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Protein

Protein PML

Gene

Pml

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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).16 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi62Zinc 1By similarity1
Metal bindingi65Zinc 1By similarity1
Metal bindingi77Zinc 2By similarity1
Metal bindingi79Zinc 2By similarity1
Metal bindingi82Zinc 1By similarity1
Metal bindingi85Zinc 1By similarity1
Metal bindingi93Zinc 2By similarity1
Metal bindingi96Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri62 – 97RING-typePROSITE-ProRule annotationAdd BLAST36
Zinc fingeri129 – 171B box-type 1PROSITE-ProRule annotationAdd BLAST43
Zinc fingeri188 – 239B box-type 2PROSITE-ProRule annotationAdd BLAST52

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActivator, DNA-binding
Biological processAntiviral defense, Apoptosis, Biological rhythms, Host-virus interaction, Immunity, Innate immunity, Transcription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-3108214 SUMOylation of DNA damage response and repair proteins
R-MMU-3232142 SUMOylation of ubiquitinylation proteins
R-MMU-6804758 Regulation of TP53 Activity through Acetylation
R-MMU-8934593 Regulation of RUNX1 Expression and Activity
R-MMU-8948747 Regulation of PTEN localization

Names & Taxonomyi

Protein namesi
Recommended name:
Protein PML
Gene namesi
Name:Pml
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:104662 Pml

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Endosome, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

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. Mice display aberrant learning and memory, lower levels of anxiety-like behavior and specific deficits in long-term plasticity. Mice display a compromised endogenous ciracadian clock with reduced precision and stability of the period length.7 Publications

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000560021 – 885Protein PMLAdd BLAST885

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei17Phosphoserine; by HIPK2Combined sources1
Modified residuei45Phosphoserine; by HIPK2 and MAPK1By similarity1
Modified residuei47Phosphoserine; by HIPK2 and MAPK1By similarity1
Cross-linki70Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki70Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki165Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki165Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki384Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki384Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei404PhosphoserineCombined sources1
Cross-linki486Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki486Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Cross-linki488Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei497N6-acetyllysine; alternateBy similarity1
Cross-linki497Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki500Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki500Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei503PhosphoserineCombined sources1
Modified residuei514PhosphoserineCombined sources1
Modified residuei515Phosphoserine; by MAPK1Combined sources1
Modified residuei522PhosphoserineBy similarity1
Modified residuei525N6-acetyllysineBy similarity1
Modified residuei528Phosphoserine; by CDK1 and CDK2Combined sources1
Modified residuei535PhosphothreonineCombined sources1
Modified residuei536PhosphoserineCombined sources1
Modified residuei540Phosphoserine; by MAPK1By similarity1
Modified residuei575Phosphoserine; by CK2By similarity1
Modified residuei609PhosphoserineCombined sources1

Post-translational modificationi

Ubiquitinated; mediated by RNF4, RNF111, UHRF1, UBE3A/E6AP, BCR(KLHL20) E3 ubiquitin 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 (By similarity). Ubiquitination by RNF111 is polysumoylation-dependent (PubMed:23530056). Ubiquitination by BCR(KLHL20) E3 ubiquitin 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).By similarity1 Publication
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).By similarity
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).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).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ60953
PaxDbiQ60953
PeptideAtlasiQ60953
PRIDEiQ60953

PTM databases

iPTMnetiQ60953
PhosphoSitePlusiQ60953

Expressioni

Gene expression databases

BgeeiENSMUSG00000036986 Expressed in 237 organ(s), highest expression level in embryonic stem cell
CleanExiMM_PML
ExpressionAtlasiQ60953 baseline and differential
GenevisibleiQ60953 MM

Interactioni

Subunit structurei

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. Interacts with ITPR3, PPP1A and RB1. Interacts with RNF4, NLRP3, MAGEA2, RBL2, PER2, E2F4 and MAPK7/BMK1. Interacts with CSNK2A1 and CSNK2A3. Interacts with ANKRD2; the interaction is direct. Interacts with PPARGC1A AND KAT2A. Interacts (via SUMO-interacting motif) with sumoylated MORC3 (By similarity). Interacts with TRIM16.By similarity9 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202265, 25 interactors
DIPiDIP-29279N
IntActiQ60953, 16 interactors
MINTiQ60953
STRINGi10090.ENSMUSP00000082816

Structurei

3D structure databases

ProteinModelPortaliQ60953
SMRiQ60953
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni458 – 565Interaction with PER2By similarityAdd BLAST108
Regioni566 – 572Sumo interaction motif (SIM)By similarity7

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili295 – 331Sequence analysisAdd BLAST37

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi486 – 500Nuclear localization signalBy similarityAdd BLAST15

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi12 – 38Pro-richAdd BLAST27

Domaini

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri62 – 97RING-typePROSITE-ProRule annotationAdd BLAST36
Zinc fingeri129 – 171B box-type 1PROSITE-ProRule annotationAdd BLAST43
Zinc fingeri188 – 239B box-type 2PROSITE-ProRule annotationAdd BLAST52

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG2177 Eukaryota
ENOG4111G04 LUCA
GeneTreeiENSGT00510000048454
HOGENOMiHOG000115586
HOVERGENiHBG000552
InParanoidiQ60953
KOiK10054
OrthoDBiEOG091G02GY
PhylomeDBiQ60953
TreeFamiTF336434

Family and domain databases

Gene3Di3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR021978 DUF3583
IPR000315 Znf_B-box
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS
PfamiView protein in Pfam
PF12126 DUF3583, 1 hit
PF00643 zf-B_box, 1 hit
SMARTiView protein in SMART
SM00336 BBOX, 1 hit
SM00184 RING, 1 hit
PROSITEiView protein in PROSITE
PS50119 ZF_BBOX, 2 hits
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 7 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q60953-1) [UniParc]FASTAAdd to basket

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.

« Hide
        10         20         30         40         50
METEPVSVQK VPAPPGSPCR QQDSALTPTP TMPPPEEPSE DYEHSQSPAE
60 70 80 90 100
QAIQEEFQFL RCPSCQAQAK CPKLLPCLHT LCSGCLEAPG LQCPICKAPG
110 120 130 140 150
QADANGEALD NVFFESLQRR LAVFRQIVDA QAACTRCKGL ADFWCFECEQ
160 170 180 190 200
LICSKCFEAH QWYLKHEARP LADLRDNSVS SFLDSTRKSN IFCSNTNHRN
210 220 230 240 250
PALTDIYCRG CAKPLCCTCA LLDRNHSHLH CDIGEEIQQW HEELGTMTQT
260 270 280 290 300
LEEQGRTFDS AHAQMCSAIG QLDHARADIE KQIRARVRQV VDYVQAQERE
310 320 330 340 350
LLEAVNDRYQ RDYQEIAGQL SCLEAVLQRI RTSGALVKRM KLYASDQEVL
360 370 380 390 400
DMHSFLRKAL CSLRQEEPQN QKVQLLTRGF EEFKLCLQDF ISCITQRINA
410 420 430 440 450
AVASPEAASN QPEAASTHPV TTSTPEDLEQ PKEVQSVQAQ ALELSKTQPV
460 470 480 490 500
AMVKTVPGAH PVPVYAFSMQ GPTYREEASQ TVGSMKRKCS HEDCSRKIIK
510 520 530 540 550
MESTEENEDR LATSSPEQSW PSTFKATSPP HLDGTSNPES TVPEKKILLP
560 570 580 590 600
NNNHVTSDTG ETEERVVVIS SSEDSDTENL SSHELDDSSS ESSSLQLEGP
610 620 630 640 650
NSLKALDESL AEPHLEDRTL VFFDLKIDNE TQKISQLAAV NRESKFRVLI
660 670 680 690 700
QPEAFSVYSK AVSLEAGLRH FLSFLTTMHR PILACSRLWG PGLPIFFQTL
710 720 730 740 750
SDINKLWEFQ DTISGFLAVL PLIRERIPGA SSFKLGNLAK TYLARNMSER
760 770 780 790 800
SALASVLAMR DLCCLLEISP GLPLAQHIYS FSSLQCFASL QPLIQASVLP
810 820 830 840 850
QSEARLLALH NVSFVELLNA YRTNRQEGLK KYVHYLSLQT TPLSSSASTQ
860 870 880
VAQFLQALST HMEGLLEGHA PAGAEGKAES KGCLA
Length:885
Mass (Da):98,242
Last modified:May 29, 2007 - v3
Checksum:i6A2F93F4CD482FDD
GO
Isoform 2 (identifier: Q60953-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     431-476: Missing.

Show »
Length:839
Mass (Da):93,263
Checksum:iAA1B497B0C2559E3
GO

Computationally mapped potential isoform sequencesi

There are 7 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D3Z3A6D3Z3A6_MOUSE
Protein PML
Pml
632Annotation score:
D3YXR5D3YXR5_MOUSE
Protein PML
Pml
641Annotation score:
F7BTZ2F7BTZ2_MOUSE
Protein PML
Pml
578Annotation score:
D3Z2V0D3Z2V0_MOUSE
Protein PML
Pml
118Annotation score:
D6RII9D6RII9_MOUSE
Protein PML
Pml
53Annotation score:
F6XUT1F6XUT1_MOUSE
Protein PML
Pml
124Annotation score:
F6RQM1F6RQM1_MOUSE
Protein PML
Pml
54Annotation score:

Sequence cautioni

The sequence AAA97601 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti210G → V in BAC25716 (PubMed:16141072).Curated1
Sequence conflicti414A → V in BAC25716 (PubMed:16141072).Curated1
Sequence conflicti424T → S in BAC25716 (PubMed:16141072).Curated1
Sequence conflicti429E → V in AAH20990 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_026028431 – 476Missing in isoform 2. 2 PublicationsAdd BLAST46

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK028044 mRNA Translation: BAC25716.1
BC020990 mRNA Translation: AAH20990.2
U33626 mRNA Translation: AAA97601.2 Different initiation.
CCDSiCCDS23239.1 [Q60953-1]
CCDS23240.2 [Q60953-2]
RefSeqiNP_001298017.1, NM_001311088.1
NP_032910.3, NM_008884.5 [Q60953-2]
NP_835188.2, NM_178087.4 [Q60953-1]
UniGeneiMm.392123

Genome annotation databases

EnsembliENSMUST00000085673; ENSMUSP00000082816; ENSMUSG00000036986 [Q60953-1]
ENSMUST00000114136; ENSMUSP00000109771; ENSMUSG00000036986 [Q60953-2]
GeneIDi18854
KEGGimmu:18854
UCSCiuc009pwp.2 mouse [Q60953-1]
uc009pwq.2 mouse [Q60953-2]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK028044 mRNA Translation: BAC25716.1
BC020990 mRNA Translation: AAH20990.2
U33626 mRNA Translation: AAA97601.2 Different initiation.
CCDSiCCDS23239.1 [Q60953-1]
CCDS23240.2 [Q60953-2]
RefSeqiNP_001298017.1, NM_001311088.1
NP_032910.3, NM_008884.5 [Q60953-2]
NP_835188.2, NM_178087.4 [Q60953-1]
UniGeneiMm.392123

3D structure databases

ProteinModelPortaliQ60953
SMRiQ60953
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202265, 25 interactors
DIPiDIP-29279N
IntActiQ60953, 16 interactors
MINTiQ60953
STRINGi10090.ENSMUSP00000082816

PTM databases

iPTMnetiQ60953
PhosphoSitePlusiQ60953

Proteomic databases

EPDiQ60953
PaxDbiQ60953
PeptideAtlasiQ60953
PRIDEiQ60953

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000085673; ENSMUSP00000082816; ENSMUSG00000036986 [Q60953-1]
ENSMUST00000114136; ENSMUSP00000109771; ENSMUSG00000036986 [Q60953-2]
GeneIDi18854
KEGGimmu:18854
UCSCiuc009pwp.2 mouse [Q60953-1]
uc009pwq.2 mouse [Q60953-2]

Organism-specific databases

CTDi5371
MGIiMGI:104662 Pml

Phylogenomic databases

eggNOGiKOG2177 Eukaryota
ENOG4111G04 LUCA
GeneTreeiENSGT00510000048454
HOGENOMiHOG000115586
HOVERGENiHBG000552
InParanoidiQ60953
KOiK10054
OrthoDBiEOG091G02GY
PhylomeDBiQ60953
TreeFamiTF336434

Enzyme and pathway databases

ReactomeiR-MMU-3108214 SUMOylation of DNA damage response and repair proteins
R-MMU-3232142 SUMOylation of ubiquitinylation proteins
R-MMU-6804758 Regulation of TP53 Activity through Acetylation
R-MMU-8934593 Regulation of RUNX1 Expression and Activity
R-MMU-8948747 Regulation of PTEN localization

Miscellaneous databases

ChiTaRSiPml mouse
PROiPR:Q60953
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000036986 Expressed in 237 organ(s), highest expression level in embryonic stem cell
CleanExiMM_PML
ExpressionAtlasiQ60953 baseline and differential
GenevisibleiQ60953 MM

Family and domain databases

Gene3Di3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR021978 DUF3583
IPR000315 Znf_B-box
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS
PfamiView protein in Pfam
PF12126 DUF3583, 1 hit
PF00643 zf-B_box, 1 hit
SMARTiView protein in SMART
SM00336 BBOX, 1 hit
SM00184 RING, 1 hit
PROSITEiView protein in PROSITE
PS50119 ZF_BBOX, 2 hits
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPML_MOUSE
AccessioniPrimary (citable) accession number: Q60953
Secondary accession number(s): Q8CEJ1, Q8VCC4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 29, 2007
Last modified: November 7, 2018
This is version 186 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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Main funding by: National Institutes of Health

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