ID RL1D1_HUMAN Reviewed; 490 AA. AC O76021; B4DJ58; D3DUG7; Q2M1T7; Q6PL22; Q8IWS7; Q8WUZ1; Q9HDA9; Q9Y3Z9; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2005, sequence version 3. DT 14-DEC-2022, entry version 192. DE RecName: Full=Ribosomal L1 domain-containing protein 1; DE AltName: Full=CATX-11; DE AltName: Full=Cellular senescence-inhibited gene protein {ECO:0000303|PubMed:18678645}; DE AltName: Full=Protein PBK1; GN Name=RSL1D1; Synonyms=CATX11, CSIG {ECO:0000303|PubMed:18678645}, PBK1; GN ORFNames=L12; 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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Placenta; RX PubMed=9859858; DOI=10.1016/s0143-4004(98)90015-7; RA Huch G., Hohn H.-P., Denker H.-W.; RT "Identification of differentially expressed genes in human trophoblast RT cells by DDRT-PCR."; RL Placenta 19:557-567(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=15334068; DOI=10.1038/sj.onc.1207921; RA Petroziello J., Yamane A., Westendorf L., Thompson M., McDonagh C., RA Cerveny C., Law C.-L., Wahl A., Carter P.; RT "Suppression subtractive hybridization and expression profiling identifies RT a unique set of genes overexpressed in non-small-cell lung cancer."; RL Oncogene 23:7734-7745(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Lung; RA Guo S.-Z., Zhang Z.-Y., Tong T.-J.; RT "Identification of a new gene associated with cellular senescence in human RT diploid fibroblast."; RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Substantia nigra; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, and Lung; 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-290 (ISOFORM 1). RC TISSUE=Brain; 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 [9] RP PROTEIN SEQUENCE OF 1-28; 90-100; 125-136; 148-160; 164-171; 179-188; RP 193-207 AND 258-276, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RA Bienvenut W.V., Waridel P., Quadroni M.; RL Submitted (MAR-2009) to UniProtKB. RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 76-401 (ISOFORM 1). RC TISSUE=Colon; RA Kairo A., Wang L., Gao Z.Q., Gao Z.P., Boman B.M.; RT "Isolation of novel genes from human colonic epithelial cells."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [11] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271; RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., RA Greco A., Hochstrasser D.F., Diaz J.-J.; RT "Functional proteomic analysis of human nucleolus."; RL Mol. Biol. Cell 13:4100-4109(2002). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION. RX PubMed=11790298; DOI=10.1016/s0960-9822(01)00650-9; RA Andersen J.S., Lyon C.E., Fox A.H., Leung A.K.L., Lam Y.W., Steen H., RA Mann M., Lamond A.I.; RT "Directed proteomic analysis of the human nucleolus."; RL Curr. Biol. 12:1-11(2002). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-340 AND SER-427, AND 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392; SER-396; THR-423; RP SER-427 AND SER-469, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=T-cell; RX PubMed=19367720; DOI=10.1021/pr800500r; RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; RT "Phosphorylation analysis of primary human T lymphocytes using sequential RT IMAC and titanium oxide enrichment."; RL J. Proteome Res. 7:5167-5176(2008). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, AND IDENTIFICATION BY RP 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 [17] RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INDUCTION. RX PubMed=18678645; DOI=10.1128/mcb.00142-08; RA Ma L., Chang N., Guo S., Li Q., Zhang Z., Wang W., Tong T.; RT "CSIG inhibits PTEN translation in replicative senescence."; RL Mol. Cell. Biol. 28:6290-6301(2008). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-358; SER-361; SER-392; RP SER-396; THR-415; THR-423; SER-427; SER-443; THR-465 AND SER-469, AND RP 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 [19] 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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, AND IDENTIFICATION BY RP 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 [21] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-468, 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 [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-340; SER-361; THR-375; RP SER-392 AND SER-427, 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 [23] 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 [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-358; SER-361; SER-396 AND RP SER-427, 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 [25] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ING1. RX PubMed=22419112; DOI=10.1038/cddis.2012.22; RA Li N., Zhao G., Chen T., Xue L., Ma L., Niu J., Tong T.; RT "Nucleolar protein CSIG is required for p33ING1 function in UV-induced RT apoptosis."; RL Cell Death Dis. 3:E283-E283(2012). RN [26] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [27] 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 [28] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361; THR-415; SER-427; RP THR-465 AND SER-469, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [29] RP IDENTIFICATION BY 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 [30] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-435, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [31] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-120; LYS-254; LYS-380 AND RP LYS-461, AND IDENTIFICATION BY MASS 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). CC -!- FUNCTION: Regulates cellular senescence through inhibition of PTEN CC translation. Acts as a pro-apoptotic regulator in response to DNA CC damage. {ECO:0000269|PubMed:18678645, ECO:0000269|PubMed:22419112}. CC -!- SUBUNIT: Interacts with ING1 (isoform 2). CC {ECO:0000269|PubMed:22419112}. CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11790298, CC ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:18678645, CC ECO:0000269|PubMed:22419112}. Note=Colocalizes with ING1 in the CC nucleolus after UV stress. {ECO:0000269|PubMed:22419112}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O76021-1; Sequence=Displayed; CC Name=2; CC IsoId=O76021-2; Sequence=VSP_056143; CC -!- TISSUE SPECIFICITY: Expressed at high intensities in the heart, CC skeletal muscle, and placenta. {ECO:0000269|PubMed:18678645, CC ECO:0000269|PubMed:9859858}. CC -!- INDUCTION: Down-regulated during cellular senescence. CC {ECO:0000269|PubMed:18678645}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family. CC Highly divergent. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF98239.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAH19069.2; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAA07491.1; 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; AJ007398; CAA07491.1; ALT_FRAME; mRNA. DR EMBL; AY598331; AAT06742.1; -; mRNA. DR EMBL; AY154473; AAN46298.1; -; mRNA. DR EMBL; AK295935; BAG58720.1; -; mRNA. DR EMBL; AC010654; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471112; EAW85133.1; -; Genomic_DNA. DR EMBL; CH471112; EAW85135.1; -; Genomic_DNA. DR EMBL; BC019069; AAH19069.2; ALT_INIT; mRNA. DR EMBL; BC112228; AAI12229.1; -; mRNA. DR EMBL; BC113699; AAI13700.1; -; mRNA. DR EMBL; AL049999; CAB43231.2; -; mRNA. DR EMBL; AF083127; AAF98239.1; ALT_FRAME; mRNA. DR CCDS; CCDS10551.1; -. [O76021-1] DR PIR; T08693; T08693. DR RefSeq; NP_056474.2; NM_015659.2. [O76021-1] DR AlphaFoldDB; O76021; -. DR SMR; O76021; -. DR BioGRID; 117587; 486. DR CORUM; O76021; -. DR IntAct; O76021; 115. DR MINT; O76021; -. DR STRING; 9606.ENSP00000460871; -. DR ChEMBL; CHEMBL1075139; -. DR GlyGen; O76021; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O76021; -. DR MetOSite; O76021; -. DR PhosphoSitePlus; O76021; -. DR SwissPalm; O76021; -. DR BioMuta; RSL1D1; -. DR SWISS-2DPAGE; O76021; -. DR EPD; O76021; -. DR jPOST; O76021; -. DR MassIVE; O76021; -. DR MaxQB; O76021; -. DR PaxDb; O76021; -. DR PeptideAtlas; O76021; -. DR ProteomicsDB; 4349; -. DR ProteomicsDB; 50348; -. [O76021-1] DR Antibodypedia; 11546; 161 antibodies from 29 providers. DR DNASU; 26156; -. DR Ensembl; ENST00000571133.6; ENSP00000460871.1; ENSG00000171490.13. [O76021-1] DR GeneID; 26156; -. DR KEGG; hsa:26156; -. DR MANE-Select; ENST00000571133.6; ENSP00000460871.1; NM_015659.3; NP_056474.2. DR UCSC; uc002dbp.3; human. [O76021-1] DR AGR; HGNC:24534; -. DR CTD; 26156; -. DR DisGeNET; 26156; -. DR GeneCards; RSL1D1; -. DR HGNC; HGNC:24534; RSL1D1. DR HPA; ENSG00000171490; Low tissue specificity. DR MIM; 615874; gene. DR neXtProt; NX_O76021; -. DR OpenTargets; ENSG00000171490; -. DR PharmGKB; PA142670966; -. DR VEuPathDB; HostDB:ENSG00000171490; -. DR eggNOG; KOG1685; Eukaryota. DR GeneTree; ENSGT00440000038603; -. DR InParanoid; O76021; -. DR OMA; KNEAIWL; -. DR OrthoDB; 1000750at2759; -. DR PhylomeDB; O76021; -. DR TreeFam; TF354254; -. DR PathwayCommons; O76021; -. DR SignaLink; O76021; -. DR BioGRID-ORCS; 26156; 770 hits in 1091 CRISPR screens. DR ChiTaRS; RSL1D1; human. DR GeneWiki; RSL1D1; -. DR GenomeRNAi; 26156; -. DR Pharos; O76021; Tbio. DR PRO; PR:O76021; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; O76021; protein. DR Bgee; ENSG00000171490; Expressed in calcaneal tendon and 209 other tissues. DR ExpressionAtlas; O76021; baseline and differential. DR Genevisible; O76021; HS. DR GO; GO:0030686; C:90S preribosome; IBA:GO_Central. DR GO; GO:0005694; C:chromosome; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:CAFA. DR GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:CAFA. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central. DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB. DR GO; GO:0042981; P:regulation of apoptotic process; IDA:UniProtKB. DR GO; GO:2000772; P:regulation of cellular senescence; IDA:UniProtKB. DR GO; GO:0032880; P:regulation of protein localization; IMP:MGI. DR CDD; cd00403; Ribosomal_L1; 1. DR Gene3D; 3.40.50.790; -; 1. DR InterPro; IPR023674; Ribosomal_L1-like. DR InterPro; IPR028364; Ribosomal_L1/biogenesis. DR InterPro; IPR016095; Ribosomal_L1_3-a/b-sand. DR Pfam; PF00687; Ribosomal_L1; 1. DR SUPFAM; SSF56808; Ribosomal protein L1; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Coiled coil; Direct protein sequencing; KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; KW Ubl conjugation. FT CHAIN 1..490 FT /note="Ribosomal L1 domain-containing protein 1" FT /id="PRO_0000125844" FT REGION 1..33 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 280..490 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 280..313 FT /evidence="ECO:0000255" FT COMPBIAS 1..26 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 281..311 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 324..345 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 423..457 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT MOD_RES 340 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231" FT MOD_RES 358 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692" FT MOD_RES 361 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 375 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 392 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231" FT MOD_RES 396 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692" FT MOD_RES 415 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 423 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648" FT MOD_RES 427 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:17081983, 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 443 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 465 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 468 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 469 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163" FT CROSSLNK 120 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 254 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 380 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 435 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447" FT CROSSLNK 461 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..220 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056143" FT CONFLICT 50 FT /note="R -> G (in Ref. 3; AAN46298)" FT /evidence="ECO:0000305" FT CONFLICT 189 FT /note="N -> D (in Ref. 8; CAB43231)" FT /evidence="ECO:0000305" FT CONFLICT 294 FT /note="R -> G (in Ref. 3; AAN46298)" FT /evidence="ECO:0000305" SQ SEQUENCE 490 AA; 54973 MW; 5E5CDB8AA8BC3709 CRC64; MEDSASASLS SAAATGTSTS TPAAPTARKQ LDKEQVRKAV DALLTHCKSR KNNYGLLLNE NESLFLMVVL WKIPSKELRV RLTLPHSIRS DSEDICLFTK DEPNSTPEKT EQFYRKLLNK HGIKTVSQII SLQTLKKEYK SYEAKLRLLS SFDFFLTDAR IRRLLPSLIG RHFYQRKKVP VSVNLLSKNL SREINDCIGG TVLNISKSGS CSAIRIGHVG MQIEHIIENI VAVTKGLSEK LPEKWESVKL LFVKTEKSAA LPIFSSFVSN WDEATKRSLL NKKKKEARRK RRERNFEKQK ERKKKRQQAR KTASVLSKDD VAPESGDTTV KKPESKKEQT PEHGKKKRGR GKAQVKATNE SEDEIPQLVP IGKKTPANEK VEIQKHATGK KSPAKSPNPS TPRGKKRKAL PASETPKAAE SETPGKSPEK KPKIKEEAVK EKSPSLGKKD ARQTPKKPEA KFFTTPSKSV RKASHTPKKW PKKPKVPQST //