ID LAGE3_HUMAN Reviewed; 143 AA. AC Q14657; Q5HY39; Q8IZ78; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 2. DT 05-OCT-2016, entry version 120. DE RecName: Full=EKC/KEOPS complex subunit LAGE3; DE AltName: Full=L antigen family member 3; DE AltName: Full=Protein ESO-3; DE AltName: Full=Protein ITBA2; GN Name=LAGE3; Synonyms=DXS9879E, ESO3, ITBA2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., RA Williams G., Williams L., Williamson A., Williamson H., Wilming L., RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Blood, and Pancreas; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-143, AND TISSUE SPECIFICITY. RC TISSUE=Liver; RX PubMed=8786131; DOI=10.1006/geno.1996.0293; RA Faranda S., Frattini A., Zucchi I., Patrosso C., Milanesi L., RA Montagna C., Vezzoni P.; RT "Characterization and fine localization of two new genes in Xq28 using RT the genomic sequence/EST database screening approach."; RL Genomics 34:323-327(1996). RN [4] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX PubMed=12384295; DOI=10.1016/S0378-1119(02)00879-X; RA Alpen B., Guere A.O., Scanlan M.J., Old L.J., Chen Y.-T.; RT "A new member of the NY-ESO-1 gene family is ubiquitously expressed in RT somatic tissues and evolutionarily conserved."; RL Gene 297:141-149(2002). RN [5] 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., RA Buerckstuemmer T., 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 [6] RP IDENTIFICATION IN THE EKC/KEOPS COMPLEX, AND SUBCELLULAR LOCATION. RX PubMed=22912744; DOI=10.1371/journal.pone.0042822; RA Costessi A., Mahrour N., Sharma V., Stunnenberg R., Stoel M.A., RA Tijchon E., Conaway J.W., Conaway R.C., Stunnenberg H.G.; RT "The human EKC/KEOPS complex is recruited to Cullin2 ubiquitin ligases RT by the human tumour antigen PRAME."; RL PLoS ONE 7:E42822-E42822(2012). RN [7] 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Component of the EKC/KEOPS complex that is required for CC the formation of a threonylcarbamoyl group on adenosine at CC position 37 (t(6)A37) in tRNAs that read codons beginning with CC adenine. The complex is probably involved in the transfer of the CC threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the CC N6 group of A37. LAGE3 functions as a dimerization module for the CC complex (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Component of the EKC/KEOPS complex composed of at least CC TP53RK, TPRKB, OSGEP and LAGE3; the whole complex dimerizes. CC {ECO:0000269|PubMed:22912744}. CC -!- INTERACTION: CC Q6A162:KRT40; NbExp=3; IntAct=EBI-1052105, EBI-10171697; CC O76083:PDE9A; NbExp=3; IntAct=EBI-1052105, EBI-742764; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22912744}. CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12384295, CC ECO:0000269|PubMed:8786131}. CC -!- SIMILARITY: Belongs to the CTAG/PCC1 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA63489.1; Type=Frameshift; Positions=54; 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; BX936365; CAI43195.1; -; Genomic_DNA. DR EMBL; BC015744; AAH15744.2; -; mRNA. DR EMBL; BC062330; AAH62330.1; -; mRNA. DR EMBL; X92896; CAA63489.1; ALT_FRAME; mRNA. DR CCDS; CCDS14753.1; -. DR RefSeq; NP_006005.2; NM_006014.4. DR UniGene; Hs.444619; -. DR ProteinModelPortal; Q14657; -. DR SMR; Q14657; 58-138, 64-131, 67-109. DR BioGrid; 113888; 46. DR IntAct; Q14657; 8. DR MINT; MINT-4719865; -. DR STRING; 9606.ENSP00000349923; -. DR iPTMnet; Q14657; -. DR PhosphoSite; Q14657; -. DR DMDM; 54041570; -. DR EPD; Q14657; -. DR MaxQB; Q14657; -. DR PaxDb; Q14657; -. DR PeptideAtlas; Q14657; -. DR PRIDE; Q14657; -. DR DNASU; 8270; -. DR Ensembl; ENST00000357360; ENSP00000349923; ENSG00000196976. DR GeneID; 8270; -. DR KEGG; hsa:8270; -. DR UCSC; uc033fbs.1; human. DR CTD; 8270; -. DR GeneCards; LAGE3; -. DR HGNC; HGNC:26058; LAGE3. DR HPA; HPA036122; -. DR HPA; HPA036123; -. DR MIM; 300060; gene. DR neXtProt; NX_Q14657; -. DR PharmGKB; PA128394540; -. DR eggNOG; ENOG410J4BY; Eukaryota. DR eggNOG; ENOG410Y0JU; LUCA. DR GeneTree; ENSGT00410000025802; -. DR HOGENOM; HOG000040003; -. DR HOVERGEN; HBG052154; -. DR InParanoid; Q14657; -. DR KO; K15902; -. DR OMA; ILVVRWK; -. DR OrthoDB; EOG091G0LGL; -. DR PhylomeDB; Q14657; -. DR TreeFam; TF337064; -. DR Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol. DR GenomeRNAi; 8270; -. DR PMAP-CutDB; Q14657; -. DR PRO; PR:Q14657; -. DR Proteomes; UP000005640; Chromosome X. DR Bgee; ENSG00000196976; -. DR CleanEx; HS_LAGE3; -. DR ExpressionAtlas; Q14657; baseline and differential. DR Genevisible; Q14657; HS. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW. DR InterPro; IPR015419; CTAG/Pcc1. DR Pfam; PF09341; Pcc1; 1. PE 1: Evidence at protein level; KW Complete proteome; Nucleus; Reference proteome; tRNA processing. FT CHAIN 1 143 EKC/KEOPS complex subunit LAGE3. FT /FTId=PRO_0000218924. SQ SEQUENCE 143 AA; 14804 MW; AD164559371449F8 CRC64; MRDADADAGG GADGGDGRGG HSCRGGVDTA AAPAGGAPPA HAPGPGRDAA SAARGSRMRP HIFTLSVPFP TPLEAEIAHG SLAPDAEPHQ RVVGKDLTVS GRILVVRWKA EDCRLLRISV INFLDQLSLV VRTMQRFGPP VSR //