Seroatlas · Human Serome Atlas

TRIR

Telomerase RNA component interacting RNase

Also known as: C19orf43, fSAP18, MGC2803, TERCIR, TRIR_HUMAN

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

Protein identityUniProt · HPA

UniProt accession: Q9BQ61
Gene: TRIR
Ensembl: ENSG00000123144
Chromosome: 19
Canonical length: 176 aa
Protein class: Predicted intracellular proteins
Subcellular location: Nucleoplasm

OverviewNCBI Gene

Enables 3'-5' exonuclease activity and 5'-3' exonuclease activity. Involved in rRNA catabolic process. [provided by Alliance of Genome Resources, Jul 2025]

Canonical amino-acid sequenceUniProt

176 residues, UniProt reviewed canonical sequence.

>Q9BQ61|TRIR
     1  MAARGRRAEP QGREAPGPAG GGGGGSRWAE SGSGTSPESG DEEVSGAGSS PVSGGVNLFA
    61  NDGSFLELFK RKMEEEQRQR QEEPPPGPQR PDQSAAAAGP GDPKRKGGPG STLSFVGKRR
   121  GGNKLALKTG IVAKKQKTED EVLTSKGDAW AKYMAEVKKY KAHQCGDDDK TRPLVK

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against TRIR 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: Unknown
Secreted: No
Transmembrane segments: 0
Mean surface accessibility (rSASA): 0.68
Highest tissue expression: 285 nTPM

Expression across tissuesHPA

Tissue

liver: 285 nTPM
blood vessel: 216 nTPM
colon: 206 nTPM
kidney: 198 nTPM
spleen: 197 nTPM
spinal cord: 193 nTPM

Single-cell type

esophageal apical cells: 940 nCPM
late spermatids: 728 nCPM
syncytiotrophoblasts: 726 nCPM
extravillous trophoblasts: 683 nCPM
esophageal suprabasal cells: 538 nCPM
esophageal basal cells: 483 nCPM

Immune cell

eosinophil: 86 nTPM
memory B-cell: 67 nTPM
naive B-cell: 49 nTPM
neutrophil: 46 nTPM
T-reg: 38 nTPM
memory CD4 T-cell: 32 nTPM

Brain region

thalamus: 142 nTPM
hypothalamus: 136 nTPM
medulla oblongata: 134 nTPM
basal ganglia: 131 nTPM
spinal cord: 130 nTPM
cerebral cortex: 130 nTPM

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): 0.82
gnomAD pLI: 0.47
DepMap mean gene effect: -0.18
DepMap dependency class: selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

rRNA catabolic process

Molecular functions

Protein domainsUniProt · Pfam · InterPro

Telomerase RNA component interacting RNase

KeywordsUniProt

InteractionsUniProt · HPA

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

SNRPA

Antibody and autoantibody relevanceSeroatlas analysis

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

TRIR 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 TRIR as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.

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