TIRR_MOUSE
ID TIRR_MOUSE Reviewed; 211 AA.
AC Q8VHN8; Q3TW47; Q8R039; Q8R3D9; Q9CR90; Q9D8M0;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Tudor-interacting repair regulator protein {ECO:0000250|UniProtKB:Q9BRJ7};
DE AltName: Full=NUDT16-like protein 1 {ECO:0000312|MGI:MGI:1914161};
DE AltName: Full=Protein syndesmos {ECO:0000303|PubMed:11805099};
GN Name=Nudt16l1 {ECO:0000312|MGI:MGI:1914161};
GN Synonyms=Sdos {ECO:0000303|PubMed:11805099},
GN Tirr {ECO:0000250|UniProtKB:Q9BRJ7};
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] (ISOFORM 1), AND INTERACTION WITH SDC4; TGFB1I1
RP AND PXN.
RX PubMed=11805099; DOI=10.1074/jbc.m110291200;
RA Denhez F., Wilcox-Adelman S.A., Baciu P.C., Saoncella S., Lee S.,
RA French B., Neveu W., Goetinck P.F.;
RT "Syndesmos, a syndecan-4 cytoplasmic domain interactor, binds to the focal
RT adhesion adaptor proteins paxillin and Hic-5.";
RL J. Biol. Chem. 277:12270-12274(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Pancreas;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=FVB/N; TISSUE=Mammary gland, and 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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
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).
RN [5] {ECO:0007744|PDB:4ZG0}
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 8-204, AND SUBUNIT.
RX PubMed=26100207; DOI=10.1016/j.bbrc.2015.06.010;
RA Kim H., Yoo J., Lee I., Kang Y.J., Cho H.S., Lee W.;
RT "Crystal structure of syndesmos and its interaction with Syndecan-4
RT proteoglycan.";
RL Biochem. Biophys. Res. Commun. 463:762-767(2015).
CC -!- FUNCTION: Key regulator of TP53BP1 required to stabilize TP53BP1 and
CC regulate its recruitment to chromatin. In absence of DNA damage,
CC interacts with the tandem Tudor-like domain of TP53BP1, masking the
CC region that binds histone H4 dimethylated at 'Lys-20' (H4K20me2),
CC thereby preventing TP53BP1 recruitment to chromatin and maintaining
CC TP53BP1 localization to the nucleus. Following DNA damage, ATM-induced
CC phosphorylation of TP53BP1 and subsequent recruitment of RIF1 leads to
CC dissociate NUDT16L1/TIRR from TP53BP1, unmasking the tandem Tudor-like
CC domain and allowing recruitment of TP53BP1 to DNA double strand breaks
CC (DSBs). Binds U8 snoRNA. {ECO:0000250|UniProtKB:Q9BRJ7}.
CC -!- SUBUNIT: Homodimer (PubMed:26100207). Interacts with TP53BP1 (via the
CC Tudor-like domain); interaction is abolished following DNA damage and
CC TP53BP1 phosphorylation by ATM (By similarity). Interacts (via the
CC cytoplasmic part) with SDC4 (PubMed:11805099). Interacts with TGFB1I1
CC and PXN (PubMed:11805099). {ECO:0000250|UniProtKB:Q9BRJ7,
CC ECO:0000269|PubMed:11805099, ECO:0000269|PubMed:26100207}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BRJ7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8VHN8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VHN8-2; Sequence=VSP_014279;
CC Name=3;
CC IsoId=Q8VHN8-3; Sequence=VSP_014277, VSP_014278;
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. TIRR subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Although strongly related to the nudix NUDT16 protein, lacks
CC the Nudix box and is therefore not related to the rest of the family.
CC Lacks a number of residues which are necessary for hydrolase activity
CC and does not play a role in U8 snoRNA decapping activity.
CC {ECO:0000305}.
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DR EMBL; AF435792; AAL57490.1; -; mRNA.
DR EMBL; AK002378; BAB22055.1; -; mRNA.
DR EMBL; AK003241; BAB22662.1; -; mRNA.
DR EMBL; AK007897; BAB25336.1; -; mRNA.
DR EMBL; AK159841; BAE35419.1; -; mRNA.
DR EMBL; BC025569; AAH25569.1; -; mRNA.
DR EMBL; BC028494; AAH28494.1; -; mRNA.
DR CCDS; CCDS27927.1; -. [Q8VHN8-1]
DR CCDS; CCDS88870.1; -. [Q8VHN8-3]
DR RefSeq; NP_001303644.1; NM_001316715.1. [Q8VHN8-3]
DR RefSeq; NP_080115.1; NM_025839.4. [Q8VHN8-1]
DR PDB; 4ZG0; X-ray; 2.01 A; A/B=8-204.
DR PDB; 5Z78; X-ray; 1.76 A; A/B=6-211.
DR PDBsum; 4ZG0; -.
DR PDBsum; 5Z78; -.
DR AlphaFoldDB; Q8VHN8; -.
DR SMR; Q8VHN8; -.
DR BioGRID; 211803; 5.
DR STRING; 10090.ENSMUSP00000054201; -.
DR iPTMnet; Q8VHN8; -.
DR PhosphoSitePlus; Q8VHN8; -.
DR SwissPalm; Q8VHN8; -.
DR EPD; Q8VHN8; -.
DR MaxQB; Q8VHN8; -.
DR PaxDb; Q8VHN8; -.
DR PeptideAtlas; Q8VHN8; -.
DR PRIDE; Q8VHN8; -.
DR ProteomicsDB; 258887; -. [Q8VHN8-1]
DR ProteomicsDB; 258888; -. [Q8VHN8-2]
DR ProteomicsDB; 258889; -. [Q8VHN8-3]
DR Antibodypedia; 24391; 60 antibodies from 17 providers.
DR DNASU; 66911; -.
DR Ensembl; ENSMUST00000050881; ENSMUSP00000054201; ENSMUSG00000022516. [Q8VHN8-3]
DR Ensembl; ENSMUST00000230931; ENSMUSP00000155142; ENSMUSG00000022516. [Q8VHN8-1]
DR GeneID; 66911; -.
DR KEGG; mmu:66911; -.
DR UCSC; uc029svr.1; mouse. [Q8VHN8-1]
DR UCSC; uc029svs.1; mouse. [Q8VHN8-3]
DR UCSC; uc029svt.1; mouse. [Q8VHN8-2]
DR CTD; 84309; -.
DR MGI; MGI:1914161; Nudt16l1.
DR VEuPathDB; HostDB:ENSMUSG00000022516; -.
DR eggNOG; ENOG502S20E; Eukaryota.
DR GeneTree; ENSGT00390000016224; -.
DR HOGENOM; CLU_110418_0_1_1; -.
DR InParanoid; Q8VHN8; -.
DR OrthoDB; 1385294at2759; -.
DR PhylomeDB; Q8VHN8; -.
DR BioGRID-ORCS; 66911; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Nudt16l1; mouse.
DR PRO; PR:Q8VHN8; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8VHN8; protein.
DR Bgee; ENSMUSG00000022516; Expressed in paneth cell and 253 other tissues.
DR ExpressionAtlas; Q8VHN8; baseline and differential.
DR Genevisible; Q8VHN8; MM.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0030515; F:snoRNA binding; ISS:UniProtKB.
DR GO; GO:2001033; P:negative regulation of double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR SUPFAM; SSF55811; SSF55811; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Isopeptide bond; Nucleus;
KW Reference proteome; RNA-binding; Ubl conjugation.
FT CHAIN 1..211
FT /note="Tudor-interacting repair regulator protein"
FT /id="PRO_0000097649"
FT REGION 118..205
FT /note="Interaction with PXN"
FT /evidence="ECO:0000269|PubMed:11805099"
FT SITE 10
FT /note="Required for interaction with TP53BP1"
FT /evidence="ECO:0000250|UniProtKB:Q9BRJ7"
FT CROSSLNK 10
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9BRJ7"
FT CROSSLNK 151
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9BRJ7"
FT VAR_SEQ 140..151
FT /note="LGLVRVPLYTQK -> GLLPGARPHSHS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014277"
FT VAR_SEQ 152..211
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014278"
FT VAR_SEQ 179..211
FT /note="VLNMMPSEKLAEALASATEKQKKALEKLLPPSS -> ALEFPRRVPSSVFAF
FT ASLLTARDMQAAVHHYCPKQSLGPSYTLRMAVPHMILFSPWGPL (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014279"
FT CONFLICT 18
FT /note="M -> I (in Ref. 1; AAL57490)"
FT /evidence="ECO:0000305"
FT CONFLICT 192..193
FT /note="LA -> WP (in Ref. 2; BAB25336)"
FT /evidence="ECO:0000305"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:4ZG0"
FT HELIX 14..19
FT /evidence="ECO:0007829|PDB:5Z78"
FT STRAND 25..40
FT /evidence="ECO:0007829|PDB:5Z78"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:5Z78"
FT STRAND 44..55
FT /evidence="ECO:0007829|PDB:5Z78"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:5Z78"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:5Z78"
FT HELIX 74..85
FT /evidence="ECO:0007829|PDB:5Z78"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:4ZG0"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:5Z78"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:5Z78"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:5Z78"
FT STRAND 108..117
FT /evidence="ECO:0007829|PDB:5Z78"
FT HELIX 119..130
FT /evidence="ECO:0007829|PDB:5Z78"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:5Z78"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:5Z78"
FT HELIX 157..161
FT /evidence="ECO:0007829|PDB:5Z78"
FT HELIX 167..179
FT /evidence="ECO:0007829|PDB:5Z78"
FT HELIX 185..202
FT /evidence="ECO:0007829|PDB:5Z78"
SQ SEQUENCE 211 AA; 23414 MW; 0FE3CAFDC3721BC9 CRC64;
MSTTTVPELK QISREEAMRL GPGWSHSCHA MLYAANPGQL FGRIPMRFSV LMQMRFDGLL
GFPGGFVDRR FWSLEDGLNR VLGLGLGGLR LTEADYLSSH LTEGPHRVVA HLYARQLTLE
QLHAVEISAV HSRDHGLEVL GLVRVPLYTQ KDRVGGFPNF LSNAFVSTAK YQLLFALKVL
NMMPSEKLAE ALASATEKQK KALEKLLPPS S
