TERF2
Telomeric repeat-binding factor 2
Also known as: TERF2_HUMAN, TRBF2, TRF2
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q15554
- Gene
- TERF2
- Ensembl
- ENSG00000132604
- Chromosome
- 16
- Canonical length
- 542 aa
- Protein class
- Predicted intracellular proteins
- Subcellular location
- Nucleoplasm,Nuclear bodies
- Quaternary structure
- Homodimer
OverviewNCBI Gene
This gene encodes a telomere specific protein, TERF2, which is a component of the telomere nucleoprotein complex. This protein is present at telomeres in metaphase of the cell cycle, is a second negative regulator of telomere length and plays a key role in the protective activity of telomeres. While having similar telomere binding activity and domain organization, TERF2 differs from TERF1 in that its N terminus is basic rather than acidic. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
542 residues, UniProt reviewed canonical sequence.
>Q15554|TERF2
1 MAAGAGTAGP ASGPGVVRDP AASQPRKRPG REGGEGARRS DTMAGGGGSS DGSGRAAGRR
61 ASRSSGRARR GRHEPGLGGP AERGAGEARL EEAVNRWVLK FYFHEALRAF RGSRYGDFRQ
121 IRDIMQALLV RPLGKEHTVS RLLRVMQCLS RIEEGENLDC SFDMEAELTP LESAINVLEM
181 IKTEFTLTEA VVESSRKLVK EAAVIICIKN KEFEKASKIL KKHMSKDPTT QKLRNDLLNI
241 IREKNLAHPV IQNFSYETFQ QKMLRFLESH LDDAEPYLLT MAKKALKSES AASSTGKEDK
301 QPAPGPVEKP PREPARQLRN PPTTIGMMTL KAAFKTLSGA QDSEAAFAKL DQKDLVLPTQ
361 ALPASPALKN KRPRKDENES SAPADGEGGS ELQPKNKRMT ISRLVLEEDS QSTEPSAGLN
421 SSQEAASAPP SKPTVLNQPL PGEKNPKVPK GKWNSSNGVE EKETWVEEDE LFQVQAAPDE
481 DSTTNITKKQ KWTVEESEWV KAGVQKYGEG NWAAISKNYP FVNRTAVMIK DRWRTMKRLG
541 MNLocalizationUniProt · AlphaFold · HPA
Whether an antibody against TERF2 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)
- 0.51
- Highest tissue expression
- 42 nTPM
Expression across tissuesHPA
Tissue
- tonsil: 42 nTPM
- lymph node: 33 nTPM
- skeletal muscle: 30 nTPM
- cerebellum: 27 nTPM
- cerebral cortex: 25 nTPM
- tongue: 21 nTPM
Single-cell type
- early spermatids: 68 nCPM
- b-cells: 48 nCPM
- myonuclei: 48 nCPM
- thymocytes: 42 nCPM
- neutrophil progenitors: 40 nCPM
- hematopoietic stem cells: 39 nCPM
Immune cell
- basophil: 13 nTPM
- memory B-cell: 13 nTPM
- naive B-cell: 8.3 nTPM
- naive CD4 T-cell: 6.2 nTPM
- naive CD8 T-cell: 6.1 nTPM
- gdT-cell: 5.8 nTPM
Brain region
- cerebral cortex: 65 nTPM
- cerebellum: 56 nTPM
- white matter: 56 nTPM
- hypothalamus: 52 nTPM
- midbrain: 51 nTPM
- basal ganglia: 50 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)
- 0.27
- gnomAD pLI
- 0.99
- gnomAD missense Z
- 2.07
- DepMap mean gene effect
- -0.97
- DepMap dependency class
- common
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
- cellular senescence
- in utero embryonic development
- negative regulation of cellular senescence
- negative regulation of t-circle formation
- negative regulation of telomere capping
- negative regulation of telomere maintenance
- negative regulation of telomere maintenance via semi-conservative replication
- negative regulation of telomere maintenance via telomerase
- negative regulation of telomere maintenance via telomere lengthening
- negative regulation of telomeric D-loop disassembly
- positive regulation of telomere maintenance
- protection from non-homologous end joining at telomere
- protein localization to chromosome, telomeric region
- regulation of telomere maintenance
- regulation of telomere maintenance via telomerase
- RNA-templated DNA biosynthetic process
- telomere capping
- telomere maintenance
- telomeric D-loop disassembly
- telomeric loop formation
- axonal transport of messenger ribonucleoprotein complex
- negative regulation of telomere maintenance via recombination
- negative regulation of telomere single strand break repair
Molecular functions
- double-stranded telomeric DNA binding
- enzyme binding
- G-rich strand telomeric DNA binding
- protein homodimerization activity
- protein-containing complex binding
- telomeric DNA binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
- SANT/Myb domain
- Homedomain-like superfamily
- Telomere repeat-binding factor, dimerisation domain
- Telomeric repeat-binding factor 1/2
- Myb domain
- Telomere repeat-binding factor, dimerisation domain superfamily
- Myb-like DNA-binding domain
- Telomere repeat binding factor (TRF)
- Telomeric repeat-binding factor 2
- Telomeric repeat-binding factor 2, Rap1-binding domain
- Telomeric repeat-binding factor 2 Rap1-binding motif
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of TERF2 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 TERF2 as an antibody target. Whether an autoantibody or antibody against TERF2 could matter depends on whether native TERF2 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
TERF2 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 TERF2 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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