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Q9QXG9 (TINF2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
TERF1-interacting nuclear factor 2
Alternative name(s):
TRF1-interacting nuclear protein 2
Gene names
Name:Tinf2
Synonyms:Tin2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Plays a role in shelterin complex assembly By similarity.

Subunit structure

Monomer. Found in a complex with POT1; TERF1 and TNKS1. Component of the shelterin complex (telosome) composed of TERF1, TERF2, TINF2, TERF2IP, ACD and POT1 By similarity. Interacts with TERF1. Ref.3

Subcellular location

Nucleus By similarity. Chromosometelomere By similarity.

Domain

The TBM domain mediates interaction with TERF1 By similarity.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 341340TERF1-interacting nuclear factor 2
PRO_0000072542

Regions

Motif243 – 26523TBM
Motif249 – 2557Nuclear localization signal Potential

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Experimental info

Sequence conflict3371S → G in AAF23504. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9QXG9 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 41A07CE00DC2B4D7

FASTA34137,887
        10         20         30         40         50         60 
MAPPPGVGPA SLRFAAAASW LVVRRRRVEH FPKVVEFLQS LRAAAPGLVC YRHHERLCMS 

        70         80         90        100        110        120 
LKAKVVVELI LQARPWDQVL NALKHHFPAE SRTTKEDRKL LEARENFCLL VKHLSEDPPS 

       130        140        150        160        170        180 
SLQELEQDYG ESFLVAMEKL LFEYLCQLEK ALPPVRAQEL QDALSWSQPG SFITSSVALH 

       190        200        210        220        230        240 
QYGMDMGWTF PESSTSGSGN LIEPMEESPH QQTRPAFHSP LPKAKLGPHQ PASLEHPEHL 

       250        260        270        280        290        300 
AGHRFNLAPL GKRKSRSHWT SAKACHKERP TVMLLPFRNM GLPAQDLSNP KSREEPGAAS 

       310        320        330        340 
AASVGTEPVC TEEAKTPSRP LGKRALEETP PDSPAASRRT V 

« Hide

References

« Hide 'large scale' references
[1]"TIN2 regulates telomere length in mouse cells."
Cheong C., Lee H.-W.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Ovary and Uterus.
[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]"GNL3L stabilizes the TRF1 complex and promotes mitotic transition."
Zhu Q., Meng L., Hsu J.K., Lin T., Teishima J., Tsai R.Y.
J. Cell Biol. 185:827-839(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TERF1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF214013 mRNA. Translation: AAF23504.1.
CT025679 Genomic DNA. No translation available.
UniGeneMm.29346.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9QXG9. 1 interaction.
STRING10090.ENSMUSP00000098104.

PTM databases

PhosphoSiteQ9QXG9.

Proteomic databases

PRIDEQ9QXG9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:107246. Tinf2.

Phylogenomic databases

eggNOGNOG43106.
HOVERGENHBG057120.
InParanoidQ9QXG9.

Enzyme and pathway databases

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

Gene expression databases

CleanExMM_TINF2.
GenevestigatorQ9QXG9.

Family and domain databases

ProtoNetSearch...

Other

PROQ9QXG9.
SOURCESearch...

Entry information

Entry nameTINF2_MOUSE
AccessionPrimary (citable) accession number: Q9QXG9
Secondary accession number(s): E9Q126
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: July 27, 2011
Last modified: March 19, 2014
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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