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Q91VL8 (TE2IP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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):
Repressor/activator protein 1 homolog
Short name=RAP1 homolog
Gene names
Name:Terf2ip
Synonyms:Rap1
ORF Names:MNCb-0448, MNCb-0628
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.8 Ref.9 Ref.10

Subunit structure

Homodimer. Component of the shelterin complex (telosome) composed of TERF1, TERF2, TINF2, TERF2IP ACD and POT1. Binds to TERF2 (but not TERF1) with its C-terminus. Interacts with SLX4/BTBD12 By similarity. Interacts with TERF2; the interaction is direct. Does not interact with TERF1. Associates with the I-kappa-B-kinase (IKK) core complex, composed of CHUK, IKBKB and IKBKG. Ref.9 Ref.10

Subcellular location

Nucleus. Cytoplasm. Chromosome. Chromosometelomere. Note: Associates with chromosomes, both at telomeres and in extratelomeric sites. Also exists as a cytoplasmic form, where it associates with the IKK complex. Ref.8 Ref.9 Ref.10

Disruption phenotype

Mice are viable and fertile. No major telomere dysfunction such as telomere fusions are observed. An increased telomere fragility and recombination due to defects in HDR are however present. Mice with conditional deletion in stratified epithelia display shorter telomeres and developed skin hyperpigmentation in adulthood. Ref.8 Ref.10

Miscellaneous

Shares a bidirectional promoter with KARS (Ref.5). This shared promoter with an essential gene complicated the task when generating knockout mice; the problem was overcome by generating conditional knockout strategies (Ref.10 and Ref.8;).

Sequence similarities

Belongs to the RAP1 family.

Contains 1 BRCT domain.

Contains 1 Myb-like domain.

Sequence caution

The sequence BAA95043.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentChromosome
Cytoplasm
Nucleus
Telomere
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of DNA recombination at telomere

Inferred from mutant phenotype Ref.10Ref.8. Source: UniProtKB

negative regulation of telomere maintenance

Inferred from electronic annotation. Source: Ensembl

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from direct assay Ref.9. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from mutant phenotype Ref.9. Source: UniProtKB

protein localization to chromosome, telomeric region

Inferred from electronic annotation. Source: Ensembl

regulation of double-strand break repair via homologous recombination

Inferred from mutant phenotype Ref.10. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.8. Source: UniProtKB

telomere maintenance via telomere lengthening

Inferred from mutant phenotype Ref.10Ref.8. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentMre11 complex

Inferred from electronic annotation. Source: Ensembl

chromosome, telomeric region

Inferred from direct assay Ref.10. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.9. Source: UniProtKB

nuclear chromosome, telomeric region

Inferred from direct assay PubMed 15968270. Source: MGI

nuclear telomere cap complex

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 393392Telomeric repeat-binding factor 2-interacting protein 1
PRO_0000197127

Regions

Domain78 – 10124BRCT
Domain125 – 18561Myb-like
Motif377 – 39317Nuclear localization signal Potential
Compositional bias232 – 29766Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue361Phosphoserine By similarity
Modified residue1511Phosphoserine By similarity
Modified residue1531Phosphoserine By similarity
Modified residue2001Phosphoserine By similarity

Experimental info

Sequence conflict281 – 2866PTPEED → HTHTQS in BAA95042. Ref.4
Sequence conflict281 – 2866PTPEED → HTHTQS in BAA95043. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q91VL8 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 7A15CFD83733BE2D

FASTA39343,353
        10         20         30         40         50         60 
MAEAMDLGKD PNGPTHSSTL FVREDGSAMS FYVRPSSAKR RLSTLILHGG GTVCRVQEPG 

        70         80         90        100        110        120 
AVLLAQPGEA LAEASGDFIS TQYILDCVDR NEKLDLEAYR LGLTEQASDP KPGASTEGST 

       130        140        150        160        170        180 
EPEPQPLTGR IAYTDAEDVA ILTYVKENAR SPSSVTGNAL WKAMEKSSLT QHSWQSLKDR 

       190        200        210        220        230        240 
YLKHLRGQEH KYLLGNAPVS PSSQKLKRKA EQDPEAADSG EPQNKRAPDL PEEECVKGEI 

       250        260        270        280        290        300 
KENGEADNKL FEEAAPEFGE AVVDESPDFE IHITMCDGDP PTPEEDSETQ PDEEEEEPKV 

       310        320        330        340        350        360 
STQEVGTAIK VIRQLMEKFN LDLSTVTQAL LKNSGELEAT SSFLESGRRP DGYPIWCRQD 

       370        380        390 
DLDLQKDDDD TKNALVKKFG AQNVARRIEF RKK 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Eye, Head, Heart, Ovary, Oviduct, Pancreas, Testis and Thymus.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary tumor.
[4]"Isolation of full-length cDNA clones from mouse brain cDNA library made by oligo-capping method."
Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-286.
Strain: C57BL/6.
Tissue: Brain.
[5]"The telomeric protein Rap1 is conserved in vertebrates and is expressed from a bidirectional promoter positioned between the Rap1 and KARS genes."
Tan M., Wei C., Price C.M.
Gene 323:1-10(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: BIDIRECTIONAL PROMOTER WITH KARS.
[6]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[7]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[8]"Mammalian Rap1 controls telomere function and gene expression through binding to telomeric and extratelomeric sites."
Martinez P., Thanasoula M., Carlos A.R., Gomez-Lopez G., Tejera A.M., Schoeftner S., Dominguez O., Pisano D.G., Tarsounas M., Blasco M.A.
Nat. Cell Biol. 12:768-780(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
[9]"Telomere-independent Rap1 is an IKK adaptor and regulates NF-kappaB-dependent gene expression."
Teo H., Ghosh S., Luesch H., Ghosh A., Wong E.T., Malik N., Orth A., de Jesus P., Perry A.S., Oliver J.D., Tran N.L., Speiser L.J., Wong M., Saez E., Schultz P., Chanda S.K., Verma I.M., Tergaonkar V.
Nat. Cell Biol. 12:758-767(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NF-KAPPA-B PATHWAY, SUBCELLULAR LOCATION, INTERACTION WITH TERF2; CHUK; IKBKB AND IKBKG.
[10]"Loss of Rap1 induces telomere recombination in the absence of NHEJ or a DNA damage signal."
Sfeir A., Kabir S., van Overbeek M., Celli G.B., de Lange T.
Science 327:1657-1661(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, INTERACTION WITH TERF2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK041613 mRNA. Translation: BAC31005.1.
AK051818 mRNA. Translation: BAC34781.1.
AK081557 mRNA. Translation: BAC38258.1.
AK087729 mRNA. Translation: BAC39985.1.
AK084563 mRNA. Translation: BAC39217.1.
AK148508 mRNA. Translation: BAE28592.1.
AK148537 mRNA. Translation: BAE28607.1.
AK161452 mRNA. Translation: BAE36404.1.
AK165074 mRNA. Translation: BAE38026.1.
AC114648 Genomic DNA. No translation available.
BC012270 mRNA. Translation: AAH12270.1.
BC017641 mRNA. Translation: AAH17641.1.
AB041557 mRNA. Translation: BAA95042.1.
AB041559 mRNA. Translation: BAA95043.1. Different initiation.
RefSeqNP_065609.2. NM_020584.2.
UniGeneMm.213064.

3D structure databases

ProteinModelPortalQ91VL8.
SMRQ91VL8. Positions 19-100, 129-187, 300-392.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ91VL8. 2 interactions.
MINTMINT-4137361.

PTM databases

PhosphoSiteQ91VL8.

Proteomic databases

PaxDbQ91VL8.
PRIDEQ91VL8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000052138; ENSMUSP00000052170; ENSMUSG00000033430.
GeneID57321.
KEGGmmu:57321.
UCSCuc012gla.1. mouse.

Organism-specific databases

CTD54386.
MGIMGI:1929871. Terf2ip.

Phylogenomic databases

eggNOGNOG39788.
GeneTreeENSGT00390000005351.
HOGENOMHOG000120115.
HOVERGENHBG054209.
InParanoidQ8C2Y1.
KOK11113.
OMASISFYVR.
OrthoDBEOG7KDFBG.
PhylomeDBQ91VL8.
TreeFamTF332348.

Enzyme and pathway databases

ReactomeREACT_188804. Cell Cycle.
REACT_198624. Meiosis.
REACT_75800. Meiotic Synapsis.

Gene expression databases

BgeeQ91VL8.
GenevestigatorQ91VL8.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
InterProIPR009057. Homeodomain-like.
IPR021661. Rap1_C.
IPR015010. Rap1_Myb_dom.
[Graphical view]
PfamPF08914. Myb_DNA-bind_2. 1 hit.
PF11626. Rap1_C. 1 hit.
[Graphical view]
SUPFAMSSF46689. SSF46689. 1 hit.
ProtoNetSearch...

Other

ChiTaRSTERF2IP. mouse.
NextBio313686.
PROQ91VL8.
SOURCESearch...

Entry information

Entry nameTE2IP_MOUSE
AccessionPrimary (citable) accession number: Q91VL8
Secondary accession number(s): D3YWE8 expand/collapse secondary AC list , Q543F4, Q8C2Y1, Q9JJE8, Q9JJE9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot