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Integrator complex subunit 3 (Int3) (SOSS complex subunit A) (Sensor of single-strand DNA complex subunit A) (SOSS-A) (Sensor of ssDNA subunit A)

 INT3_HUMAN              Reviewed;        1043 AA.
Q68E01; A8K1W0; B4DQC8; B4E3U9; D3DV57; Q4G0E5; Q5VUQ5; Q5VUQ6;
Q5VUR0; Q5VUR1; Q68DJ1; Q69YR5; Q6AI57; Q6DKG7; Q6MZQ4; Q6MZZ9;
Q8NC46; Q8TB23; Q9H6S9;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
27-SEP-2017, entry version 120.
RecName: Full=Integrator complex subunit 3;
Short=Int3;
AltName: Full=SOSS complex subunit A;
AltName: Full=Sensor of single-strand DNA complex subunit A;
Short=SOSS-A;
Short=Sensor of ssDNA subunit A;
Name=INTS3; Synonyms=C1orf193, C1orf60;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Amygdala, Cervix, Fetal kidney, Retina, and Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
TISSUE=Hepatoma, Hippocampus, Teratocarcinoma, and Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain, Lung, Skin, Testis, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
INTEGRATOR COMPLEX.
PubMed=16239144; DOI=10.1016/j.cell.2005.08.019;
Baillat D., Hakimi M.-A., Naeaer A.M., Shilatifard A., Cooch N.,
Shiekhattar R.;
"Integrator, a multiprotein mediator of small nuclear RNA processing,
associates with the C-terminal repeat of RNA polymerase II.";
Cell 123:265-276(2005).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502 AND SER-537, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE SOSS
COMPLEX.
PubMed=19605351; DOI=10.1074/jbc.C109.039586;
Li Y., Bolderson E., Kumar R., Muniandy P.A., Xue Y., Richard D.J.,
Seidman M., Pandita T.K., Khanna K.K., Wang W.;
"hSSB1 and hSSB2 form similar multiprotein complexes that participate
in DNA damage response.";
J. Biol. Chem. 284:23525-23531(2009).
[10]
FUNCTION IN THE SOSS COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION IN
THE SOSS COMPLEX, AND INTERACTION WITH NABP1; INIP AND NBN.
PubMed=19683501; DOI=10.1016/j.molcel.2009.06.011;
Huang J., Gong Z., Ghosal G., Chen J.;
"SOSS complexes participate in the maintenance of genomic stability.";
Mol. Cell 35:384-393(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-995, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502 AND SER-537, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23904267; DOI=10.1091/mbc.E13-05-0254;
Jodoin J.N., Sitaram P., Albrecht T.R., May S.B., Shboul M., Lee E.,
Reversade B., Wagner E.J., Lee L.A.;
"Nuclear-localized Asunder regulates cytoplasmic dynein localization
via its role in the integrator complex.";
Mol. Biol. Cell 24:2954-2965(2013).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Component of the Integrator (INT) complex. The
Integrator complex is involved in the small nuclear RNAs (snRNA)
U1 and U2 transcription and in their 3'-box-dependent processing.
The Integrator complex is associated with the C-terminal domain
(CTD) of RNA polymerase II largest subunit (POLR2A) and is
recruited to the U1 and U2 snRNAs genes (Probable). Mediates
recruitment of cytoplasmic dynein to the nuclear envelope,
probably as component of the INT complex (PubMed:23904267).
{ECO:0000269|PubMed:23904267, ECO:0000305|PubMed:16239144}.
-!- FUNCTION: Component of the SOSS complex, a multiprotein complex
that functions downstream of the MRN complex to promote DNA repair
and G2/M checkpoint. The SOSS complex associates with single-
stranded DNA at DNA lesions and influences diverse endpoints in
the cellular DNA damage response including cell-cycle checkpoint
activation, recombinational repair and maintenance of genomic
stability. The SOSS complex is required for efficient homologous
recombination-dependent repair of double-strand breaks (DSBs) and
ATM-dependent signaling pathways. In the SOSS complex, it is
required for the assembly of the complex and for stabilization of
the complex at DNA damage sites. {ECO:0000269|PubMed:19605351,
ECO:0000269|PubMed:19683501}.
-!- SUBUNIT: Belongs to the multiprotein complex Integrator, at least
composed of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7,
INTS8, INTS9/RC74, INTS10, INTS11/CPSF3L and INTS12. Component of
the SOSS complex, composed of SOSS-B (SOSS-B1/NABP2 or SOSS-
B2/NABP1), SOSS-A/INTS3 and SOSS-C/INIP. SOSS complexes containing
SOSS-B1/NABP2 are more abundant than complexes containing SOSS-
B2/NABP1. Interacts with SOSS-B1/NABP2, SOSS-B2/NABP1 and SOSS-
C/INIP; the interaction is direct. Interacts with NBN/NBS1.
{ECO:0000269|PubMed:16239144, ECO:0000269|PubMed:19605351,
ECO:0000269|PubMed:19683501}.
-!- INTERACTION:
Q9NRY2:INIP; NbExp=6; IntAct=EBI-2680854, EBI-2881520;
Q96AH0:NABP1; NbExp=5; IntAct=EBI-2680854, EBI-2889252;
Q9BQ15:NABP2; NbExp=7; IntAct=EBI-2680854, EBI-2120336;
O60934:NBN; NbExp=2; IntAct=EBI-2680854, EBI-494844;
O43829:ZBTB14; NbExp=3; IntAct=EBI-2680854, EBI-10176632;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19605351,
ECO:0000269|PubMed:19683501, ECO:0000269|PubMed:23904267}.
Cytoplasm {ECO:0000269|PubMed:23904267}. Note=Localizes to nuclear
foci following DNA damage.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q68E01-1; Sequence=Displayed;
Name=2;
IsoId=Q68E01-2; Sequence=VSP_021446;
Name=3;
IsoId=Q68E01-3; Sequence=VSP_038131, VSP_038132;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q68E01-4; Sequence=VSP_038130;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the Integrator subunit 3 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH25254.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH54513.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB15174.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC11329.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAH18229.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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EMBL; AL832133; CAH10398.1; -; mRNA.
EMBL; AK290025; BAF82714.1; -; mRNA.
EMBL; AK298746; BAG60890.1; -; mRNA.
EMBL; AK304874; BAG65611.1; -; mRNA.
EMBL; BX640786; CAE45876.1; -; mRNA.
EMBL; BX640950; CAE45974.1; -; mRNA.
EMBL; CR627233; CAH10366.1; -; mRNA.
EMBL; CR749212; CAH18069.1; -; mRNA.
EMBL; CR749376; CAH18229.1; ALT_SEQ; mRNA.
EMBL; AL513523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW53279.1; -; Genomic_DNA.
EMBL; CH471121; EAW53283.1; -; Genomic_DNA.
EMBL; BC025254; AAH25254.1; ALT_INIT; mRNA.
EMBL; BC054513; AAH54513.1; ALT_INIT; mRNA.
EMBL; BC073985; AAH73985.1; -; mRNA.
EMBL; BC098431; AAH98431.1; -; mRNA.
EMBL; BC105092; AAI05093.1; -; mRNA.
EMBL; BC105094; AAI05095.1; -; mRNA.
EMBL; BC116458; AAI16459.1; -; mRNA.
EMBL; AK025572; BAB15174.1; ALT_INIT; mRNA.
EMBL; AK074979; BAC11329.1; ALT_INIT; mRNA.
EMBL; BK005722; DAA05722.1; -; Genomic_DNA.
CCDS; CCDS1052.1; -. [Q68E01-2]
RefSeq; NP_001311404.1; NM_001324475.1. [Q68E01-2]
RefSeq; NP_075391.3; NM_023015.4. [Q68E01-2]
RefSeq; XP_005245518.1; XM_005245461.2. [Q68E01-4]
UniGene; Hs.438723; -.
UniGene; Hs.516522; -.
PDB; 4OWT; X-ray; 2.00 A; A=35-499.
PDB; 4OWW; X-ray; 2.30 A; A=1-501.
PDB; 4OWX; X-ray; 2.30 A; A=1-501.
PDBsum; 4OWT; -.
PDBsum; 4OWW; -.
PDBsum; 4OWX; -.
ProteinModelPortal; Q68E01; -.
SMR; Q68E01; -.
BioGrid; 122401; 64.
CORUM; Q68E01; -.
IntAct; Q68E01; 19.
MINT; MINT-4534920; -.
STRING; 9606.ENSP00000318641; -.
iPTMnet; Q68E01; -.
PhosphoSitePlus; Q68E01; -.
BioMuta; INTS3; -.
DMDM; 74724494; -.
EPD; Q68E01; -.
MaxQB; Q68E01; -.
PaxDb; Q68E01; -.
PeptideAtlas; Q68E01; -.
PRIDE; Q68E01; -.
Ensembl; ENST00000318967; ENSP00000318641; ENSG00000143624. [Q68E01-2]
Ensembl; ENST00000435409; ENSP00000404290; ENSG00000143624. [Q68E01-2]
Ensembl; ENST00000512605; ENSP00000425437; ENSG00000143624. [Q68E01-3]
Ensembl; ENST00000571768; ENSP00000458631; ENSG00000262826. [Q68E01-2]
Ensembl; ENST00000576030; ENSP00000460221; ENSG00000262826. [Q68E01-2]
Ensembl; ENST00000576422; ENSP00000459907; ENSG00000262826. [Q68E01-3]
GeneID; 65123; -.
KEGG; hsa:65123; -.
UCSC; uc001fct.4; human. [Q68E01-1]
CTD; 65123; -.
DisGeNET; 65123; -.
EuPathDB; HostDB:ENSG00000143624.13; -.
GeneCards; INTS3; -.
H-InvDB; HIX0001090; -.
HGNC; HGNC:26153; INTS3.
HPA; HPA074391; -.
MIM; 611347; gene.
neXtProt; NX_Q68E01; -.
OpenTargets; ENSG00000143624; -.
PharmGKB; PA142672510; -.
eggNOG; KOG4262; Eukaryota.
eggNOG; ENOG410XRCW; LUCA.
GeneTree; ENSGT00390000014184; -.
HOVERGEN; HBG081800; -.
InParanoid; Q68E01; -.
KO; K13140; -.
OMA; RFLQCRL; -.
OrthoDB; EOG091G02QS; -.
PhylomeDB; Q68E01; -.
TreeFam; TF323623; -.
Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
ChiTaRS; INTS3; human.
GeneWiki; INTS3; -.
GenomeRNAi; 65123; -.
PRO; PR:Q68E01; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000143624; -.
ExpressionAtlas; Q68E01; baseline and differential.
Genevisible; Q68E01; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0032039; C:integrator complex; IDA:HGNC.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0070876; C:SOSS complex; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
GO; GO:0007093; P:mitotic cell cycle checkpoint; IMP:UniProtKB.
GO; GO:0010212; P:response to ionizing radiation; IMP:UniProtKB.
GO; GO:0016180; P:snRNA processing; IDA:HGNC.
GO; GO:0042795; P:snRNA transcription from RNA polymerase II promoter; TAS:Reactome.
InterPro; IPR019333; Int_cplx_su3.
Pfam; PF10189; Ints3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; DNA damage; DNA repair; Nucleus; Phosphoprotein;
Reference proteome.
CHAIN 1 1043 Integrator complex subunit 3.
/FTId=PRO_0000259534.
COMPBIAS 9 34 Ala/Gly-rich.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 502 502 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 537 537 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 995 995 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
VAR_SEQ 1 488 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038130.
VAR_SEQ 1 207 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038131.
VAR_SEQ 173 173 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_021446.
VAR_SEQ 942 942 F -> CMPSTLGVQCRRCCPGPDYAWSQAGGRGRTPGATTH
TRDKTTCACCLISSQTSDCFSFPALPFLPLV (in
isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038132.
CONFLICT 134 134 Y -> C (in Ref. 1; CAE45974).
{ECO:0000305}.
CONFLICT 300 300 K -> E (in Ref. 2; BAF82714).
{ECO:0000305}.
CONFLICT 363 363 E -> G (in Ref. 1; CAE45974).
{ECO:0000305}.
CONFLICT 685 685 P -> T (in Ref. 1; CAE45974).
{ECO:0000305}.
CONFLICT 803 803 W -> R (in Ref. 1; CAE45876).
{ECO:0000305}.
CONFLICT 827 827 P -> L (in Ref. 2; BAC11329).
{ECO:0000305}.
CONFLICT 896 896 L -> P (in Ref. 2; BAG60890).
{ECO:0000305}.
CONFLICT 952 952 L -> P (in Ref. 2; BAG65611).
{ECO:0000305}.
CONFLICT 967 967 F -> L (in Ref. 1; CAE45876).
{ECO:0000305}.
CONFLICT 972 972 S -> P (in Ref. 2; BAB15174).
{ECO:0000305}.
STRAND 35 37 {ECO:0000244|PDB:4OWT}.
STRAND 41 43 {ECO:0000244|PDB:4OWT}.
HELIX 47 63 {ECO:0000244|PDB:4OWT}.
HELIX 69 79 {ECO:0000244|PDB:4OWT}.
HELIX 83 99 {ECO:0000244|PDB:4OWT}.
TURN 101 103 {ECO:0000244|PDB:4OWT}.
HELIX 104 114 {ECO:0000244|PDB:4OWT}.
HELIX 120 132 {ECO:0000244|PDB:4OWT}.
HELIX 134 136 {ECO:0000244|PDB:4OWT}.
HELIX 139 154 {ECO:0000244|PDB:4OWT}.
HELIX 160 169 {ECO:0000244|PDB:4OWT}.
HELIX 179 194 {ECO:0000244|PDB:4OWT}.
HELIX 196 199 {ECO:0000244|PDB:4OWT}.
HELIX 203 217 {ECO:0000244|PDB:4OWT}.
HELIX 224 243 {ECO:0000244|PDB:4OWT}.
HELIX 245 248 {ECO:0000244|PDB:4OWT}.
HELIX 249 251 {ECO:0000244|PDB:4OWT}.
HELIX 253 261 {ECO:0000244|PDB:4OWT}.
TURN 262 264 {ECO:0000244|PDB:4OWT}.
HELIX 266 277 {ECO:0000244|PDB:4OWT}.
HELIX 279 282 {ECO:0000244|PDB:4OWT}.
HELIX 289 293 {ECO:0000244|PDB:4OWT}.
HELIX 299 304 {ECO:0000244|PDB:4OWT}.
HELIX 308 317 {ECO:0000244|PDB:4OWT}.
STRAND 320 322 {ECO:0000244|PDB:4OWW}.
HELIX 327 337 {ECO:0000244|PDB:4OWT}.
STRAND 338 341 {ECO:0000244|PDB:4OWT}.
HELIX 342 345 {ECO:0000244|PDB:4OWT}.
HELIX 346 356 {ECO:0000244|PDB:4OWT}.
HELIX 362 366 {ECO:0000244|PDB:4OWT}.
STRAND 367 369 {ECO:0000244|PDB:4OWW}.
HELIX 372 381 {ECO:0000244|PDB:4OWT}.
HELIX 386 396 {ECO:0000244|PDB:4OWT}.
TURN 397 402 {ECO:0000244|PDB:4OWT}.
TURN 405 407 {ECO:0000244|PDB:4OWT}.
HELIX 410 423 {ECO:0000244|PDB:4OWT}.
TURN 424 426 {ECO:0000244|PDB:4OWT}.
HELIX 428 444 {ECO:0000244|PDB:4OWT}.
HELIX 447 449 {ECO:0000244|PDB:4OWT}.
HELIX 450 466 {ECO:0000244|PDB:4OWT}.
STRAND 469 471 {ECO:0000244|PDB:4OWT}.
HELIX 474 477 {ECO:0000244|PDB:4OWT}.
HELIX 484 493 {ECO:0000244|PDB:4OWT}.
HELIX 495 497 {ECO:0000244|PDB:4OWT}.
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


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