ID INT13_HUMAN Reviewed; 706 AA. AC Q9NVM9; B4DNK1; Q86WE2; Q96HM2; Q9BTX2; Q9NTB6; Q9NVM5; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 2. DT 27-MAR-2024, entry version 152. DE RecName: Full=Integrator complex subunit 13 {ECO:0000312|HGNC:HGNC:20174}; DE AltName: Full=Cell cycle regulator Mat89Bb homolog; DE AltName: Full=Germ cell tumor 1; DE AltName: Full=Protein asunder homolog; DE AltName: Full=Sarcoma antigen NY-SAR-95; GN Name=INTS13 {ECO:0000312|HGNC:HGNC:20174}; GN Synonyms=ASUN {ECO:0000312|HGNC:HGNC:20174}, C12orf11, GCT1; 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). 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Eye, and Lymph; 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 [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 269-513 (ISOFORM 1). RX PubMed=12601173; DOI=10.1073/pnas.0437972100; RA Lee S.-Y., Obata Y., Yoshida M., Stockert E., Williamson B., RA Jungbluth A.A., Chen Y.-T., Old L.J., Scanlan M.J.; RT "Immunomic analysis of human sarcoma."; RL Proc. Natl. Acad. Sci. U.S.A. 100:2651-2656(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 568-706 (ISOFORM 1). RC TISSUE=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 [6] RP TISSUE SPECIFICITY. RX PubMed=12414650; RA Bourdon V., Naef F., Rao P.H., Reuter V., Mok S.C., Bosl G.J., Koul S., RA Murty V.V., Kucherlapati R.S., Chaganti R.S.; RT "Genomic and expression analysis of the 12p11-p12 amplicon using EST arrays RT identifies two novel amplified and overexpressed genes."; RL Cancer Res. 62:6218-6223(2002). RN [7] RP FUNCTION. RX PubMed=15737938; DOI=10.1016/j.devcel.2004.12.008; RA Lee L.A., Lee E., Anderson M.A., Vardy L., Tahinci E., Ali S.M., RA Kashevsky H., Benasutti M., Kirschner M.W., Orr-Weaver T.L.; RT "Drosophila genome-scale screen for PAN GU kinase substrates identifies RT Mat89Bb as a cell cycle regulator."; RL Dev. Cell 8:435-442(2005). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, AND IDENTIFICATION BY RP 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, 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 [11] 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 [12] 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 [13] RP FUNCTION, INTERACTION WITH PAFAH1B1, AND SUBCELLULAR LOCATION. RX PubMed=23097494; DOI=10.1091/mbc.e12-07-0558; RA Jodoin J.N., Shboul M., Sitaram P., Zein-Sabatto H., Reversade B., Lee E., RA Lee L.A.; RT "Human Asunder promotes dynein recruitment and centrosomal tethering to the RT nucleus at mitotic entry."; RL Mol. Biol. Cell 23:4713-4724(2012). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-623 AND SER-626, 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 [15] RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 577-ARG--ASP-582, AND RP DOMAIN. 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, 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). RN [17] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-611, AND IDENTIFICATION BY MASS RP SPECTROMETRY [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 [18] RP VARIANT [LARGE SCALE ANALYSIS] PRO-227. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Crucial regulator of the mitotic cell cycle and development. CC At prophase, required for dynein anchoring to the nuclear envelope CC important for proper centrosome-nucleus coupling. At G2/M phase, may be CC required for proper spindle formation and execution of cytokinesis. CC Probable component of the Integrator (INT) complex, a complex involved CC in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their CC 3'-box-dependent processing (PubMed:23904267). CC {ECO:0000269|PubMed:15737938, ECO:0000269|PubMed:23097494, CC ECO:0000269|PubMed:23904267, ECO:0000305|PubMed:23097494, CC ECO:0000305|PubMed:23904267}. CC -!- SUBUNIT: Interacts with PAFAH1B1; this interaction may be required for CC proper recruitment of dynein complexes to the nuclear envelope at CC prophase. {ECO:0000269|PubMed:23097494}. CC -!- INTERACTION: CC Q9NVM9; Q13951: CBFB; NbExp=2; IntAct=EBI-741429, EBI-718750; CC Q9NVM9; Q96SY0: INTS14; NbExp=16; IntAct=EBI-741429, EBI-4409724; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23904267}. Cytoplasm CC {ECO:0000269|PubMed:23097494, ECO:0000269|PubMed:23904267}. CC Note=Nuclear location is required for recruitment of dynein motors to CC nuclear envelope at G2/M. {ECO:0000269|PubMed:17974005}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9NVM9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NVM9-2; Sequence=VSP_056514; CC -!- TISSUE SPECIFICITY: Widely expressed. Tends to be up-regulated in CC seminomas compared to normal testis. {ECO:0000269|PubMed:12414650}. CC -!- MISCELLANEOUS: RNAi in HeLa cells results in a multinucleated CC phenotype. CC -!- SIMILARITY: Belongs to the asunder family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAO65180.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK001492; BAA91721.1; -; mRNA. DR EMBL; AK001499; BAA91725.1; -; mRNA. DR EMBL; AK297948; BAG60263.1; -; mRNA. DR EMBL; AC024093; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC003081; AAH03081.1; -; mRNA. DR EMBL; BC008368; AAH08368.1; -; mRNA. DR EMBL; AY211927; AAO65180.1; ALT_FRAME; mRNA. DR EMBL; AL137401; CAB70726.1; -; mRNA. DR CCDS; CCDS8708.1; -. [Q9NVM9-1] DR PIR; T46457; T46457. DR RefSeq; NP_060634.2; NM_018164.2. [Q9NVM9-1] DR RefSeq; XP_016875121.1; XM_017019632.1. [Q9NVM9-1] DR PDB; 6SN1; X-ray; 2.54 A; A=1-706. DR PDBsum; 6SN1; -. DR AlphaFoldDB; Q9NVM9; -. DR SMR; Q9NVM9; -. DR BioGRID; 120846; 64. DR ComplexPortal; CPX-6441; Integrator complex. DR IntAct; Q9NVM9; 21. DR MINT; Q9NVM9; -. DR STRING; 9606.ENSP00000261191; -. DR GlyGen; Q9NVM9; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9NVM9; -. DR MetOSite; Q9NVM9; -. DR PhosphoSitePlus; Q9NVM9; -. DR SwissPalm; Q9NVM9; -. DR BioMuta; INTS13; -. DR DMDM; 71153010; -. DR EPD; Q9NVM9; -. DR jPOST; Q9NVM9; -. DR MassIVE; Q9NVM9; -. DR MaxQB; Q9NVM9; -. DR PaxDb; 9606-ENSP00000261191; -. DR PeptideAtlas; Q9NVM9; -. DR ProteomicsDB; 4703; -. DR ProteomicsDB; 82831; -. [Q9NVM9-1] DR Pumba; Q9NVM9; -. DR Antibodypedia; 42367; 75 antibodies from 20 providers. DR DNASU; 55726; -. DR Ensembl; ENST00000261191.12; ENSP00000261191.7; ENSG00000064102.15. [Q9NVM9-1] DR GeneID; 55726; -. DR KEGG; hsa:55726; -. DR MANE-Select; ENST00000261191.12; ENSP00000261191.7; NM_018164.3; NP_060634.2. DR UCSC; uc001rhk.5; human. [Q9NVM9-1] DR AGR; HGNC:20174; -. DR CTD; 55726; -. DR DisGeNET; 55726; -. DR GeneCards; INTS13; -. DR HGNC; HGNC:20174; INTS13. DR HPA; ENSG00000064102; Low tissue specificity. DR MIM; 615079; gene. DR neXtProt; NX_Q9NVM9; -. DR OpenTargets; ENSG00000064102; -. DR PharmGKB; PA134892469; -. DR VEuPathDB; HostDB:ENSG00000064102; -. DR eggNOG; KOG3711; Eukaryota. DR GeneTree; ENSGT00390000002793; -. DR HOGENOM; CLU_012654_1_0_1; -. DR InParanoid; Q9NVM9; -. DR OMA; CMDEAPS; -. DR OrthoDB; 2882611at2759; -. DR PhylomeDB; Q9NVM9; -. DR TreeFam; TF105815; -. DR PathwayCommons; Q9NVM9; -. DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes. DR SignaLink; Q9NVM9; -. DR SIGNOR; Q9NVM9; -. DR BioGRID-ORCS; 55726; 341 hits in 1157 CRISPR screens. DR ChiTaRS; ASUN; human. DR GeneWiki; C12orf11; -. DR GenomeRNAi; 55726; -. DR Pharos; Q9NVM9; Tbio. DR PRO; PR:Q9NVM9; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q9NVM9; Protein. DR Bgee; ENSG00000064102; Expressed in esophagus squamous epithelium and 203 other cell types or tissues. DR ExpressionAtlas; Q9NVM9; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0032039; C:integrator complex; IBA:GO_Central. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0051642; P:centrosome localization; IMP:MGI. DR GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB. DR GO; GO:0007052; P:mitotic spindle organization; IMP:MGI. DR GO; GO:0090435; P:protein localization to nuclear envelope; IMP:MGI. DR GO; GO:0080154; P:regulation of fertilization; ISS:UniProtKB. DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:UniProtKB. DR GO; GO:0034243; P:regulation of transcription elongation by RNA polymerase II; NAS:ComplexPortal. DR GO; GO:0016180; P:snRNA processing; NAS:ComplexPortal. DR InterPro; IPR019355; Cell_cycle_regulator_Mat89Bb. DR PANTHER; PTHR12955:SF1; INTEGRATOR COMPLEX SUBUNIT 13; 1. DR PANTHER; PTHR12955; SARCOMA ANTIGEN NY-SAR-95-RELATED; 1. DR Pfam; PF10221; Mat89Bb; 1. DR Genevisible; Q9NVM9; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Coiled coil; KW Cytoplasm; Isopeptide bond; Mitosis; Nucleus; Phosphoprotein; KW Reference proteome; Ubl conjugation. FT CHAIN 1..706 FT /note="Integrator complex subunit 13" FT /id="PRO_0000089845" FT REGION 564..603 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 615..650 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 567..622 FT /evidence="ECO:0000255" FT MOTIF 572..582 FT /note="Nuclear localization signal (NLS)" FT /evidence="ECO:0000269|PubMed:23904267" FT COMPBIAS 615..644 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 623 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 626 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT CROSSLNK 611 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..101 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056514" FT VARIANT 66 FT /note="M -> T (in dbSNP:rs2306852)" FT /id="VAR_050864" FT VARIANT 227 FT /note="S -> P (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035673" FT MUTAGEN 577..582 FT /note="REDKED->AAAAAA: Loss of nuclear location. Location FT is mainly cytoplasmic or diffuse. Loss of Dynein FT recruitment to nuclear envelope." FT /evidence="ECO:0000269|PubMed:23904267" FT CONFLICT 29 FT /note="E -> G (in Ref. 1; BAA91725)" FT /evidence="ECO:0000305" FT CONFLICT 53 FT /note="T -> P (in Ref. 1; BAA91725)" FT /evidence="ECO:0000305" FT CONFLICT 75 FT /note="L -> P (in Ref. 1; BAA91725)" FT /evidence="ECO:0000305" FT CONFLICT 454 FT /note="K -> R (in Ref. 1; BAA91721)" FT /evidence="ECO:0000305" FT CONFLICT 457 FT /note="R -> P (in Ref. 1; BAA91721)" FT /evidence="ECO:0000305" FT CONFLICT 459 FT /note="W -> R (in Ref. 1; BAA91725)" FT /evidence="ECO:0000305" FT CONFLICT 484 FT /note="E -> K (in Ref. 4; AAO65180)" FT /evidence="ECO:0000305" FT CONFLICT 490 FT /note="D -> N (in Ref. 4; AAO65180)" FT /evidence="ECO:0000305" FT CONFLICT 699 FT /note="E -> K (in Ref. 3; AAH03081)" FT /evidence="ECO:0000305" FT STRAND 2..5 FT /evidence="ECO:0007829|PDB:6SN1" FT HELIX 6..8 FT /evidence="ECO:0007829|PDB:6SN1" FT STRAND 9..15 FT /evidence="ECO:0007829|PDB:6SN1" FT HELIX 18..21 FT /evidence="ECO:0007829|PDB:6SN1" FT STRAND 22..28 FT /evidence="ECO:0007829|PDB:6SN1" FT STRAND 47..50 FT /evidence="ECO:0007829|PDB:6SN1" FT HELIX 51..69 FT /evidence="ECO:0007829|PDB:6SN1" FT STRAND 71..73 FT /evidence="ECO:0007829|PDB:6SN1" FT STRAND 75..87 FT /evidence="ECO:0007829|PDB:6SN1" FT HELIX 93..95 FT /evidence="ECO:0007829|PDB:6SN1" FT HELIX 98..108 FT /evidence="ECO:0007829|PDB:6SN1" FT HELIX 123..133 FT /evidence="ECO:0007829|PDB:6SN1" FT HELIX 138..147 FT /evidence="ECO:0007829|PDB:6SN1" FT STRAND 157..164 FT /evidence="ECO:0007829|PDB:6SN1" FT HELIX 169..191 FT /evidence="ECO:0007829|PDB:6SN1" FT STRAND 200..210 FT /evidence="ECO:0007829|PDB:6SN1" FT STRAND 221..225 FT /evidence="ECO:0007829|PDB:6SN1" FT STRAND 227..238 FT /evidence="ECO:0007829|PDB:6SN1" FT HELIX 241..254 FT /evidence="ECO:0007829|PDB:6SN1" FT STRAND 257..263 FT /evidence="ECO:0007829|PDB:6SN1" FT STRAND 281..286 FT /evidence="ECO:0007829|PDB:6SN1" FT HELIX 287..290 FT /evidence="ECO:0007829|PDB:6SN1" FT TURN 291..293 FT /evidence="ECO:0007829|PDB:6SN1" FT STRAND 314..319 FT /evidence="ECO:0007829|PDB:6SN1" FT STRAND 331..336 FT /evidence="ECO:0007829|PDB:6SN1" FT TURN 340..343 FT /evidence="ECO:0007829|PDB:6SN1" FT HELIX 345..356 FT /evidence="ECO:0007829|PDB:6SN1" FT STRAND 360..364 FT /evidence="ECO:0007829|PDB:6SN1" FT STRAND 372..380 FT /evidence="ECO:0007829|PDB:6SN1" FT STRAND 383..389 FT /evidence="ECO:0007829|PDB:6SN1" FT TURN 402..404 FT /evidence="ECO:0007829|PDB:6SN1" FT TURN 406..409 FT /evidence="ECO:0007829|PDB:6SN1" FT HELIX 415..424 FT /evidence="ECO:0007829|PDB:6SN1" FT STRAND 426..429 FT /evidence="ECO:0007829|PDB:6SN1" FT STRAND 436..440 FT /evidence="ECO:0007829|PDB:6SN1" FT HELIX 444..455 FT /evidence="ECO:0007829|PDB:6SN1" FT HELIX 463..465 FT /evidence="ECO:0007829|PDB:6SN1" FT HELIX 468..470 FT /evidence="ECO:0007829|PDB:6SN1" FT HELIX 472..474 FT /evidence="ECO:0007829|PDB:6SN1" FT HELIX 475..481 FT /evidence="ECO:0007829|PDB:6SN1" FT STRAND 483..485 FT /evidence="ECO:0007829|PDB:6SN1" FT HELIX 488..507 FT /evidence="ECO:0007829|PDB:6SN1" FT HELIX 525..541 FT /evidence="ECO:0007829|PDB:6SN1" FT HELIX 542..546 FT /evidence="ECO:0007829|PDB:6SN1" FT HELIX 548..560 FT /evidence="ECO:0007829|PDB:6SN1" SQ SEQUENCE 706 AA; 80225 MW; 925C733184461EA6 CRC64; MKIFSESHKT VFVVDHCPYM AESCRQHVEF DMLVKNRTQG IIPLAPISKS LWTCSVESSM EYCRIMYDIF PFKKLVNFIV SDSGAHVLNS WTQEDQNLQE LMAALAAVGP PNPRADPECC SILHGLVAAV ETLCKITEYQ HEARTLLMEN AERVGNRGRI ICITNAKSDS HVRMLEDCVQ ETIHEHNKLA ANSDHLMQIQ KCELVLIHTY PVGEDSLVSD RSKKELSPVL TSEVHSVRAG RHLATKLNIL VQQHFDLAST TITNIPMKEE QHANTSANYD VELLHHKDAH VDFLKSGDSH LGGGSREGSF KETITLKWCT PRTNNIELHY CTGAYRISPV DVNSRPSSCL TNFLLNGRSV LLEQPRKSGS KVISHMLSSH GGEIFLHVLS SSRSILEDPP SISEGCGGRV TDYRITDFGE FMRENRLTPF LDPRYKIDGS LEVPLERAKD QLEKHTRYWP MIISQTTIFN MQAVVPLASV IVKESLTEED VLNCQKTIYN LVDMERKNDP LPISTVGTRG KGPKRDEQYR IMWNELETLV RAHINNSEKH QRVLECLMAC RSKPPEEEER KKRGRKREDK EDKSEKAVKD YEQEKSWQDS ERLKGILERG KEELAEAEII KDSPDSPEPP NKKPLVEMDE TPQVEKSKGP VSLLSLWSNR INTANSRKHQ EFAGRLNSVN NRAELYQHLK EENGMETTEN GKASRQ //