TDIF2_MOUSE
ID TDIF2_MOUSE Reviewed; 758 AA.
AC Q8R2M2; Q3TQW8; Q3UX19;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Deoxynucleotidyltransferase terminal-interacting protein 2;
GN Name=Dnttip2;
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=Amnion, and Egg;
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=FVB/N; 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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; SER-248; SER-255 AND
RP SER-476, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, 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).
CC -!- FUNCTION: Regulates the transcriptional activity of DNTT and ESR1. May
CC function as a chromatin remodeling protein (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Forms a ternary complex with DNTT and core histone;
CC interaction with PCNA releases DNTT and H2A/H2B histones from this
CC ternary complex. Interacts with ESR1, ESR2, PPARG and RXRA (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR EMBL; AK135957; BAE22744.1; -; mRNA.
DR EMBL; AK163260; BAE37264.1; -; mRNA.
DR EMBL; AK168536; BAE40414.1; -; mRNA.
DR EMBL; BC028305; AAH28305.1; -; mRNA.
DR CCDS; CCDS17809.1; -.
DR RefSeq; NP_722501.1; NM_153806.1.
DR AlphaFoldDB; Q8R2M2; -.
DR SMR; Q8R2M2; -.
DR BioGRID; 221260; 4.
DR STRING; 10090.ENSMUSP00000045043; -.
DR iPTMnet; Q8R2M2; -.
DR PhosphoSitePlus; Q8R2M2; -.
DR SwissPalm; Q8R2M2; -.
DR EPD; Q8R2M2; -.
DR jPOST; Q8R2M2; -.
DR MaxQB; Q8R2M2; -.
DR PaxDb; Q8R2M2; -.
DR PeptideAtlas; Q8R2M2; -.
DR PRIDE; Q8R2M2; -.
DR ProteomicsDB; 263028; -.
DR Antibodypedia; 48013; 21 antibodies from 8 providers.
DR Ensembl; ENSMUST00000035776; ENSMUSP00000045043; ENSMUSG00000039756.
DR GeneID; 99480; -.
DR KEGG; mmu:99480; -.
DR UCSC; uc008rep.1; mouse.
DR CTD; 30836; -.
DR MGI; MGI:1923173; Dnttip2.
DR VEuPathDB; HostDB:ENSMUSG00000039756; -.
DR eggNOG; KOG3100; Eukaryota.
DR GeneTree; ENSGT00510000048142; -.
DR HOGENOM; CLU_018725_0_0_1; -.
DR InParanoid; Q8R2M2; -.
DR OMA; SENMSCD; -.
DR OrthoDB; 887634at2759; -.
DR PhylomeDB; Q8R2M2; -.
DR TreeFam; TF105964; -.
DR BioGRID-ORCS; 99480; 20 hits in 75 CRISPR screens.
DR ChiTaRS; Dnttip2; mouse.
DR PRO; PR:Q8R2M2; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8R2M2; protein.
DR Bgee; ENSMUSG00000039756; Expressed in otic placode and 267 other tissues.
DR Genevisible; Q8R2M2; MM.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0006396; P:RNA processing; IBA:GO_Central.
DR InterPro; IPR039883; Fcf2/DNTTIP2.
DR InterPro; IPR014810; Fcf2_C.
DR PANTHER; PTHR21686; PTHR21686; 1.
DR Pfam; PF08698; Fcf2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..758
FT /note="Deoxynucleotidyltransferase terminal-interacting
FT protein 2"
FT /id="PRO_0000318506"
FT REGION 1..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..607
FT /note="TdBR region; mediates interaction with DNTT"
FT /evidence="ECO:0000250"
FT REGION 621..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 512..541
FT /evidence="ECO:0000255"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..546
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT MOD_RES 612
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT CROSSLNK 210
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT CROSSLNK 317
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT CROSSLNK 345
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT CROSSLNK 384
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT CROSSLNK 560
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT CROSSLNK 586
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT CROSSLNK 608
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT CROSSLNK 628
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT CROSSLNK 651
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT CROSSLNK 660
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT CROSSLNK 688
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT CROSSLNK 733
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5QJE6"
FT CONFLICT 517
FT /note="E -> D (in Ref. 1; BAE37264)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 758 AA; 84277 MW; 7B6A7EED68F8A0EF CRC64;
MVVTRSGLSR TRLQESSQQK RSAPRRIGTH LESTKESGSD GSTAESQPAE KQHSRSSSRT
TGPAEIIVLI SDDEASETES HTSGVTSVLE DQEPIVRVTR KRQIVIASTS KSTVRKRQKV
APQHASADEV VVSEAESHVS GVSMVVPSTE RSSRNKANSQ RDSSQESQSG TVSDAELSCS
GISSLEILPR TTARNVKKKL QFPAEKNDTK ITPGNKKQIV GMSVCSEDSD ATQLSARPLS
QRNMPNVSDS ETYNSDFDDS SPRNSGKKLT AQNHQNLHIQ EEKRANVVSL TEVRKENCKS
LDEEDLKITE EKVINEKDSQ RSLSEAQDTS LQQSVSQNHS STPNKKPTFQ LSSPDRKALM
KSLEHKFAVV NVERWNDKRG GSGKKSDLAQ LGGGGGGGDD NEPTGAGISD DKSSQSGVPL
ECDTKPCKSE LSMTQDTTDS PVLLFLSSDE SQQSDSSENE RDTLCSVENN GQKEASAEDL
EDAACDSALF VIDKTPGLSA DKNFYLEDKA PSEVAIEEEK EEEEKEEENS EEDSSDSDEN
KDESSDEEDL LSNTKSKLLK LTSSSIDPGL NIKQLGGLYI NFNVDKLQPH KETLTQIKEK
KKNELLQKAV ITPDFEKKHC VPPYSESKHR LQKQRRKERQ KTAGNGWFGM KAPELTDELK
NDLRALKMRA GMDPKRFYKK NDRDGFPKYF QVGTIVDNPA DFYHSRIPKK QRKKTIVEEL
LADSEFRRFN RRKYSEIMAE KAANAEGKKF KKKKKFRN
