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Protein

Telomeric repeat-binding factor 2-interacting protein 1

Gene

TERF2IP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  • G-rich strand telomeric DNA binding Source: BHF-UCL
  • telomeric DNA binding Source: BHF-UCL

GO - Biological processi

  • negative regulation of DNA recombination at telomere Source: UniProtKB
  • negative regulation of telomere maintenance Source: UniProtKB
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • positive regulation of peptidyl-serine phosphorylation Source: UniProtKB
  • positive regulation of protein acetylation Source: UniProtKB
  • protection from non-homologous end joining at telomere Source: BHF-UCL
  • protein localization to chromosome, telomeric region Source: BHF-UCL
  • regulation of double-strand break repair via homologous recombination Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB
  • telomere capping Source: Reactome
  • telomere maintenance Source: BHF-UCL
  • telomere maintenance via telomerase Source: ProtInc
  • telomere maintenance via telomere lengthening Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciZFISH:ENSG00000166848-MONOMER.
ReactomeiR-HSA-1221632. Meiotic synapsis.
R-HSA-171306. Packaging Of Telomere Ends.
R-HSA-2559586. DNA Damage/Telomere Stress Induced Senescence.

Names & Taxonomyi

Protein namesi
Recommended name:
Telomeric repeat-binding factor 2-interacting protein 1
Short name:
TERF2-interacting telomeric protein 1
Short name:
TRF2-interacting telomeric protein 1
Alternative name(s):
Dopamine receptor-interacting protein 5
Repressor/activator protein 1 homolog
Short name:
RAP1 homolog
Short name:
hRap1
Gene namesi
Name:TERF2IP
Synonyms:DRIP5, RAP1
ORF Names:PP8000
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:19246. TERF2IP.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity
  • Chromosome By similarity
  • Chromosometelomere By similarity

  • Note: Associates with chromosomes, both at telomeres and in extratelomeric sites. Also exists as a cytoplasmic form, where it associates with the IKK complex.By similarity

GO - Cellular componenti

  • chromosome, telomeric region Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • nuclear chromosome Source: ProtInc
  • nuclear chromosome, telomeric region Source: BHF-UCL
  • nuclear envelope Source: Ensembl
  • nuclear telomere cap complex Source: BHF-UCL
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • telosome Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus, Telomere

Pathology & Biotechi

Organism-specific databases

DisGeNETi54386.
OpenTargetsiENSG00000166848.
PharmGKBiPA134976325.

Polymorphism and mutation databases

BioMutaiTERF2IP.
DMDMi21542267.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001971262 – 399Telomeric repeat-binding factor 2-interacting protein 1Add BLAST398

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei36PhosphoserineCombined sources1
Modified residuei43PhosphoserineCombined sources1
Cross-linki114Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei154PhosphoserineCombined sources1
Modified residuei156PhosphoserineCombined sources1
Modified residuei203PhosphoserineCombined sources1
Modified residuei206PhosphoserineCombined sources1
Cross-linki212Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki240Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9NYB0.
MaxQBiQ9NYB0.
PaxDbiQ9NYB0.
PeptideAtlasiQ9NYB0.
PRIDEiQ9NYB0.

PTM databases

iPTMnetiQ9NYB0.
PhosphoSitePlusiQ9NYB0.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed.

Gene expression databases

BgeeiENSG00000166848.
CleanExiHS_TERF2IP.
ExpressionAtlasiQ9NYB0. baseline and differential.
GenevisibleiQ9NYB0. HS.

Organism-specific databases

HPAiCAB018660.
CAB018749.
HPA006719.

Interactioni

Subunit structurei

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.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AIMP2Q131552EBI-750109,EBI-745226
AKR1A1P145502EBI-750109,EBI-372388
AKR1B10O602182EBI-750109,EBI-1572139
AKR7A3O951542EBI-750109,EBI-748869
AKT1P317492EBI-750109,EBI-296087
BABAM1Q9NWV82EBI-750109,EBI-745725
BCL7BQ9BQE92EBI-750109,EBI-2560588
C1orf174Q8IYL32EBI-750109,EBI-715898
C9orf78Q9NZ632EBI-750109,EBI-2557577
CALML3P274822EBI-750109,EBI-747537
CHMP2BQ9UQN32EBI-750109,EBI-718324
COTL1Q140192EBI-750109,EBI-79926
CPNE2Q96FN42EBI-750109,EBI-7097057
CRKP461082EBI-750109,EBI-886
CTBP1Q133632EBI-750109,EBI-908846
DHX38Q926202EBI-750109,EBI-1043041
ENAHQ8N8S72EBI-750109,EBI-2834410
EPS8L1Q8TE682EBI-750109,EBI-7487998
FABP2P121042EBI-750109,EBI-3905109
FAM122AQ96E092EBI-750109,EBI-9355758
GAGE5Q130692EBI-750109,EBI-745702
GPKOWQ929172EBI-750109,EBI-746309
HAGHQ167752EBI-750109,EBI-3905342
HMGB3O153472EBI-750109,EBI-2214136
HMGN4O004792EBI-750109,EBI-2867693
HNRNPKP619782EBI-750109,EBI-304185
IL1RNP185102EBI-750109,EBI-1026330
LANCL2Q9NS862EBI-750109,EBI-2510837
MAGOHBQ96A722EBI-750109,EBI-746778
MCM2P497362EBI-750109,EBI-374819
MRTO4Q9UKD22EBI-750109,EBI-1046493
MT1XP802972EBI-750109,EBI-11308402
MT3P257132EBI-750109,EBI-8084264
NASPP493212EBI-750109,EBI-716205
NUDT14O958482EBI-750109,EBI-536866
NUDT18Q6ZVK82EBI-750109,EBI-740486
NUMA1Q149802EBI-750109,EBI-521611
OGFRQ9NZT22EBI-750109,EBI-1044212
PCNPQ8WW122EBI-750109,EBI-10972020
PCP4P485392EBI-750109,EBI-4287270
PEA15Q151212EBI-750109,EBI-714410
PGLSO953362EBI-750109,EBI-11307753
POLD1P283402EBI-750109,EBI-716569
PPP6R3Q5H9R72EBI-750109,EBI-355498
PRXQ9BXM02EBI-750109,EBI-1753064
PTMAP064542EBI-750109,EBI-2682091
RABIFP472242EBI-750109,EBI-713992
RBBP9O758842EBI-750109,EBI-11310604
RGMAQ96B862EBI-750109,EBI-722102
RPP25Q9BUL92EBI-750109,EBI-366570
S100PP258152EBI-750109,EBI-743700
SCLYQ96I152EBI-750109,EBI-2823066
SLX4Q8IY924EBI-750109,EBI-2370740
SMARCC2Q8TAQ22EBI-750109,EBI-357418
TALDO1P378372EBI-750109,EBI-1056712
TBCAO753472EBI-750109,EBI-2686341
TERF2Q1555412EBI-750109,EBI-706637
TINF2Q9BSI4-33EBI-750109,EBI-717418
TMSB4YO146042EBI-750109,EBI-751196
TOR1AIP1Q5JTV82EBI-750109,EBI-2559665
TSSC4Q9Y5U22EBI-750109,EBI-717229
TWF2Q6IBS02EBI-750109,EBI-722204
UCHL1P099362EBI-750109,EBI-714860
VGLL4Q141352EBI-750109,EBI-5278589
WDR5P619642EBI-750109,EBI-540834
XAGE2Q96GT92EBI-750109,EBI-750167
XRCC6P129563EBI-750109,EBI-353208
ZNF414Q96IQ92EBI-750109,EBI-744257

Protein-protein interaction databases

BioGridi119942. 156 interactors.
DIPiDIP-34868N.
IntActiQ9NYB0. 147 interactors.
MINTiMINT-1454139.
STRINGi9606.ENSP00000300086.

Structurei

Secondary structure

1399
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi93 – 97Combined sources5
Helixi138 – 150Combined sources13
Turni155 – 159Combined sources5
Helixi162 – 169Combined sources8
Beta strandi172 – 174Combined sources3
Helixi178 – 187Combined sources10
Helixi308 – 324Combined sources17
Helixi329 – 338Combined sources10
Turni339 – 341Combined sources3
Helixi343 – 352Combined sources10
Helixi364 – 370Combined sources7
Helixi375 – 385Combined sources11
Helixi387 – 397Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FEXNMR-A132-190[»]
3K6GX-ray1.95A/B/C303-399[»]
4RQIX-ray2.44E/F/G/H89-106[»]
ProteinModelPortaliQ9NYB0.
SMRiQ9NYB0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NYB0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini78 – 101BRCTAdd BLAST24
Domaini128 – 188Myb-likeAdd BLAST61

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi383 – 399Nuclear localization signalSequence analysisAdd BLAST17

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi214 – 304Asp/Glu-rich (acidic)Add BLAST91

Sequence similaritiesi

Belongs to the RAP1 family.Curated
Contains 1 BRCT domain.Curated
Contains 1 Myb-like domain.Curated

Phylogenomic databases

eggNOGiENOG410IJNC. Eukaryota.
ENOG4111QPC. LUCA.
GeneTreeiENSGT00390000005351.
HOGENOMiHOG000120115.
HOVERGENiHBG054209.
InParanoidiQ9NYB0.
KOiK11113.
OMAiGFEIHIT.
OrthoDBiEOG091G0NZ2.
PhylomeDBiQ9NYB0.
TreeFamiTF332348.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiIPR001357. BRCT_dom.
IPR009057. Homeodomain-like.
IPR021661. Rap1_C.
IPR015010. Rap1_Myb_dom.
[Graphical view]
PfamiPF16589. BRCT_2. 1 hit.
PF08914. Myb_DNA-bind_2. 1 hit.
PF11626. Rap1_C. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9NYB0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEAMDLGKD PNGPTHSSTL FVRDDGSSMS FYVRPSPAKR RLSTLILHGG
60 70 80 90 100
GTVCRVQEPG AVLLAQPGEA LAEASGDFIS TQYILDCVER NERLELEAYR
110 120 130 140 150
LGPASAADTG SEAKPGALAE GAAEPEPQRH AGRIAFTDAD DVAILTYVKE
160 170 180 190 200
NARSPSSVTG NALWKAMEKS SLTQHSWQSL KDRYLKHLRG QEHKYLLGDA
210 220 230 240 250
PVSPSSQKLK RKAEEDPEAA DSGEPQNKRT PDLPEEEYVK EEIQENEEAV
260 270 280 290 300
KKMLVEATRE FEEVVVDESP PDFEIHITMC DDDPPTPEED SETQPDEEEE
310 320 330 340 350
EEEEKVSQPE VGAAIKIIRQ LMEKFNLDLS TVTQAFLKNS GELEATSAFL
360 370 380 390
ASGQRADGYP IWSRQDDIDL QKDDEDTREA LVKKFGAQNV ARRIEFRKK
Length:399
Mass (Da):44,260
Last modified:October 1, 2000 - v1
Checksum:iEAA615777F9D3D3D
GO

Sequence cautioni

The sequence AAL55783 differs from that shown. Reason: Frameshift at position 151.Curated
The sequence BAA91317 differs from that shown. Reason: Erroneous termination at position 299. Translated as Glu.Curated
The sequence BAG60996 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti83Y → H in BAA91317 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_050195324K → E.Corresponds to variant rs4888444dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF262988 mRNA. Translation: AAF72711.1.
AF250393 mRNA. Translation: AAQ14259.1.
AF289599 mRNA. Translation: AAL55783.1. Frameshift.
AK000669 mRNA. Translation: BAA91317.1. Sequence problems.
AK298880 mRNA. Translation: BAG60996.1. Different initiation.
AC025287 Genomic DNA. No translation available.
CH471114 Genomic DNA. Translation: EAW95616.1.
CH471114 Genomic DNA. Translation: EAW95618.1.
BC004465 mRNA. Translation: AAH04465.1.
BC005841 mRNA. Translation: AAH05841.1.
BC022428 mRNA. Translation: AAH22428.1.
BC078171 mRNA. Translation: AAH78171.1.
CCDSiCCDS32491.1.
RefSeqiNP_061848.2. NM_018975.3.
UniGeneiHs.301419.

Genome annotation databases

EnsembliENST00000300086; ENSP00000300086; ENSG00000166848.
GeneIDi54386.
KEGGihsa:54386.
UCSCiuc002fet.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF262988 mRNA. Translation: AAF72711.1.
AF250393 mRNA. Translation: AAQ14259.1.
AF289599 mRNA. Translation: AAL55783.1. Frameshift.
AK000669 mRNA. Translation: BAA91317.1. Sequence problems.
AK298880 mRNA. Translation: BAG60996.1. Different initiation.
AC025287 Genomic DNA. No translation available.
CH471114 Genomic DNA. Translation: EAW95616.1.
CH471114 Genomic DNA. Translation: EAW95618.1.
BC004465 mRNA. Translation: AAH04465.1.
BC005841 mRNA. Translation: AAH05841.1.
BC022428 mRNA. Translation: AAH22428.1.
BC078171 mRNA. Translation: AAH78171.1.
CCDSiCCDS32491.1.
RefSeqiNP_061848.2. NM_018975.3.
UniGeneiHs.301419.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FEXNMR-A132-190[»]
3K6GX-ray1.95A/B/C303-399[»]
4RQIX-ray2.44E/F/G/H89-106[»]
ProteinModelPortaliQ9NYB0.
SMRiQ9NYB0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119942. 156 interactors.
DIPiDIP-34868N.
IntActiQ9NYB0. 147 interactors.
MINTiMINT-1454139.
STRINGi9606.ENSP00000300086.

PTM databases

iPTMnetiQ9NYB0.
PhosphoSitePlusiQ9NYB0.

Polymorphism and mutation databases

BioMutaiTERF2IP.
DMDMi21542267.

Proteomic databases

EPDiQ9NYB0.
MaxQBiQ9NYB0.
PaxDbiQ9NYB0.
PeptideAtlasiQ9NYB0.
PRIDEiQ9NYB0.

Protocols and materials databases

DNASUi54386.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000300086; ENSP00000300086; ENSG00000166848.
GeneIDi54386.
KEGGihsa:54386.
UCSCiuc002fet.3. human.

Organism-specific databases

CTDi54386.
DisGeNETi54386.
GeneCardsiTERF2IP.
HGNCiHGNC:19246. TERF2IP.
HPAiCAB018660.
CAB018749.
HPA006719.
MIMi605061. gene.
neXtProtiNX_Q9NYB0.
OpenTargetsiENSG00000166848.
PharmGKBiPA134976325.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJNC. Eukaryota.
ENOG4111QPC. LUCA.
GeneTreeiENSGT00390000005351.
HOGENOMiHOG000120115.
HOVERGENiHBG054209.
InParanoidiQ9NYB0.
KOiK11113.
OMAiGFEIHIT.
OrthoDBiEOG091G0NZ2.
PhylomeDBiQ9NYB0.
TreeFamiTF332348.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000166848-MONOMER.
ReactomeiR-HSA-1221632. Meiotic synapsis.
R-HSA-171306. Packaging Of Telomere Ends.
R-HSA-2559586. DNA Damage/Telomere Stress Induced Senescence.

Miscellaneous databases

ChiTaRSiTERF2IP. human.
EvolutionaryTraceiQ9NYB0.
GeneWikiiTERF2IP.
GenomeRNAii54386.
PROiQ9NYB0.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000166848.
CleanExiHS_TERF2IP.
ExpressionAtlasiQ9NYB0. baseline and differential.
GenevisibleiQ9NYB0. HS.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiIPR001357. BRCT_dom.
IPR009057. Homeodomain-like.
IPR021661. Rap1_C.
IPR015010. Rap1_Myb_dom.
[Graphical view]
PfamiPF16589. BRCT_2. 1 hit.
PF08914. Myb_DNA-bind_2. 1 hit.
PF11626. Rap1_C. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiTE2IP_HUMAN
AccessioniPrimary (citable) accession number: Q9NYB0
Secondary accession number(s): B4DQN4
, Q4W4Y2, Q8WYZ3, Q9NWR2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: October 1, 2000
Last modified: November 2, 2016
This is version 166 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Shares a bidirectional promoter with KARS.1 Publication

Caution

Was reported to participate in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair in the absence of TERF2 (PubMed:19763083). However, this probably does not corresponds to its primary function and experiments in mouse showed that it is dispensible for such process and is required for repressiion of homology-directed repair (HDR).1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.