Q9NYB0 · TE2IP_HUMAN
- ProteinTelomeric repeat-binding factor 2-interacting protein 1
- GeneTERF2IP
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids399 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acts both as a regulator of telomere function and as a transcription regulator. Involved in the regulation of telomere length and protection as a component of the shelterin complex (telosome). In contrast to other components of the shelterin complex, it is dispensible for telomere capping and does not participate in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair. Instead, it is required to negatively regulate telomere recombination and is essential for repressing homology-directed repair (HDR), which can affect telomere length. Does not bind DNA directly: recruited to telomeric double-stranded 5'-TTAGGG-3' repeats via its interaction with TERF2. Independently of its function in telomeres, also acts as a transcription regulator: recruited to extratelomeric 5'-TTAGGG-3' sites via its association with TERF2 or other factors, and regulates gene expression. When cytoplasmic, associates with the I-kappa-B-kinase (IKK) complex and acts as a regulator of the NF-kappa-B signaling by promoting IKK-mediated phosphorylation of RELA/p65, leading to activate expression of NF-kappa-B target genes.
Miscellaneous
Shares a bidirectional promoter with KARS1.
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTelomeric repeat-binding factor 2-interacting protein 1
- Short namesTERF2-interacting telomeric protein 1; TRF2-interacting telomeric protein 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9NYB0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Associates with chromosomes, both at telomeres and in extratelomeric sites. Also exists as a cytoplasmic form, where it associates with the IKK complex.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_050195 | 324 | in dbSNP:rs4888444 | |||
Sequence: K → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 517 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000197126 | 2-399 | UniProt | Telomeric repeat-binding factor 2-interacting protein 1 | |||
Sequence: AEAMDLGKDPNGPTHSSTLFVRDDGSSMSFYVRPSPAKRRLSTLILHGGGTVCRVQEPGAVLLAQPGEALAEASGDFISTQYILDCVERNERLELEAYRLGPASAADTGSEAKPGALAEGAAEPEPQRHAGRIAFTDADDVAILTYVKENARSPSSVTGNALWKAMEKSSLTQHSWQSLKDRYLKHLRGQEHKYLLGDAPVSPSSQKLKRKAEEDPEAADSGEPQNKRTPDLPEEEYVKEEIQENEEAVKKMLVEATREFEEVVVDESPPDFEIHITMCDDDPPTPEEDSETQPDEEEEEEEEKVSQPEVGAAIKIIRQLMEKFNLDLSTVTQAFLKNSGELEATSAFLASGQRADGYPIWSRQDDIDLQKDDEDTREALVKKFGAQNVARRIEFRKK | |||||||
Modified residue (large scale data) | 28 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 30 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 36 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 36 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 43 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 43 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 44 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 105 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 114 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 154 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 154 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 156 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 156 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 176 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 179 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 194 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 195 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 203 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 203 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 205 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 206 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 206 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 208 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 212 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 222 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 230 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 240 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 372 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitous. Highly expressed.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Associates with the I-kappa-B-kinase (IKK) core complex, composed of CHUK, IKBKB and IKBKG (By similarity).
Homodimer. Component of the shelterin complex (telosome) composed of TERF1, TERF2, TINF2, TERF2IP ACD and POT1. Interacts with TERF2; the interaction is direct. Does not interact with TERF1. Interacts with SLX4/BTBD12
Homodimer. Component of the shelterin complex (telosome) composed of TERF1, TERF2, TINF2, TERF2IP ACD and POT1. Interacts with TERF2; the interaction is direct. Does not interact with TERF1. Interacts with SLX4/BTBD12
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 78-101 | BRCT | ||||
Sequence: FISTQYILDCVERNERLELEAYRL | ||||||
Region | 104-132 | Disordered | ||||
Sequence: ASAADTGSEAKPGALAEGAAEPEPQRHAG | ||||||
Domain | 128-188 | Myb-like | ||||
Sequence: QRHAGRIAFTDADDVAILTYVKENARSPSSVTGNALWKAMEKSSLTQHSWQSLKDRYLKHL | ||||||
Region | 196-244 | Disordered | ||||
Sequence: LLGDAPVSPSSQKLKRKAEEDPEAADSGEPQNKRTPDLPEEEYVKEEIQ | ||||||
Compositional bias | 208-237 | Basic and acidic residues | ||||
Sequence: KLKRKAEEDPEAADSGEPQNKRTPDLPEEE | ||||||
Compositional bias | 264-283 | Basic and acidic residues | ||||
Sequence: VVVDESPPDFEIHITMCDDD | ||||||
Region | 264-311 | Disordered | ||||
Sequence: VVVDESPPDFEIHITMCDDDPPTPEEDSETQPDEEEEEEEEKVSQPEV | ||||||
Compositional bias | 284-306 | Acidic residues | ||||
Sequence: PPTPEEDSETQPDEEEEEEEEKV | ||||||
Motif | 383-399 | Nuclear localization signal | ||||
Sequence: KKFGAQNVARRIEFRKK |
Sequence similarities
Belongs to the RAP1 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length399
- Mass (Da)44,260
- Last updated2000-10-01 v1
- ChecksumEAA615777F9D3D3D
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H3BR63 | H3BR63_HUMAN | TERF2IP | 122 | ||
H3BMI8 | H3BMI8_HUMAN | TERF2IP | 99 | ||
A0A590UJT3 | A0A590UJT3_HUMAN | TERF2IP | 342 |
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 83 | in Ref. 4; BAA91317 | ||||
Sequence: Y → H | ||||||
Compositional bias | 208-237 | Basic and acidic residues | ||||
Sequence: KLKRKAEEDPEAADSGEPQNKRTPDLPEEE | ||||||
Compositional bias | 264-283 | Basic and acidic residues | ||||
Sequence: VVVDESPPDFEIHITMCDDD | ||||||
Compositional bias | 284-306 | Acidic residues | ||||
Sequence: PPTPEEDSETQPDEEEEEEEEKV |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF262988 EMBL· GenBank· DDBJ | AAF72711.1 EMBL· GenBank· DDBJ | mRNA | ||
AF250393 EMBL· GenBank· DDBJ | AAQ14259.1 EMBL· GenBank· DDBJ | mRNA | ||
AF289599 EMBL· GenBank· DDBJ | AAL55783.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AK000669 EMBL· GenBank· DDBJ | BAA91317.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AK298880 EMBL· GenBank· DDBJ | BAG60996.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC025287 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471114 EMBL· GenBank· DDBJ | EAW95616.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471114 EMBL· GenBank· DDBJ | EAW95618.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC004465 EMBL· GenBank· DDBJ | AAH04465.1 EMBL· GenBank· DDBJ | mRNA | ||
BC005841 EMBL· GenBank· DDBJ | AAH05841.1 EMBL· GenBank· DDBJ | mRNA | ||
BC022428 EMBL· GenBank· DDBJ | AAH22428.1 EMBL· GenBank· DDBJ | mRNA | ||
BC078171 EMBL· GenBank· DDBJ | AAH78171.1 EMBL· GenBank· DDBJ | mRNA |