MGI:Pml

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Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes
	GO:0001666	response to hypoxia	MGI:MGI:3654795 PMID:16915281^[1]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2429949	P	From MGI
	GO:0001666	response to hypoxia	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	P	From MGI
	GO:0001932	regulation of protein phosphorylation	MGI:MGI:4849347 PMID:21030605^[2]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0002230	positive regulation of defense response to virus by host	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	P	From MGI
	GO:0003677	DNA binding	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0238	F	From MGI
	GO:0003713	transcription coactivator activity	MGI:MGI:3580934 PMID:15626733^[3]	TAS: Traceable Author Statement		F	From MGI
	GO:0003713	transcription coactivator activity	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	F	From MGI
	GO:0005515	protein binding	MGI:MGI:2449749 PMID:12529400^[4]	IPI: Inferred from Physical Interaction	RefSeq:NP_110467	F	From MGI
	GO:0005515	protein binding	MGI:MGI:3054278 PMID:15356634^[5]	IPI: Inferred from Physical Interaction	RefSeq:NP_899123	F	From MGI
	GO:0005515	protein binding	MGI:MGI:3579722 PMID:15925207^[6]	IPI: Inferred from Physical Interaction	RefSeq:NP_110467	F	From MGI
	GO:0005515	protein binding	MGI:MGI:3654795 PMID:16915281^[1]	IPI: Inferred from Physical Interaction	RefSeq:NP_110467	F	From MGI
	GO:0005515	protein binding	MGI:MGI:4849347 PMID:21030605^[2]	IPI: Inferred from Physical Interaction	UniProtKB:P70227	F	From MGI
	GO:0005515	protein binding	MGI:MGI:5315336 PMID:21057547^[7]	IPI: Inferred from Physical Interaction	UniProtKB:Q14DJ8	F	From MGI
	GO:0005622	intracellular	MGI:MGI:2152098	IEA: Inferred from Electronic Annotation	InterPro:IPR000315	C	From MGI
	GO:0005626	insoluble fraction	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	C	From MGI
	GO:0005634	nucleus	MGI:MGI:1891512 PMID:10716735^[8]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0005634	nucleus	MGI:MGI:4357758 PMID:19416967^[9]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0005634	nucleus	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	C	From MGI
	GO:0005634	nucleus	MGI:MGI:4849347 PMID:21030605^[2]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0005654	nucleoplasm	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	C	From MGI
	GO:0005730	nucleolus	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	C	From MGI
	GO:0005737	cytoplasm	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	C	From MGI
	GO:0005768	endosome	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0967	C	From MGI
	GO:0005783	endoplasmic reticulum	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0256	C	From MGI
	GO:0005829	cytosol	MGI:MGI:4849347 PMID:21030605^[2]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0006351	transcription, DNA-dependent	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0804	P	From MGI
	GO:0006355	regulation of transcription, DNA-dependent	MGI:MGI:1314996 PMID:9845074^[10]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0006461	protein complex assembly	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	P	From MGI
	GO:0006605	protein targeting	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	P	From MGI
	GO:0006915	apoptotic process	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0053	P	From MGI
	GO:0006917	induction of apoptosis	MGI:MGI:1306978 PMID:9806545^[11]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2429949	P	From MGI
	GO:0006917	induction of apoptosis	MGI:MGI:3034149 PMID:14992722^[12]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0006917	induction of apoptosis	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	P	From MGI
	GO:0006917	induction of apoptosis	MGI:MGI:4849347 PMID:21030605^[2]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0006917	induction of apoptosis	MGI:MGI:4942266 PMID:10684855^[13]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0006919	activation of cysteine-type endopeptidase activity involved in apoptotic process	MGI:MGI:1306978 PMID:9806545^[11]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2429949	P	From MGI
	GO:0006977	DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest	MGI:MGI:3580934 PMID:15626733^[3]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0007050	cell cycle arrest	MGI:MGI:3717518 PMID:10910364^[14]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0007050	cell cycle arrest	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	P	From MGI
	GO:0007179	transforming growth factor beta receptor signaling pathway	MGI:MGI:3054278 PMID:15356634^[5]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2429949	P	From MGI
	GO:0007182	common-partner SMAD protein phosphorylation	MGI:MGI:3054278 PMID:15356634^[5]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2429949	P	From MGI
	GO:0007184	SMAD protein import into nucleus	MGI:MGI:3054278 PMID:15356634^[5]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2429949	P	From MGI
	GO:0007569	cell aging	MGI:MGI:3717518 PMID:10910364^[14]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0008270	zinc ion binding	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	F	From MGI
	GO:0008285	negative regulation of cell proliferation	MGI:MGI:1197798 PMID:9488655^[15]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2429949	P	From MGI
	GO:0008285	negative regulation of cell proliferation	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	P	From MGI
	GO:0008630	DNA damage response, signal transduction resulting in induction of apoptosis	MGI:MGI:1306978 PMID:9806545^[11]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2429949	P	From MGI
	GO:0008630	DNA damage response, signal transduction resulting in induction of apoptosis	MGI:MGI:3580934 PMID:15626733^[3]	IMP: Inferred from Mutant Phenotype	MGI:MGI:104662	P	From MGI
	GO:0008630	DNA damage response, signal transduction resulting in induction of apoptosis	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	P	From MGI
	GO:0009411	response to UV	MGI:MGI:3580934 PMID:15626733^[3]	IMP: Inferred from Mutant Phenotype	MGI:MGI:104662	P	From MGI
	GO:0009615	response to virus	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0051	P	From MGI
	GO:0010332	response to gamma radiation	MGI:MGI:1306978 PMID:9806545^[11]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2429949	P	From MGI
	GO:0010332	response to gamma radiation	MGI:MGI:3701394 PMID:11025664^[16]	IMP: Inferred from Mutant Phenotype	MGI:MGI:104662	P	From MGI
	GO:0010522	regulation of calcium ion transport into cytosol	MGI:MGI:4849347 PMID:21030605^[2]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0016020	membrane	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0472	C	From MGI
	GO:0016363	nuclear matrix	MGI:MGI:3051070 PMID:15252119^[17]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0016363	nuclear matrix	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	C	From MGI
	GO:0016525	negative regulation of angiogenesis	MGI:MGI:3654795 PMID:16915281^[1]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2429949	P	From MGI
	GO:0016525	negative regulation of angiogenesis	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	P	From MGI
	GO:0016605	PML body	MGI:MGI:3616374 PMID:16461359^[18]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0016605	PML body	MGI:MGI:3717519 PMID:10779416^[19]	IMP: Inferred from Mutant Phenotype		C	From MGI
	GO:0016605	PML body	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	C	From MGI
	GO:0030099	myeloid cell differentiation	MGI:MGI:1197798 PMID:9488655^[15]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2429949	P	From MGI
	GO:0030308	negative regulation of cell growth	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	P	From MGI
	GO:0030578	PML body organization	MGI:MGI:2449749 PMID:12529400^[4]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0030578	PML body organization	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	P	From MGI
	GO:0031065	positive regulation of histone deacetylation	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	P	From MGI
	GO:0031625	ubiquitin protein ligase binding	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	F	From MGI
	GO:0031965	nuclear membrane	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	C	From MGI
	GO:0032183	SUMO binding	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	F	From MGI
	GO:0032211	negative regulation of telomere maintenance via telomerase	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	P	From MGI
	GO:0032469	endoplasmic reticulum calcium ion homeostasis	MGI:MGI:4849347 PMID:21030605^[2]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0032938	negative regulation of translation in response to oxidative stress	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	P	From MGI
	GO:0034097	response to cytokine stimulus	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	P	From MGI
	GO:0042406	extrinsic to endoplasmic reticulum membrane	MGI:MGI:4849347 PMID:21030605^[2]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0042771	DNA damage response, signal transduction by p53 class mediator resulting in induction of apoptosis	MGI:MGI:3580934 PMID:15626733^[3]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0042803	protein homodimerization activity	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	F	From MGI
	GO:0044419	interspecies interaction between organisms	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0945	P	From MGI
	GO:0045165	cell fate commitment	MGI:MGI:3839212 PMID:19261859^[20]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2429949	P	From MGI
	GO:0045343	regulation of MHC class I biosynthetic process	MGI:MGI:1314996 PMID:9845074^[10]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0045892	negative regulation of transcription, DNA-dependent	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	P	From MGI
	GO:0045930	negative regulation of mitotic cell cycle	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	P	From MGI
	GO:0046332	SMAD binding	MGI:MGI:3054278 PMID:15356634^[5]	IDA: Inferred from Direct Assay		F	From MGI
	GO:0046872	metal ion binding	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0479	F	From MGI
	GO:0046982	protein heterodimerization activity	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	F	From MGI
	GO:0048384	retinoic acid receptor signaling pathway	MGI:MGI:1197798 PMID:9488655^[15]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2429949	P	From MGI
	GO:0050821	protein stabilization	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	P	From MGI
	GO:0050897	cobalt ion binding	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	F	From MGI
	GO:0051457	maintenance of protein location in nucleus	MGI:MGI:3763815 PMID:17332504^[21]	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	P	From MGI
	GO:0051974	negative regulation of telomerase activity	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	P	From MGI
	GO:0060444	branching involved in mammary gland duct morphogenesis	MGI:MGI:3839212 PMID:19261859^[20]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2429949	P	From MGI
	GO:2000059	negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	P	From MGI
	GO:2001141	regulation of RNA biosynthetic process	MGI:MGI:3580934 PMID:15626733^[3]	TAS: Traceable Author Statement		P	From MGI
	GO:2001238	positive regulation of extrinsic apoptotic signaling pathway	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P29590	P	From MGI
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 Bernardi R et al. (2006) PML inhibits HIF-1alpha translation and neoangiogenesis through repression of mTOR. Nature 442: 779-85 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 ^2.6 ^2.7 Giorgi C et al. (2010) PML regulates apoptosis at endoplasmic reticulum by modulating calcium release. Science 330: 1247-51 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 Salomoni P et al. (2005) The promyelocytic leukemia protein PML regulates c-Jun function in response to DNA damage. Blood 105: 3686-90 PubMed GONUTS page
↑ ^4.0 ^4.1 Ecsedy JA et al. (2003) Homeodomain-interacting protein kinase 1 modulates Daxx localization, phosphorylation, and transcriptional activity. Mol Cell Biol 23: 950-60 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 ^5.4 Lin HK et al. (2004) Cytoplasmic PML function in TGF-beta signalling. Nature 431: 205-11 PubMed GONUTS page
↑ Nagy I et al. (2005) Promyelocytic leukemia zinc finger protein localizes to the cochlear outer hair cells and interacts with prestin, the outer hair cell motor protein. Hear Res 204: 216-22 PubMed GONUTS page
↑ Li Q et al. (2011) AXIN is an essential co-activator for the promyelocytic leukemia protein in p53 activation. Oncogene 30: 1194-204 PubMed GONUTS page
↑ Misawa K et al. (2000) A method to identify cDNAs based on localization of green fluorescent protein fusion products. Proc Natl Acad Sci U S A 97: 3062-6 PubMed GONUTS page
↑ Cho G et al. (2009) SUMO interaction motifs in Sizn1 are required for promyelocytic leukemia protein nuclear body localization and for transcriptional activation. J Biol Chem 284: 19592-600 PubMed GONUTS page
↑ ^10.0 ^10.1 Zheng P et al. (1998) Proto-oncogene PML controls genes devoted to MHC class I antigen presentation. Nature 396: 373-6 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 ^11.3 Wang ZG et al. (1998) PML is essential for multiple apoptotic pathways. Nat Genet 20: 266-72 PubMed GONUTS page
↑ de Stanchina E et al. (2004) PML is a direct p53 target that modulates p53 effector functions. Mol Cell 13: 523-35 PubMed GONUTS page
↑ Zhong S et al. (2000) Promyelocytic leukemia protein (PML) and Daxx participate in a novel nuclear pathway for apoptosis. J Exp Med 191: 631-40 PubMed GONUTS page
↑ ^14.0 ^14.1 Pearson M et al. (2000) PML regulates p53 acetylation and premature senescence induced by oncogenic Ras. Nature 406: 207-10 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 Wang ZG et al. (1998) Role of PML in cell growth and the retinoic acid pathway. Science 279: 1547-51 PubMed GONUTS page
↑ Guo A et al. (2000) The function of PML in p53-dependent apoptosis. Nat Cell Biol 2: 730-6 PubMed GONUTS page
↑ Ishov AM et al. (2004) Heterochromatin and ND10 are cell-cycle regulated and phosphorylation-dependent alternate nuclear sites of the transcription repressor Daxx and SWI/SNF protein ATRX. J Cell Sci 117: 3807-20 PubMed GONUTS page
↑ Qin Q et al. (2006) A novel GTPase, CRAG, mediates promyelocytic leukemia protein-associated nuclear body formation and degradation of expanded polyglutamine protein. J Cell Biol 172: 497-504 PubMed GONUTS page
↑ Zhong S et al. (2000) Role of SUMO-1-modified PML in nuclear body formation. Blood 95: 2748-52 PubMed GONUTS page
↑ ^20.0 ^20.1 Li W et al. (2009) PML depletion disrupts normal mammary gland development and skews the composition of the mammary luminal cell progenitor pool. Proc Natl Acad Sci U S A 106: 4725-30 PubMed GONUTS page
↑ Takahashi K et al. (2007) Dynamic regulation of p53 subnuclear localization and senescence by MORC3. Mol Biol Cell 18: 1701-9 PubMed GONUTS page

[PMID:16915281-0] 1.0 ^1.1 ^1.2 Bernardi R et al. (2006) PML inhibits HIF-1alpha translation and neoangiogenesis through repression of mTOR. Nature 442: 779-85 PubMed GONUTS page

[PMID:21030605-1] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 ^2.6 ^2.7 Giorgi C et al. (2010) PML regulates apoptosis at endoplasmic reticulum by modulating calcium release. Science 330: 1247-51 PubMed GONUTS page

[PMID:15626733-2] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 Salomoni P et al. (2005) The promyelocytic leukemia protein PML regulates c-Jun function in response to DNA damage. Blood 105: 3686-90 PubMed GONUTS page

[PMID:12529400-3] 4.0 ^4.1 Ecsedy JA et al. (2003) Homeodomain-interacting protein kinase 1 modulates Daxx localization, phosphorylation, and transcriptional activity. Mol Cell Biol 23: 950-60 PubMed GONUTS page

[PMID:15356634-4] 5.0 ^5.1 ^5.2 ^5.3 ^5.4 Lin HK et al. (2004) Cytoplasmic PML function in TGF-beta signalling. Nature 431: 205-11 PubMed GONUTS page

[PMID:15925207-5] Nagy I et al. (2005) Promyelocytic leukemia zinc finger protein localizes to the cochlear outer hair cells and interacts with prestin, the outer hair cell motor protein. Hear Res 204: 216-22 PubMed GONUTS page

[PMID:21057547-6] Li Q et al. (2011) AXIN is an essential co-activator for the promyelocytic leukemia protein in p53 activation. Oncogene 30: 1194-204 PubMed GONUTS page

[PMID:10716735-7] Misawa K et al. (2000) A method to identify cDNAs based on localization of green fluorescent protein fusion products. Proc Natl Acad Sci U S A 97: 3062-6 PubMed GONUTS page

[PMID:19416967-8] Cho G et al. (2009) SUMO interaction motifs in Sizn1 are required for promyelocytic leukemia protein nuclear body localization and for transcriptional activation. J Biol Chem 284: 19592-600 PubMed GONUTS page

[PMID:9845074-9] 10.0 ^10.1 Zheng P et al. (1998) Proto-oncogene PML controls genes devoted to MHC class I antigen presentation. Nature 396: 373-6 PubMed GONUTS page

[PMID:9806545-10] 11.0 ^11.1 ^11.2 ^11.3 Wang ZG et al. (1998) PML is essential for multiple apoptotic pathways. Nat Genet 20: 266-72 PubMed GONUTS page

[PMID:14992722-11] Stanchina E et al. (2004) PML is a direct p53 target that modulates p53 effector functions. Mol Cell 13: 523-35 PubMed GONUTS page

[PMID:10684855-12] Zhong S et al. (2000) Promyelocytic leukemia protein (PML) and Daxx participate in a novel nuclear pathway for apoptosis. J Exp Med 191: 631-40 PubMed GONUTS page

[PMID:10910364-13] 14.0 ^14.1 Pearson M et al. (2000) PML regulates p53 acetylation and premature senescence induced by oncogenic Ras. Nature 406: 207-10 PubMed GONUTS page

[PMID:9488655-14] 15.0 ^15.1 ^15.2 Wang ZG et al. (1998) Role of PML in cell growth and the retinoic acid pathway. Science 279: 1547-51 PubMed GONUTS page

[PMID:11025664-15] Guo A et al. (2000) The function of PML in p53-dependent apoptosis. Nat Cell Biol 2: 730-6 PubMed GONUTS page

[PMID:15252119-16] Ishov AM et al. (2004) Heterochromatin and ND10 are cell-cycle regulated and phosphorylation-dependent alternate nuclear sites of the transcription repressor Daxx and SWI/SNF protein ATRX. J Cell Sci 117: 3807-20 PubMed GONUTS page

[PMID:16461359-17] Qin Q et al. (2006) A novel GTPase, CRAG, mediates promyelocytic leukemia protein-associated nuclear body formation and degradation of expanded polyglutamine protein. J Cell Biol 172: 497-504 PubMed GONUTS page

[PMID:10779416-18] Zhong S et al. (2000) Role of SUMO-1-modified PML in nuclear body formation. Blood 95: 2748-52 PubMed GONUTS page

[PMID:19261859-19] 20.0 ^20.1 Li W et al. (2009) PML depletion disrupts normal mammary gland development and skews the composition of the mammary luminal cell progenitor pool. Proc Natl Acad Sci U S A 106: 4725-30 PubMed GONUTS page

[PMID:17332504-20] Takahashi K et al. (2007) Dynamic regulation of p53 subnuclear localization and senescence by MORC3. Mol Biol Cell 18: 1701-9 PubMed GONUTS page

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Species (Taxon ID)	Mus musculus (house mouse) (taxon:10090)
Gene Name(s)	Pml ( synonyms: Trim19 )
Protein Name(s)	promyelocytic leukemia,
External Links
MGI	MGI:104662

MGI:Pml

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