TRIM27
Zinc finger protein RFP
Also known as: RFP, RNF76, TRI27_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P14373
- Gene
- TRIM27
- Ensembl
- ENSG00000204713
- Chromosome
- 6
- Canonical length
- 513 aa
- Protein class
- Cancer-related genes, Disease related genes, Enzymes, Potential drug targets, Predicted intracellular proteins
- Subcellular location
- Nucleoplasm,Nucleoli
- Quaternary structure
- Homomultimer
OverviewNCBI Gene
This gene encodes 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 protein localizes to the nuclear matrix. It interacts with the enhancer of polycomb protein and represses gene transcription. It is also thought to be involved in the differentiation of male germ cells. Fusion of the N-terminus of this protein with the truncated C-terminus of the RET gene product has been shown to result in production of the ret transforming protein. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
513 residues, UniProt reviewed canonical sequence.
>P14373|TRIM27
1 MASGSVAECL QQETTCPVCL QYFAEPMMLD CGHNICCACL ARCWGTAETN VSCPQCRETF
61 PQRHMRPNRH LANVTQLVKQ LRTERPSGPG GEMGVCEKHR EPLKLYCEED QMPICVVCDR
121 SREHRGHSVL PLEEAVEGFK EQIQNQLDHL KRVKDLKKRR RAQGEQARAE LLSLTQMERE
181 KIVWEFEQLY HSLKEHEYRL LARLEELDLA IYNSINGAIT QFSCNISHLS SLIAQLEEKQ
241 QQPTRELLQD IGDTLSRAER IRIPEPWITP PDLQEKIHIF AQKCLFLTES LKQFTEKMQS
301 DMEKIQELRE AQLYSVDVTL DPDTAYPSLI LSDNLRQVRY SYLQQDLPDN PERFNLFPCV
361 LGSPCFIAGR HYWEVEVGDK AKWTIGVCED SVCRKGGVTS APQNGFWAVS LWYGKEYWAL
421 TSPMTALPLR TPLQRVGIFL DYDAGEVSFY NVTERCHTFT FSHATFCGPV RPYFSLSYSG
481 GKSAAPLIIC PMSGIDGFSG HVGNHGHSME TSPLocalizationUniProt · AlphaFold · HPA
Whether an antibody against TRIM27 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
- Intracellular
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.36
- Highest tissue expression
- 58 nTPM
Expression across tissuesHPA
Tissue
- liver: 58 nTPM
- pancreas: 51 nTPM
- spleen: 45 nTPM
- prostate: 34 nTPM
- pituitary gland: 34 nTPM
- cervix: 31 nTPM
Single-cell type
- microglia: 63 nCPM
- choroid plexus epithelial cells: 47 nCPM
- renal collecting duct intercalated cells: 41 nCPM
- proximal tubule cells: 38 nCPM
- renal connecting tubule cells: 33 nCPM
- distal convoluted tubule cells: 33 nCPM
Immune cell
- intermediate monocyte: 13 nTPM
- MAIT T-cell: 11 nTPM
- memory CD4 T-cell: 11 nTPM
- total PBMC: 9.8 nTPM
- myeloid DC: 8.7 nTPM
- naive CD8 T-cell: 7.7 nTPM
Brain region
- cerebral cortex: 4 nTPM
- choroid plexus: 3.2 nTPM
- medulla oblongata: 3.2 nTPM
- midbrain: 3.1 nTPM
- thalamus: 3 nTPM
- white matter: 2.5 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)
- 0.24
- gnomAD pLI
- 1
- gnomAD missense Z
- 3.7
- DepMap mean gene effect
- 0.03
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 9% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- Arp2/3 complex-mediated actin nucleation
- innate immune response
- negative regulation of autophagy
- negative regulation of gene expression, epigenetic
- negative regulation of transcription by RNA polymerase II
- negative regulation of type I interferon production
- negative regulation of viral transcription
- positive regulation of actin nucleation
- protein K63-linked ubiquitination
- protein sumoylation
- retrograde transport, endosome to Golgi
- spermatogenesis
- suppression of viral release by host
Molecular functions
- DNA binding
- identical protein binding
- metal ion binding
- nucleic acid binding
- phosphatidylinositol 3-kinase inhibitor activity
- SUMO transferase activity
- transcription coactivator activity
- ubiquitin protein ligase activity
- ubiquitin-protein transferase activity
- zinc ion binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
- B-box-type zinc finger
- Zinc finger, RING-type
- B30.2/SPRY domain
- SPRY domain
- Butyrophylin-like, SPRY domain
- SPRY-associated
- Zinc finger, RING/FYVE/PHD-type
- Concanavalin A-like lectin/glucanase domain superfamily
- Zinc finger, RING-type, conserved site
- Zinc finger, B-box, chordata
- B30.2/SPRY domain superfamily
- Tripartite motif-containing
- SPRY domain
- B-box zinc finger
- SPRY-associated domain
- zinc finger of C3HC4-type, RING
- TRIM27, PRY/SPRY domain
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of TRIM27 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 TRIM27 as an antibody target. Whether an autoantibody or antibody against TRIM27 could matter depends on whether native TRIM27 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
TRIM27 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 TRIM27 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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