TTI1_MOUSE
ID TTI1_MOUSE Reviewed; 1085 AA.
AC Q91V83; Q7TS79; Q9CSY0;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=TELO2-interacting protein 1 homolog;
GN Name=Tti1;
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 [MRNA].
RC STRAIN=ILS, and ISS;
RX PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT "High-throughput sequence identification of gene coding variants within
RT alcohol-related QTLs.";
RL Mamm. Genome 12:657-663(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
RN [5]
RP PROTEIN SEQUENCE OF 951-964, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 997-1085.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. Promotes
CC assembly, stabilizes and maintains the activity of mTORC1 and mTORC2
CC complexes, which regulate cell growth and survival in response to
CC nutrient and hormonal signals (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the TTT complex composed of TELO2, TTI1 and TTI2.
CC Interacts with ATM, ATR, MTOR, PRKDC, SMG1, TELO2, TRRAP AND TTI2.
CC Component of the mTORC1 and mTORC2 complexes. Interacts with WAC; WAC
CC positively regulates MTOR activity by promoting the assembly of the TTT
CC complex and the RUVBL complex composed of RUVBL1 and RUVBL2 into the
CC TTT-RUVBL complex which leads to the dimerization of the mTORC1 complex
CC and its subsequent activation. {ECO:0000250|UniProtKB:O43156}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Phosphorylated at Ser-823 by CK2 following growth factor
CC deprivation, leading to its subsequent ubiquitination by the SCF(FBXO9)
CC complex. Phosphorylation by CK2 only takes place when TELO2 is bound to
CC mTORC1, not mTORC2; leading to selective ubiquitination of mTORC1-
CC associated protein (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated by the SCF(FBXO9) complex following phosphorylation
CC by CK2 in response to growth factor deprivation, leading to its
CC degradation by the proteasome. Only mTORC1-associated protein is
CC ubiquitinated and degraded, leading to selective inactivation of mTORC1
CC to restrain cell growth and protein translation, while mTORC2 is
CC activated due to the relief of feedback inhibition by mTORC1 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tti1 family. {ECO:0000305}.
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DR EMBL; AF332067; AAK56095.1; -; mRNA.
DR EMBL; AF332068; AAK56096.1; -; mRNA.
DR EMBL; AL663092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL845511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466551; EDL06248.1; -; Genomic_DNA.
DR EMBL; BC053067; AAH53067.1; -; mRNA.
DR EMBL; AK011692; BAB27782.1; -; mRNA.
DR CCDS; CCDS16983.1; -.
DR RefSeq; NP_083558.1; NM_029282.1.
DR RefSeq; XP_006500395.1; XM_006500332.2.
DR RefSeq; XP_011238128.1; XM_011239826.2.
DR AlphaFoldDB; Q91V83; -.
DR STRING; 10090.ENSMUSP00000029179; -.
DR iPTMnet; Q91V83; -.
DR PhosphoSitePlus; Q91V83; -.
DR EPD; Q91V83; -.
DR jPOST; Q91V83; -.
DR MaxQB; Q91V83; -.
DR PaxDb; Q91V83; -.
DR PeptideAtlas; Q91V83; -.
DR PRIDE; Q91V83; -.
DR ProteomicsDB; 297679; -.
DR Antibodypedia; 57267; 133 antibodies from 22 providers.
DR DNASU; 75425; -.
DR Ensembl; ENSMUST00000029179; ENSMUSP00000029179; ENSMUSG00000027650.
DR Ensembl; ENSMUST00000109522; ENSMUSP00000105148; ENSMUSG00000027650.
DR GeneID; 75425; -.
DR KEGG; mmu:75425; -.
DR UCSC; uc008npj.1; mouse.
DR CTD; 9675; -.
DR MGI; MGI:1922675; Tti1.
DR VEuPathDB; HostDB:ENSMUSG00000027650; -.
DR eggNOG; KOG4524; Eukaryota.
DR GeneTree; ENSGT00390000009748; -.
DR HOGENOM; CLU_004815_0_0_1; -.
DR InParanoid; Q91V83; -.
DR OMA; GAHTCQV; -.
DR OrthoDB; 89960at2759; -.
DR PhylomeDB; Q91V83; -.
DR TreeFam; TF315296; -.
DR BioGRID-ORCS; 75425; 20 hits in 57 CRISPR screens.
DR ChiTaRS; Tti1; mouse.
DR PRO; PR:Q91V83; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q91V83; protein.
DR Bgee; ENSMUSG00000027650; Expressed in animal zygote and 246 other tissues.
DR ExpressionAtlas; Q91V83; baseline and differential.
DR Genevisible; Q91V83; MM.
DR GO; GO:0070209; C:ASTRA complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031931; C:TORC1 complex; ISS:UniProtKB.
DR GO; GO:0031932; C:TORC2 complex; ISS:UniProtKB.
DR GO; GO:0110078; C:TTT complex; ISO:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0032006; P:regulation of TOR signaling; ISS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR016441; Tti1.
DR PIRSF; PIRSF005250; UCP005250; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..1085
FT /note="TELO2-interacting protein 1 homolog"
FT /id="PRO_0000050752"
FT REGION 777..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..844
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43156"
FT MOD_RES 823
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:O43156"
FT CONFLICT 216
FT /note="A -> V (in Ref. 1; AAK56095/AAK56096)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1085 AA; 120814 MW; BB4CC0F849BC05E4 CRC64;
MAVFDTPEEA FGVLRPVCVQ LTKTQTVENV EHLQTQLQAI SDTALQELQQ YILFPLRFAL
KTPGPKRERL VQSVVECLTF VLSSTCVREQ ELLQELFSEL SACLYSPSSQ KPAALSEELK
LAVIQGLSTL MHSAYRDIIL TFYEPSILPR LGFAVSLLLG LAEQEKSKQI KIAALQCLQV
LLLQCDCQDH PRPLDELEQQ QLGDLLASFL PGISTALTRI ITGDFKQGHS IVVSSLKVFY
KTVGFIMADE QLTRIPKAQA KPVVEHRVAA LMIHREADWV KSTGDKLAIF IKKIIDCVSV
HPHWKVRLEL VEFVEILLLK CTQSLVESTG PLLKVLVGLV NDESPEVQAR CSTVLRRLAD
QKVVVGSRAL ADILSESLHS LATSLPRLMN TQDDQGKFST LSLLLGYLKL LGPKVHVILN
SVAHVQRLSR ALIQVLELEV TDVKMVEERR WNSDNLSASA EVSAARPWSR VQRRYFRCFT
DERVFLLLRK ICQLLGYYGD LYLLVDHFME LYHTSVVYRK QAAMILNELV VGAAGLDVED
IHNKCPSMGP EELREIVKSI LEEYTSQENW YLITCFEAEE GEEVMMKQQG FQAVTSGVHT
CQVVSFPALS KPSPTICSMN SNIWQICIQL EGIGQFAYAL GKDFRLLLMS ALYPILEKAG
DPTLLISQVA TSTMVDICHA CGYNSVQHLI NQNSDYLVNG ISLNLRHLAL HPHAPKVLEA
MLRNADASLL PLVADVVQDV LATLDQFYDK RAASFVSVLH ALLAALAHWF PDSGSTGQLQ
QRSLEEEGRQ LPAAGEASTT AEDIEQFVLS YLQEKDVAEG NVSDLEAEEE VQSAPPKVDE
NDTLPDVEPP LPTHIQIAKD VMERCIHLSA DKNLKIRLKV LDVLGLCVEV LQTHKNQLLP
LAHRAWPSLV HRLTSDDPLA VLRAFKVLQT LGSRCGDFLR SRFCKDVLPK LTSSLITQAP
ISARAGPVYS HTLAFKLQLA VLQGLGPLCE NLDLGEGDLN KVADACVIYL STKQPVKLQE
AARSVFLHLM RVDPDSTWLL LHELYCPVQQ FTAPHPSLHP VQLQGATQPQ NPYATNVCHL
LLQLQ
