ID   TDIF2_HUMAN             Reviewed;         756 AA.
AC   Q5QJE6; Q12987; Q53H59; Q5TFJ4; Q6TLI0; Q76MJ8; Q86WX9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=Deoxynucleotidyltransferase terminal-interacting protein 2;
DE   AltName: Full=Estrogen receptor-binding protein;
DE   AltName: Full=LPTS-interacting protein 2;
DE            Short=LPTS-RP2;
DE   AltName: Full=Terminal deoxynucleotidyltransferase-interacting factor 2;
DE            Short=TdIF2;
DE            Short=TdT-interacting factor 2;
GN   Name=DNTTIP2 {ECO:0000312|HGNC:HGNC:24013}; Synonyms=ERBP, TDIF2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASP-309, FUNCTION, IDENTIFICATION IN A
RP   COMPLEX WITH DNTT; PCNA AND CORE HISTONE, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Thymus;
RX   PubMed=12786946; DOI=10.1046/j.1365-2443.2003.00656.x;
RA   Fujita K., Shimazaki N., Ohta Y., Kubota T., Ibe S., Toji S., Tamai K.,
RA   Fujisaki S., Hayano T., Koiwai O.;
RT   "Terminal deoxynucleotidyltransferase forms a ternary complex with a novel
RT   chromatin remodeling protein with 82 kDa and core histone.";
RL   Genes Cells 8:559-571(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ESR1; ESR2; PPARG
RP   AND RXRA, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=15047147; DOI=10.1016/j.bbrc.2004.02.179;
RA   Bu H., Kashireddy P., Chang J., Zhu Y.T., Zhang Z., Zheng W., Rao S.M.,
RA   Zhu Y.-J.;
RT   "ERBP, a novel estrogen receptor binding protein enhancing the activity of
RT   estrogen receptor.";
RL   Biochem. Biophys. Res. Commun. 317:54-59(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Carlsson P.;
RT   "cDNA encoding an acidic 82 kDa protein.";
RL   Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASP-309.
RC   TISSUE=Liver;
RA   Song H., Zhao M., Li T.;
RT   "LPTS-RP2, one LPTS-interacting protein.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASP-309.
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-309.
RC   TISSUE=Brain, and Skin;
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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-232, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-117; THR-129;
RP   SER-141; SER-145; SER-148; SER-184; SER-194; THR-232; SER-324 AND SER-381,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-184, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-117; SER-141;
RP   THR-232; SER-251; SER-330; SER-434; SER-512 AND THR-610, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141; SER-434 AND SER-512, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117; SER-141; THR-232;
RP   SER-239; SER-251; SER-253; SER-330 AND SER-569, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [19]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-558; LYS-626; LYS-649; LYS-658
RP   AND LYS-686, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [20]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-558; LYS-626 AND LYS-658, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA   Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL   Cell Rep. 10:1778-1791(2015).
RN   [21]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-217; LYS-220; LYS-257; LYS-316;
RP   LYS-321; LYS-345; LYS-384; LYS-558; LYS-584; LYS-606; LYS-626; LYS-649;
RP   LYS-658; LYS-686 AND LYS-731, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [22] {ECO:0007744|PDB:7MQ8, ECO:0007744|PDB:7MQ9, ECO:0007744|PDB:7MQA}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=34516797; DOI=10.1126/science.abj5338;
RA   Singh S., Vanden Broeck A., Miller L., Chaker-Margot M., Klinge S.;
RT   "Nucleolar maturation of the human small subunit processome.";
RL   Science 373:eabj5338-eabj5338(2021).
CC   -!- FUNCTION: Regulates the transcriptional activity of DNTT and ESR1. May
CC       function as a chromatin remodeling protein (PubMed:12786946,
CC       PubMed:15047147). Part of the small subunit (SSU) processome, first
CC       precursor of the small eukaryotic ribosomal subunit. During the
CC       assembly of the SSU processome in the nucleolus, many ribosome
CC       biogenesis factors, an RNA chaperone and ribosomal proteins associate
CC       with the nascent pre-rRNA and work in concert to generate RNA folding,
CC       modifications, rearrangements and cleavage as well as targeted
CC       degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797).
CC       {ECO:0000269|PubMed:12786946, ECO:0000269|PubMed:15047147,
CC       ECO:0000269|PubMed:34516797}.
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
CC       (PubMed:12786946, PubMed:15047147). Part of the small subunit (SSU)
CC       processome, composed of more than 70 proteins and the RNA chaperone
CC       small nucleolar RNA (snoRNA) U3 (PubMed:34516797).
CC       {ECO:0000269|PubMed:12786946, ECO:0000269|PubMed:15047147,
CC       ECO:0000269|PubMed:34516797}.
CC   -!- INTERACTION:
CC       Q5QJE6; Q6NZI2: CAVIN1; NbExp=3; IntAct=EBI-5666736, EBI-2559016;
CC       Q5QJE6; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-5666736, EBI-739624;
CC       Q5QJE6; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-5666736, EBI-79165;
CC       Q5QJE6; O76064: RNF8; NbExp=3; IntAct=EBI-5666736, EBI-373337;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12786946,
CC       ECO:0000269|PubMed:15047147}. Nucleus, nucleolus
CC       {ECO:0000269|PubMed:34516797}.
CC   -!- TISSUE SPECIFICITY: Widely expressed with higher levels in testis.
CC       {ECO:0000269|PubMed:12786946, ECO:0000269|PubMed:15047147}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA50601.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAH47688.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR   EMBL; AB046574; BAD08331.1; -; mRNA.
DR   EMBL; AY394925; AAQ95169.1; -; mRNA.
DR   EMBL; U15552; AAA50601.1; ALT_FRAME; mRNA.
DR   EMBL; AY336729; AAR02407.1; -; mRNA.
DR   EMBL; AK292379; BAF85068.1; -; mRNA.
DR   EMBL; AK222722; BAD96442.1; -; mRNA.
DR   EMBL; AL049796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471097; EAW73064.1; -; Genomic_DNA.
DR   EMBL; BC047688; AAH47688.1; ALT_SEQ; mRNA.
DR   EMBL; BC130622; AAI30623.1; -; mRNA.
DR   CCDS; CCDS44174.1; -.
DR   PIR; G01522; G01522.
DR   RefSeq; NP_055412.2; NM_014597.4.
DR   PDB; 7MQ8; EM; 3.60 A; SQ=1-756.
DR   PDB; 7MQ9; EM; 3.87 A; SQ=1-756.
DR   PDB; 7MQA; EM; 2.70 A; SQ=1-756.
DR   PDBsum; 7MQ8; -.
DR   PDBsum; 7MQ9; -.
DR   PDBsum; 7MQA; -.
DR   AlphaFoldDB; Q5QJE6; -.
DR   EMDB; EMD-23936; -.
DR   EMDB; EMD-23937; -.
DR   EMDB; EMD-23938; -.
DR   SMR; Q5QJE6; -.
DR   BioGRID; 119052; 138.
DR   ComplexPortal; CPX-2511; Small ribosomal subunit processome.
DR   CORUM; Q5QJE6; -.
DR   IntAct; Q5QJE6; 30.
DR   MINT; Q5QJE6; -.
DR   STRING; 9606.ENSP00000411010; -.
DR   GlyCosmos; Q5QJE6; 1 site, 1 glycan.
DR   GlyGen; Q5QJE6; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q5QJE6; -.
DR   PhosphoSitePlus; Q5QJE6; -.
DR   SwissPalm; Q5QJE6; -.
DR   BioMuta; DNTTIP2; -.
DR   DMDM; 166987398; -.
DR   EPD; Q5QJE6; -.
DR   jPOST; Q5QJE6; -.
DR   MassIVE; Q5QJE6; -.
DR   MaxQB; Q5QJE6; -.
DR   PaxDb; 9606-ENSP00000411010; -.
DR   PeptideAtlas; Q5QJE6; -.
DR   ProteomicsDB; 63620; -.
DR   Pumba; Q5QJE6; -.
DR   Antibodypedia; 48013; 26 antibodies from 9 providers.
DR   DNASU; 30836; -.
DR   Ensembl; ENST00000436063.7; ENSP00000411010.2; ENSG00000067334.14.
DR   GeneID; 30836; -.
DR   KEGG; hsa:30836; -.
DR   MANE-Select; ENST00000436063.7; ENSP00000411010.2; NM_014597.5; NP_055412.2.
DR   UCSC; uc001dqf.4; human.
DR   AGR; HGNC:24013; -.
DR   CTD; 30836; -.
DR   DisGeNET; 30836; -.
DR   GeneCards; DNTTIP2; -.
DR   HGNC; HGNC:24013; DNTTIP2.
DR   HPA; ENSG00000067334; Low tissue specificity.
DR   MIM; 611199; gene.
DR   neXtProt; NX_Q5QJE6; -.
DR   OpenTargets; ENSG00000067334; -.
DR   PharmGKB; PA142671963; -.
DR   VEuPathDB; HostDB:ENSG00000067334; -.
DR   eggNOG; KOG3100; Eukaryota.
DR   GeneTree; ENSGT00510000048142; -.
DR   HOGENOM; CLU_018725_0_0_1; -.
DR   InParanoid; Q5QJE6; -.
DR   OMA; MSCDNAL; -.
DR   OrthoDB; 5475774at2759; -.
DR   PhylomeDB; Q5QJE6; -.
DR   TreeFam; TF105964; -.
DR   PathwayCommons; Q5QJE6; -.
DR   SignaLink; Q5QJE6; -.
DR   BioGRID-ORCS; 30836; 510 hits in 1182 CRISPR screens.
DR   ChiTaRS; DNTTIP2; human.
DR   GeneWiki; DNTTIP2; -.
DR   GenomeRNAi; 30836; -.
DR   Pharos; Q5QJE6; Tdark.
DR   PRO; PR:Q5QJE6; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q5QJE6; Protein.
DR   Bgee; ENSG00000067334; Expressed in calcaneal tendon and 201 other cell types or tissues.
DR   ExpressionAtlas; Q5QJE6; baseline and differential.
DR   GO; GO:0005694; C:chromosome; IDA:HPA.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0032040; C:small-subunit processome; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:UniProtKB.
DR   GO; GO:0006396; P:RNA processing; IBA:GO_Central.
DR   InterPro; IPR039883; Fcf2/DNTTIP2.
DR   InterPro; IPR014810; Fcf2_C.
DR   PANTHER; PTHR21686:SF12; DEOXYNUCLEOTIDYLTRANSFERASE TERMINAL-INTERACTING PROTEIN 2; 1.
DR   PANTHER; PTHR21686; UNCHARACTERIZED; 1.
DR   Pfam; PF08698; Fcf2; 1.
DR   Genevisible; Q5QJE6; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..756
FT                   /note="Deoxynucleotidyltransferase terminal-interacting
FT                   protein 2"
FT                   /id="PRO_0000318505"
FT   REGION          1..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          156..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          510..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          548..605
FT                   /note="TdBR region; mediates interaction with DNTT"
FT   COILED          505..542
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        10..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..92
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..223
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..260
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..546
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         21
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231"
FT   MOD_RES         117
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         129
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         141
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18220336,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         145
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         148
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         184
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332"
FT   MOD_RES         194
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         232
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         239
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         251
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         253
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         324
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         330
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         381
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         434
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692"
FT   MOD_RES         512
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692"
FT   MOD_RES         569
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         610
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   CROSSLNK        217
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        220
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        257
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        316
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        321
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        345
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        384
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        558
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT   CROSSLNK        584
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        606
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        626
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT   CROSSLNK        649
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        658
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT   CROSSLNK        686
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        731
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VARIANT         309
FT                   /note="E -> D (in dbSNP:rs3747965)"
FT                   /evidence="ECO:0000269|PubMed:12786946,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4,
FT                   ECO:0000269|Ref.8"
FT                   /id="VAR_038748"
FT   VARIANT         341
FT                   /note="T -> A (in dbSNP:rs3179879)"
FT                   /id="VAR_038749"
FT   VARIANT         430
FT                   /note="A -> V (in dbSNP:rs35650636)"
FT                   /id="VAR_038750"
FT   VARIANT         477
FT                   /note="G -> E (in dbSNP:rs41292661)"
FT                   /id="VAR_061710"
FT   VARIANT         676
FT                   /note="Y -> F (in dbSNP:rs12748154)"
FT                   /id="VAR_038751"
FT   CONFLICT        47
FT                   /note="A -> D (in Ref. 2; AAQ95169 and 3; AAA50601)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        67
FT                   /note="R -> S (in Ref. 2; AAQ95169 and 3; AAA50601)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        648
FT                   /note="M -> I (in Ref. 6; BAD96442)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   756 AA;  84469 MW;  5C58EFABA2B42E4B CRC64;
     MVVTRSARAK ASIQAASAES SGQKSFAANG IQAHPESSTG SDARTTAESQ TTGKQSLIPR
     TPKARKRKSR TTGSLPKGTE PSTDGETSEA ESNYSVSEHH DTILRVTRRR QILIACSPVS
     SVRKKPKVTP TKESYTEEIV SEAESHVSGI SRIVLPTEKT TGARRSKAKS LTDPSQESHT
     EAISDAETSS SDISFSGIAT RRTRSMQRKL KAQTEKKDSK IVPGNEKQIV GTPVNSEDSD
     TRQTSHLQAR SLSEINKPNF YNNDFDDDFS HRSSENILTV HEQANVESLK ETKQNCKDLD
     EDANGITDEG KEINEKSSQL KNLSELQDTS LQQLVSQRHS TPQNKNAVSV HSNLNSEAVM
     KSLTQTFATV EVGRWNNNKK SPIKASDLTK FGDCGGSDDE EESTVISVSE DMNSEGNVDF
     ECDTKLYTSA PNTSQGKDNS VLLVLSSDES QQSENSENEE DTLCFVENSG QRESLSGDTG
     SLSCDNALFV IDTTPGMSAD KNFYLEEEDK ASEVAIEEEK EEEEDEKSEE DSSDHDENED
     EFSDEEDFLN STKAKLLKLT SSSIDPGLSI KQLGGLYINF NADKLQSNKR TLTQIKEKKK
     NELLQKAVIT PDFEKNHCVP PYSESKYQLQ KKRRKERQKT AGDGWFGMKA PEMTNELKND
     LKALKMRASM DPKRFYKKND RDGFPKYFQI GTIVDNPADF YHSRIPKKQR KRTIVEELLA
     DSEFRRYNRR KYSEIMAEKA ANAAGKKFRK KKKFRN
//