INT3_HUMAN
ID INT3_HUMAN Reviewed; 1043 AA.
AC Q68E01; A8K1W0; B4DQC8; B4E3U9; D3DV57; Q4G0E5; Q5VUQ5; Q5VUQ6; Q5VUR0;
AC Q5VUR1; Q68DJ1; Q69YR5; Q6AI57; Q6DKG7; Q6MZQ4; Q6MZZ9; Q8NC46; Q8TB23;
AC Q9H6S9;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Integrator complex subunit 3;
DE Short=Int3;
DE AltName: Full=SOSS complex subunit A;
DE AltName: Full=Sensor of single-strand DNA complex subunit A;
DE Short=SOSS-A;
DE Short=Sensor of ssDNA subunit A;
GN Name=INTS3; Synonyms=C1orf193, C1orf60;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Amygdala, Cervix, Fetal kidney, Retina, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC TISSUE=Hepatoma, Hippocampus, Teratocarcinoma, and Uterus;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain, Lung, Skin, Testis, and Uterus;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE INTEGRATOR
RP COMPLEX.
RX PubMed=16239144; DOI=10.1016/j.cell.2005.08.019;
RA Baillat D., Hakimi M.-A., Naeaer A.M., Shilatifard A., Cooch N.,
RA Shiekhattar R.;
RT "Integrator, a multiprotein mediator of small nuclear RNA processing,
RT associates with the C-terminal repeat of RNA polymerase II.";
RL Cell 123:265-276(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502 AND SER-537, AND
RP 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 [8]
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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE SOSS COMPLEX.
RX PubMed=19605351; DOI=10.1074/jbc.c109.039586;
RA Li Y., Bolderson E., Kumar R., Muniandy P.A., Xue Y., Richard D.J.,
RA Seidman M., Pandita T.K., Khanna K.K., Wang W.;
RT "hSSB1 and hSSB2 form similar multiprotein complexes that participate in
RT DNA damage response.";
RL J. Biol. Chem. 284:23525-23531(2009).
RN [10]
RP FUNCTION IN THE SOSS COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION IN THE
RP SOSS COMPLEX, AND INTERACTION WITH NABP1; INIP AND NBN.
RX PubMed=19683501; DOI=10.1016/j.molcel.2009.06.011;
RA Huang J., Gong Z., Ghosal G., Chen J.;
RT "SOSS complexes participate in the maintenance of genomic stability.";
RL Mol. Cell 35:384-393(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-995, AND IDENTIFICATION BY
RP 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, AND IDENTIFICATION BY
RP 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502 AND SER-537, AND
RP IDENTIFICATION BY MASS 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 [16]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23904267; DOI=10.1091/mbc.e13-05-0254;
RA Jodoin J.N., Sitaram P., Albrecht T.R., May S.B., Shboul M., Lee E.,
RA Reversade B., Wagner E.J., Lee L.A.;
RT "Nuclear-localized Asunder regulates cytoplasmic dynein localization via
RT its role in the integrator complex.";
RL Mol. Biol. Cell 24:2954-2965(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Component of the Integrator (INT) complex. The Integrator
CC complex is involved in the small nuclear RNAs (snRNA) U1 and U2
CC transcription and in their 3'-box-dependent processing. The Integrator
CC complex is associated with the C-terminal domain (CTD) of RNA
CC polymerase II largest subunit (POLR2A) and is recruited to the U1 and
CC U2 snRNAs genes (Probable). Mediates recruitment of cytoplasmic dynein
CC to the nuclear envelope, probably as component of the INT complex
CC (PubMed:23904267). {ECO:0000269|PubMed:23904267,
CC ECO:0000305|PubMed:16239144}.
CC -!- FUNCTION: Component of the SOSS complex, a multiprotein complex that
CC functions downstream of the MRN complex to promote DNA repair and G2/M
CC checkpoint. The SOSS complex associates with single-stranded DNA at DNA
CC lesions and influences diverse endpoints in the cellular DNA damage
CC response including cell-cycle checkpoint activation, recombinational
CC repair and maintenance of genomic stability. The SOSS complex is
CC required for efficient homologous recombination-dependent repair of
CC double-strand breaks (DSBs) and ATM-dependent signaling pathways. In
CC the SOSS complex, it is required for the assembly of the complex and
CC for stabilization of the complex at DNA damage sites.
CC {ECO:0000269|PubMed:19605351, ECO:0000269|PubMed:19683501}.
CC -!- SUBUNIT: Belongs to the multiprotein complex Integrator, at least
CC composed of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7, INTS8,
CC INTS9/RC74, INTS10, INTS11/CPSF3L and INTS12. Component of the SOSS
CC complex, composed of SOSS-B (SOSS-B1/NABP2 or SOSS-B2/NABP1), SOSS-
CC A/INTS3 and SOSS-C/INIP. SOSS complexes containing SOSS-B1/NABP2 are
CC more abundant than complexes containing SOSS-B2/NABP1. Interacts with
CC SOSS-B1/NABP2, SOSS-B2/NABP1 and SOSS-C/INIP; the interaction is
CC direct. Interacts with NBN/NBS1. {ECO:0000269|PubMed:16239144,
CC ECO:0000269|PubMed:19605351, ECO:0000269|PubMed:19683501}.
CC -!- INTERACTION:
CC Q68E01; Q9NRY2: INIP; NbExp=6; IntAct=EBI-2680854, EBI-2881520;
CC Q68E01; Q96AH0: NABP1; NbExp=5; IntAct=EBI-2680854, EBI-2889252;
CC Q68E01; Q9BQ15: NABP2; NbExp=9; IntAct=EBI-2680854, EBI-2120336;
CC Q68E01; O60934: NBN; NbExp=2; IntAct=EBI-2680854, EBI-494844;
CC Q68E01; O43829: ZBTB14; NbExp=3; IntAct=EBI-2680854, EBI-10176632;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19605351,
CC ECO:0000269|PubMed:19683501, ECO:0000269|PubMed:23904267}. Cytoplasm
CC {ECO:0000269|PubMed:23904267}. Note=Localizes to nuclear foci following
CC DNA damage.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q68E01-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q68E01-2; Sequence=VSP_021446;
CC Name=3;
CC IsoId=Q68E01-3; Sequence=VSP_038131, VSP_038132;
CC Name=4;
CC IsoId=Q68E01-4; Sequence=VSP_038130;
CC -!- SIMILARITY: Belongs to the Integrator subunit 3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH25254.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH54513.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15174.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC11329.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAH18229.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AL832133; CAH10398.1; -; mRNA.
DR EMBL; AK290025; BAF82714.1; -; mRNA.
DR EMBL; AK298746; BAG60890.1; -; mRNA.
DR EMBL; AK304874; BAG65611.1; -; mRNA.
DR EMBL; BX640786; CAE45876.1; -; mRNA.
DR EMBL; BX640950; CAE45974.1; -; mRNA.
DR EMBL; CR627233; CAH10366.1; -; mRNA.
DR EMBL; CR749212; CAH18069.1; -; mRNA.
DR EMBL; CR749376; CAH18229.1; ALT_SEQ; mRNA.
DR EMBL; AL513523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53279.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53283.1; -; Genomic_DNA.
DR EMBL; BC025254; AAH25254.1; ALT_INIT; mRNA.
DR EMBL; BC054513; AAH54513.1; ALT_INIT; mRNA.
DR EMBL; BC073985; AAH73985.1; -; mRNA.
DR EMBL; BC098431; AAH98431.1; -; mRNA.
DR EMBL; BC105092; AAI05093.1; -; mRNA.
DR EMBL; BC105094; AAI05095.1; -; mRNA.
DR EMBL; BC116458; AAI16459.1; -; mRNA.
DR EMBL; AK025572; BAB15174.1; ALT_INIT; mRNA.
DR EMBL; AK074979; BAC11329.1; ALT_INIT; mRNA.
DR EMBL; BK005722; DAA05722.1; -; Genomic_DNA.
DR CCDS; CCDS1052.1; -. [Q68E01-2]
DR RefSeq; NP_001311404.1; NM_001324475.1. [Q68E01-2]
DR RefSeq; NP_075391.3; NM_023015.4. [Q68E01-2]
DR RefSeq; XP_005245518.1; XM_005245461.2.
DR PDB; 4OWT; X-ray; 2.00 A; A=35-499.
DR PDB; 4OWW; X-ray; 2.30 A; A=1-501.
DR PDB; 4OWX; X-ray; 2.30 A; A=1-501.
DR PDB; 6WLG; X-ray; 3.11 A; A/B=555-977.
DR PDB; 7BV7; X-ray; 2.40 A; A/B=560-995.
DR PDBsum; 4OWT; -.
DR PDBsum; 4OWW; -.
DR PDBsum; 4OWX; -.
DR PDBsum; 6WLG; -.
DR PDBsum; 7BV7; -.
DR AlphaFoldDB; Q68E01; -.
DR SMR; Q68E01; -.
DR BioGRID; 122401; 132.
DR ComplexPortal; CPX-482; SOSS1 complex.
DR ComplexPortal; CPX-614; SOSS2 complex.
DR ComplexPortal; CPX-6441; Integrator complex.
DR CORUM; Q68E01; -.
DR IntAct; Q68E01; 31.
DR MINT; Q68E01; -.
DR STRING; 9606.ENSP00000318641; -.
DR GlyGen; Q68E01; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q68E01; -.
DR PhosphoSitePlus; Q68E01; -.
DR SwissPalm; Q68E01; -.
DR BioMuta; INTS3; -.
DR DMDM; 74724494; -.
DR EPD; Q68E01; -.
DR jPOST; Q68E01; -.
DR MassIVE; Q68E01; -.
DR MaxQB; Q68E01; -.
DR PaxDb; Q68E01; -.
DR PeptideAtlas; Q68E01; -.
DR PRIDE; Q68E01; -.
DR ProteomicsDB; 66123; -. [Q68E01-1]
DR ProteomicsDB; 66124; -. [Q68E01-2]
DR ProteomicsDB; 66125; -. [Q68E01-3]
DR ProteomicsDB; 66126; -. [Q68E01-4]
DR Antibodypedia; 34136; 107 antibodies from 20 providers.
DR DNASU; 65123; -.
DR Ensembl; ENST00000318967.7; ENSP00000318641.2; ENSG00000143624.14. [Q68E01-2]
DR Ensembl; ENST00000435409.6; ENSP00000404290.2; ENSG00000143624.14. [Q68E01-2]
DR Ensembl; ENST00000512605.4; ENSP00000425437.1; ENSG00000143624.14. [Q68E01-3]
DR Ensembl; ENST00000571768.5; ENSP00000458631.1; ENSG00000262826.5. [Q68E01-2]
DR Ensembl; ENST00000576030.5; ENSP00000460221.1; ENSG00000262826.5. [Q68E01-2]
DR Ensembl; ENST00000576422.4; ENSP00000459907.1; ENSG00000262826.5. [Q68E01-3]
DR GeneID; 65123; -.
DR KEGG; hsa:65123; -.
DR MANE-Select; ENST00000318967.7; ENSP00000318641.2; NM_023015.5; NP_075391.3. [Q68E01-2]
DR UCSC; uc001fct.4; human. [Q68E01-1]
DR CTD; 65123; -.
DR DisGeNET; 65123; -.
DR GeneCards; INTS3; -.
DR HGNC; HGNC:26153; INTS3.
DR HPA; ENSG00000143624; Low tissue specificity.
DR MIM; 611347; gene.
DR neXtProt; NX_Q68E01; -.
DR OpenTargets; ENSG00000143624; -.
DR PharmGKB; PA142672510; -.
DR VEuPathDB; HostDB:ENSG00000143624; -.
DR eggNOG; KOG4262; Eukaryota.
DR GeneTree; ENSGT00390000014184; -.
DR HOGENOM; CLU_007659_0_0_1; -.
DR InParanoid; Q68E01; -.
DR OMA; LCHEDNI; -.
DR OrthoDB; 644334at2759; -.
DR PhylomeDB; Q68E01; -.
DR TreeFam; TF323623; -.
DR PathwayCommons; Q68E01; -.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR SignaLink; Q68E01; -.
DR SIGNOR; Q68E01; -.
DR BioGRID-ORCS; 65123; 735 hits in 1091 CRISPR screens.
DR ChiTaRS; INTS3; human.
DR GeneWiki; INTS3; -.
DR GenomeRNAi; 65123; -.
DR Pharos; Q68E01; Tbio.
DR PRO; PR:Q68E01; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q68E01; protein.
DR Bgee; ENSG00000143624; Expressed in right uterine tube and 93 other tissues.
DR ExpressionAtlas; Q68E01; baseline and differential.
DR Genevisible; Q68E01; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0032039; C:integrator complex; IDA:HGNC-UCL.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
DR GO; GO:0070876; C:SOSS complex; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:ComplexPortal.
DR GO; GO:0044818; P:mitotic G2/M transition checkpoint; IDA:ComplexPortal.
DR GO; GO:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; IC:ComplexPortal.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:UniProtKB.
DR GO; GO:0016180; P:snRNA processing; IDA:HGNC-UCL.
DR InterPro; IPR045334; INTS3.
DR InterPro; IPR019333; INTS3_N.
DR PANTHER; PTHR13587; PTHR13587; 1.
DR Pfam; PF10189; Ints3_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; DNA damage;
KW DNA repair; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1043
FT /note="Integrator complex subunit 3"
FT /id="PRO_0000259534"
FT REGION 977..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1013
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1043
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 995
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1..488
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038130"
FT VAR_SEQ 1..207
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038131"
FT VAR_SEQ 173
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_021446"
FT VAR_SEQ 942
FT /note="F -> CMPSTLGVQCRRCCPGPDYAWSQAGGRGRTPGATTHTRDKTTCACCL
FT ISSQTSDCFSFPALPFLPLV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038132"
FT CONFLICT 134
FT /note="Y -> C (in Ref. 1; CAE45974)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="K -> E (in Ref. 2; BAF82714)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="E -> G (in Ref. 1; CAE45974)"
FT /evidence="ECO:0000305"
FT CONFLICT 685
FT /note="P -> T (in Ref. 1; CAE45974)"
FT /evidence="ECO:0000305"
FT CONFLICT 803
FT /note="W -> R (in Ref. 1; CAE45876)"
FT /evidence="ECO:0000305"
FT CONFLICT 827
FT /note="P -> L (in Ref. 2; BAC11329)"
FT /evidence="ECO:0000305"
FT CONFLICT 896
FT /note="L -> P (in Ref. 2; BAG60890)"
FT /evidence="ECO:0000305"
FT CONFLICT 952
FT /note="L -> P (in Ref. 2; BAG65611)"
FT /evidence="ECO:0000305"
FT CONFLICT 967
FT /note="F -> L (in Ref. 1; CAE45876)"
FT /evidence="ECO:0000305"
FT CONFLICT 972
FT /note="S -> P (in Ref. 2; BAB15174)"
FT /evidence="ECO:0000305"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:4OWT"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 47..63
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 69..79
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 83..99
FT /evidence="ECO:0007829|PDB:4OWT"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 120..132
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 139..154
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 160..169
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 179..194
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 203..217
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 224..243
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 253..261
FT /evidence="ECO:0007829|PDB:4OWT"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 266..277
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 289..293
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 299..304
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 308..317
FT /evidence="ECO:0007829|PDB:4OWT"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:4OWW"
FT HELIX 327..337
FT /evidence="ECO:0007829|PDB:4OWT"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 346..356
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 362..366
FT /evidence="ECO:0007829|PDB:4OWT"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:4OWW"
FT HELIX 372..381
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 386..396
FT /evidence="ECO:0007829|PDB:4OWT"
FT TURN 397..402
FT /evidence="ECO:0007829|PDB:4OWT"
FT TURN 405..407
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 410..423
FT /evidence="ECO:0007829|PDB:4OWT"
FT TURN 424..426
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 428..444
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 450..466
FT /evidence="ECO:0007829|PDB:4OWT"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 474..477
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 484..493
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 495..497
FT /evidence="ECO:0007829|PDB:4OWT"
FT TURN 584..586
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 596..606
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 617..626
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 643..649
FT /evidence="ECO:0007829|PDB:7BV7"
FT STRAND 650..652
FT /evidence="ECO:0007829|PDB:6WLG"
FT HELIX 653..660
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 672..683
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 687..697
FT /evidence="ECO:0007829|PDB:7BV7"
FT TURN 701..703
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 706..713
FT /evidence="ECO:0007829|PDB:7BV7"
FT STRAND 715..717
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 720..734
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 736..749
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 752..755
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 759..765
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 770..781
FT /evidence="ECO:0007829|PDB:7BV7"
FT TURN 790..792
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 793..800
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 805..817
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 822..825
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 826..830
FT /evidence="ECO:0007829|PDB:7BV7"
FT TURN 834..836
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 838..848
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 856..862
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 872..883
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 885..897
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 921..934
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 935..937
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 942..944
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 946..955
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 956..958
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 961..966
FT /evidence="ECO:0007829|PDB:7BV7"
FT HELIX 968..971
FT /evidence="ECO:0007829|PDB:7BV7"
FT TURN 973..975
FT /evidence="ECO:0007829|PDB:6WLG"
SQ SEQUENCE 1043 AA; 118070 MW; 66A49C646077C3F4 CRC64;
MELQKGKGAA AAAAASGAAG GGGGGAGAGA PGGGRLLLST SLDAKDELEE RLERCMSIVT
SMTAGVSERE ANDALNAYVC KGLPQHEEIC LGLFTLILTE PAQAQKCYRD LALVSRDGMN
IVLNKINQIL MEKYLKLQDT CRTQLVWLVR ELVKSGVLGA DGVCMTFMKQ IAGGGDVTAK
NIWLAESVLD ILTEQREWVL KSSILIAMAV YTYLRLIVDH HGTAQLQALR QKEVDFCISL
LRERFMECLM IGRDLVRLLQ NVARIPEFEL LWKDIIHNPQ ALSPQFTGIL QLLQSRTSRK
FLACRLTPDM ETKLLFMTSR VRFGQQKRYQ DWFQRQYLST PDSQSLRCDL IRYICGVVHP
SNEVLSSDIL PRWAIIGWLL TTCTSNVAAS NAKLALFYDW LFFSPDKDSI MNIEPAILVM
HHSMKPHPAI TATLLDFMCR IIPNFYPPLE GHVRQGVFSS LNHIVEKRVL AHLAPLFDNP
KLDKELRAML REKFPEFCSS PSPPVEVKIE EPVSMEMDNH MSDKDESCYD NAEAAFSDDE
EDLNSKGKKR EFRFHPIKET VVEEPVDITP YLDQLDESLR DKVLQLQKGS DTEAQCEVMQ
EIVDQVLEED FDSEQLSVLA SCLQELFKAH FRGEVLPEEI TEESLEESVG KPLYLIFRNL
CQMQEDNSSF SLLLDLLSEL YQKQPKIGYH LLYYLRASKA AAGKMNLYES FAQATQLGDL
HTCLMMDMKA CQEDDVRLLC HLTPSIYTEF PDETLRSGEL LNMIVAVIDS AQLQELVCHV
MMGNLVMFRK DSVLNILIQS LDWETFEQYC AWQLFLAHNI PLETIIPILQ HLKYKEHPEA
LSCLLLQLRR EKPSEEMVKM VLSRPCHPDD QFTTSILRHW CMKHDELLAE HIKSLLIKNN
SLPRKRQSLR SSSSKLAQLT LEQILEHLDN LRLNLTNTKQ NFFSQTPILQ ALQHVQASCD
EAHKMKFSDL FSLAEEYEDS STKPPKSRRK AALSSPRSRK NATQPPNAEE ESGSSSASEE
EDTKPKPTKR KRKGSSAVGS DSD
