INT11_HUMAN
ID INT11_HUMAN Reviewed; 600 AA.
AC Q5TA45; A8K5S2; B3KPR3; B4DM87; G3V1S5; Q5TA46; Q5TA48; Q5TA52; Q5TA53;
AC Q5TA54; Q7L3D7; Q96HY1; Q9BW36; Q9H0F9; Q9H8R5; Q9HAA6; Q9NWX9;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Integrator complex subunit 11;
DE Short=Int11;
DE EC=3.1.27.-;
DE AltName: Full=Cleavage and polyadenylation-specific factor 3-like protein;
DE Short=CPSF3-like protein;
DE AltName: Full=Protein related to CPSF subunits of 68 kDa;
DE Short=RC-68;
GN Name=INTS11 {ECO:0000312|HGNC:HGNC:26052}; Synonyms=CPSF3L, RC68;
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] (ISOFORM 1).
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 5).
RC TISSUE=Brain, and Embryo;
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 MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon, Lymph, and Ovary;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE INTEGRATOR
RP COMPLEX, FUNCTION, AND MUTAGENESIS OF GLU-203.
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 [8]
RP IDENTIFICATION, SUBCELLULAR LOCATION, AND INTERACTION WITH INTS9.
RX PubMed=15684398; DOI=10.1128/mcb.25.4.1489-1500.2005;
RA Dominski Z., Yang X.-C., Purdy M., Wagner E.J., Marzluff W.F.;
RT "A CPSF-73 homologue is required for cell cycle progression but not cell
RT growth and interacts with a protein having features of CPSF-100.";
RL Mol. Cell. Biol. 25:1489-1500(2005).
RN [9]
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 [10]
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).
CC -!- FUNCTION: Catalytic component of the Integrator (INT) complex, a
CC complex 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. Mediates the snRNAs 3' cleavage. Mediates recruitment
CC of cytoplasmic dynein to the nuclear envelope, probably as component of
CC the INT complex (PubMed:23904267). {ECO:0000269|PubMed:16239144,
CC ECO:0000269|PubMed:23904267}.
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.
CC {ECO:0000269|PubMed:16239144}.
CC -!- INTERACTION:
CC Q5TA45; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-748258, EBI-946029;
CC Q5TA45; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-748258, EBI-744556;
CC Q5TA45; Q02930-3: CREB5; NbExp=3; IntAct=EBI-748258, EBI-10192698;
CC Q5TA45; Q8WU58: FAM222B; NbExp=3; IntAct=EBI-748258, EBI-2807642;
CC Q5TA45; Q13227: GPS2; NbExp=3; IntAct=EBI-748258, EBI-713355;
CC Q5TA45; Q9ULV5-2: HSF4; NbExp=3; IntAct=EBI-748258, EBI-12056251;
CC Q5TA45; Q9NV88: INTS9; NbExp=16; IntAct=EBI-748258, EBI-2866634;
CC Q5TA45; Q3LI76: KRTAP15-1; NbExp=3; IntAct=EBI-748258, EBI-11992140;
CC Q5TA45; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-748258, EBI-3957672;
CC Q5TA45; Q14847-2: LASP1; NbExp=3; IntAct=EBI-748258, EBI-9088686;
CC Q5TA45; Q96PV6: LENG8; NbExp=3; IntAct=EBI-748258, EBI-739546;
CC Q5TA45; P32242: OTX1; NbExp=3; IntAct=EBI-748258, EBI-740446;
CC Q5TA45; Q8TDS5: OXER1; NbExp=3; IntAct=EBI-748258, EBI-12813389;
CC Q5TA45; Q16512: PKN1; NbExp=3; IntAct=EBI-748258, EBI-602382;
CC Q5TA45; Q9NRQ2: PLSCR4; NbExp=3; IntAct=EBI-748258, EBI-769257;
CC Q5TA45; O75360: PROP1; NbExp=3; IntAct=EBI-748258, EBI-9027467;
CC Q5TA45; P0CG20: PRR35; NbExp=3; IntAct=EBI-748258, EBI-11986293;
CC Q5TA45; P09234: SNRPC; NbExp=3; IntAct=EBI-748258, EBI-766589;
CC Q5TA45; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-748258, EBI-11959123;
CC Q5TA45; Q8N5J4: SPIC; NbExp=3; IntAct=EBI-748258, EBI-12261246;
CC Q5TA45; O95947: TBX6; NbExp=3; IntAct=EBI-748258, EBI-2824328;
CC Q5TA45; Q9NQB0-10: TCF7L2; NbExp=3; IntAct=EBI-748258, EBI-11746252;
CC Q5TA45; Q92734: TFG; NbExp=3; IntAct=EBI-748258, EBI-357061;
CC Q5TA45; O43711: TLX3; NbExp=3; IntAct=EBI-748258, EBI-3939165;
CC Q5TA45; O75604: USP2; NbExp=3; IntAct=EBI-748258, EBI-743272;
CC Q5TA45; Q08AM6: VAC14; NbExp=3; IntAct=EBI-748258, EBI-2107455;
CC Q5TA45; O95231: VENTX; NbExp=3; IntAct=EBI-748258, EBI-10191303;
CC Q5TA45; Q96K80: ZC3H10; NbExp=3; IntAct=EBI-748258, EBI-742550;
CC Q5TA45; Q15915: ZIC1; NbExp=3; IntAct=EBI-748258, EBI-11963196;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15684398,
CC ECO:0000269|PubMed:23904267}. Cytoplasm {ECO:0000269|PubMed:15684398,
CC ECO:0000269|PubMed:23904267}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q5TA45-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5TA45-2; Sequence=VSP_021472;
CC Name=3;
CC IsoId=Q5TA45-3; Sequence=VSP_021473;
CC Name=4;
CC IsoId=Q5TA45-4; Sequence=VSP_045428;
CC Name=5;
CC IsoId=Q5TA45-5; Sequence=VSP_046643;
CC -!- DOMAIN: The HXHXDH motif is essential for the endoribonuclease activity
CC of the CPSF complex. {ECO:0000250|UniProtKB:Q9VAH9}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC metabolizing metallo-beta-lactamase-like family. INTS11 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91246.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB14541.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL136813; CAB66747.1; -; mRNA.
DR EMBL; AK000549; BAA91246.1; ALT_SEQ; mRNA.
DR EMBL; AK021939; BAB13943.1; -; mRNA.
DR EMBL; AK023356; BAB14541.1; ALT_FRAME; mRNA.
DR EMBL; AK056652; BAG51775.1; -; mRNA.
DR EMBL; AK291387; BAF84076.1; -; mRNA.
DR EMBL; AK297350; BAG59799.1; -; mRNA.
DR EMBL; CR533557; CAG38588.1; -; mRNA.
DR EMBL; AL139287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471183; EAW56238.1; -; Genomic_DNA.
DR EMBL; BC000675; AAH00675.2; -; mRNA.
DR EMBL; BC007978; AAH07978.1; -; mRNA.
DR EMBL; BC013904; AAH13904.2; -; mRNA.
DR EMBL; BK005728; DAA05728.1; -; mRNA.
DR EMBL; BK005673; DAA05669.1; -; mRNA.
DR CCDS; CCDS21.1; -. [Q5TA45-1]
DR CCDS; CCDS57959.1; -. [Q5TA45-4]
DR CCDS; CCDS57960.1; -. [Q5TA45-5]
DR CCDS; CCDS57961.1; -. [Q5TA45-2]
DR RefSeq; NP_001243385.1; NM_001256456.1. [Q5TA45-5]
DR RefSeq; NP_001243389.1; NM_001256460.1. [Q5TA45-4]
DR RefSeq; NP_001243391.1; NM_001256462.1.
DR RefSeq; NP_001243392.1; NM_001256463.1. [Q5TA45-2]
DR RefSeq; NP_060341.2; NM_017871.5. [Q5TA45-1]
DR PDB; 5V8W; X-ray; 2.10 A; B/D/F/H=491-600.
DR PDB; 7BFP; EM; 3.50 A; B=1-600.
DR PDB; 7BFQ; EM; 3.50 A; B=1-600.
DR PDB; 7CUN; EM; 3.50 A; K=1-600.
DR PDB; 7PKS; EM; 3.60 A; k=1-600.
DR PDBsum; 5V8W; -.
DR PDBsum; 7BFP; -.
DR PDBsum; 7BFQ; -.
DR PDBsum; 7CUN; -.
DR PDBsum; 7PKS; -.
DR AlphaFoldDB; Q5TA45; -.
DR SMR; Q5TA45; -.
DR BioGRID; 120310; 90.
DR ComplexPortal; CPX-6441; Integrator complex.
DR CORUM; Q5TA45; -.
DR IntAct; Q5TA45; 64.
DR MINT; Q5TA45; -.
DR STRING; 9606.ENSP00000445001; -.
DR iPTMnet; Q5TA45; -.
DR PhosphoSitePlus; Q5TA45; -.
DR BioMuta; INTS11; -.
DR DMDM; 118572557; -.
DR EPD; Q5TA45; -.
DR jPOST; Q5TA45; -.
DR MassIVE; Q5TA45; -.
DR MaxQB; Q5TA45; -.
DR PaxDb; Q5TA45; -.
DR PeptideAtlas; Q5TA45; -.
DR PRIDE; Q5TA45; -.
DR ProteomicsDB; 32426; -.
DR ProteomicsDB; 4590; -.
DR ProteomicsDB; 64825; -. [Q5TA45-1]
DR ProteomicsDB; 64826; -. [Q5TA45-2]
DR ProteomicsDB; 64827; -. [Q5TA45-3]
DR Antibodypedia; 26257; 201 antibodies from 26 providers.
DR DNASU; 54973; -.
DR Ensembl; ENST00000419704.5; ENSP00000404886.1; ENSG00000127054.22. [Q5TA45-2]
DR Ensembl; ENST00000435064.6; ENSP00000413493.2; ENSG00000127054.22. [Q5TA45-1]
DR Ensembl; ENST00000450926.6; ENSP00000392848.2; ENSG00000127054.22. [Q5TA45-3]
DR Ensembl; ENST00000540437.5; ENSP00000445001.1; ENSG00000127054.22. [Q5TA45-5]
DR Ensembl; ENST00000545578.5; ENSP00000444672.1; ENSG00000127054.22. [Q5TA45-4]
DR GeneID; 54973; -.
DR KEGG; hsa:54973; -.
DR MANE-Select; ENST00000435064.6; ENSP00000413493.2; NM_017871.6; NP_060341.2.
DR UCSC; uc001aee.3; human. [Q5TA45-1]
DR CTD; 54973; -.
DR DisGeNET; 54973; -.
DR GeneCards; INTS11; -.
DR HGNC; HGNC:26052; INTS11.
DR HPA; ENSG00000127054; Low tissue specificity.
DR MIM; 611354; gene.
DR neXtProt; NX_Q5TA45; -.
DR OpenTargets; ENSG00000127054; -.
DR PharmGKB; PA142672080; -.
DR VEuPathDB; HostDB:ENSG00000127054; -.
DR eggNOG; KOG1136; Eukaryota.
DR GeneTree; ENSGT00940000157644; -.
DR HOGENOM; CLU_009673_3_0_1; -.
DR InParanoid; Q5TA45; -.
DR OMA; YLDGMIW; -.
DR OrthoDB; 218195at2759; -.
DR PhylomeDB; Q5TA45; -.
DR TreeFam; TF105878; -.
DR PathwayCommons; Q5TA45; -.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR SignaLink; Q5TA45; -.
DR SIGNOR; Q5TA45; -.
DR BioGRID-ORCS; 54973; 763 hits in 1078 CRISPR screens.
DR ChiTaRS; CPSF3L; human.
DR GeneWiki; CPSF3L; -.
DR GenomeRNAi; 54973; -.
DR Pharos; Q5TA45; Tbio.
DR PRO; PR:Q5TA45; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5TA45; protein.
DR Bgee; ENSG00000127054; Expressed in right hemisphere of cerebellum and 95 other tissues.
DR ExpressionAtlas; Q5TA45; baseline and differential.
DR Genevisible; Q5TA45; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0032039; C:integrator complex; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004521; F:endoribonuclease activity; IMP:FlyBase.
DR GO; GO:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; IC:ComplexPortal.
DR GO; GO:0016180; P:snRNA processing; IDA:BHF-UCL.
DR CDD; cd16291; INTS11-like_MBL-fold; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR022712; Beta_Casp.
DR InterPro; IPR041897; INTS11-like_MBL-fold.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR011108; RMMBL.
DR Pfam; PF10996; Beta-Casp; 1.
DR Pfam; PF16661; Lactamase_B_6; 1.
DR Pfam; PF07521; RMMBL; 1.
DR SMART; SM01027; Beta-Casp; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Hydrolase; Nucleus;
KW Reference proteome.
FT CHAIN 1..600
FT /note="Integrator complex subunit 11"
FT /id="PRO_0000259563"
FT MOTIF 68..73
FT /note="HXHXDH motif"
FT VAR_SEQ 1..29
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045428"
FT VAR_SEQ 1..9
FT /note="MPEIRVTPL -> MCGAGFGHFEWLAGG (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046643"
FT VAR_SEQ 43..143
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021472"
FT VAR_SEQ 143..164
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021473"
FT MUTAGEN 203
FT /note="E->Q: Abolishes the ability of the Integrator
FT complex to process U1 and U2 snRNA genes."
FT /evidence="ECO:0000269|PubMed:16239144"
FT CONFLICT 95
FT /note="P -> S (in Ref. 1; CAB66747 and 3; CAG38588)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="E -> K (in Ref. 2; BAB13943)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="N -> D (in Ref. 2; BAF84076)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="A -> V (in Ref. 2; BAG51775)"
FT /evidence="ECO:0000305"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:7BFP"
FT TURN 49..53
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:7BFP"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:7BFP"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:7BFP"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:7BFP"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:7BFP"
FT HELIX 94..113
FT /evidence="ECO:0007829|PDB:7BFP"
FT HELIX 123..130
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 213..229
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:7BFP"
FT HELIX 242..258
FT /evidence="ECO:0007829|PDB:7BFP"
FT HELIX 272..281
FT /evidence="ECO:0007829|PDB:7BFP"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:7BFP"
FT HELIX 288..296
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:7CUN"
FT HELIX 305..311
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 326..331
FT /evidence="ECO:0007829|PDB:7BFP"
FT HELIX 332..340
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:7BFP"
FT HELIX 358..365
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 382..386
FT /evidence="ECO:0007829|PDB:7BFP"
FT HELIX 395..405
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 408..415
FT /evidence="ECO:0007829|PDB:7BFP"
FT HELIX 417..430
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 444..447
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 453..457
FT /evidence="ECO:0007829|PDB:7BFP"
FT HELIX 458..469
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:7CUN"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:7BFP"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:7BFP"
FT HELIX 495..500
FT /evidence="ECO:0007829|PDB:5V8W"
FT TURN 501..503
FT /evidence="ECO:0007829|PDB:5V8W"
FT STRAND 508..518
FT /evidence="ECO:0007829|PDB:5V8W"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:7BFQ"
FT HELIX 523..537
FT /evidence="ECO:0007829|PDB:5V8W"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:5V8W"
FT STRAND 551..553
FT /evidence="ECO:0007829|PDB:5V8W"
FT STRAND 556..560
FT /evidence="ECO:0007829|PDB:5V8W"
FT STRAND 569..577
FT /evidence="ECO:0007829|PDB:5V8W"
FT HELIX 578..580
FT /evidence="ECO:0007829|PDB:5V8W"
FT HELIX 581..591
FT /evidence="ECO:0007829|PDB:5V8W"
SQ SEQUENCE 600 AA; 67663 MW; 47C4E2E16202B130 CRC64;
MPEIRVTPLG AGQDVGRSCI LVSIAGKNVM LDCGMHMGFN DDRRFPDFSY ITQNGRLTDF
LDCVIISHFH LDHCGALPYF SEMVGYDGPI YMTHPTQAIC PILLEDYRKI AVDKKGEANF
FTSQMIKDCM KKVVAVHLHQ TVQVDDELEI KAYYAGHVLG AAMFQIKVGS ESVVYTGDYN
MTPDRHLGAA WIDKCRPNLL ITESTYATTI RDSKRCRERD FLKKVHETVE RGGKVLIPVF
ALGRAQELCI LLETFWERMN LKVPIYFSTG LTEKANHYYK LFIPWTNQKI RKTFVQRNMF
EFKHIKAFDR AFADNPGPMV VFATPGMLHA GQSLQIFRKW AGNEKNMVIM PGYCVQGTVG
HKILSGQRKL EMEGRQVLEV KMQVEYMSFS AHADAKGIMQ LVGQAEPESV LLVHGEAKKM
EFLKQKIEQE LRVNCYMPAN GETVTLPTSP SIPVGISLGL LKREMAQGLL PEAKKPRLLH
GTLIMKDSNF RLVSSEQALK ELGLAEHQLR FTCRVHLHDT RKEQETALRV YSHLKSVLKD
HCVQHLPDGS VTVESVLLQA AAPSEDPGTK VLLVSWTYQD EELGSFLTSL LKKGLPQAPS
