TTC1

TTC1
Identifiers
Aliases	TTC1 , TPR1, tetratricopeptide repeat domain 1
External IDs	OMIM: 601963 MGI: 1914077 HomoloGene: 2485 GeneCards: TTC1
Gene location (Human)
Chr.	Chromosome 5 (human)
End	160,065,543 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	43,638,835 bp
RNA expression pattern
	Top expressed in
	Achilles tendon; ; cingulate gyrus; ; left ventricle; ; Brodmann area 9; ; prefrontal cortex; ; islet of Langerhans; ; amygdala; ; frontal pole; ; substantia nigra; ; Brodmann area 10;
	Top expressed in
	morula; ; spermatocyte; ; spermatid; ; secondary oocyte; ; blastocyst; ; yolk sac; ; temporal muscle; ; medial vestibular nucleus; ; anterior horn of spinal cord; ; digastric muscle;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	unfolded protein binding ; protein binding ;
Cellular component	peroxisomal membrane ; cytosol ;
Biological process	protein folding ;
	Sources:Amigo / QuickGO
Orthologs
	7265
	66827
	ENSG00000113312
	ENSMUSG00000041278
	Q99614
	Q91Z38
	NM_003314 ; NM_001282500
	NM_133795
	NP_001269429 ; NP_003305
	NP_598556
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated January 16, 2024

Tetratricopeptide repeat protein 1 is a protein that in humans is encoded by the TTC1 gene.^[5]^[6]

Interactions

TTC1 has been shown to interact with HSPA4.^[7]

Related Research Articles

The 70 kilodalton heat shock proteins are a family of conserved ubiquitously expressed heat shock proteins. Proteins with similar structure exist in virtually all living organisms. Intracellularly localized Hsp70s are an important part of the cell's machinery for protein folding, performing chaperoning functions, and helping to protect cells from the adverse effects of physiological stresses. Additionally, membrane-bound Hsp70s have been identified as a potential target for cancer therapies and their extracellularly localized counterparts have been identified as having both membrane-bound and membrane-free structures.

Hop, occasionally written HOP, is an abbreviation for Hsp70-Hsp90 Organizing Protein. It functions as a co-chaperone which reversibly links together the protein chaperones Hsp70 and Hsp90.

RoXaN also known as ZC3H7B, is a protein that in humans is encoded by the ZC3H7B gene. RoXaN is a protein that contains tetratricopeptide repeat and leucine-aspartate repeat as well as zinc finger domains. This protein also interacts with the rotavirus non-structural protein NSP3.

Heat shock 70 kDa protein 1, also termed Hsp72, is a protein that in humans is encoded by the HSPA1A gene. As a member of the heat shock protein 70 family and a chaperone protein, it facilitates the proper folding of newly translated and misfolded proteins, as well as stabilize or degrade mutant proteins. In addition, Hsp72 also facilitates DNA repair. Its functions contribute to biological processes including signal transduction, apoptosis, protein homeostasis, and cell growth and differentiation. It has been associated with an extensive number of cancers, neurodegenerative diseases, cell senescence and aging, and inflammatory diseases such as Diabetes mellitus type 2 and rheumatoid arthritis.

Heat shock protein HSP 90-beta also called HSP90beta is a protein that in humans is encoded by the HSP90AB1 gene.

DnaJ homolog subfamily A member 3, mitochondrial, also known as Tumorous imaginal disc 1 (TID1), is a protein that in humans is encoded by the DNAJA3 gene on chromosome 16. This protein belongs to the DNAJ/Hsp40 protein family, which is known for binding and activating Hsp70 chaperone proteins to perform protein folding, degradation, and complex assembly. As a mitochondrial protein, it is involved in maintaining membrane potential and mitochondrial DNA (mtDNA) integrity, as well as cellular processes such as cell movement, growth, and death. Furthermore, it is associated with a broad range of diseases, including neurodegenerative diseases, inflammatory diseases, and cancers.

Heat shock 70 kDa protein 4 is a protein that in humans is encoded by the HSPA4 gene.

DnaJ homolog subfamily B member 1 is a protein that in humans is encoded by the DNAJB1 gene.

DnaJ homolog subfamily A member 1 is a protein that in humans is encoded by the DNAJA1 gene.

DnaJ homolog subfamily B member 6 is a protein that in humans is encoded by the DNAJB6 gene.

Hsp70-binding protein 1 is a protein that in humans is encoded by the HSPBP1 gene.

Interferon-induced protein with tetratricopeptide repeats 1 is a protein that in humans is encoded by the IFIT1 gene.

NEDD8-activating enzyme E1 catalytic subunit is a protein that in humans is encoded by the UBA3 gene.

Heat shock 70 kDa protein 14 also known as HSP70-like protein 1 or heat shock protein HSP60 is a protein that in humans is encoded by the HSPA14 gene.

DnaJ homolog subfamily A member 2 is a protein that in humans is encoded by the DNAJA2 gene.

Leucine-rich repeat serine/threonine-protein kinase 1 is an enzyme that in humans is encoded by the LRRK1 gene.

DnaJ homolog subfamily C member 7 is a protein that in humans is encoded by the DNAJC7 gene.

WD repeat-containing protein 1 is a protein that in humans is encoded by the WDR1 gene.

Melanoma-associated antigen B2 is a protein that in humans is encoded by the MAGEB2 gene.

Tetratricopeptide repeat protein 4 is a protein that in humans is encoded by the TTC4 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000113312 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000041278 - 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.
↑ Murthy AE, Bernards A, Church D, Wasmuth J, Gusella JF (Nov 1996). "Identification and characterization of two novel tetratricopeptide repeat-containing genes". DNA Cell Biol. 15 (9): 727–35. doi:10.1089/dna.1996.15.727. PMID 8836031.
↑ "Entrez Gene: TTC1 tetratricopeptide repeat domain 1".
↑ Oh W, Song Jaewhan (Aug 2003). "Cooperative interaction of Hsp40 and TPR1 with Hsp70 reverses Hsp70-HspBp1 complex formation". Mol. Cells. Korea (South). 16 (1): 84–91. doi: 10.1016/S1016-8478(23)13770-8 . ISSN 1016-8478. PMID 14503850.

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.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (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.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC 139241 . PMID 12477932.
Marty C, Browning DD, Ye RD (2003). "Identification of tetratricopeptide repeat 1 as an adaptor protein that interacts with heterotrimeric G proteins and the small GTPase Ras". Mol. Cell. Biol. 23 (11): 3847–58. doi:10.1128/MCB.23.11.3847-3858.2003. PMC 155206 . PMID 12748287.
Oh WK, Song J (2004). "Cooperative interaction of Hsp40 and TPR1 with Hsp70 reverses Hsp70-HspBp1 complex formation". Mol. Cells. 16 (1): 84–91. doi: 10.1016/S1016-8478(23)13770-8 . PMID 14503850.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928 . PMID 15489334.
Barrios-Rodiles M, Brown KR, Ozdamar B, et al. (2005). "High-throughput mapping of a dynamic signaling network in mammalian cells". Science. 307 (5715): 1621–5. Bibcode:2005Sci...307.1621B. doi:10.1126/science.1105776. PMID 15761153. S2CID 39457788.
Rual JF, Venkatesan K, Hao T, et al. (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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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000113312 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000041278 - 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.

[pmid8836031-5] Murthy AE, Bernards A, Church D, Wasmuth J, Gusella JF (Nov 1996). "Identification and characterization of two novel tetratricopeptide repeat-containing genes". DNA Cell Biol. 15 (9): 727–35. doi:10.1089/dna.1996.15.727. PMID 8836031.

[entrez-6] "Entrez Gene: TTC1 tetratricopeptide repeat domain 1".

[pmid14503850-7] Oh W, Song Jaewhan (Aug 2003). "Cooperative interaction of Hsp40 and TPR1 with Hsp70 reverses Hsp70-HspBp1 complex formation". Mol. Cells. Korea (South). 16 (1): 84–91. doi: 10.1016/S1016-8478(23)13770-8 . ISSN 1016-8478. PMID 14503850.

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TTC1

Contents

Interactions

Related Research Articles

References

Further reading