Q60953 (PML_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified May 29, 2013. Version 129. History...
Names and origin
|Protein names||Recommended name:|
|Organism||Mus musculus (Mouse) [Reference proteome]|
|Taxonomic identifier||10090 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus|
|Sequence length||885 AA.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
Functions via its association with PML-nuclear bodies (PML-NBs) in a wide range of important cellular processes, including tumor suppression, transcriptional regulation, apoptosis, senescence, DNA damage response, and viral defense mechanisms. Acts as the scaffold of PML-NBs allowing other proteins to shuttle in and out, a process which is regulated by SUMO-mediated modifications and interactions. Positively regulates p53/TP53 by acting at different levels (by promoting its acetylation and phosphorylation and by inhibiting its MDM2-dependent degradation). Regulates phosphorylation of ITPR3 and plays a role in the regulation of calcium homeostasis at the endoplasmic reticulum. Regulates RB1 phosphorylation and activity. Acts as both a negative regulator of PPARGC1A acetylation and a potent activator of PPAR signaling and fatty acid oxidation. Regulates translation of HIF1A by sequestering MTOR, and thereby plays a role in neoangiogenesis and tumor vascularization. Regulates PER2 nuclear localization and circadian function. Cytoplasmic PML is involved in the regulation of the TGF-beta signaling pathway. Required for normal development of the brain cortex during embryogenesis. Plays a role in granulopoiesis or monopoiesis of myeloid progenitor cells. May play a role regulating stem and progenitor cell fate in tissues as diverse as blood, brain and breast. Shows antiviral activity towards lymphocytic choriomeningitis virus (LCMV) and the vesicular stomatitis virus (VSV). Ref.5 Ref.6 Ref.7 Ref.9 Ref.10 Ref.12 Ref.14 Ref.15 Ref.16 Ref.22 Ref.23 Ref.24 Ref.25 Ref.27 Ref.28 Ref.29
Key component of PML bodies. PML bodies are formed by the interaction of PML homodimers (via SUMO-binding motif) with sumoylated PML, leading to the assembly of higher oligomers. Several types of PML bodies have been observed. PML bodies can form hollow spheres that can sequester target proteins inside. Interacts (via SUMO-binding motif) with sumoylated proteins. Interacts (via C-terminus) with p53/TP53. Recruits p53/TP53 and CHEK2 into PML bodies, which promotes p53/TP53 phosphorylation at 'Ser-20' and prevents its proteasomal degradation. Interacts with MDM2, and sequesters MDM2 in the nucleolus, thereby preventing ubiquitination of p53/TP53. Interaction with PML-RARA oncoprotein and certain viral proteins causes disassembly of PML bodies and abolishes the normal PML function. Interacts with TERT, SIRT1, TOPBP1, TRIM27 and TRIM69. Interacts with ELF4 (via C-terminus). Interacts with Lassa virus Z protein and rabies virus phosphoprotein. Interacts (in the cytoplasm) with TGFBR1, TGFBR2 and PKM. Interacts (via the coiled-coil domain and when sumoylated) with SATB1. Interacts with UBE2I; the interaction is enhanced by arsenic binding. Interacts with SMAD2, SMAD3, DAXX, RPL11, HIPK2 and MTOR By similarity. Interacts with ITPR3, PPP1A and RB1. Interacts with RNF4, NLRP3, MAGEA2, RBL2, PER2, E2F4 and MAPK7/BMK1. Interacts with CSNK2A1 and CSNK2A3 By similarity. Interacts with PPARGC1A AND KAT2A. Ref.8 Ref.11 Ref.13 Ref.14 Ref.16 Ref.22 Ref.23 Ref.29
Nucleus By similarity. Nucleus › nucleoplasm. Cytoplasm. Nucleus › PML body. Nucleus › nucleolus By similarity. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Early endosome membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: Detected in the nucleolus after DNA damage. Acetylation at Lys-497 is essential for its nuclear localization. Within the nucleus, most of PML is expressed in the diffuse nuclear fraction of the nucleoplasm and only a small fraction is found in the matrix-associated nuclear bodies (PML-NBs). The transfer of PML from the nucleoplasm to PML-NBs depends on its phosphorylation and sumoylation. The B1 box and the RING finger are also required for the localization in PML-NBs. Also found in specific membrane structures termed mitochondria-associated membranes (MAMs) which connect the endoplasmic reticulum (ER) and the mitochondria By similarity. Ref.8 Ref.14 Ref.23 Ref.27 Ref.29
The coiled-coil domain mediates a strong homo/multidimerization activity essential for core assembly of PML-NBs By similarity.
Binds arsenic via the RING-type zinc finger By similarity.
The Sumo interaction motif (SIM) is required for efficient ubiquitination, recruitment of proteasome components within PML-NBs and PML degradation in response to arsenic trioxide By similarity.
Ubiquitinated; mediated by RNF4, UHRF1, UBE3A/E6AP, KLHL20-based E3 ligase complex, SIAH1 or SIAH2 and leading to subsequent proteasomal degradation. Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4 is polysumoylation-dependent. Ubiquitination by KLHL20-based E3 ligase complex requires CDK1/2-mediated phosphorylation at Ser-528 which in turn is recognized by prolyl-isopeptidase PIN1 and PIN1-catalyzed isomerization further potentiates PML interaction with KLHL20 By similarity. Ref.13
Sumoylation regulates PML's: stability in response to extracellular or intracellular stimuli, transcription directly and indirectly, through sequestration of or dissociation of the transcription factors from PML-NBs, ability to regulate apoptosis and its anti-viral activities. It is also essential for: maintaining proper PML nuclear bodies (PML-NBs) structure and normal function, recruitment of components of PML-NBs, the turnover and retention of PML in PML-NBs and the integrity of PML-NBs. Undergoes 'Lys-11'-linked sumoylation. Sumoylation on all three sites (Lys-70, Lys-165 and Lys-500) is required for nuclear body formation. Sumoylation on Lys-165 is a prerequisite for sumoylation on Lys-70. Lys-70 and Lys-165 are sumoylated by PISA1 and PIAS2. PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 and phosphorylation at Ser-575 which in turn triggers its ubiquitin-mediated degradation. Sumoylation at Lys-500 by RANBP2 is essential for the proper assembly of PML-NBs. Desumoylated by SENP1, SENP2, SENP3, SENP5 and SENP6 By similarity. Ref.8
Phosphorylation is a major regulatory mechanism that controls PML protein abundance and the number and size of PML nuclear bodies (PML-NBs). Phosphorylated in response to DNA damage, probably by ATR. HIPK2-mediated phosphorylation at Ser-17, Ser-45 and Ser-47 leads to increased accumulation of PML protein and its sumoylation and is required for the maximal pro-apoptotic activity of PML after DNA damage. MAPK1- mediated phosphorylations at Ser-404, Ser-515 and Ser-540 and CDK1/2-mediated phosphorylation at Ser-528 promote PIN1-dependent PML degradation. CK2-mediated phosphorylation at Ser-575 primes PML ubiquitination via an unidentified ubiquitin ligase By similarity.
Acetylation at Lys-497 is essential for its nuclear localization. Deacetylated at Lys-497 by SIRT1 and this deacetylation promotes PML control of PER2 nuclear localization By similarity.
Mice are born at the expected Mendelian rate and are fertile. They show leukopenia with reduced levels of circulating granulocytes and myeloid cells. They are highly susceptible to infections, causing a reduced life span. Mice do not exhibit normal apoptosis of hematopoietic stem cells after DNA damage due to irradiation. They do not exhibit normal apoptosis in response to FAS, TNF, TGFB1, interferons and ceramide, and show impaired activation of caspases in response to pro-apoptotic stimuli. Mice are highly susceptible to chemical carcinogens. Mice display accelerated revascularization after ischemia. Newborns have smaller brains with a reduced size of the brain cortex. Cultured embryonic fibroblasts show impaired growth inhibition by retinoic acid, and are defective in the activation of CDKN1A in response to retinoic acid. Mice display aberrant learning and memory, lower levels of anxiety-like behavior and specific deficits in long-term plasticity. Ref.5 Ref.6 Ref.10 Ref.16 Ref.22 Ref.28
Contains 2 B box-type zinc fingers.
Contains 1 RING-type zinc finger.
The sequence AAA97601.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
|This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]|
|Isoform 1 (identifier: Q60953-1) |
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
|Isoform 2 (identifier: Q60953-2) |
The sequence of this isoform differs from the canonical sequence as follows:
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 885||885||Protein PML||PRO_0000056002|
|Zinc finger||62 – 97||36||RING-type|
|Zinc finger||129 – 171||43||B box-type 1|
|Zinc finger||188 – 239||52||B box-type 2|
|Region||458 – 565||108||Interaction with PER2 By similarity|
|Region||486 – 500||15||Nuclear localization signal By similarity|
|Region||566 – 572||7||Sumo interaction motif (SIM) By similarity|
|Coiled coil||295 – 331||37||Potential|
|Compositional bias||12 – 38||27||Pro-rich|
|Metal binding||62||1||Zinc 1 By similarity|
|Metal binding||65||1||Zinc 1 By similarity|
|Metal binding||77||1||Zinc 2 By similarity|
|Metal binding||79||1||Zinc 2 By similarity|
|Metal binding||82||1||Zinc 1 By similarity|
|Metal binding||85||1||Zinc 1 By similarity|
|Metal binding||93||1||Zinc 2 By similarity|
|Metal binding||96||1||Zinc 2 By similarity|
Amino acid modifications
|Modified residue||17||1||Phosphoserine; by HIPK2 Ref.18|
|Modified residue||45||1||Phosphoserine; by HIPK2 and MAPK1 By similarity|
|Modified residue||47||1||Phosphoserine; by HIPK2 and MAPK1 By similarity|
|Modified residue||404||1||Phosphoserine; by MAPK1 and MAPK7 By similarity|
|Modified residue||497||1||N6-acetyllysine By similarity|
|Modified residue||514||1||Phosphoserine Ref.17|
|Modified residue||515||1||Phosphoserine; by MAPK1 Ref.17|
|Modified residue||525||1||N6-acetyllysine By similarity|
|Modified residue||527||1||Phosphothreonine Ref.17|
|Modified residue||528||1||Phosphoserine; by CDK1 and CDK2 Ref.17 Ref.21|
|Modified residue||540||1||Phosphoserine; by MAPK1 By similarity|
|Modified residue||556||1||Phosphothreonine Ref.17|
|Modified residue||575||1||Phosphoserine; by CK2 By similarity|
|Modified residue||609||1||Phosphoserine Ref.19|
|Cross-link||70||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity|
|Cross-link||165||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity|
|Cross-link||384||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity|
|Cross-link||486||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity|
|Cross-link||500||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity|
|Alternative sequence||431 – 476||46||Missing in isoform 2.||VSP_026028|
|Sequence conflict||210||1||G → V in BAC25716. Ref.1|
|Sequence conflict||414||1||A → V in BAC25716. Ref.1|
|Sequence conflict||424||1||T → S in BAC25716. Ref.1|
|Sequence conflict||429||1||E → V in AAH20990. Ref.2|
|||"The transcriptional landscape of the mammalian genome."|
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
|||"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."|
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Salivary gland.
|||"Cloning of the murine homolog of the leukemia-associated PML gene."|
Goddard A.D., Yuan J.Q., Fairbairn L., Dexter M., Borrow J., Kozak C., Solomon E.
Mamm. Genome 6:732-737(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-839 (ISOFORM 2).
|||Goddard A.D., Howe K., Solomon E.|
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 130; 212; 284; 638; 731; 750; 770-772; 820 AND 839.
|||"PML is essential for multiple apoptotic pathways."|
Wang Z.G., Ruggero D., Ronchetti S., Zhong S., Gaboli M., Rivi R., Pandolfi P.P.
Nat. Genet. 20:266-272(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
|||"Role of PML in cell growth and the retinoic acid pathway."|
Wang Z.G., Delva L., Gaboli M., Rivi R., Giorgio M., Cordon-Cardo C., Grosveld F., Pandolfi P.P.
Science 279:1547-1551(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
|||"A role for PML and the nuclear body in genomic stability."|
Zhong S., Hu P., Ye T.Z., Stan R., Ellis N.A., Pandolfi P.P.
Oncogene 18:7941-7947(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
|||"Role of SUMO-1-modified PML in nuclear body formation."|
Zhong S., Muller S., Ronchetti S., Freemont P.S., Dejean A., Pandolfi P.P.
Blood 95:2748-2752(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION, SUBCELLULAR LOCATION, SUBUNIT.
|||"Effects of promyelocytic leukemia protein on virus-host balance."|
Bonilla W.V., Pinschewer D.D., Klenerman P., Rousson V., Gaboli M., Pandolfi P.P., Zinkernagel R.M., Salvato M.S., Hengartner H.
J. Virol. 76:3810-3818(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN LCMV AND VSV RESTRICTION.
|||"Rabies virus P and small P products interact directly with PML and reorganize PML nuclear bodies."|
Blondel D., Regad T., Poisson N., Pavie B., Harper F., Pandolfi P.P., De The H., Chelbi-Alix M.K.
Oncogene 21:7957-7970(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
|||"Forced expression of RNF36 induces cell apoptosis."|
Shyu H.-W., Hsu S.-H., Hsieh-Li H.-M., Li H.
Exp. Cell Res. 287:301-313(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRIM69.
|||"Impairment of p53 acetylation, stability and function by an oncogenic transcription factor."|
Insinga A., Monestiroli S., Ronzoni S., Carbone R., Pearson M., Pruneri G., Viale G., Appella E., Pelicci P., Minucci S.
EMBO J. 23:1144-1154(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
|||"The coiled-coil domain is the structural determinant for mammalian homologues of Drosophila Sina-mediated degradation of promyelocytic leukemia protein and other tripartite motif proteins by the proteasome."|
Fanelli M., Fantozzi A., De Luca P., Caprodossi S., Matsuzawa S., Lazar M.A., Pelicci P.G., Minucci S.
J. Biol. Chem. 279:5374-5379(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SIAH2, DEGRADATION.
|||"PML regulates p53 stability by sequestering Mdm2 to the nucleolus."|
Bernardi R., Scaglioni P.P., Bergmann S., Horn H.F., Vousden K.H., Pandolfi P.P.
Nat. Cell Biol. 6:665-672(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MDM2 AND RPL11, SUBCELLULAR LOCATION.
|||"Cytoplasmic PML function in TGF-beta signalling."|
Lin H.K., Bergmann S., Pandolfi P.P.
Nature 431:205-211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
|||"PML inhibits HIF-1alpha translation and neoangiogenesis through repression of mTOR."|
Bernardi R., Guernah I., Jin D., Grisendi S., Alimonti A., Teruya-Feldstein J., Cordon-Cardo C., Simon M.C., Rafii S., Pandolfi P.P.
Nature 442:779-785(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION, INTERACTION WITH MTOR.
|||"Large-scale phosphorylation analysis of mouse liver."|
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-514; SER-515; THR-527; SER-528 AND THR-556, MASS SPECTROMETRY.
|||"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."|
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, MASS SPECTROMETRY.
|||"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."|
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-609, MASS SPECTROMETRY.
|||"PML: a tumor suppressor that regulates cell fate in mammary gland."|
Li W., Rich T., Watson C.J.
Cell Cycle 8:2711-2717(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
|||"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."|
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528, MASS SPECTROMETRY.
Tissue: Embryonic fibroblast.
|||"The tumor suppressor Pml regulates cell fate in the developing neocortex."|
Regad T., Bellodi C., Nicotera P., Salomoni P.
Nat. Neurosci. 12:132-140(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, INTERACTION WITH RB1, FUNCTION.
|||"PML regulates apoptosis at endoplasmic reticulum by modulating calcium release."|
Giorgi C., Ito K., Lin H.K., Santangelo C., Wieckowski M.R., Lebiedzinska M., Bononi A., Bonora M., Duszynski J., Bernardi R., Rizzuto R., Tacchetti C., Pinton P., Pandolfi P.P.
Science 330:1247-1251(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ITPR3, SUBCELLULAR LOCATION.
|||"A role for PML in innate immunity."|
Lunardi A., Gaboli M., Giorgio M., Rivi R., Bygrave A., Antoniou M., Drabek D., Dzierzak E., Fagioli M., Salmena L., Botto M., Cordon-Cardo C., Luzzatto L., Pelicci P.G., Grosveld F., Pandolfi P.P.
Genes Cancer 2:10-19(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
|||"PML is a key component for the differentiation of myeloid progenitor cells to macrophages."|
Khalfin-Rabinovich Y., Weinstein A., Levi B.Z.
Int. Immunol. 23:287-296(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
|||"The role of PML in the nervous system."|
Salomoni P., Betts-Henderson J.
Mol. Neurobiol. 43:114-123(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
|||"PML regulates PER2 nuclear localization and circadian function."|
Miki T., Xu Z., Chen-Goodspeed M., Liu M., Van Oort-Jansen A., Rea M.A., Zhao Z., Lee C.C., Chang K.S.
EMBO J. 31:1427-1439(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
|||"Impaired cognitive function and reduced anxiety-related behavior in a promyelocytic leukemia (PML) tumor suppressor protein-deficient mouse."|
Butler K., Martinez L.A., Tejada-Simon M.V.
Genes Brain Behav. 0:0-0(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
|||"A metabolic prosurvival role for PML in breast cancer."|
Carracedo A., Weiss D., Leliaert A.K., Bhasin M., de Boer V.C., Laurent G., Adams A.C., Sundvall M., Song S.J., Ito K., Finley L.S., Egia A., Libermann T., Gerhart-Hines Z., Puigserver P., Haigis M.C., Maratos-Flier E., Richardson A.L., Schafer Z.T., Pandolfi P.P.
J. Clin. Invest. 122:3088-3100(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PPARGC1A AND KAT2A.
|+||Additional computationally mapped references.|
|AK028044 mRNA. Translation: BAC25716.1.|
BC020990 mRNA. Translation: AAH20990.2.
U33626 mRNA. Translation: AAA97601.2. Different initiation.
|RefSeq||NP_032910.3. NM_008884.5. |
3D structure databases
|SMR||Q60953. Positions 54-109. |
Protein-protein interaction databases
|IntAct||Q60953. 8 interactions.|
Protocols and materials databases
Genome annotation databases
|Ensembl||ENSMUST00000085673; ENSMUSP00000082816; ENSMUSG00000036986. |
ENSMUST00000114136; ENSMUSP00000109771; ENSMUSG00000036986.
|UCSC||uc009pwp.2. mouse. |
|MGI||MGI:104662. Pml. |
Gene expression databases
|GermOnline||ENSMUSG00000036986. Mus musculus. |
Family and domain databases
|Gene3D||126.96.36.199. 1 hit. |
|InterPro||IPR021978. DUF3583. |
|Pfam||PF12126. DUF3583. 1 hit. |
PF00643. zf-B_box. 1 hit.
|SMART||SM00336. BBOX. 1 hit. |
SM00184. RING. 1 hit.
|PROSITE||PS50119. ZF_BBOX. 2 hits. |
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
|ChiTaRS||PML. mouse. |
|Accession||Primary (citable) accession number: Q60953|
Secondary accession number(s): Q8CEJ1, Q8VCC4
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|