INT13_HUMAN
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 03-AUG-2022, entry version 143.
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};
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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; 44.
DR ComplexPortal; CPX-6441; Integrator complex.
DR IntAct; Q9NVM9; 21.
DR MINT; Q9NVM9; -.
DR STRING; 9606.ENSP00000261191; -.
DR iPTMnet; Q9NVM9; -.
DR MetOSite; Q9NVM9; -.
DR PhosphoSitePlus; Q9NVM9; -.
DR BioMuta; INTS13; -.
DR DMDM; 71153010; -.
DR EPD; Q9NVM9; -.
DR jPOST; Q9NVM9; -.
DR MassIVE; Q9NVM9; -.
DR MaxQB; Q9NVM9; -.
DR PaxDb; Q9NVM9; -.
DR PeptideAtlas; Q9NVM9; -.
DR PRIDE; Q9NVM9; -.
DR ProteomicsDB; 4703; -.
DR ProteomicsDB; 82831; -. [Q9NVM9-1]
DR Antibodypedia; 42367; 70 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 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; 676663at2759; -.
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; 318 hits in 1077 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 201 other tissues.
DR ExpressionAtlas; Q9NVM9; baseline and differential.
DR Genevisible; Q9NVM9; HS.
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 from RNA polymerase II promoter; IC:ComplexPortal.
DR GO; GO:0016180; P:snRNA processing; IC:ComplexPortal.
DR InterPro; IPR019355; Cell_cycle_regulator_Mat89Bb.
DR PANTHER; PTHR12955; PTHR12955; 1.
DR Pfam; PF10221; DUF2151; 1.
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
