ID UBL5_HUMAN Reviewed; 73 AA. AC Q9BZL1; Q2NL89; DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 159. DE RecName: Full=Ubiquitin-like protein 5; GN Name=UBL5; 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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Iris; RX PubMed=11161819; DOI=10.1006/geno.2000.6439; RA Friedman J.S., Koop B.F., Raymond V., Walter M.A.; RT "Isolation of a ubiquitin-like (UBL5) gene from a screen identifying highly RT expressed and conserved iris genes."; RL Genomics 71:252-255(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney, and Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP INTERACTION WITH CLK1; CLK3 AND CLK4. RX PubMed=12705895; DOI=10.1016/s0006-291x(03)00549-7; RA Kantham L., Kerr-Bayles L., Godde N., Quick M., Webb R., Sunderland T., RA Bond J., Walder K., Augert G., Collier G.; RT "Beacon interacts with cdc2/cdc28-like kinases."; RL Biochem. Biophys. Res. Commun. 304:125-129(2003). 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., 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 [6] RP IDENTIFICATION BY MASS 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 [7] RP SUBCELLULAR LOCATION, AND INTERACTION WITH COILIN/COIL. RX PubMed=23726919; DOI=10.1016/j.bbrc.2013.05.083; RA Sveda M., Castoralova M., Lipov J., Ruml T., Knejzlik Z.; RT "Human UBL5 protein interacts with coilin and meets the Cajal bodies."; RL Biochem. Biophys. Res. Commun. 436:240-245(2013). RN [8] 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 [9] RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-22, AND INTERACTION WITH RP SART1 AND EFTUD2. RX PubMed=25092792; DOI=10.15252/embr.201438679; RA Oka Y., Varmark H., Vitting-Seerup K., Beli P., Waage J., Hakobyan A., RA Mistrik M., Choudhary C., Rohde M., Bekker-Jensen S., Mailand N.; RT "UBL5 is essential for pre-mRNA splicing and sister chromatid cohesion in RT human cells."; RL EMBO Rep. 15:956-964(2014). RN [10] RP FUNCTION, AND INTERACTION WITH FANCI. RX PubMed=25862789; DOI=10.15252/embj.201490376; RA Oka Y., Bekker-Jensen S., Mailand N.; RT "Ubiquitin-like protein UBL5 promotes the functional integrity of the RT Fanconi anemia pathway."; RL EMBO J. 34:1385-1398(2015). RN [11] RP FUNCTION, SUBCELLULAR LOCATION, AND DEPLETION DURING ER STRESS-INDUCED CELL RP DEATH. RX PubMed=37315790; DOI=10.1016/j.jbc.2023.104915; RA Wang W., Hawkridge A.M., Ma Y., Zhang B., Mangrum J.B., Hassan Z.H., He T., RA Blat S., Guo C., Zhou H., Liu J., Wang X.Y., Fang X.; RT "Ubiquitin-like protein 5 is a novel player in the UPR-PERK arm and ER RT stress-induced cell death."; RL J. Biol. Chem. 0:0-0(2023). RN [12] RP STRUCTURE BY NMR, AND INTERACTION WITH CLK4. RX PubMed=12824502; DOI=10.1110/ps.0382803; RA McNally T., Huang Q., Janis R.S., Liu Z., Olejniczak E.T., Reilly R.M.; RT "Structural analysis of UBL5, a novel ubiquitin-like modifier."; RL Protein Sci. 12:1562-1566(2003). CC -!- FUNCTION: Ubiquitin-like protein that plays a role in cell CC proliferation and sister chromatid cohesion by associating with CC spliceosomal proteins (PubMed:25092792). Participates thereby in pre- CC mRNA splicing by maintaining spliceosome integrity. Promotes the CC functional integrity of the Fanconi anemia DNA repair pathway by CC interacting with FANCI component and subsequently mediating the CC formation of FANCI homodimers (PubMed:25862789). Plays also a CC protective role against ER stress-induced apoptosis (PubMed:37315790). CC {ECO:0000269|PubMed:25092792, ECO:0000269|PubMed:25862789, CC ECO:0000269|PubMed:37315790}. CC -!- SUBUNIT: Interacts with CLK1, CLK3 and CLK4. Interacts with coilin/COIL CC (PubMed:23726919). Interacts with spliceosome components SART1 and CC EFTUD2 (PubMed:25092792). Interacts with FANCI; this interaction CC promotes FANCI dimerization (PubMed:25862789). CC {ECO:0000269|PubMed:12705895, ECO:0000269|PubMed:12824502, CC ECO:0000269|PubMed:23726919, ECO:0000269|PubMed:25092792, CC ECO:0000269|PubMed:25862789}. CC -!- INTERACTION: CC Q9BZL1; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-607755, EBI-10181188; CC Q9BZL1; Q9NQY0: BIN3; NbExp=3; IntAct=EBI-607755, EBI-2653038; CC Q9BZL1; Q9BXJ1-2: C1QTNF1; NbExp=3; IntAct=EBI-607755, EBI-11536642; CC Q9BZL1; A0A1B0GWI1: CCDC196; NbExp=3; IntAct=EBI-607755, EBI-10181422; CC Q9BZL1; Q9BUN5-3: CCDC28B; NbExp=3; IntAct=EBI-607755, EBI-12920646; CC Q9BZL1; Q5T4B2: CERCAM; NbExp=3; IntAct=EBI-607755, EBI-12261896; CC Q9BZL1; P78358: CTAG1B; NbExp=3; IntAct=EBI-607755, EBI-1188472; CC Q9BZL1; Q9Y247: FAM50B; NbExp=3; IntAct=EBI-607755, EBI-742802; CC Q9BZL1; Q5JQS6: GCSAML; NbExp=3; IntAct=EBI-607755, EBI-17857617; CC Q9BZL1; Q9UBX0: HESX1; NbExp=3; IntAct=EBI-607755, EBI-8470369; CC Q9BZL1; Q8IV36: HID1; NbExp=3; IntAct=EBI-607755, EBI-743438; CC Q9BZL1; Q9UGU5: HMGXB4; NbExp=3; IntAct=EBI-607755, EBI-7261162; CC Q9BZL1; P49639: HOXA1; NbExp=3; IntAct=EBI-607755, EBI-740785; CC Q9BZL1; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-607755, EBI-10171774; CC Q9BZL1; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-607755, EBI-10241252; CC Q9BZL1; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-607755, EBI-726510; CC Q9BZL1; Q8WWY6: MBD3L1; NbExp=3; IntAct=EBI-607755, EBI-12516603; CC Q9BZL1; P23511-2: NFYA; NbExp=3; IntAct=EBI-607755, EBI-11061759; CC Q9BZL1; O00746: NME4; NbExp=3; IntAct=EBI-607755, EBI-744871; CC Q9BZL1; Q9NQ35: NRIP3; NbExp=3; IntAct=EBI-607755, EBI-10311735; CC Q9BZL1; Q3KNR5: PAX4; NbExp=3; IntAct=EBI-607755, EBI-10240813; CC Q9BZL1; Q96KR7: PHACTR3; NbExp=3; IntAct=EBI-607755, EBI-717068; CC Q9BZL1; Q96BK5: PINX1; NbExp=3; IntAct=EBI-607755, EBI-721782; CC Q9BZL1; Q9NR22: PRMT8; NbExp=3; IntAct=EBI-607755, EBI-745545; CC Q9BZL1; Q9UL46: PSME2; NbExp=3; IntAct=EBI-607755, EBI-741630; CC Q9BZL1; O43290: SART1; NbExp=4; IntAct=EBI-607755, EBI-607761; CC Q9BZL1; Q15019-3: SEPTIN2; NbExp=3; IntAct=EBI-607755, EBI-11525407; CC Q9BZL1; Q9UJW9: SERTAD3; NbExp=4; IntAct=EBI-607755, EBI-748621; CC Q9BZL1; Q15637-4: SF1; NbExp=3; IntAct=EBI-607755, EBI-12223157; CC Q9BZL1; P49901: SMCP; NbExp=3; IntAct=EBI-607755, EBI-750494; CC Q9BZL1; Q9NS25: SPANXB1; NbExp=3; IntAct=EBI-607755, EBI-17197485; CC Q9BZL1; Q9H0A9-2: SPATC1L; NbExp=3; IntAct=EBI-607755, EBI-11995806; CC Q9BZL1; Q5T0J7-2: TEX35; NbExp=3; IntAct=EBI-607755, EBI-12833746; CC Q9BZL1; Q8WTV1: THAP3; NbExp=3; IntAct=EBI-607755, EBI-17438286; CC Q9BZL1; Q08117-2: TLE5; NbExp=3; IntAct=EBI-607755, EBI-11741437; CC Q9BZL1; Q9HCM9-2: TRIM39; NbExp=3; IntAct=EBI-607755, EBI-11523450; CC Q9BZL1; Q9BRX9: WDR83; NbExp=2; IntAct=EBI-607755, EBI-7705033; CC Q9BZL1; Q8N8Y5: ZFP41; NbExp=3; IntAct=EBI-607755, EBI-12224489; CC Q9BZL1; Q15973: ZNF124; NbExp=3; IntAct=EBI-607755, EBI-2555767; CC Q9BZL1; Q5T7W0: ZNF618; NbExp=3; IntAct=EBI-607755, EBI-6255994; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11161819, CC ECO:0000269|PubMed:23726919, ECO:0000269|PubMed:37315790}. Nucleus CC {ECO:0000269|PubMed:23726919, ECO:0000269|PubMed:37315790}. Nucleus, CC Cajal body {ECO:0000269|PubMed:37315790}. CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest level of expression in heart, CC skeletal muscle, kidney, liver, iris and lymphoblasts. CC {ECO:0000269|PubMed:11161819}. CC -!- INDUCTION: Depleted by ER stress-induced mediated by the ubiquitin- CC independent proteasome system independent of transcriptional regulation CC and downstream of PERK activation. {ECO:0000269|PubMed:37315790}. 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; AF313915; AAK14178.1; -; mRNA. DR EMBL; BT007355; AAP36019.1; -; mRNA. DR EMBL; BC007053; AAH07053.1; -; mRNA. DR EMBL; BC110839; AAI10840.1; -; mRNA. DR CCDS; CCDS12219.1; -. DR RefSeq; NP_001041706.1; NM_001048241.2. DR RefSeq; NP_077268.1; NM_024292.3. DR PDB; 1P0R; NMR; -; A=1-73. DR PDB; 4PYU; X-ray; 2.00 A; A/B/G/K/O/S=1-73. DR PDB; 6AHD; EM; 3.80 A; A0=1-73. DR PDB; 7AAV; EM; 4.20 A; q=1-73. DR PDB; 7ABF; EM; 3.90 A; q=1-73. DR PDB; 7ABG; EM; 7.80 A; q=1-73. DR PDB; 7ABI; EM; 8.00 A; q=1-73. DR PDBsum; 1P0R; -. DR PDBsum; 4PYU; -. DR PDBsum; 6AHD; -. DR PDBsum; 7AAV; -. DR PDBsum; 7ABF; -. DR PDBsum; 7ABG; -. DR PDBsum; 7ABI; -. DR AlphaFoldDB; Q9BZL1; -. DR BMRB; Q9BZL1; -. DR EMDB; EMD-11693; -. DR EMDB; EMD-11694; -. DR EMDB; EMD-11695; -. DR EMDB; EMD-11697; -. DR EMDB; EMD-9624; -. DR SMR; Q9BZL1; -. DR BioGRID; 121872; 85. DR IntAct; Q9BZL1; 54. DR MINT; Q9BZL1; -. DR STRING; 9606.ENSP00000351492; -. DR GlyGen; Q9BZL1; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9BZL1; -. DR MetOSite; Q9BZL1; -. DR PhosphoSitePlus; Q9BZL1; -. DR BioMuta; UBL5; -. DR DMDM; 52082771; -. DR EPD; Q9BZL1; -. DR jPOST; Q9BZL1; -. DR MassIVE; Q9BZL1; -. DR MaxQB; Q9BZL1; -. DR PaxDb; 9606-ENSP00000351492; -. DR PeptideAtlas; Q9BZL1; -. DR ProteomicsDB; 79866; -. DR Pumba; Q9BZL1; -. DR Antibodypedia; 25091; 132 antibodies from 20 providers. DR DNASU; 59286; -. DR Ensembl; ENST00000358666.7; ENSP00000351492.2; ENSG00000198258.11. DR Ensembl; ENST00000586895.6; ENSP00000468656.1; ENSG00000198258.11. DR Ensembl; ENST00000590068.1; ENSP00000466910.1; ENSG00000198258.11. DR GeneID; 59286; -. DR KEGG; hsa:59286; -. DR MANE-Select; ENST00000586895.6; ENSP00000468656.1; NM_001048241.3; NP_001041706.1. DR UCSC; uc002mmi.3; human. DR AGR; HGNC:13736; -. DR CTD; 59286; -. DR DisGeNET; 59286; -. DR GeneCards; UBL5; -. DR HGNC; HGNC:13736; UBL5. DR HPA; ENSG00000198258; Low tissue specificity. DR MIM; 606849; gene. DR neXtProt; NX_Q9BZL1; -. DR OpenTargets; ENSG00000198258; -. DR PharmGKB; PA37805; -. DR VEuPathDB; HostDB:ENSG00000198258; -. DR eggNOG; KOG3493; Eukaryota. DR GeneTree; ENSGT00390000001945; -. DR HOGENOM; CLU_156193_2_0_1; -. DR InParanoid; Q9BZL1; -. DR OMA; HIKLEDY; -. DR OrthoDB; 4364at2759; -. DR PhylomeDB; Q9BZL1; -. DR PathwayCommons; Q9BZL1; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR SignaLink; Q9BZL1; -. DR BioGRID-ORCS; 59286; 848 hits in 1151 CRISPR screens. DR ChiTaRS; UBL5; human. DR EvolutionaryTrace; Q9BZL1; -. DR GeneWiki; UBL5; -. DR GenomeRNAi; 59286; -. DR Pharos; Q9BZL1; Tbio. DR PRO; PR:Q9BZL1; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q9BZL1; Protein. DR Bgee; ENSG00000198258; Expressed in adenohypophysis and 206 other cell types or tissues. DR ExpressionAtlas; Q9BZL1; baseline and differential. DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0031386; F:protein tag activity; IBA:GO_Central. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central. DR GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; HMP:ParkinsonsUK-UCL. DR GO; GO:0036211; P:protein modification process; IEA:InterPro. DR CDD; cd01791; Ubl_UBL5; 1. DR IDEAL; IID00735; -. DR InterPro; IPR039732; Hub1/Ubl5. DR InterPro; IPR000626; Ubiquitin-like_dom. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR13042; UBIQUITIN-LIKE PROTEIN 5; 1. DR PANTHER; PTHR13042:SF3; UBIQUITIN-LIKE PROTEIN 5; 1. DR Pfam; PF00240; ubiquitin; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR Genevisible; Q9BZL1; HS. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Nucleus; Reference proteome; KW Ubl conjugation pathway. FT CHAIN 1..73 FT /note="Ubiquitin-like protein 5" FT /id="PRO_0000114866" FT DOMAIN 1..73 FT /note="Ubiquitin-like" FT MUTAGEN 22 FT /note="D->A: Does not impair binding to SART1 nor its FT pre-mRNA splicing function." FT /evidence="ECO:0000269|PubMed:25092792" FT STRAND 1..7 FT /evidence="ECO:0007829|PDB:4PYU" FT TURN 9..11 FT /evidence="ECO:0007829|PDB:1P0R" FT STRAND 13..19 FT /evidence="ECO:0007829|PDB:4PYU" FT HELIX 24..34 FT /evidence="ECO:0007829|PDB:4PYU" FT HELIX 39..41 FT /evidence="ECO:0007829|PDB:4PYU" FT STRAND 42..46 FT /evidence="ECO:0007829|PDB:4PYU" FT TURN 57..61 FT /evidence="ECO:0007829|PDB:4PYU" FT STRAND 67..72 FT /evidence="ECO:0007829|PDB:4PYU" SQ SEQUENCE 73 AA; 8547 MW; D68BC941536AA39F CRC64; MIEVVCNDRL GKKVRVKCNT DDTIGDLKKL IAAQTGTRWN KIVLKKWYTI FKDHVSLGDY EIHDGMNLEL YYQ //