Seroatlas · Human Serome Atlas

PML

Protein PML

Also known as: MYL, PML_HUMAN, RNF71, TRIM19

Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene

Protein identityUniProt · HPA

UniProt accession
P29590
Gene
PML
Ensembl
ENSG00000140464
Chromosome
15
Canonical length
882 aa
Protein class
Cancer-related genes, Disease related genes, Human disease related genes, Plasma proteins, Predicted intracellular proteins
Subcellular location
Nuclear bodies
Quaternary structure
Homodimer

OverviewNCBI Gene

The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This phosphoprotein localizes to nuclear bodies where it functions as a transcription factor and tumor suppressor. Its expression is cell-cycle related and it regulates the p53 response to oncogenic signals. The gene is often involved in the translocation with the retinoic acid receptor alpha gene associated with acute promyelocytic leukemia (APL). Extensive alternative splicing of this gene results in several variations of the protein's central and C-terminal regions; all variants encode the same N-terminus. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

882 residues, UniProt reviewed canonical sequence.

>P29590|PML
     1  MEPAPARSPR PQQDPARPQE PTMPPPETPS EGRQPSPSPS PTERAPASEE EFQFLRCQQC
    61  QAEAKCPKLL PCLHTLCSGC LEASGMQCPI CQAPWPLGAD TPALDNVFFE SLQRRLSVYR
   121  QIVDAQAVCT RCKESADFWC FECEQLLCAK CFEAHQWFLK HEARPLAELR NQSVREFLDG
   181  TRKTNNIFCS NPNHRTPTLT SIYCRGCSKP LCCSCALLDS SHSELKCDIS AEIQQRQEEL
   241  DAMTQALQEQ DSAFGAVHAQ MHAAVGQLGR ARAETEELIR ERVRQVVAHV RAQERELLEA
   301  VDARYQRDYE EMASRLGRLD AVLQRIRTGS ALVQRMKCYA SDQEVLDMHG FLRQALCRLR
   361  QEEPQSLQAA VRTDGFDEFK VRLQDLSSCI TQGKDAAVSK KASPEAASTP RDPIDVDLPE
   421  EAERVKAQVQ ALGLAEAQPM AVVQSVPGAH PVPVYAFSIK GPSYGEDVSN TTTAQKRKCS
   481  QTQCPRKVIK MESEEGKEAR LARSSPEQPR PSTSKAVSPP HLDGPPSPRS PVIGSEVFLP
   541  NSNHVASGAG EAEERVVVIS SSEDSDAENS SSRELDDSSS ESSDLQLEGP STLRVLDENL
   601  ADPQAEDRPL VFFDLKIDNE TQKISQLAAV NRESKFRVVI QPEAFFSIYS KAVSLEVGLQ
   661  HFLSFLSSMR RPILACYKLW GPGLPNFFRA LEDINRLWEF QEAISGFLAA LPLIRERVPG
   721  ASSFKLKNLA QTYLARNMSE RSAMAAVLAM RDLCRLLEVS PGPQLAQHVY PFSSLQCFAS
   781  LQPLVQAAVL PRAEARLLAL HNVSFMELLS AHRRDRQGGL KKYSRYLSLQ TTTLPPAQPA
   841  FNLQALGTYF EGLLEGPALA RAEGVSTPLA GRGLAERASQ QS

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against PML can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability
Other membrane
Secreted
No
Transmembrane segments
0
Mean surface accessibility (rSASA)
0.45
Highest tissue expression
79 nTPM

Expression across tissuesHPA

Tissue

  • adipose tissue: 79 nTPM
  • breast: 73 nTPM
  • lung: 71 nTPM
  • cervix: 48 nTPM
  • spleen: 46 nTPM
  • thyroid gland: 45 nTPM

Single-cell type

  • vascular endothelial cells: 79 nCPM
  • foveolar cells: 74 nCPM
  • lymphatic endothelial cells: 59 nCPM
  • epididymal basal cells: 54 nCPM
  • hofbauer cells: 52 nCPM
  • erythrocyte progenitors: 50 nCPM

Immune cell

  • eosinophil: 23 nTPM
  • non-classical monocyte: 23 nTPM
  • intermediate monocyte: 20 nTPM
  • classical monocyte: 15 nTPM
  • myeloid DC: 15 nTPM
  • NK-cell: 15 nTPM

Brain region

  • medulla oblongata: 34 nTPM
  • cerebral cortex: 29 nTPM
  • thalamus: 29 nTPM
  • pons: 27 nTPM
  • spinal cord: 27 nTPM
  • amygdala: 26 nTPM

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about PML.

Disease | AutoantibodyPubMed

Conditions in which antibodies against PML are reported. Each links to that disease's full target list.

ReferencesPubMed · IEDB

Publications for PML from three distinct lines of evidence, kept separate because they answer different questions: whether antibodies are directed at the protein, whether a B-cell epitope has been mapped on it, and whether a T-cell epitope has. Each is labelled with its source.

Reference: AutoantibodyPubMed

9 publications

Show 4 more

Sources: PubMed — antigen-level antibody evidence from a custom retrieval. Records matching a controlled set of autoantibody terms (the MeSH descriptors Autoantibodies and Autoantigens, with title and abstract term variants) were obtained through NCBI E-utilities, and their titles and abstracts parsed for constructions that direct an antibody at a named protein rather than for co-occurrence. Captured names were resolved against UniProt nomenclature and each antigen adjudicated individually against the source text. Bibliographic records from PubMed and MeSH, U.S. National Library of Medicine; citation metrics from NIH iCite (Hutchins et al., PLoS Biology 2016). Titles link to PubMed; abstracts are not reproduced here. The NLM does not endorse this analysis.

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)
0.43
gnomAD pLI
0.21
gnomAD missense Z
1.74
DepMap mean gene effect
-0.01
DepMap dependency class
selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

Molecular functions

Cellular components

Protein domainsUniProt · Pfam · InterPro

KeywordsUniProt

InteractionsUniProt · HPA

Protein binding partners of PML in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

Antibody and autoantibody relevanceSeroatlas analysis

Seroatlas reads PML as an antibody target. Whether an autoantibody or antibody against PML could matter depends on whether native PML is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.

PML is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.

Annotation status

The present source text does not explicitly label PML as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.

Canonical record: https://seroatlas.com/gene/PML. Study-independent annotations aggregated from UniProt, Human Protein Atlas, PubMed, IEDB, Pfam, InterPro, Gene Ontology, AlphaFold, gnomAD, DepMap, ClinVar, TCGA. Catalog release seroatlas-reviewed-human-uniprot-20260313.

Seroatlas is the reference for exploring autoantibody and antibody serology at the human-protein level: the autoreactome and human serome, multiplex serology (HuProt, HuScan, VirScan, PhIP-Seq).

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