutage/15.2.105 . PMID 10719033.
Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM (2004). "Functional proteomics mapping of a human signaling pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148 . PMID 15231748.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
Hosoi Y, Kapp LN, Murnane JP, Matsumoto Y, Enomoto A, Ono T, Miyagawa K (2006). "Suppression of anchorage-independent growth by expression of the ataxia-telangiectasia group D complementing gene, ATDC". Biochem. Biophys. Res. Commun. 348 (2): 728–34. doi:10.1016/j.bbrc.2006.07.115. PMID 16890201.
Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243. S2CID 14294292.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000137699 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000032013 - 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.

[pmid11331580-5] 1 2 Reymond A, Meroni G, Fantozzi A, Merla G, Cairo S, Luzi L, Riganelli D, Zanaria E, Messali S, Cainarca S, Guffanti A, Minucci S, Pelicci PG, Ballabio A (May 2001). "The tripartite motif family identifies cell compartments". EMBO J. 20 (9): 2140–51. doi:10.1093/emboj/20.9.2140. PMC 125245 . PMID 11331580.

[entrez-6] 1 2 "Entrez Gene: TRIM29 tripartite motif-containing 29".

[pmid16189514-7] Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

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TRIM29

Contents

Function

Interactions

Related Research Articles

References

Further reading