UBP2L_HUMAN
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 03-AUG-2022, entry version 186.
DE RecName: Full=Ubiquitin-associated protein 2-like {ECO:0000305};
DE AltName: Full=Protein NICE-4;
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).
CC -!- FUNCTION: Plays an important role in the activity of long-term
CC repopulating hematopoietic stem cells (LT-HSCs). Required for efficient
CC formation of stress granules (PubMed:29395067).
CC {ECO:0000250|UniProtKB:Q80X50, ECO:0000269|PubMed:29395067}.
CC -!- SUBUNIT: Interacts with BMI1 (PubMed:25185265). Part of a complex
CC consisting of UBAP2L, BMI1 and RNF2(PubMed:25185265).
CC {ECO:0000269|PubMed:25185265}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm, Stress granule
CC {ECO:0000305|PubMed:29395067}.
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; 223.
DR CORUM; Q14157; -.
DR IntAct; Q14157; 48.
DR MINT; Q14157; -.
DR STRING; 9606.ENSP00000389445; -.
DR ChEMBL; CHEMBL4295819; -.
DR GlyConnect; 2895; 1 O-Linked glycan (2 sites).
DR GlyGen; Q14157; 90 sites, 2 O-linked glycans (88 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; Q14157; -.
DR PeptideAtlas; Q14157; -.
DR PRIDE; 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 Antibodypedia; 34148; 203 antibodies from 25 providers.
DR DNASU; 9898; -.
DR Ensembl; ENST00000343815.10; ENSP00000345308.6; ENSG00000143569.19. [Q14157-1]
DR Ensembl; ENST00000361546.6; ENSP00000355343.2; ENSG00000143569.19. [Q14157-2]
DR Ensembl; ENST00000428931.6; ENSP00000389445.1; ENSG00000143569.19. [Q14157-2]
DR Ensembl; ENST00000613315.4; ENSP00000478447.1; ENSG00000143569.19. [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 CTD; 9898; -.
DR DisGeNET; 9898; -.
DR GeneCards; UBAP2L; -.
DR HGNC; HGNC:29877; UBAP2L.
DR HPA; ENSG00000143569; Low tissue specificity.
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; PPYNIAG; -.
DR OrthoDB; 234795at2759; -.
DR PhylomeDB; Q14157; -.
DR TreeFam; TF328468; -.
DR PathwayCommons; Q14157; -.
DR SignaLink; Q14157; -.
DR SIGNOR; Q14157; -.
DR BioGRID-ORCS; 9898; 76 hits in 1090 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 208 other tissues.
DR ExpressionAtlas; Q14157; baseline and differential.
DR Genevisible; Q14157; HS.
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:0034063; P:stress granule assembly; IMP:UniProtKB.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR022166; UBAP2/Lig.
DR Pfam; PF12478; DUF3697; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Methylation; Phosphoprotein;
KW 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
