Q91VL8 (TE2IP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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):
Repressor/activator protein 1 homolog
Short name=RAP1 homolog

Gene names

Name:	Terf2ip
Synonyms:	Rap1
ORF Names:	MNCb-0448, MNCb-0628

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	393 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Chromosome › telomere. 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.7). 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 process	Transcription Transcription regulation
Cellular component	Chromosome Cytoplasm Nucleus Telomere
Molecular function	Activator
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative 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: Compara positive regulation of I-kappaB kinase/NF-kappaB cascade 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: Compara regulation of double-strand break repair via homologous recombination Inferred from mutant phenotype Ref.10. Source: UniProtKB telomere maintenance via telomere lengthening Inferred from mutant phenotype Ref.10Ref.8. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Mre11 complex Inferred from electronic annotation. Source: Compara 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: Compara nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 393	393	Telomeric repeat-binding factor 2-interacting protein 1		PRO_0000197127
Regions
	Domain	78 – 101	24	BRCT
	Domain	125 – 185	61	Myb-like
	Motif	377 – 393	17	Nuclear localization signal Potential
	Compositional bias	232 – 297	66	Asp/Glu-rich (acidic)
Amino acid modifications
	Modified residue	36	1	Phosphoserine By similarity
	Modified residue	151	1	Phosphoserine By similarity
	Modified residue	153	1	Phosphoserine By similarity
	Modified residue	200	1	Phosphoserine Ref.5 Ref.6
Experimental info
	Sequence conflict	281 – 286	6	PTPEED → HTHTQS in BAA95042. Ref.4
	Sequence conflict	281 – 286	6	PTPEED → HTHTQS in BAA95043. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q91VL8 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 7A15CFD83733BE2D	FASTA	393	43,353
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, MASS SPECTROMETRY. Tissue: Embryonic brain.
[6]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, MASS SPECTROMETRY. Tissue: Liver.
[7]	"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.
[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.
IPI	IPI00127014.
RefSeq	NP_065609.2. NM_020584.2.
UniGene	Mm.213064.
3D structure databases
ProteinModelPortal	Q91VL8.
SMR	Q91VL8. Positions 129-187, 300-392.
ModBase	Search...
PTM databases
PhosphoSite	Q91VL8.
Proteomic databases
PaxDb	Q91VL8.
PRIDE	Q91VL8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000052138; ENSMUSP00000052170; ENSMUSG00000033430.
GeneID	57321.
KEGG	mmu:57321.
UCSC	uc012gla.1. mouse.
Organism-specific databases
CTD	54386.
MGI	MGI:1929871. Terf2ip.
Phylogenomic databases
eggNOG	NOG39788.
GeneTree	ENSGT00390000005351.
HOGENOM	HOG000120115.
HOVERGEN	HBG054209.
InParanoid	Q8C2Y1.
KO	K11113.
OMA	SISFYVR.
OrthoDB	EOG4K6G59.
Enzyme and pathway databases
Reactome	REACT_118161. Cell Cycle. REACT_120463. Meiosis. REACT_75800. Meiotic Synapsis (mouse).
Gene expression databases
Bgee	Q91VL8.
Genevestigator	Q91VL8.
GermOnline	ENSMUSG00000033430. Mus musculus.
Family and domain databases
Gene3D	1.10.10.60. 1 hit.
InterPro	IPR009057. Homeodomain-like. IPR015010. Rap1_Myb_dom. [Graphical view]
Pfam	PF08914. Myb_DNA-bind_2. 1 hit. [Graphical view]
SUPFAM	SSF46689. Homeodomain_like. 1 hit.
PROSITE	PS50172. BRCT. False negative. PS50090. MYB_LIKE. False negative. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	TERF2IP. mouse.
NextBio	313686.
SOURCE	Search...

Entry information

Entry name

TE2IP_MOUSE

Accession

Primary (citable) accession number: Q91VL8
Secondary accession number(s): D3YWE8 , Q543F4, Q8C2Y1, Q9JJE8, Q9JJE9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2002
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program