TTI2_MOUSE
ID TTI2_MOUSE Reviewed; 512 AA.
AC Q8BGV4; Q3UTH3; Q8VE31;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=TELO2-interacting protein 2;
GN Name=Tti2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, and Corpora quadrigemina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Regulator of the DNA damage response (DDR). Part of the TTT
CC complex that is required to stabilize protein levels of the
CC phosphatidylinositol 3-kinase-related protein kinase (PIKK) family
CC proteins. The TTT complex is involved in the cellular resistance to DNA
CC damage stresses, like ionizing radiation (IR), ultraviolet (UV) and
CC mitomycin C (MMC). Together with the TTT complex and HSP90 may
CC participate in the proper folding of newly synthesized PIKKs (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the TTT complex composed of TELO2, TTI1 and TTI2.
CC Interacts with TELO2 and TTI1. Interacts with WAC; WAC positively
CC regulates MTOR activity by promoting the assembly of the TTT complex
CC and the RUVBL complex composed of RUVBL1 and RUVBL2 into the TTT-RUVBL
CC complex which leads to the dimerization of the mTORC1 complex and its
CC subsequent activation. {ECO:0000250|UniProtKB:Q6NXR4}.
CC -!- SIMILARITY: Belongs to the TTI2 family. {ECO:0000305}.
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DR EMBL; AK045392; BAC32341.1; -; mRNA.
DR EMBL; AK046031; BAC32576.1; -; mRNA.
DR EMBL; AK139425; BAE24007.1; -; mRNA.
DR EMBL; BC019943; AAH19943.1; -; mRNA.
DR CCDS; CCDS22221.1; -.
DR RefSeq; NP_659176.2; NM_144927.3.
DR AlphaFoldDB; Q8BGV4; -.
DR STRING; 10090.ENSMUSP00000096441; -.
DR iPTMnet; Q8BGV4; -.
DR PhosphoSitePlus; Q8BGV4; -.
DR EPD; Q8BGV4; -.
DR MaxQB; Q8BGV4; -.
DR PaxDb; Q8BGV4; -.
DR PeptideAtlas; Q8BGV4; -.
DR PRIDE; Q8BGV4; -.
DR ProteomicsDB; 297680; -.
DR Antibodypedia; 10728; 52 antibodies from 17 providers.
DR Ensembl; ENSMUST00000098842; ENSMUSP00000096441; ENSMUSG00000031577.
DR Ensembl; ENSMUST00000209851; ENSMUSP00000148056; ENSMUSG00000031577.
DR Ensembl; ENSMUST00000209986; ENSMUSP00000147846; ENSMUSG00000031577.
DR GeneID; 234138; -.
DR KEGG; mmu:234138; -.
DR UCSC; uc009ljf.2; mouse.
DR CTD; 80185; -.
DR MGI; MGI:2384576; Tti2.
DR VEuPathDB; HostDB:ENSMUSG00000031577; -.
DR eggNOG; ENOG502QVMM; Eukaryota.
DR GeneTree; ENSGT00390000003878; -.
DR HOGENOM; CLU_047507_0_0_1; -.
DR InParanoid; Q8BGV4; -.
DR OMA; WDVHTDQ; -.
DR PhylomeDB; Q8BGV4; -.
DR TreeFam; TF328871; -.
DR BioGRID-ORCS; 234138; 23 hits in 75 CRISPR screens.
DR ChiTaRS; Tti2; mouse.
DR PRO; PR:Q8BGV4; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8BGV4; protein.
DR Bgee; ENSMUSG00000031577; Expressed in ear vesicle and 225 other tissues.
DR ExpressionAtlas; Q8BGV4; baseline and differential.
DR Genevisible; Q8BGV4; MM.
DR GO; GO:0070209; C:ASTRA complex; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0110078; C:TTT complex; ISO:MGI.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR018870; Tti2.
DR PANTHER; PTHR32226; PTHR32226; 1.
DR Pfam; PF10521; Tti2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 2: Evidence at transcript level;
KW Reference proteome.
FT CHAIN 1..512
FT /note="TELO2-interacting protein 2"
FT /id="PRO_0000279415"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 31
FT /note="K -> R (in Ref. 1; BAE24007)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="H -> P (in Ref. 2; AAH19943)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 56702 MW; 6C3101225DCE1F5E CRC64;
MKLDSAEEKS GVGCSLPAEG SPPALEPAFS KILNRLSRPK SSGQGGARNA ALKDLGALIE
AAEGDRFFEG SGSGGSLRGM PEILGQVVRA LEKFAAPEEK ADGVEEHPEV PEKATEVGSL
FLKLLGKVEA AKSSPDCPAW KTGLRHMSGP VYIFAITHRL KQPWTSPASQ HVAGEVLSLL
LRVTECSSVA GFLCGENEDD RGRFAVVLGL LKPHLNKETW KKNPAVKHVF SWTLQQVTQP
WLNQHLEKIL PPSLLISDDY QTENKILGVQ CLHHIVVTVP AADLLQYNRA QVLYHALFNH
LYMPEHHLIQ AVLLCLLDLF PVLEKALHWK GDTARVTTHC HEVLQLILTH MEPEHRLLLR
RTYARHLPAF VKRLGILTVR HLKRLEQVIL GYLEVYDEPE DETRLKILET LKLVMQYTWP
RIPCRVVVLL KALLKLICDI SRDTIPTTEA AKSTMLQEAT DCLILLDHCS QGQVKGLLAK
IAVSCEDSTV VSCIRKVQQG SADSPGDDTE GD
