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Basic Information Integrated Annotations

Tag Content
iUUCD ID IUUC-Hsa-045861
UUCD1 version UUC-HoS-00062
Ensembl Protein ID ENSP00000268058.3
UniProt Accession P29590; E9PBR7; P29591; P29592; P29593; Q00755; Q15959; Q59FP9; Q8WUA0; Q96S41; Q9BPW2; Q9BWP7; Q9BZX6; Q9BZX7; Q9BZX8; Q9BZX9; Q9BZY0; Q9BZY2; Q9BZY3; PML_HUMAN
Genbank Protein ID AAB19601.2; AAA60388.1; AAA60351.1; AAA60390.1; CAA44841.1; AAA60125.1; AAA60352.1; AAG50180.1; AAG50181.1; AAG50182.1; AAG50184.1; AAG50185.1; AAG50186.1; AAG50187.1; AAG50188.1; AAG50189.1; AAG50190.1; AAP88913.1; BAD92648.1; AAH00080.2; AAH20994.1; CAA46026.1; BAB62809.1
Protein Name Protein PML; Promyelocytic leukemia protein; RING finger protein 71; Tripartite motif-containing protein 19
Genbank Nucleotide ID S50913; M79462; M79463; M79464; X63131; M73778; M80185; AF230401; AF230402; AF230403; AF230405; AF230406; AF230407; AF230408; AF230409; AF230410; AF230411; BT009911; AB209411; AC013486; BC020994; X64800; AB067754
Gene Name PML; MYL; PP8675; RNF71; TRIM19
Ensembl Information
Ensembl Gene ID Ensembl Transcript ID Ensembl Protein ID
ENSG00000140464.19 ENST00000395135.7 ENSP00000378567.3
ENSG00000140464.19 ENST00000395132.6 ENSP00000378564.2
ENSG00000140464.19 ENST00000268059.10 ENSP00000268059.6
ENSG00000140464.19 ENST00000354026.10 ENSP00000315434.8
ENSG00000140464.19 ENST00000268058.7 ENSP00000268058.3
ENSG00000140464.19 ENST00000565898.5 ENSP00000455838.1
ENSG00000140464.19 ENST00000569477.5 ENSP00000455612.1
ENSG00000140464.19 ENST00000569965.5 ENSP00000456486.1
ENSG00000140464.19 ENST00000567543.5 ENSP00000456277.1
ENSG00000140464.19 ENST00000435786.6 ENSP00000395576.2
ENSG00000140464.19 ENST00000564428.5 ENSP00000457023.1
ENSG00000140464.19 ENST00000563500.5 ENSP00000457032.1
ENSG00000140464.19 ENST00000565239.5 ENSP00000456989.1
ENSG00000140464.19 ENST00000567606.5 ENSP00000457669.1
ENSG00000140464.19 ENST00000566068.1 ENSP00000458061.1
Annotation
Cancer Mutation
TCGAICGCCOSMICCGAP
IntOGen
Single Nucleotide Polymorphisms (SNP)
dbSNP
mRNA Expression
GEOArrayExpressTCGAICGC
COSMICTHPAHPM
DNA & RNA Element
UTRdbAREsitecircBasecircRNADb
CircNetmiRTarBasemicroRNATRANSFAC
miRWalkRepTarSomamiRmiRcode
RAID2LncRNADisease
Protein-protein Interaction
IIDiRefIndexPINAHINT
MenthaInWeb_IM
Protein 3D Structure
PDBMMDB
Disease-associated Information
ClinVarGWASdbOMIM
Post-translational Modifications (PTMs)
CPLMdbPAFPhosphositePlusdbPTM
HPRDPhospho.ELMUniProtPHOSIDA
BioGRIDmUbiSiDa
DNA Methylation
MethyCancerTCGAICGCCOSMIC
Protein Expression/Proteomics
THPAHPMGPMDB
Status Reviewed
Details
Family Domain References (PMIDs)
E3 activity/RING/RING RING 20130140
Reviewed
Classification
Family Identity E-value Score Source Orthology
E3 activity/RING/RING 69.29 0.00e+00 1087.00 IUUC-Mmu-063118
Organism Homo sapiens
Functional Description
(View)

Functional Description



     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 HIPK2, TERT, SIRT1, TOPBP1, TRIM27 and TRIM69. Interacts with ELF4 (via C-terminus). Interacts with Lassa virus Z protein and rabies virus phosphoprotein. Interacts with ITPR3. 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 (PML-RARA oncoprotein, via the coiled-coil domain) with UBE2I; the interaction is enhanced by arsenic binding and is required for PML-RARA oncoprotein sumoylation and inhibition of RARA transactivational activity. Interacts with RB1, PPP1A, SMAD2, SMAD3, DAXX, RPL11 and MTOR. Interacts with PPARGC1A and KAT2A. Interacts with CSNK2A1 and CSNK2A3. Interacts with ANKRD2; the interaction is direct. Interacts (via SUMO-interacting motif) with sumoylated MORC3 (PubMed:20501696). Isoform PML-1, isoform PML-2, isoform PML-3, isoform PML-4, isoform PML-5 and isoform PML-6 interact with RNF4. Isoform PML-1 interacts with NLRP3. Isoform PML-1, isoform PML-2, isoform PML-3, isoform PML-4 and isoform PML-5 interact with MAGEA2, RBL2, PER2 and E2F4. Isoform PML-2 interacts with CIITA. Isoform PML-2, isoform PML-3 and isoform PML-4 interact with TBX2. Isoform PML-4 interacts with RANBP2, HDAC7, KAT6A, WRN, PIN1, TBX3 and phosphorylated MAPK1/ERK2. Isoform PML-4 interacts with the CTNNB1 and TCF7L2/TCF4 complex. Isoform PML-4 preferentially interacts with MAPK7/BMK1 although other isoforms (isoform PML-1, isoform PML-2, isoform PML-3 and isoform PML-6) also interact with it. Isoform PML-12 interacts with PIAS1, PIAS2 (isoform PIAS2-alpha) and CSNK2A1/CK2. Isoform PML-3 interacts with HFV bel1/tas and bet. Isoform PML-4 interacts with VZV capsid protein VP26/ORF23 capsid protein. Ths sumoylated isoform PML-4 interacts with encephalomyocarditis virus (EMCV) RNA-directed RNA polymerase 3D-POL (P3D-POL). Isoform PML-1 interacts with herpes simplex virus-1 (HHV-1) ICP0. Isoform PML-2 interacts with human adenovirus 2 E1A and this interaction stimulates E1A-dependent transcriptional activation (PubMed:23135708). Isoform PML-6 interacts with moloney murine leukemia virus (MoMLV) integrase (IN) and reverse transcriptase (RT). Isoform PML-4 and isoform PML-5 interact with human adenovirus 5 E1B-55K protein; these interactions promote efficient subnuclear targeting of E1B-55K to PML nuclear bodies (PubMed:20639899, PubMed:25772236).
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 HIPK2, TERT, SIRT1, TOPBP1, TRIM27 and TRIM69. Interacts with ELF4 (via C-terminus). Interacts with Lassa virus Z protein and rabies virus phosphoprotein. Interacts with ITPR3. 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 (PML-RARA oncoprotein, via the coiled-coil domain) with UBE2I; the interaction is enhanced by arsenic binding and is required for PML-RARA oncoprotein sumoylation and inhibition of RARA transactivational activity. Interacts with RB1, PPP1A, SMAD2, SMAD3, DAXX, RPL11 and MTOR. Interacts with PPARGC1A and KAT2A. Interacts with CSNK2A1 and CSNK2A3. Interacts with ANKRD2; the interaction is direct. Interacts (via SUMO-interacting motif) with sumoylated MORC3 (PubMed:20501696). Isoform PML-1, isoform PML-2, isoform PML-3, isoform PML-4, isoform PML-5 and isoform PML-6 interact with RNF4. Isoform PML-1 interacts with NLRP3. Isoform PML-1, isoform PML-2, isoform PML-3, isoform PML-4 and isoform PML-5 interact with MAGEA2, RBL2, PER2 and E2F4. Isoform PML-2 interacts with CIITA. Isoform PML-2, isoform PML-3 and isoform PML-4 interact with TBX2. Isoform PML-4 interacts with RANBP2, HDAC7, KAT6A, WRN, PIN1, TBX3 and phosphorylated MAPK1/ERK2. Isoform PML-4 interacts with the CTNNB1 and TCF7L2/TCF4 complex. Isoform PML-4 preferentially interacts with MAPK7/BMK1 although other isoforms (isoform PML-1, isoform PML-2, isoform PML-3 and isoform PML-6) also interact with it. Isoform PML-12 interacts with PIAS1, PIAS2 (isoform PIAS2-alpha) and CSNK2A1/CK2. Isoform PML-3 interacts with HFV bel1/tas and bet. Isoform PML-4 interacts with VZV capsid protein VP26/ORF23 capsid protein. Ths sumoylated isoform PML-4 interacts with encephalomyocarditis virus (EMCV) RNA-directed RNA polymerase 3D-POL (P3D-POL). Isoform PML-1 interacts with herpes simplex virus-1 (HHV-1) ICP0. Isoform PML-2 interacts with human adenovirus 2 E1A and this interaction stimulates E1A-dependent transcriptional activation (PubMed:23135708). Isoform PML-6 interacts with moloney murine leukemia virus (MoMLV) integrase (IN) and reverse transcriptase (RT). Isoform PML-4 and isoform PML-5 interact with human adenovirus 5 E1B-55K protein; these interactions promote efficient subnuclear targeting of E1B-55K to PML nuclear bodies (PubMed:20639899, PubMed:25772236).
Protein Sequence
(Fasta)
MEPAPARSPR PQQDPARPQE PTMPPPETPS EGRQPSPSPS PTERAPASEE EFQFLRCQQC 60
QAEAKCPKLL PCLHTLCSGC LEASGMQCPI CQAPWPLGAD TPALDNVFFE SLQRRLSVYR 120
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Protein Fasta Sequence



>IUUC-Hsa-045861|E3,RING|Homo sapiens
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Nucleotide Sequence
(Fasta)
CTCTCCAGAG GCGGGCCCTG AGCCGGCACC TCCCCTTTCG GACAGCTCAA GGGACTCAGC 60
CAACTGGCTC ACGCCTCCCC TTCAGCTTCT CTTCACGCAC TCCAAGATCT AAACCGAGAA 120
It may take some time, please wait.

Nucleotide Fasta Sequence



>IUUC-Hsa-045861|E3,RING|Homo sapiens
Please wait for a moment...
Sequence Source Ensembl
Keyword

KW-0002--3D-structure
KW-0007--Acetylation
KW-0010--Activator
KW-0025--Alternative splicing
KW-0051--Antiviral defense
KW-0053--Apoptosis
KW-0090--Biological rhythms
KW-0160--Chromosomal rearrangement
KW-0175--Coiled coil
KW-0181--Complete proteome
KW-0963--Cytoplasm
KW-0238--DNA-binding
KW-0256--Endoplasmic reticulum
KW-0967--Endosome
KW-0945--Host-virus interaction
KW-0391--Immunity
KW-0399--Innate immunity
KW-1017--Isopeptide bond
KW-0472--Membrane
KW-0479--Metal-binding
KW-0539--Nucleus
KW-0597--Phosphoprotein
KW-0621--Polymorphism
KW-0656--Proto-oncogene
KW-1185--Reference proteome
KW-0677--Repeat
KW-0804--Transcription
KW-0805--Transcription regulation
KW-0043--Tumor suppressor
KW-0832--Ubl conjugation
KW-0862--Zinc
KW-0863--Zinc-finger

Interpro

IPR021978--DUF3583
IPR000315--Znf_B-box
IPR001841--Znf_RING
IPR013083--Znf_RING/FYVE/PHD
IPR017907--Znf_RING_CS

PROSITE

PS50119--ZF_BBOX
PS00518--ZF_RING_1
PS50089--ZF_RING_2

Pfam

PF12126--DUF3583
PF00643--zf-B_box

SMART

SM00336--BBOX
SM00184--RING

Gene Ontology

GO:0005737--C:cytoplasm
GO:0005829--C:cytosol
GO:0031901--C:early endosome membrane
GO:0042406--C:extrinsic component of endoplasmic reticulum membrane
GO:0000784--C:nuclear chromosome, telomeric region
GO:0016363--C:nuclear matrix
GO:0031965--C:nuclear membrane
GO:0005730--C:nucleolus
GO:0005654--C:nucleoplasm
GO:0005634--C:nucleus
GO:0016605--C:PML body
GO:0050897--F:cobalt ion binding
GO:0003677--F:DNA binding
GO:0046982--F:protein heterodimerization activity
GO:0042803--F:protein homodimerization activity
GO:0032183--F:SUMO binding
GO:0003713--F:transcription coactivator activity
GO:0031625--F:ubiquitin protein ligase binding
GO:0008270--F:zinc ion binding
GO:0006919--P:activation of cysteine-type endopeptidase activity involved in apoptotic process
GO:0006915--P:apoptotic process
GO:0060444--P:branching involved in mammary gland duct morphogenesis
GO:0007050--P:cell cycle arrest
GO:0045165--P:cell fate commitment
GO:0071353--P:cellular response to interleukin-4
GO:0090398--P:cellular senescence
GO:0032922--P:circadian regulation of gene expression
GO:0007182--P:common-partner SMAD protein phosphorylation
GO:0051607--P:defense response to virus
GO:0006977--P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest
GO:0032469--P:endoplasmic reticulum calcium ion homeostasis
GO:0043153--P:entrainment of circadian clock by photoperiod
GO:0097191--P:extrinsic apoptotic signaling pathway
GO:0010761--P:fibroblast migration
GO:0045087--P:innate immune response
GO:0060333--P:interferon-gamma-mediated signaling pathway
GO:0008630--P:intrinsic apoptotic signaling pathway in response to DNA damage
GO:0042771--P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator
GO:0070059--P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress
GO:0008631--P:intrinsic apoptotic signaling pathway in response to oxidative stress
GO:0051457--P:maintenance of protein location in nucleus
GO:0030099--P:myeloid cell differentiation
GO:0016525--P:negative regulation of angiogenesis
GO:0030308--P:negative regulation of cell growth
GO:0008285--P:negative regulation of cell proliferation
GO:0050713--P:negative regulation of interleukin-1 beta secretion
GO:0045930--P:negative regulation of mitotic cell cycle
GO:2000059--P:negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process
GO:0051974--P:negative regulation of telomerase activity
GO:0032211--P:negative regulation of telomere maintenance via telomerase
GO:0045892--P:negative regulation of transcription, DNA-templated
GO:0032938--P:negative regulation of translation in response to oxidative stress
GO:1902187--P:negative regulation of viral release from host cell
GO:0030578--P:PML body organization
GO:0060058--P:positive regulation of apoptotic process involved in mammary gland involution
GO:0002230--P:positive regulation of defense response to virus by host
GO:2001238--P:positive regulation of extrinsic apoptotic signaling pathway
GO:0048146--P:positive regulation of fibroblast proliferation
GO:0031065--P:positive regulation of histone deacetylation
GO:0045345--P:positive regulation of MHC class I biosynthetic process
GO:1904816--P:positive regulation of protein localization to chromosome, telomeric region
GO:0032206--P:positive regulation of telomere maintenance
GO:0045944--P:positive regulation of transcription from RNA polymerase II promoter
GO:0043161--P:proteasome-mediated ubiquitin-dependent protein catabolic process
GO:0006461--P:protein complex assembly
GO:0050821--P:protein stabilization
GO:0006605--P:protein targeting
GO:0010522--P:regulation of calcium ion transport into cytosol
GO:0030155--P:regulation of cell adhesion
GO:0042752--P:regulation of circadian rhythm
GO:2000779--P:regulation of double-strand break repair
GO:0001932--P:regulation of protein phosphorylation
GO:1901796--P:regulation of signal transduction by p53 class mediator
GO:0006355--P:regulation of transcription, DNA-templated
GO:0034097--P:response to cytokine
GO:0010332--P:response to gamma radiation
GO:0001666--P:response to hypoxia
GO:0009411--P:response to UV
GO:0048384--P:retinoic acid receptor signaling pathway
GO:0007184--P:SMAD protein import into nucleus
GO:0006351--P:transcription, DNA-templated
GO:0007179--P:transforming growth factor beta receptor signaling pathway

KEGG hsa:5371
Orthology
iUUCD ID Species Identity E-value Score
IUUC-Aml-001901 Ailuropoda melanoleuca 79.71 0.00e+00 1242.00
IUUC-Bta-012427 Bos taurus 75.37 0.00e+00 1239.00
IUUC-Cja-019029 Callithrix jacchus 92.85 0.00e+00 1480.00
IUUC-Cfa-021127 Canis familiaris 78.05 0.00e+00 1231.00
IUUC-Cpo-022553 Cavia porcellus 71.45 0.00e+00 1077.00
IUUC-Csa-023187 Chlorocebus sabaeus 94.93 0.00e+00 1056.00
IUUC-Cho-024937 Choloepus hoffmanni 72.61 1.00e-106 380.00
IUUC-Dno-029326 Dasypus novemcinctus 78.02 0.00e+00 1187.00
IUUC-Dor-030808 Dipodomys ordii 63.68 0.00e+00 754.00
IUUC-Ete-032746 Echinops telfairi 57.42 0.00e+00 635.00
IUUC-Eca-033234 Equus caballus 80.93 0.00e+00 1222.00
IUUC-Fca-035648 Felis catus 82.29 0.00e+00 1311.00
IUUC-Ggo-044927 Gorilla gorilla 99.77 0.00e+00 1652.00
IUUC-Itr-047861 Ictidomys tridecemlineatus 82.84 0.00e+00 1364.00
IUUC-Loc-052276 Lepisosteus oculatus 35.22 2.00e-53 204.00
IUUC-Laf-054059 Loxodonta africana 76.75 0.00e+00 1202.00
IUUC-Meu-056495 Macropus eugenii 55.41 1.00e-107 384.00
IUUC-Mga-059224 Meleagris gallopavo 32.85 4.00e-84 306.00
IUUC-Mmr-061507 Microcebus murinus 80.05 0.00e+00 1273.00
IUUC-Mdo-062196 Monodelphis domestica 46.78 0.00e+00 662.00
IUUC-Mmu-063118 Mus musculus 69.29 0.00e+00 1131.00
IUUC-Mpu-066024 Mustela putorius furo 73.89 0.00e+00 1161.00
IUUC-Mlu-066980 Myotis lucifugus 78.65 0.00e+00 1201.00
IUUC-Nle-069779 Nomascus leucogenys 97.73 0.00e+00 1536.00
IUUC-Ocu-074016 Oryctolagus cuniculus 65.91 0.00e+00 1043.00
IUUC-Oga-089085 Otolemur garnettii 71.44 0.00e+00 1125.00
IUUC-Oar-089980 Ovis aries 72.99 0.00e+00 1172.00
IUUC-Ptr-091681 Pan troglodytes 99.66 0.00e+00 1650.00
IUUC-Pan-091965 Papio anubis 94.56 0.00e+00 1494.00
IUUC-Psi-093577 Pelodiscus sinensis 37.88 4.00e-126 445.00
IUUC-Pab-098215 Pongo abelii 85.75 0.00e+00 1367.00
IUUC-Pca-100883 Procavia capensis 72.50 0.00e+00 858.00
IUUC-Pva-102465 Pteropus vampyrus 74.31 0.00e+00 822.00
IUUC-Rno-105120 Rattus norvegicus 69.06 0.00e+00 1167.00
IUUC-Sar-113320 Sorex araneus 62.21 1.00e-91 331.00
IUUC-Ssc-116042 Sus scrofa 76.92 0.00e+00 1239.00
IUUC-Tbe-127880 Tupaia belangeri 69.14 0.00e+00 903.00
Created Date 25-Jun-2017

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