ID UBP2L_HUMAN Reviewed; 1087 AA. AC Q14157; B4E0U8; Q5VU75; Q5VU76; Q9BTU3; Q9UGL2; Q9UGL3; Q9UGL4; Q9UGL5; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 27-JUN-2006, sequence version 2. DT 27-MAR-2024, entry version 195. DE RecName: Full=Ubiquitin-associated protein 2-like {ECO:0000305}; DE AltName: Full=Protein NICE-4; DE AltName: Full=RNA polymerase II degradation factor UBAP2L {ECO:0000303|PubMed:35633597}; GN Name=UBAP2L {ECO:0000312|HGNC:HGNC:29877}; Synonyms=KIAA0144, NICE4; 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 2). RC TISSUE=Bone marrow; RX PubMed=8590280; DOI=10.1093/dnares/2.4.167; RA Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. IV. The RT coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of RT cDNA clones from human cell line KG-1."; RL DNA Res. 2:167-174(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Thymus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Skin; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-137 (ISOFORMS 1/2/3), NUCLEOTIDE SEQUENCE RP [MRNA] OF 671-1087 (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 760-1087 RP (ISOFORM 5), AND TISSUE SPECIFICITY. RC TISSUE=Keratinocyte; RX PubMed=11230159; DOI=10.1101/gr.114801; RA Marenholz I., Zirra M., Fischer D.F., Backendorf C., Ziegler A., RA Mischke D.; RT "Identification of human epidermal differentiation complex (EDC)-encoded RT genes by subtractive hybridization of entire YACs to a gridded keratinocyte RT cDNA library."; RL Genome Res. 11:341-355(2001). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=15144186; DOI=10.1021/ac035352d; RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., RA Peters E.C.; RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from RT human T cells using immobilized metal affinity chromatography and tandem RT mass spectrometry."; RL Anal. Chem. 76:2763-2772(2004). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [8] RP IDENTIFICATION BY 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-454, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells RT and high confident phosphopeptide identification by cross-validation of RT MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416; SER-439 AND SER-467, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416; SER-439; SER-454; RP SER-467; SER-471; SER-477; SER-605; SER-608; SER-609; SER-852 AND SER-859, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-454; SER-470; SER-477 AND RP SER-859, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-976 (ISOFORM 2), ACETYLATION RP [LARGE SCALE ANALYSIS] AT LYS-969 (ISOFORM 4), AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416; THR-425; SER-439; RP SER-454 AND SER-609, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [19] 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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416; SER-467; SER-477 AND RP SER-609, AND 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 [21] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; SER-360; SER-410; RP SER-416; SER-454; SER-477; SER-604; SER-605; SER-608; SER-609; SER-852 AND RP SER-859, AND 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 [23] RP INTERACTION WITH BMI1, AND IDENTIFICATION IN THE COMPLEX WITH BMI1 AND RP RNF2. RX PubMed=25185265; DOI=10.1182/blood-2014-01-548651; RA Bordeleau M.E., Aucagne R., Chagraoui J., Girard S., Mayotte N., RA Bonneil E., Thibault P., Pabst C., Bergeron A., Barabe F., Hebert J., RA Sauvageau M., Boutonnet C., Meloche S., Sauvageau G.; RT "UBAP2L is a novel BMI1-interacting protein essential for hematopoietic RT stem cell activity."; RL Blood 124:2362-2369(2014). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-609, 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 [25] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-187 AND ARG-190, METHYLATION RP [LARGE SCALE ANALYSIS] AT ARG-969 (ISOFORM 2), METHYLATION [LARGE SCALE RP ANALYSIS] AT ARG-962 (ISOFORM 4), AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [26] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [27] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=29395067; DOI=10.1016/j.molcel.2017.12.020; RA Youn J.Y., Dunham W.H., Hong S.J., Knight J.D.R., Bashkurov M., Chen G.I., RA Bagci H., Rathod B., MacLeod G., Eng S.W.M., Angers S., Morris Q., RA Fabian M., Cote J.F., Gingras A.C.; RT "High-Density Proximity Mapping Reveals the Subcellular Organization of RT mRNA-Associated Granules and Bodies."; RL Mol. Cell 69:517.e11-532.e11(2018). RN [28] RP INTERACTION WITH G3BP1. RX PubMed=32302570; DOI=10.1016/j.cell.2020.03.050; RA Sanders D.W., Kedersha N., Lee D.S.W., Strom A.R., Drake V., Riback J.A., RA Bracha D., Eeftens J.M., Iwanicki A., Wang A., Wei M.T., Whitney G., RA Lyons S.M., Anderson P., Jacobs W.M., Ivanov P., Brangwynne C.P.; RT "Competing protein-RNA interaction networks control multiphase RT intracellular organization."; RL Cell 181:306-324(2020). RN [29] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=35633597; DOI=10.1016/j.dnarep.2022.103343; RA Herlihy A.E., Boeing S., Weems J.C., Walker J., Dirac-Svejstrup A.B., RA Lehner M.H., Conaway R.C., Conaway J.W., Svejstrup J.Q.; RT "UBAP2/UBAP2L regulate UV-induced ubiquitylation of RNA polymerase II and RT are the human orthologues of yeast Def1."; RL DNA Repair 115:103343-103343(2022). CC -!- FUNCTION: Recruits the ubiquitination machinery to RNA polymerase II CC for polyubiquitination, removal and degradation, when the CC transcription-coupled nucleotide excision repair (TC-NER) machinery CC fails to resolve DNA damage (PubMed:35633597). Plays an important role CC in the activity of long-term repopulating hematopoietic stem cells (LT- CC HSCs) (By similarity). Required for efficient formation of stress CC granules (PubMed:29395067). {ECO:0000250|UniProtKB:Q80X50, CC ECO:0000269|PubMed:29395067, ECO:0000269|PubMed:35633597}. CC -!- SUBUNIT: Interacts with BMI1 (PubMed:25185265). Part of a complex CC consisting of UBAP2L, BMI1 and RNF2(PubMed:25185265). Interacts with CC G3BP1 (via NTF2 domain); promoting stress granule formation CC (PubMed:32302570). {ECO:0000269|PubMed:25185265, CC ECO:0000269|PubMed:32302570}. CC -!- INTERACTION: CC Q14157; P51114-2: FXR1; NbExp=3; IntAct=EBI-347762, EBI-11022345; CC Q14157; P51116: FXR2; NbExp=4; IntAct=EBI-347762, EBI-740459; CC Q14157; Q13283: G3BP1; NbExp=3; IntAct=EBI-347762, EBI-1047359; CC Q14157; PRO_0000449629 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-347762, EBI-25475885; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:35633597}. Chromosome CC {ECO:0000269|PubMed:35633597}. Cytoplasm {ECO:0000269|PubMed:35633597}. CC Cytoplasm, Stress granule {ECO:0000305|PubMed:29395067}. CC Note=Associates with nuclear chromatin. {ECO:0000269|PubMed:35633597}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q14157-2; Sequence=Displayed; CC Name=2; CC IsoId=Q14157-1; Sequence=VSP_019417; CC Name=3; CC IsoId=Q14157-3; Sequence=VSP_021728; CC Name=4; CC IsoId=Q14157-4; Sequence=VSP_038235, VSP_019417; CC Name=5; CC IsoId=Q14157-5; Sequence=VSP_042167; CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11230159}. CC -!- PTM: Acetylated. CC -!- SEQUENCE CAUTION: CC Sequence=CAB65100.2; 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; D63478; BAA09765.1; -; mRNA. DR EMBL; AK303533; BAG64560.1; -; mRNA. DR EMBL; AL590431; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC003170; AAH03170.1; -; mRNA. DR EMBL; AJ243668; CAB65099.1; -; mRNA. DR EMBL; AJ243670; CAB65101.2; -; mRNA. DR EMBL; AJ243669; CAB65100.2; ALT_FRAME; mRNA. DR CCDS; CCDS1063.1; -. [Q14157-2] DR CCDS; CCDS44229.1; -. [Q14157-1] DR CCDS; CCDS72925.1; -. [Q14157-4] DR RefSeq; NP_001120792.1; NM_001127320.2. [Q14157-1] DR RefSeq; NP_001274744.1; NM_001287815.1. [Q14157-4] DR RefSeq; NP_001274745.1; NM_001287816.1. DR RefSeq; NP_055662.3; NM_014847.3. [Q14157-2] DR RefSeq; XP_005245731.1; XM_005245674.1. DR RefSeq; XP_011508518.1; XM_011510216.1. DR RefSeq; XP_016858467.1; XM_017002978.1. DR RefSeq; XP_016858468.1; XM_017002979.1. DR RefSeq; XP_016858475.1; XM_017002986.1. DR RefSeq; XP_016858476.1; XM_017002987.1. DR RefSeq; XP_016858478.1; XM_017002989.1. DR RefSeq; XP_016858479.1; XM_017002990.1. DR AlphaFoldDB; Q14157; -. DR SMR; Q14157; -. DR BioGRID; 115227; 269. DR CORUM; Q14157; -. DR IntAct; Q14157; 50. DR MINT; Q14157; -. DR STRING; 9606.ENSP00000389445; -. DR ChEMBL; CHEMBL4295819; -. DR GlyConnect; 2895; 1 O-GlcNAc glycan (2 sites). DR GlyCosmos; Q14157; 88 sites, 2 glycans. DR GlyGen; Q14157; 103 sites, 3 O-linked glycans (101 sites). DR iPTMnet; Q14157; -. DR MetOSite; Q14157; -. DR PhosphoSitePlus; Q14157; -. DR BioMuta; UBAP2L; -. DR DMDM; 109940042; -. DR CPTAC; CPTAC-599; -. DR CPTAC; CPTAC-600; -. DR EPD; Q14157; -. DR jPOST; Q14157; -. DR MassIVE; Q14157; -. DR MaxQB; Q14157; -. DR PaxDb; 9606-ENSP00000389445; -. DR PeptideAtlas; Q14157; -. DR ProteomicsDB; 59867; -. [Q14157-2] DR ProteomicsDB; 59868; -. [Q14157-1] DR ProteomicsDB; 59869; -. [Q14157-3] DR ProteomicsDB; 59870; -. [Q14157-4] DR ProteomicsDB; 59871; -. [Q14157-5] DR Pumba; Q14157; -. DR Antibodypedia; 34148; 225 antibodies from 25 providers. DR DNASU; 9898; -. DR Ensembl; ENST00000343815.10; ENSP00000345308.6; ENSG00000143569.20. [Q14157-1] DR Ensembl; ENST00000361546.6; ENSP00000355343.2; ENSG00000143569.20. [Q14157-2] DR Ensembl; ENST00000428931.6; ENSP00000389445.1; ENSG00000143569.20. [Q14157-2] DR Ensembl; ENST00000613315.4; ENSP00000478447.1; ENSG00000143569.20. [Q14157-4] DR GeneID; 9898; -. DR KEGG; hsa:9898; -. DR MANE-Select; ENST00000428931.6; ENSP00000389445.1; NM_014847.4; NP_055662.3. DR UCSC; uc001fep.5; human. [Q14157-2] DR AGR; HGNC:29877; -. DR CTD; 9898; -. DR DisGeNET; 9898; -. DR GeneCards; UBAP2L; -. DR HGNC; HGNC:29877; UBAP2L. DR HPA; ENSG00000143569; Low tissue specificity. DR MalaCards; UBAP2L; -. DR MIM; 616472; gene. DR neXtProt; NX_Q14157; -. DR OpenTargets; ENSG00000143569; -. DR PharmGKB; PA134883839; -. DR VEuPathDB; HostDB:ENSG00000143569; -. DR eggNOG; ENOG502QPRH; Eukaryota. DR GeneTree; ENSGT00390000003453; -. DR HOGENOM; CLU_009850_0_0_1; -. DR InParanoid; Q14157; -. DR OMA; TNDNYRG; -. DR OrthoDB; 5402202at2759; -. DR PhylomeDB; Q14157; -. DR TreeFam; TF328468; -. DR PathwayCommons; Q14157; -. DR SignaLink; Q14157; -. DR SIGNOR; Q14157; -. DR BioGRID-ORCS; 9898; 97 hits in 1171 CRISPR screens. DR ChiTaRS; UBAP2L; human. DR GeneWiki; UBAP2L; -. DR GenomeRNAi; 9898; -. DR Pharos; Q14157; Tbio. DR PRO; PR:Q14157; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q14157; Protein. DR Bgee; ENSG00000143569; Expressed in sural nerve and 210 other cell types or tissues. DR ExpressionAtlas; Q14157; baseline and differential. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0031519; C:PcG protein complex; IDA:MGI. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0007339; P:binding of sperm to zona pellucida; IMP:UniProtKB. DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; IGI:MGI. DR GO; GO:0062029; P:positive regulation of stress granule assembly; IDA:UniProtKB. DR GO; GO:0034063; P:stress granule assembly; IMP:UniProtKB. DR CDD; cd14277; UBA_UBP2_like; 1. DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1. DR InterPro; IPR015940; UBA. DR InterPro; IPR009060; UBA-like_sf. DR InterPro; IPR022166; UBAP2/Lig. DR PANTHER; PTHR16308; UBIQUITIN ASSOCIATED PROTEIN 2-LIKE/LINGERER; 1. DR PANTHER; PTHR16308:SF18; UBIQUITIN-ASSOCIATED PROTEIN 2-LIKE; 1. DR Pfam; PF12478; UBAP2-Lig; 1. DR SMART; SM00165; UBA; 1. DR SUPFAM; SSF46934; UBA-like; 1. DR PROSITE; PS50030; UBA; 1. DR Genevisible; Q14157; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Chromosome; Cytoplasm; Methylation; KW Nucleus; Phosphoprotein; Reference proteome. FT CHAIN 1..1087 FT /note="Ubiquitin-associated protein 2-like" FT /id="PRO_0000211020" FT DOMAIN 49..89 FT /note="UBA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212" FT REGION 1..33 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 92..234 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 377..420 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 440..493 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 530..656 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 669..794 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 865..901 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1040..1087 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 114..155 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 210..230 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 459..493 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 669..786 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 874..901 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22814378" FT MOD_RES 187 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 190 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 356 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 360 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 410 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 416 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:15144186, FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 425 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 439 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231" FT MOD_RES 454 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 467 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, FT ECO:0007744|PubMed:21406692" FT MOD_RES 470 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 471 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 477 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 604 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 605 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 608 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 609 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 852 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 859 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT VAR_SEQ 143..150 FT /note="GASRGREF -> V (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_038235" FT VAR_SEQ 969..1087 FT /note="VSVTSSNTGVPDISGSVYSKTQQSFEKQGFHSGTPAASFNLPSALGSGGPIN FT PATAAAYPPAPFMHILTPHQQPHSQILHHHLQQDGQTGSGQRSQTSSIPQKPQTNKSAY FT NSYSWGAN -> RKYPPPYKHFWTAES (in isoform 2 and isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:8590280" FT /id="VSP_019417" FT VAR_SEQ 1055 FT /note="G -> GQLPYLQMILCCQRQQEE (in isoform 5)" FT /evidence="ECO:0000303|PubMed:11230159" FT /id="VSP_042167" FT VAR_SEQ 1057..1087 FT /note="TGSGQRSQTSSIPQKPQTNKSAYNSYSWGAN -> DILNFVDDQLGE (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:11230159" FT /id="VSP_021728" FT VARIANT 482 FT /note="Q -> H (in dbSNP:rs17849745)" FT /id="VAR_026829" FT CONFLICT 91 FT /note="P -> S (in Ref. 2; BAG64560)" FT /evidence="ECO:0000305" FT MOD_RES Q14157-1:969 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES Q14157-1:976 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES Q14157-4:962 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES Q14157-4:969 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" SQ SEQUENCE 1087 AA; 114535 MW; FED18847387AA1F5 CRC64; MMTSVGTNRA RGNWEQPQNQ NQTQHKQRPQ ATAEQIRLAQ MISDHNDADF EEKVKQLIDI TGKNQDECVI ALHDCNGDVN RAINVLLEGN PDTHSWEMVG KKKGVSGQKD GGQTESNEEG KENRDRDRDY SRRRGGPPRR GRGASRGREF RGQENGLDGT KSGGPSGRGT ERGRRGRGRG RGGSGRRGGR FSAQGMGTFN PADYAEPANT DDNYGNSSGN TWNNTGHFEP DDGTSAWRTA TEEWGTEDWN EDLSETKIFT ASNVSSVPLP AENVTITAGQ RIDLAVLLGK TPSTMENDSS NLDPSQAPSL AQPLVFSNSK QTAISQPASG NTFSHHSMVS MLGKGFGDVG EAKGGSTTGS QFLEQFKTAQ ALAQLAAQHS QSGSTTTSSW DMGSTTQSPS LVQYDLKNPS DSAVHSPFTK RQAFTPSSTM MEVFLQEKSP AVATSTAAPP PPSSPLPSKS TSAPQMSPGS SDNQSSSPQP AQQKLKQQKK KASLTSKIPA LAVEMPGSAD ISGLNLQFGA LQFGSEPVLS DYESTPTTSA SSSQAPSSLY TSTASESSST ISSNQSQESG YQSGPIQSTT YTSQNNAQGP LYEQRSTQTR RYPSSISSSP QKDLTQAKNG FSSVQATQLQ TTQSVEGATG SAVKSDSPST SSIPPLNETV SAASLLTTTN QHSSSLGGLS HSEEIPNTTT TQHSSTLSTQ QNTLSSSTSS GRTSTSTLLH TSVESEANLH SSSSTFSTTS STVSAPPPVV SVSSSLNSGS SLGLSLGSNS TVTASTRSSV ATTSGKAPPN LPPGVPPLLP NPYIMAPGLL HAYPPQVYGY DDLQMLQTRF PLDYYSIPFP TPTTPLTGRD GSLASNPYSG DLTKFGRGDA SSPAPATTLA QPQQNQTQTH HTTQQTFLNP ALPPGYSYTS LPYYTGVPGL PSTFQYGPAV FPVAPTSSKQ HGVNVSVNAS ATPFQQPSGY GSHGYNTGVS VTSSNTGVPD ISGSVYSKTQ QSFEKQGFHS GTPAASFNLP SALGSGGPIN PATAAAYPPA PFMHILTPHQ QPHSQILHHH LQQDGQTGSG QRSQTSSIPQ KPQTNKSAYN SYSWGAN //