TPD52L2

Tumor protein D54 is a protein that in humans is encoded by the TPD52L2 gene.[5][6]

TPD52L2
Identifiers
Aliases	TPD52L2, D54, TPD54, tumor protein D52 like 2, TPD52 like 2
External IDs	OMIM: 603747 MGI: 1913564 HomoloGene: 2469 GeneCards: TPD52L2
Gene location (Human) Chr. Chromosome 20 (human)[1] Band 20q13.33 Start 63,865,228 bp[1] End 63,891,545 bp[1]
Gene location (Mouse) Chr. Chromosome 2 (mouse)[2] Band 2|2 H4 Start 181,497,142 bp[2] End 181,517,966 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0001948 protein binding • protein homodimerization activity • protein heterodimerization activity • RNA binding • catalytic activity Cellular component • cytoplasm • perinuclear region of cytoplasm Biological process • regulation of cell proliferation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	7165	66314
Ensembl	ENSG00000101150	ENSMUSG00000000827
UniProt	O43399 Q6FGS1	Q9CYZ2
RefSeq (mRNA)	NM_001243891 NM_001243892 NM_001243894 NM_001243895 NM_003288 NM_199359 NM_199360 NM_199361 NM_199362 NM_199363	NM_001291197 NM_001291200 NM_001291201 NM_001291202 NM_001291203 NM_001291204 NM_025482 NM_001373959 NM_001373960 NM_001373961
RefSeq (protein)	NP_001230820 NP_001230821 NP_001230823 NP_001230824 NP_003279 NP_955391 NP_955392 NP_955393 NP_955394 NP_955395 NP_003279.2	NP_001278126 NP_001278129 NP_001278130 NP_001278131 NP_001278132 NP_001278133 NP_079758 NP_001360888 NP_001360889 NP_001360890
Location (UCSC)	Chr 20: 63.87 – 63.89 Mb	Chr 2: 181.5 – 181.52 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Model organisms

Tpd52l2 knockout mouse phenotype

Characteristic	Phenotype
Homozygote viability	Normal
Body weight	Normal
Anxiety	Normal
Neurological assessment	Normal
Grip strength	Normal
Hot plate	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Abnormal[7]
Radiography	Normal
Body temperature	Normal
Eye morphology	Normal
Clinical chemistry	Normal
Haematology	Normal
Peripheral blood lymphocytes	Normal
Micronucleus test	Normal
Heart weight	Normal
Skin Histopathology	Normal
Brain histopathology	Normal
Salmonella infection	Normal[8]
All tests and analysis from[9][10]

Model organisms have been used in the study of TPD52L2 function. A conditional knockout mouse line, called Tpd52l2^{tm1a(KOMP)Wtsi}[11][12] was generated as part of the International Knockout Mouse Consortium program—a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[13][14][15]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[9][16]

Twenty two tests were carried out on mutant mice and one significant abnormality was observed: homozygous adult females displayed a decrease in body length by DEXA.[9]

Interactions

TPD52L2 has been shown to interact with TPD52L1[5] and TPD52.[5]

Cellular function

TPD52L2 has a role in membrane traffic.[17] TPD52L2 is found on small transport vesicles, termed intracellular nanovesicles, that transfer proteins between different cellular compartments. When TPD52L2 is depleted from HeLa cells, the following trafficking pathways are impaired: anterograde traffic, recycling of cargo and Golgi integrity.[17] Proteomic analysis indicates that TPD52L2 is one of the most abundant proteins expressed in HeLa cells.[18]

References

1. GRCh38: Ensembl release 89: ENSG00000101150 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000000827 - 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. Byrne JA, Nourse CR, Basset P, Gunning P (Mar 1998). "Identification of homo- and heteromeric interactions between members of the breast carcinoma-associated D52 protein family using the yeast two-hybrid system". Oncogene. 16 (7): 873–81. doi:10.1038/sj.onc.1201604. PMID 9484778.
6. "Entrez Gene: TPD52L2 tumor protein D52-like 2".
7. "DEXA data for Tpd52l2". Wellcome Trust Sanger Institute.
8. "Salmonella infection data for Tpd52l2". Wellcome Trust Sanger Institute.
9. Gerdin, AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 0. doi:10.1111/j.1755-3768.2010.4142.x. S2CID 85911512.
10. Mouse Resources Portal, Wellcome Trust Sanger Institute.
11. "International Knockout Mouse Consortium".
12. "Mouse Genome Informatics".
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 (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 (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 (2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247. S2CID 18872015.
16. van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biol. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
17. Larocque G, La-Borde PJ, Clarke NI, Carter NJ, Royle SJ (2019). "Tumor protein D54 defines a new class of intracellular transport vesicle". J Cell Biol. 219. doi:10.1083/jcb.201812044. PMID 31672706.
18. Hein MY, Hubner NC, Poser I, Cox J, Nagaraj N, Toyoda Y, Gak IA, Weisswange I, Mansfeld J, Buchholz F, Hyman AA, Mann M (2017). "A human interactome in three quantitative dimensions organized by stoichiometries and abundances". Cell. 163 (3): 712–23. doi:10.1016/j.cell.2015.09.053. PMID 26496610.

Further reading

• 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.
• Byrne JA, Mattei MG, Basset P (1996). "Definition of the tumor protein D52 (TPD52) gene family through cloning of D52 homologues in human (hD53) and mouse (mD52)". Genomics. 35 (3): 523–32. doi:10.1006/geno.1996.0393. PMID 8812487.
• 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.
• Nourse CR, Mattei MG, Gunning P, Byrne JA (1998). "Cloning of a third member of the D52 gene family indicates alternative coding sequence usage in D52-like transcripts". Biochim. Biophys. Acta. 1443 (1–2): 155–68. doi:10.1016/S0167-4781(98)00211-5. PMID 9838088.
• Wilson SH, Bailey AM, Nourse CR, Mattei MG, Byrne JA (2001). "Identification of MAL2, a novel member of the mal proteolipid family, though interactions with TPD52-like proteins in the yeast two-hybrid system". Genomics. 76 (1–3): 81–8. doi:10.1006/geno.2001.6610. PMID 11549320.
• Boutros R, Byrne JA (2005). "D53 (TPD52L1) is a cell cycle-regulated protein maximally expressed at the G2-M transition in breast cancer cells". Exp. Cell Res. 310 (1): 152–65. doi:10.1016/j.yexcr.2005.07.009. PMID 16112108.
• Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Barbaric D, Byth K, Dalla-Pozza L, Byrne JA (2006). "Expression of tumor protein D52-like genes in childhood leukemia at diagnosis: clinical and sample considerations". Leuk. Res. 30 (11): 1355–63. doi:10.1016/j.leukres.2006.03.009. PMID 16620967.
• Cao Q, Chen J, Zhu L, Liu Y, Zhou Z, Sha J, Wang S, Li J (2006). "A testis-specific and testis developmentally regulated tumor protein D52 (TPD52)-like protein TPD52L3/hD55 interacts with TPD52 family proteins". Biochem. Biophys. Res. Commun. 344 (3): 798–806. doi:10.1016/j.bbrc.2006.03.208. PMID 16631610.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.