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AP5M1

February 27, 2024

AP-5 complex subunit mu (AP5M1), otherwise known as MUDENG (MuD), is a protein that is encoded by the AP5M1 gene.[4] The AP5M1 gene was originally discovered when screening for genes which helped to promote death in Fas-mediated apoptosis.[5][6] It is a highly conserved gene.[5][7][6]

AP5M1
Identifiers
AliasesAP5M1, C14orf108, MUDENG, Mu5, MuD, adaptor related protein complex 5 mu 1 subunit, adaptor related protein complex 5 subunit mu 1
External IDsOMIM: 614368 MGI: 1921635 HomoloGene: 10081 GeneCards: AP5M1
Orthologs
SpeciesHumanMouse
Entrez

55745

74385

Ensembl

ENSG00000053770

n/a

UniProt

Q9H0R1

Q8BJ63

RefSeq (mRNA)

NM_018229

NM_144535
NM_001360070

RefSeq (protein)

NP_060699

NP_653118
NP_001346999

Location (UCSC)Chr 14: 57.27 – 57.3 Mbn/a
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse
The 3D structure of the protein AP5M1. The alpha fold structure was obtained from Uniprot (AF-Q9H0R1-F1) and modeled using ChimeraX. The three domains are emphasized with color. The first domain is yellow, the second domain is teal, and the third domain is pink.

MuD is the medium-sized subunit of the AP5 adaptor complex.[8] MuD is expressed throughout the body and is located within both the mitochondria as well as the endoplasmic reticulum (ER) of cells.[5][7][6]

MuD has been shown to have the ability to induce apoptosis; however, there is evidence that it plays an anti-apoptotic role in apoptosis mediated by tumor necrosis factor-related apoptosis-inducing ligand (TRAIL).[5][7][6][9][10]

Structure edit

MuD consists of 490 amino acids that interact to form a tertiary structure with three domains.[11][12]

The overall structure shares similarities with adaptor protein (AP) complexes that are related to clathrin-mediated endocytosis; amino acids 197 through 417 are a shared adaptin domain found in AP μ subunits.[13][14]

Within the adaptin domain are two aspartic acids, D276 and D290, which serve as binding sites for caspase-3.[14]

Function edit

The overall function of MuD remains unclear.[15] It is known, however, that MuD regulates the expression of BAX, a pro-apoptotic member of the Bcl-2 family of proteins.[16][15] Due to— and dependent upon— this relationship, MuD has been able to induce cell death in tumor cells.[17][16][15]

Additionally, MuD has been suggested to be involved in endosomal trafficking.[17][16][18][15]

TRAIL and MuD edit

TRAIL, an apoptosis-inducing ligand, activates caspase-8 and caspase-3, which initiate the intrinsic pathway of apoptosis by cleaving BH3 interacting-domain death agonist (Bid) into tBid, another pro-apoptotic member of the Bl-2 protein family.[19][20][21][22] MuD interferes with this process because D276 and D290 act as alternative binding sites for caspase-3, decreasing the amount of Bid that gets cleaved.[20][19][21] Tumor cells being treated with TRAIL are 32% more likely to survive when MuD is being expressed.[19]   

References edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000053770 - Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ Hirst, Jennifer; Barlow, Lael D.; Francisco, Gabriel Casey; Sahlender, Daniela A.; Seaman, Matthew N. J.; Dacks, Joel B.; Robinson, Margaret S. (2011-10-11). "The fifth adaptor protein complex". PLOS Biology. 9 (10): e1001170. doi:10.1371/journal.pbio.1001170. ISSN 1545-7885. PMC 3191125. PMID 22022230.
  5. ^ a b c d Lee, Mi-Rha; Shin, Jin Na; Moon, Ae Ran; Park, Sun-Young; Hong, Gilsun; Lee, Mi-Ja; Yun, Cheol-Won; Seol, Dai-Wu; Piya, Sujan; Bae, Jeehyeon; Oh, Jae-Wook; Kim, Tae-Hyoung (2008-06-06). "A novel protein, MUDENG, induces cell death in cytotoxic T cells". Biochemical and Biophysical Research Communications. 370 (3): 504–508. doi:10.1016/j.bbrc.2008.03.139. ISSN 1090-2104. PMID 18395520.
  6. ^ a b c d Choi, J.-H.; Lim, J.-B.; Wickramanayake, D. D.; Wagley, Y.; Kim, J.; Lee, H.-C.; Seo, H. G.; Kim, T.-H.; Oh, J.-W. (2016). "Characterization of MUDENG, a novel anti-apoptotic protein". Oncogenesis. 5 (5): e221. doi:10.1038/oncsis.2016.30. ISSN 2157-9024. PMC 4945747. PMID 27136675.
  7. ^ a b c Muthu, Manikandan; Chun, Sechul; Gopal, Judy; Park, Gyun-Seok; Nile, Arti; Shin, Jisoo; Shin, Juhyun; Kim, Tae-Hyoung; Oh, Jae-Wook (2020-08-04). "The MUDENG Augmentation: A Genesis in Anti-Cancer Therapy?". International Journal of Molecular Sciences. 21 (15): 5583. doi:10.3390/ijms21155583. ISSN 1422-0067. PMC 7432215. PMID 32759789.
  8. ^ Hirst, Jennifer; Irving, Carol; Borner, Georg H. H. (2012-11-21). "Adaptor protein complexes AP-4 and AP-5: new players in endosomal trafficking and progressive spastic paraplegia". Traffic. 14 (2): 153–164. doi:10.1111/tra.12028. ISSN 1600-0854. PMID 23167973. S2CID 13766991.
  9. ^ Shin, Jin Na; Han, Ji Hye; Kim, Ji-Young; Moon, Ae-Ran; Kim, Ji Eun; Chang, Jeong Hwan; Bae, Jeehyeon; Oh, Jae Wook; Kim, Tae-Hyoung (2013-05-31). "MUDENG is cleaved by caspase-3 during TRAIL-induced cell death". Biochemical and Biophysical Research Communications. 435 (2): 234–238. doi:10.1016/j.bbrc.2013.04.075. ISSN 1090-2104. PMID 23665015.
  10. ^ Won, Miae; Luo, Yongyang; Lee, Dong-Ho; Shin, Eunkyoung; Suh, Dae-Shik; Kim, Tae-Hyoung; Jin, Hanyong; Bae, Jeehyeon (2019-10-15). "BAX is an essential key mediator of AP5M1-induced apoptosis in cervical carcinoma cells". Biochemical and Biophysical Research Communications. 518 (2): 368–373. doi:10.1016/j.bbrc.2019.08.065. ISSN 1090-2104. PMID 31427081. S2CID 201095590.
  11. ^ Muthu, Manikandan; Chun, Sechul; Gopal, Judy; Park, Gyun-Seok; Nile, Arti; Shin, Jisoo; Shin, Juhyun; Kim, Tae-Hyoung; Oh, Jae-Wook (2020-08-04). "The MUDENG Augmentation: A Genesis in Anti-Cancer Therapy?". International Journal of Molecular Sciences. 21 (15): 5583. doi:10.3390/ijms21155583. ISSN 1422-0067. PMC 7432215. PMID 32759789.
  12. ^ Choi, J.-H.; Lim, J.-B.; Wickramanayake, D. D.; Wagley, Y.; Kim, J.; Lee, H.-C.; Seo, H. G.; Kim, T.-H.; Oh, J.-W. (2016). "Characterization of MUDENG, a novel anti-apoptotic protein". Oncogenesis. 5 (5): e221. doi:10.1038/oncsis.2016.30. ISSN 2157-9024. PMC 4945747. PMID 27136675.
  13. ^ Lee, Mi-Rha; Shin, Jin Na; Moon, Ae Ran; Park, Sun-Young; Hong, Gilsun; Lee, Mi-Ja; Yun, Cheol-Won; Seol, Dai-Wu; Piya, Sujan; Bae, Jeehyeon; Oh, Jae-Wook; Kim, Tae-Hyoung (2008-06-06). "A novel protein, MUDENG, induces cell death in cytotoxic T cells". Biochemical and Biophysical Research Communications. 370 (3): 504–508. doi:10.1016/j.bbrc.2008.03.139. ISSN 1090-2104. PMID 18395520.
  14. ^ a b Shin, Jin Na; Han, Ji Hye; Kim, Ji-Young; Moon, Ae-Ran; Kim, Ji Eun; Chang, Jeong Hwan; Bae, Jeehyeon; Oh, Jae Wook; Kim, Tae-Hyoung (2013-05-31). "MUDENG is cleaved by caspase-3 during TRAIL-induced cell death". Biochemical and Biophysical Research Communications. 435 (2): 234–238. doi:10.1016/j.bbrc.2013.04.075. ISSN 1090-2104. PMID 23665015.
  15. ^ a b c d Won, Miae; Luo, Yongyang; Lee, Dong-Ho; Shin, Eunkyoung; Suh, Dae-Shik; Kim, Tae-Hyoung; Jin, Hanyong; Bae, Jeehyeon (2019-10-15). "BAX is an essential key mediator of AP5M1-induced apoptosis in cervical carcinoma cells". Biochemical and Biophysical Research Communications. 518 (2): 368–373. doi:10.1016/j.bbrc.2019.08.065. ISSN 1090-2104. PMID 31427081. S2CID 201095590.
  16. ^ a b c Muthu, Manikandan; Chun, Sechul; Gopal, Judy; Park, Gyun-Seok; Nile, Arti; Shin, Jisoo; Shin, Juhyun; Kim, Tae-Hyoung; Oh, Jae-Wook (2020-08-04). "The MUDENG Augmentation: A Genesis in Anti-Cancer Therapy?". International Journal of Molecular Sciences. 21 (15): 5583. doi:10.3390/ijms21155583. ISSN 1422-0067. PMC 7432215. PMID 32759789.
  17. ^ a b Lee, Mi-Rha; Shin, Jin Na; Moon, Ae Ran; Park, Sun-Young; Hong, Gilsun; Lee, Mi-Ja; Yun, Cheol-Won; Seol, Dai-Wu; Piya, Sujan; Bae, Jeehyeon; Oh, Jae-Wook; Kim, Tae-Hyoung (2008-06-06). "A novel protein, MUDENG, induces cell death in cytotoxic T cells". Biochemical and Biophysical Research Communications. 370 (3): 504–508. doi:10.1016/j.bbrc.2008.03.139. ISSN 1090-2104. PMID 18395520.
  18. ^ Hirst, Jennifer; Irving, Carol; Borner, Georg H. H. (2012-11-21). "Adaptor protein complexes AP-4 and AP-5: new players in endosomal trafficking and progressive spastic paraplegia". Traffic. 14 (2): 153–164. doi:10.1111/tra.12028. ISSN 1600-0854. PMID 23167973. S2CID 13766991.
  19. ^ a b c Choi, J.-H.; Lim, J.-B.; Wickramanayake, D. D.; Wagley, Y.; Kim, J.; Lee, H.-C.; Seo, H. G.; Kim, T.-H.; Oh, J.-W. (2016). "Characterization of MUDENG, a novel anti-apoptotic protein". Oncogenesis. 5 (5): e221. doi:10.1038/oncsis.2016.30. ISSN 2157-9024. PMC 4945747. PMID 27136675.
  20. ^ a b Muthu, Manikandan; Chun, Sechul; Gopal, Judy; Park, Gyun-Seok; Nile, Arti; Shin, Jisoo; Shin, Juhyun; Kim, Tae-Hyoung; Oh, Jae-Wook (2020-08-04). "The MUDENG Augmentation: A Genesis in Anti-Cancer Therapy?". International Journal of Molecular Sciences. 21 (15): 5583. doi:10.3390/ijms21155583. ISSN 1422-0067. PMC 7432215. PMID 32759789.
  21. ^ a b Shin, Jin Na; Han, Ji Hye; Kim, Ji-Young; Moon, Ae-Ran; Kim, Ji Eun; Chang, Jeong Hwan; Bae, Jeehyeon; Oh, Jae Wook; Kim, Tae-Hyoung (2013-05-31). "MUDENG is cleaved by caspase-3 during TRAIL-induced cell death". Biochemical and Biophysical Research Communications. 435 (2): 234–238. doi:10.1016/j.bbrc.2013.04.075. ISSN 1090-2104. PMID 23665015.
  22. ^ Dimberg, L. Y.; Anderson, C. K.; Camidge, R.; Behbakht, K.; Thorburn, A.; Ford, H. L. (2013-03-14). "On the TRAIL to successful cancer therapy? Predicting and counteracting resistance against TRAIL-based therapeutics". Oncogene. 32 (11): 1341–1350. doi:10.1038/onc.2012.164. ISSN 1476-5594. PMC 4502956. PMID 22580613.


 

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February 27, 2024
ap5m1, complex, subunit, otherwise, known, mudeng, protein, that, encoded, gene, gene, originally, discovered, when, screening, genes, which, helped, promote, death, mediated, apoptosis, highly, conserved, gene, identifiersaliases, c14orf108, mudeng, adaptor, . AP 5 complex subunit mu AP5M1 otherwise known as MUDENG MuD is a protein that is encoded by the AP5M1 gene 4 The AP5M1 gene was originally discovered when screening for genes which helped to promote death in Fas mediated apoptosis 5 6 It is a highly conserved gene 5 7 6 AP5M1IdentifiersAliasesAP5M1 C14orf108 MUDENG Mu5 MuD adaptor related protein complex 5 mu 1 subunit adaptor related protein complex 5 subunit mu 1External IDsOMIM 614368 MGI 1921635 HomoloGene 10081 GeneCards AP5M1Gene location Human Chr Chromosome 14 human 1 Band14q22 3Start57 268 924 bp 1 End57 298 742 bp 1 RNA expression patternBgeeHumanMouse ortholog Top expressed injejunal mucosaendothelial cellretinal pigment epitheliumpalpebral conjunctivarectumright ventricleduodenumkidney tubuleBrodmann area 23biceps brachiin aMore reference expression dataBioGPSn aGene ontologyMolecular functionprotein bindingCellular componentcytoplasm lysosomal membrane cytosol endosome late endosome lysosome AP type membrane coat adaptor complex membrane late endosome membraneBiological processprotein transport endosomal transportSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez5574574385EnsemblENSG00000053770n aUniProtQ9H0R1Q8BJ63RefSeq mRNA NM 018229NM 144535NM 001360070RefSeq protein NP 060699NP 653118NP 001346999Location UCSC Chr 14 57 27 57 3 Mbn aPubMed search 2 3 WikidataView Edit HumanView Edit MouseThe 3D structure of the protein AP5M1 The alpha fold structure was obtained from Uniprot AF Q9H0R1 F1 and modeled using ChimeraX The three domains are emphasized with color The first domain is yellow the second domain is teal and the third domain is pink MuD is the medium sized subunit of the AP5 adaptor complex 8 MuD is expressed throughout the body and is located within both the mitochondria as well as the endoplasmic reticulum ER of cells 5 7 6 MuD has been shown to have the ability to induce apoptosis however there is evidence that it plays an anti apoptotic role in apoptosis mediated by tumor necrosis factor related apoptosis inducing ligand TRAIL 5 7 6 9 10 Contents 1 Structure 2 Function 3 TRAIL and MuD 4 ReferencesStructure editMuD consists of 490 amino acids that interact to form a tertiary structure with three domains 11 12 The overall structure shares similarities with adaptor protein AP complexes that are related to clathrin mediated endocytosis amino acids 197 through 417 are a shared adaptin domain found in AP m subunits 13 14 Within the adaptin domain are two aspartic acids D276 and D290 which serve as binding sites for caspase 3 14 Function editThe overall function of MuD remains unclear 15 It is known however that MuD regulates the expression of BAX a pro apoptotic member of the Bcl 2 family of proteins 16 15 Due to and dependent upon this relationship MuD has been able to induce cell death in tumor cells 17 16 15 Additionally MuD has been suggested to be involved in endosomal trafficking 17 16 18 15 TRAIL and MuD editTRAIL an apoptosis inducing ligand activates caspase 8 and caspase 3 which initiate the intrinsic pathway of apoptosis by cleaving BH3 interacting domain death agonist Bid into tBid another pro apoptotic member of the Bl 2 protein family 19 20 21 22 MuD interferes with this process because D276 and D290 act as alternative binding sites for caspase 3 decreasing the amount of Bid that gets cleaved 20 19 21 Tumor cells being treated with TRAIL are 32 more likely to survive when MuD is being expressed 19 References edit a b c GRCh38 Ensembl release 89 ENSG00000053770 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 Hirst Jennifer Barlow Lael D Francisco Gabriel Casey Sahlender Daniela A Seaman Matthew N J Dacks Joel B Robinson Margaret S 2011 10 11 The fifth adaptor protein complex PLOS Biology 9 10 e1001170 doi 10 1371 journal pbio 1001170 ISSN 1545 7885 PMC 3191125 PMID 22022230 a b c d Lee Mi Rha Shin Jin Na Moon Ae Ran Park Sun Young Hong Gilsun Lee Mi Ja Yun Cheol Won Seol Dai Wu Piya Sujan Bae Jeehyeon Oh Jae Wook Kim Tae Hyoung 2008 06 06 A novel protein MUDENG induces cell death in cytotoxic T cells Biochemical and Biophysical Research Communications 370 3 504 508 doi 10 1016 j bbrc 2008 03 139 ISSN 1090 2104 PMID 18395520 a b c d Choi J H Lim J B Wickramanayake D D Wagley Y Kim J Lee H C Seo H G Kim T H Oh J W 2016 Characterization of MUDENG a novel anti apoptotic protein Oncogenesis 5 5 e221 doi 10 1038 oncsis 2016 30 ISSN 2157 9024 PMC 4945747 PMID 27136675 a b c Muthu Manikandan Chun Sechul Gopal Judy Park Gyun Seok Nile Arti Shin Jisoo Shin Juhyun Kim Tae Hyoung Oh Jae Wook 2020 08 04 The MUDENG Augmentation A Genesis in Anti Cancer Therapy International Journal of Molecular Sciences 21 15 5583 doi 10 3390 ijms21155583 ISSN 1422 0067 PMC 7432215 PMID 32759789 Hirst Jennifer Irving Carol Borner Georg H H 2012 11 21 Adaptor protein complexes AP 4 and AP 5 new players in endosomal trafficking and progressive spastic paraplegia Traffic 14 2 153 164 doi 10 1111 tra 12028 ISSN 1600 0854 PMID 23167973 S2CID 13766991 Shin Jin Na Han Ji Hye Kim Ji Young Moon Ae Ran Kim Ji Eun Chang Jeong Hwan Bae Jeehyeon Oh Jae Wook Kim Tae Hyoung 2013 05 31 MUDENG is cleaved by caspase 3 during TRAIL induced cell death Biochemical and Biophysical Research Communications 435 2 234 238 doi 10 1016 j bbrc 2013 04 075 ISSN 1090 2104 PMID 23665015 Won Miae Luo Yongyang Lee Dong Ho Shin Eunkyoung Suh Dae Shik Kim Tae Hyoung Jin Hanyong Bae Jeehyeon 2019 10 15 BAX is an essential key mediator of AP5M1 induced apoptosis in cervical carcinoma cells Biochemical and Biophysical Research Communications 518 2 368 373 doi 10 1016 j bbrc 2019 08 065 ISSN 1090 2104 PMID 31427081 S2CID 201095590 Muthu Manikandan Chun Sechul Gopal Judy Park Gyun Seok Nile Arti Shin Jisoo Shin Juhyun Kim Tae Hyoung Oh Jae Wook 2020 08 04 The MUDENG Augmentation A Genesis in Anti Cancer Therapy International Journal of Molecular Sciences 21 15 5583 doi 10 3390 ijms21155583 ISSN 1422 0067 PMC 7432215 PMID 32759789 Choi J H Lim J B Wickramanayake D D Wagley Y Kim J Lee H C Seo H G Kim T H Oh J W 2016 Characterization of MUDENG a novel anti apoptotic protein Oncogenesis 5 5 e221 doi 10 1038 oncsis 2016 30 ISSN 2157 9024 PMC 4945747 PMID 27136675 Lee Mi Rha Shin Jin Na Moon Ae Ran Park Sun Young Hong Gilsun Lee Mi Ja Yun Cheol Won Seol Dai Wu Piya Sujan Bae Jeehyeon Oh Jae Wook Kim Tae Hyoung 2008 06 06 A novel protein MUDENG induces cell death in cytotoxic T cells Biochemical and Biophysical Research Communications 370 3 504 508 doi 10 1016 j bbrc 2008 03 139 ISSN 1090 2104 PMID 18395520 a b Shin Jin Na Han Ji Hye Kim Ji Young Moon Ae Ran Kim Ji Eun Chang Jeong Hwan Bae Jeehyeon Oh Jae Wook Kim Tae Hyoung 2013 05 31 MUDENG is cleaved by caspase 3 during TRAIL induced cell death Biochemical and Biophysical Research Communications 435 2 234 238 doi 10 1016 j bbrc 2013 04 075 ISSN 1090 2104 PMID 23665015 a b c d Won Miae Luo Yongyang Lee Dong Ho Shin Eunkyoung Suh Dae Shik Kim Tae Hyoung Jin Hanyong Bae Jeehyeon 2019 10 15 BAX is an essential key mediator of AP5M1 induced apoptosis in cervical carcinoma cells Biochemical and Biophysical Research Communications 518 2 368 373 doi 10 1016 j bbrc 2019 08 065 ISSN 1090 2104 PMID 31427081 S2CID 201095590 a b c Muthu Manikandan Chun Sechul Gopal Judy Park Gyun Seok Nile Arti Shin Jisoo Shin Juhyun Kim Tae Hyoung Oh Jae Wook 2020 08 04 The MUDENG Augmentation A Genesis in Anti Cancer Therapy International Journal of Molecular Sciences 21 15 5583 doi 10 3390 ijms21155583 ISSN 1422 0067 PMC 7432215 PMID 32759789 a b Lee Mi Rha Shin Jin Na Moon Ae Ran Park Sun Young Hong Gilsun Lee Mi Ja Yun Cheol Won Seol Dai Wu Piya Sujan Bae Jeehyeon Oh Jae Wook Kim Tae Hyoung 2008 06 06 A novel protein MUDENG induces cell death in cytotoxic T cells Biochemical and Biophysical Research Communications 370 3 504 508 doi 10 1016 j bbrc 2008 03 139 ISSN 1090 2104 PMID 18395520 Hirst Jennifer Irving Carol Borner Georg H H 2012 11 21 Adaptor protein complexes AP 4 and AP 5 new players in endosomal trafficking and progressive spastic paraplegia Traffic 14 2 153 164 doi 10 1111 tra 12028 ISSN 1600 0854 PMID 23167973 S2CID 13766991 a b c Choi J H Lim J B Wickramanayake D D Wagley Y Kim J Lee H C Seo H G Kim T H Oh J W 2016 Characterization of MUDENG a novel anti apoptotic protein Oncogenesis 5 5 e221 doi 10 1038 oncsis 2016 30 ISSN 2157 9024 PMC 4945747 PMID 27136675 a b Muthu Manikandan Chun Sechul Gopal Judy Park Gyun Seok Nile Arti Shin Jisoo Shin Juhyun Kim Tae Hyoung Oh Jae Wook 2020 08 04 The MUDENG Augmentation A Genesis in Anti Cancer Therapy International Journal of Molecular Sciences 21 15 5583 doi 10 3390 ijms21155583 ISSN 1422 0067 PMC 7432215 PMID 32759789 a b Shin Jin Na Han Ji Hye Kim Ji Young Moon Ae Ran Kim Ji Eun Chang Jeong Hwan Bae Jeehyeon Oh Jae Wook Kim Tae Hyoung 2013 05 31 MUDENG is cleaved by caspase 3 during TRAIL induced cell death Biochemical and Biophysical Research Communications 435 2 234 238 doi 10 1016 j bbrc 2013 04 075 ISSN 1090 2104 PMID 23665015 Dimberg L Y Anderson C K Camidge R Behbakht K Thorburn A Ford H L 2013 03 14 On the TRAIL to successful cancer therapy Predicting and counteracting resistance against TRAIL based therapeutics Oncogene 32 11 1341 1350 doi 10 1038 onc 2012 164 ISSN 1476 5594 PMC 4502956 PMID 22580613 nbsp This protein related article is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title AP5M1 amp oldid 1187738051, wikipedia, wiki, book, books, library,

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