TRIAP1
TP53-regulated inhibitor of apoptosis 1
Also known as: HSPC132, MDM35, P53CSV, TRIA1_HUMAN, WF-1
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- O43715
- Gene
- TRIAP1
- Ensembl
- ENSG00000170855
- Chromosome
- 12
- Canonical length
- 76 aa
- Protein class
- Predicted intracellular proteins, Transporters
- Subcellular location
- Nucleoplasm,Mitochondria
OverviewNCBI Gene
Enables p53 binding activity. Contributes to phosphatidic acid transfer activity. Involved in several processes, including DNA damage response, signal transduction by p53 class mediator; negative regulation of apoptotic signaling pathway; and positive regulation of phospholipid transport. Located in mitochondrial intermembrane space and nucleoplasm. Part of protein-containing complex. [provided by Alliance of Genome Resources, Jul 2025]
Canonical amino-acid sequenceUniProt
76 residues, UniProt reviewed canonical sequence.
>O43715|TRIAP1
1 MNSVGEACTD MKREYDQCFN RWFAEKFLKG DSSGDPCTDL FKRYQQCVQK AIKEKEIPIE
61 GLEFMGHGKE KPENSSLocalizationUniProt · AlphaFold · HPA
Whether an antibody against TRIAP1 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)
- 0.47
- Highest tissue expression
- 62 nTPM
Expression across tissuesHPA
Tissue
- liver: 62 nTPM
- skeletal muscle: 57 nTPM
- pancreas: 50 nTPM
- tongue: 37 nTPM
- bone marrow: 31 nTPM
- rectum: 29 nTPM
Single-cell type
- migrating cytotrophoblasts: 162 nCPM
- cytotrophoblasts: 148 nCPM
- esophageal suprabasal cells: 97 nCPM
- extravillous trophoblasts: 92 nCPM
- esophageal basal cells: 91 nCPM
- oocytes: 83 nCPM
Immune cell
- myeloid DC: 59 nTPM
- plasmacytoid DC: 53 nTPM
- intermediate monocyte: 53 nTPM
- NK-cell: 50 nTPM
- MAIT T-cell: 49 nTPM
- naive CD4 T-cell: 48 nTPM
Brain region
- choroid plexus: 10 nTPM
- white matter: 10 nTPM
- hypothalamus: 8.7 nTPM
- spinal cord: 8.2 nTPM
- cerebellum: 8 nTPM
- cerebral cortex: 7.9 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)
- 1.61
- gnomAD pLI
- 0.06
- gnomAD missense Z
- 0.23
- DepMap mean gene effect
- -1.2
- DepMap dependency class
- common
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 6% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- apoptotic process
- cellular response to UV
- DNA damage response, signal transduction by p53 class mediator
- intermembrane lipid transfer
- mitotic G1 DNA damage checkpoint signaling
- negative regulation of apoptotic process
- negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator
- negative regulation of release of cytochrome c from mitochondria
- phospholipid translocation
- phospholipid transport
- positive regulation of phospholipid transport
- positive regulation of transcription by RNA polymerase II
- regulation of membrane lipid distribution
Molecular functions
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Mitochondrial distribution/morphology family 35/apoptosis
- Uncharacterised protein family (UPF0203)
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of TRIAP1 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 TRIAP1 as an antibody target. Whether an autoantibody or antibody against TRIAP1 could matter depends on whether native TRIAP1 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
TRIAP1 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 TRIAP1 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
Loading the interactive Seroatlas protein explorer...