ID UFM1_HUMAN Reviewed; 85 AA. AC P61960; Q14346; Q5VXS0; Q6IAG6; Q9CPX2; Q9NZF2; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2004, sequence version 1. DT 28-JAN-2026, entry version 180. DE RecName: Full=Ubiquitin-fold modifier 1 {ECO:0000303|PubMed:15071506}; DE Flags: Precursor; GN Name=UFM1 {ECO:0000303|PubMed:15071506, ECO:0000312|HGNC:HGNC:20597}; GN Synonyms=C13orf20 {ECO:0000312|HGNC:HGNC:20597}; GN ORFNames=BM-002 {ECO:0000303|PubMed:11042152}; 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), FUNCTION, SUBCELLULAR LOCATION, AND RP MUTAGENESIS OF GLY-83. RX PubMed=15071506; DOI=10.1038/sj.emboj.7600205; RA Komatsu M., Chiba T., Tatsumi K., Iemura S., Tanida I., Okazaki N., RA Ueno T., Kominami E., Natsume T., Tanaka K.; RT "A novel protein-conjugating system for Ufm1, a ubiquitin-fold modifier."; RL EMBO J. 23:1977-1986(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Bone marrow; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT cells."; RL Genome Res. 10:1546-1560(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Neuroblastoma; RX PubMed=16344560; DOI=10.1101/gr.4039406; RA Kimura K., Wakamatsu A., Suzuki Y., Ota T., Nishikawa T., Yamashita R., RA Yamamoto J., Sekine M., Tsuritani K., Wakaguri H., Ishii S., Sugiyama T., RA Saito K., Isono Y., Irie R., Kushida N., Yoneyama T., Otsuka R., Kanda K., RA Yokoi T., Kondo H., Wagatsuma M., Murakawa K., Ishida S., Ishibashi T., RA Takahashi-Fujii A., Tanase T., Nagai K., Kikuchi H., Nakai K., Isogai T., RA Sugano S.; RT "Diversification of transcriptional modulation: large-scale identification RT and characterization of putative alternative promoters of human genes."; RL Genome Res. 16:55-65(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Kidney; 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 [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-80 (ISOFORM 1). RC TISSUE=Brain; RA Dmitrenko V.V., Garifulin O.M., Kavsan V.M.; RT "Characterization of different mRNA types expressed in human brain."; RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases. RN [8] RP FUNCTION. RX PubMed=20018847; DOI=10.1074/jbc.m109.036814; RA Tatsumi K., Sou Y.S., Tada N., Nakamura E., Iemura S., Natsume T., RA Kang S.H., Chung C.H., Kasahara M., Kominami E., Yamamoto M., Tanaka K., RA Komatsu M.; RT "A novel type of E3 ligase for the Ufm1 conjugation system."; RL J. Biol. Chem. 285:5417-5427(2010). RN [9] 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 [10] RP INDUCTION. RX PubMed=23152784; DOI=10.1371/journal.pone.0048587; RA Zhang Y., Zhang M., Wu J., Lei G., Li H.; RT "Transcriptional regulation of the Ufm1 conjugation system in response to RT disturbance of the endoplasmic reticulum homeostasis and inhibition of RT vesicle trafficking."; RL PLoS ONE 7:E48587-E48587(2012). RN [11] RP FUNCTION, AND UFMYLATION AT LYS-69. RX PubMed=25219498; DOI=10.1016/j.molcel.2014.08.007; RA Yoo H.M., Kang S.H., Kim J.Y., Lee J.E., Seong M.W., Lee S.W., Ka S.H., RA Sou Y.S., Komatsu M., Tanaka K., Lee S.T., Noh D.Y., Baek S.H., Jeon Y.J., RA Chung C.H.; RT "Modification of ASC1 by UFM1 is crucial for ERalpha transactivation and RT breast cancer development."; RL Mol. Cell 56:261-274(2014). RN [12] RP INTERACTION WITH UBA5. RX PubMed=26872069; DOI=10.1371/journal.pone.0149039; RA Duan R., Shi Y., Yu L., Zhang G., Li J., Lin Y., Guo J., Wang J., Shen L., RA Jiang H., Wang G., Tang B.; RT "UBA5 mutations cause a new form of autosomal recessive cerebellar RT ataxia."; RL PLoS ONE 11:E0149039-E0149039(2016). RN [13] RP INVOLVEMENT IN HLD14. RX PubMed=28931644; DOI=10.1212/wnl.0000000000004578; RG Recessive H-ABC Research Group; RA Hamilton E.M.C., Bertini E., Kalaydjieva L., Morar B., Dojcakova D., RA Liu J., Vanderver A., Curiel J., Persoon C.M., Diodato D., Pinelli L., RA van der Meij N.L., Plecko B., Blaser S., Wolf N.I., Waisfisz Q., RA Abbink T.E.M., van der Knaap M.S.; RT "founder mutation in the Roma population causes recessive variant of H- RT ABC."; RL Neurology 89:1821-1828(2017). RN [14] RP FUNCTION, INTERACTION WITH UFC1, INVOLVEMENT IN HLD14, VARIANT HLD14 RP CYS-81, AND CHARACTERIZATION OF VARIANT HLD14 CYS-81. RX PubMed=29868776; DOI=10.1093/brain/awy135; RA Nahorski M.S., Maddirevula S., Ishimura R., Alsahli S., Brady A.F., RA Begemann A., Mizushima T., Guzman-Vega F.J., Obata M., Ichimura Y., RA Alsaif H.S., Anazi S., Ibrahim N., Abdulwahab F., Hashem M., Monies D., RA Abouelhoda M., Meyer B.F., Alfadhel M., Eyaid W., Zweier M., Steindl K., RA Rauch A., Arold S.T., Woods C.G., Komatsu M., Alkuraya F.S.; RT "Biallelic UFM1 and UFC1 mutations expand the essential role of ufmylation RT in brain development."; RL Brain 141:1934-1945(2018). RN [15] RP INTERACTION WITH UBA5. RX PubMed=29295865; DOI=10.1096/fj.201701057r; RA Mashahreh B., Hassouna F., Soudah N., Cohen-Kfir E., Strulovich R., RA Haitin Y., Wiener R.; RT "Trans-binding of UFM1 to UBA5 stimulates UBA5 homodimerization and ATP RT binding."; RL FASEB J. 32:2794-2802(2018). RN [16] RP FUNCTION. RX PubMed=30626644; DOI=10.1073/pnas.1816202116; RA Walczak C.P., Leto D.E., Zhang L., Riepe C., Muller R.Y., DaRosa P.A., RA Ingolia N.T., Elias J.E., Kopito R.R.; RT "Ribosomal protein RPL26 is the principal target of UFMylation."; RL Proc. Natl. Acad. Sci. U.S.A. 116:1299-1308(2019). RN [17] RP FUNCTION. RX PubMed=32160526; DOI=10.1016/j.cell.2020.02.017; RA Liang J.R., Lingeman E., Luong T., Ahmed S., Muhar M., Nguyen T., RA Olzmann J.A., Corn J.E.; RT "A genome-wide ER-phagy screen highlights key roles of mitochondrial RT metabolism and ER-Resident UFMylation."; RL Cell 180:1160-1177(2020). RN [18] RP PROTEOLYTIC CLEAVAGE. RX PubMed=35926457; DOI=10.1016/j.celrep.2022.111168; RA Millrine D., Cummings T., Matthews S.P., Peter J.J., Magnussen H.M., RA Lange S.M., Macartney T., Lamoliatte F., Knebel A., Kulathu Y.; RT "Human UFSP1 is an active protease that regulates UFM1 maturation and RT UFMylation."; RL Cell Rep. 40:111168-111168(2022). RN [19] RP PROTEOLYTIC CLEAVAGE. RX PubMed=35525273; DOI=10.1016/j.jbc.2022.102016; RA Liang Q., Jin Y., Xu S., Zhou J., Mao J., Ma X., Wang M., Cong Y.S.; RT "Human UFSP1 translated from an upstream near-cognate initiation codon RT functions as an active UFM1-specific protease."; RL J. Biol. Chem. 298:102016-102016(2022). RN [20] RP FUNCTION, AND MUTAGENESIS OF 83-GLY--CYS-85. RX PubMed=38377992; DOI=10.1016/j.molcel.2024.01.024; RA He C., Xing X., Chen H.Y., Gao M., Shi J., Xiang B., Xiao X., Sun Y., RA Yu H., Xu G., Yao Y., Xie Z., Xing Y., Budiarto B.R., Chen S.Y., Gao Y., RA Lee Y.R., Zhang J.; RT "UFL1 ablation in T cells suppresses PD-1 UFMylation to enhance anti-tumor RT immunity."; RL Mol. Cell 0:0-0(2024). RN [21] {ECO:0007744|PDB:1WXS} RP STRUCTURE BY NMR. RX PubMed=16527251; DOI=10.1016/j.bbrc.2006.02.107; RA Sasakawa H., Sakata E., Yamaguchi Y., Komatsu M., Tatsumi K., Kominami E., RA Tanaka K., Kato K.; RT "Solution structure and dynamics of Ufm1, a ubiquitin-fold modifier 1."; RL Biochem. Biophys. Res. Commun. 343:21-26(2006). RN [22] {ECO:0007744|PDB:5IAA, ECO:0007744|PDB:5L95} RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-83 IN COMPLEX WITH UBA5, RP FUNCTION, INTERACTION WITH UBA5, AND MUTAGENESIS OF ALA-48 AND ARG-79. RX PubMed=27653677; DOI=10.1016/j.celrep.2016.08.067; RA Oweis W., Padala P., Hassouna F., Cohen-Kfir E., Gibbs D.R., Todd E.A., RA Berndsen C.E., Wiener R.; RT "Trans-binding mechanism of ubiquitin-like protein activation revealed by a RT UBA5-UFM1 Complex."; RL Cell Rep. 16:3113-3120(2016). RN [23] {ECO:0007744|PDB:5HKH} RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 2-83 IN COMPLEX WITH UBA5, AND RP INTERACTION WITH UBA5. RX PubMed=26929408; DOI=10.1074/jbc.m116.715474; RA Habisov S., Huber J., Ichimura Y., Akutsu M., Rogova N., Loehr F., RA McEwan D.G., Johansen T., Dikic I., Doetsch V., Komatsu M., Rogov V.V., RA Kirkin V.; RT "Structural and functional analysis of a novel interaction motif within RT UFM1-activating enzyme 5 (UBA5) required for binding to ubiquitin-like RT proteins and ufmylation."; RL J. Biol. Chem. 291:9025-9041(2016). RN [24] {ECO:0007744|PDB:5IA7, ECO:0007744|PDB:5IA8} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-83 IN COMPLEX WITH UBA5, RP INTERACTION WITH UBA5, AND MUTAGENESIS OF LEU-21 AND GLU-38. RX PubMed=28360427; DOI=10.1038/s41598-017-00610-0; RA Padala P., Oweis W., Mashahreh B., Soudah N., Cohen-Kfir E., Todd E.A., RA Berndsen C.E., Wiener R.; RT "Novel insights into the interaction of UBA5 with UFM1 via a UFM1- RT interacting sequence."; RL Sci. Rep. 7:508-508(2017). RN [25] {ECO:0007744|PDB:6H77} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-78 IN COMPLEX WITH UBA5, AND RP INTERACTION WITH UBA5. RX PubMed=30412706; DOI=10.1016/j.jmb.2018.10.007; RA Soudah N., Padala P., Hassouna F., Kumar M., Mashahreh B., Lebedev A.A., RA Isupov M.N., Cohen-Kfir E., Wiener R.; RT "An N-terminal extension to UBA5 adenylation domain boosts UFM1 activation: RT isoform-specific differences in ubiquitin-like protein activation."; RL J. Mol. Biol. 431:463-478(2019). RN [26] {ECO:0007744|PDB:8BZR, ECO:0007744|PDB:8OJ0} RP STRUCTURE BY ELECTRON MICROSCOPY (2.9 ANGSTROMS) OF THE UREL COMPLEX IN RP COMPLEX WITH THE 60S RIBOSOME, X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF RP 1-83 IN COMPLEX WITH UFC1, AND FUNCTION. RX PubMed=38383785; DOI=10.1038/s41586-024-07073-0; RA DaRosa P.A., Penchev I., Gumbin S.C., Scavone F., Wachalska M., Paulo J.A., RA Ordureau A., Peter J.J., Kulathu Y., Harper J.W., Becker T., Beckmann R., RA Kopito R.R.; RT "UFM1 E3 ligase promotes recycling of 60S ribosomal subunits from the ER."; RL Nature 627:445-452(2024). CC -!- FUNCTION: Ubiquitin-like modifier which can be covalently attached via CC an isopeptide bond to lysine residues of substrate proteins as a CC monomer or a lysine-linked polymer (PubMed:15071506, PubMed:20018847, CC PubMed:27653677, PubMed:29868776, PubMed:30626644, PubMed:38377992, CC PubMed:38383785). The so-called ufmylation, requires the UFM1- CC activating E1 enzyme UBA5, the UFM1-conjugating E2 enzyme UFC1, and the CC UFM1-ligase E3 enzyme UFL1 (PubMed:15071506, PubMed:20018847, CC PubMed:27653677, PubMed:29868776). Ufmylation is involved in various CC processes, such as ribosome recycling, response to DNA damage, CC transcription or reticulophagy (also called ER-phagy) induced in CC response to endoplasmic reticulum stress (PubMed:25219498, CC PubMed:32160526, PubMed:38383785). {ECO:0000269|PubMed:15071506, CC ECO:0000269|PubMed:20018847, ECO:0000269|PubMed:25219498, CC ECO:0000269|PubMed:27653677, ECO:0000269|PubMed:29868776, CC ECO:0000269|PubMed:30626644, ECO:0000269|PubMed:32160526, CC ECO:0000269|PubMed:38377992, ECO:0000269|PubMed:38383785}. CC -!- SUBUNIT: Interacts with UBA5 (PubMed:26872069, PubMed:26929408, CC PubMed:27653677, PubMed:28360427, PubMed:29295865, PubMed:30412706). CC Interacts with UFC1 (PubMed:29868776). {ECO:0000269|PubMed:26872069, CC ECO:0000269|PubMed:26929408, ECO:0000269|PubMed:27653677, CC ECO:0000269|PubMed:28360427, ECO:0000269|PubMed:29295865, CC ECO:0000269|PubMed:29868776, ECO:0000269|PubMed:30412706}. CC -!- INTERACTION: CC P61960; Q96JB5: CDK5RAP3; NbExp=4; IntAct=EBI-1045061, EBI-718818; CC P61960; Q0VD86: INCA1; NbExp=3; IntAct=EBI-1045061, EBI-6509505; CC P61960; Q4G0X4: KCTD21; NbExp=3; IntAct=EBI-1045061, EBI-11976683; CC P61960; P06703: S100A6; NbExp=2; IntAct=EBI-1045061, EBI-352877; CC P61960; Q9GZZ9: UBA5; NbExp=8; IntAct=EBI-1045061, EBI-747805; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15071506}. Cytoplasm CC {ECO:0000269|PubMed:15071506}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P61960-1; Sequence=Displayed; CC Name=2; CC IsoId=P61960-2; Sequence=VSP_041186; CC -!- INDUCTION: Up-regulated by thapsigargin. {ECO:0000269|PubMed:23152784}. CC -!- PTM: UFM1 precursor is cleaved by UFSP1, promoting its maturation: CC processing of the C-terminal Ser-Cys dipeptide is required to expose CC its C-terminal conserved Gly residue. {ECO:0000269|PubMed:35525273, CC ECO:0000269|PubMed:35926457}. CC -!- DISEASE: Leukodystrophy, hypomyelinating, 14 (HLD14) [MIM:617899]: An CC autosomal recessive, severe disorder characterized by atrophy of the CC basal ganglia and cerebellum, hypomyelination, severe developmental CC delay, typically without intentional movements and language CC development, and microcephaly. Almost all patients exhibit spasticity, CC extrapyramidal movement abnormalities, and severe drug-resistant CC epilepsy. Disease onset is early in infancy, and most patients die in CC the first years of life. {ECO:0000269|PubMed:28931644, CC ECO:0000269|PubMed:29868776}. Note=The disease is caused by variants CC affecting the gene represented in this entry. The disease-causing CC variant may be a homozygous 3-bp deletion in the promoter region of the CC UFM1 gene, which segregates with the disorder in affected families. In CC vitro expression studies in different cell lines showed that the CC mutation significantly reduces transcriptional activity in certain CC neuronal cell lines (SY5Y and U373), but not in other cell lines, CC including HeLa and HOF-F2. {ECO:0000269|PubMed:28931644}. CC -!- SIMILARITY: Belongs to the UFM1 family. {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; AB154404; BAD15373.1; -; mRNA. DR EMBL; AF208844; AAF64258.1; -; mRNA. DR EMBL; CR457189; CAG33470.1; -; mRNA. DR EMBL; DA664581; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AL356863; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC005193; AAH05193.1; -; mRNA. DR EMBL; Z70222; CAA94181.1; -; mRNA. DR CCDS; CCDS66533.1; -. [P61960-2] DR CCDS; CCDS9366.1; -. [P61960-1] DR RefSeq; NP_001273632.1; NM_001286703.1. DR RefSeq; NP_001273633.1; NM_001286704.2. [P61960-2] DR RefSeq; NP_001273634.1; NM_001286705.1. DR RefSeq; NP_001273635.1; NM_001286706.1. DR RefSeq; NP_057701.1; NM_016617.4. [P61960-1] DR PDB; 1WXS; NMR; -; A=1-85. DR PDB; 5HKH; X-ray; 2.55 A; A/C=2-83. DR PDB; 5IA7; X-ray; 2.00 A; A/B=1-83. DR PDB; 5IA8; X-ray; 2.00 A; A/B=2-83. DR PDB; 5IAA; X-ray; 1.85 A; C/D=1-83. DR PDB; 5L95; X-ray; 2.10 A; C/D=4-83. DR PDB; 6H77; X-ray; 2.10 A; Q/R/S/T=1-78. DR PDB; 7W3N; X-ray; 1.60 A; A=1-83. DR PDB; 8BZR; X-ray; 1.78 A; B=1-83. DR PDB; 8OHD; EM; 3.10 A; D=1-85. DR PDB; 8OJ0; EM; 3.30 A; D=1-85. DR PDB; 8OJ5; EM; 2.90 A; D=1-85. DR PDB; 8QFC; EM; 3.20 A; E=1-83. DR PDB; 9GY4; EM; 3.00 A; D=1-85. DR PDBsum; 1WXS; -. DR PDBsum; 5HKH; -. DR PDBsum; 5IA7; -. DR PDBsum; 5IA8; -. DR PDBsum; 5IAA; -. DR PDBsum; 5L95; -. DR PDBsum; 6H77; -. DR PDBsum; 7W3N; -. DR PDBsum; 8BZR; -. DR PDBsum; 8OHD; -. DR PDBsum; 8OJ0; -. DR PDBsum; 8OJ5; -. DR PDBsum; 8QFC; -. DR PDBsum; 9GY4; -. DR AlphaFoldDB; P61960; -. DR EMDB; EMD-16880; -. DR EMDB; EMD-16902; -. DR EMDB; EMD-16905; -. DR EMDB; EMD-51681; -. DR SASBDB; P61960; -. DR SMR; P61960; -. DR BioGRID; 119616; 114. DR FunCoup; P61960; 3132. DR IntAct; P61960; 34. DR MINT; P61960; -. DR STRING; 9606.ENSP00000368970; -. DR GlyGen; P61960; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P61960; -. DR PhosphoSitePlus; P61960; -. DR BioMuta; UFM1; -. DR DMDM; 48428799; -. DR jPOST; P61960; -. DR MassIVE; P61960; -. DR PaxDb; 9606-ENSP00000368970; -. DR PeptideAtlas; P61960; -. DR ProteomicsDB; 57344; -. [P61960-1] DR ProteomicsDB; 57345; -. [P61960-2] DR Pumba; P61960; -. DR TopDownProteomics; P61960-1; -. [P61960-1] DR TopDownProteomics; P61960-2; -. [P61960-2] DR Antibodypedia; 42138; 75 antibodies from 24 providers. DR DNASU; 51569; -. DR Ensembl; ENST00000239878.9; ENSP00000239878.4; ENSG00000120686.13. [P61960-1] DR Ensembl; ENST00000379649.5; ENSP00000368970.1; ENSG00000120686.13. [P61960-2] DR GeneID; 51569; -. DR KEGG; hsa:51569; -. DR MANE-Select; ENST00000239878.9; ENSP00000239878.4; NM_016617.4; NP_057701.1. DR UCSC; uc001uwu.5; human. [P61960-1] DR AGR; HGNC:20597; -. DR ClinPGx; PA134863405; -. DR CTD; 51569; -. DR DisGeNET; 51569; -. DR GeneCards; UFM1; -. DR HGNC; HGNC:20597; UFM1. DR HPA; ENSG00000120686; Low tissue specificity. DR MalaCards; UFM1; -. DR MIM; 610553; gene. DR MIM; 617899; phenotype. DR OpenTargets; ENSG00000120686; -. DR Orphanet; 139441; Hypomyelination with atrophy of basal ganglia and cerebellum. DR VEuPathDB; HostDB:ENSG00000120686; -. DR eggNOG; KOG3483; Eukaryota. DR GeneTree; ENSGT00390000010391; -. DR HOGENOM; CLU_175114_2_0_1; -. DR InParanoid; P61960; -. DR OMA; MEHAVGK; -. DR OrthoDB; 284357at2759; -. DR PAN-GO; P61960; 3 GO annotations based on evolutionary models. DR PhylomeDB; P61960; -. DR PathwayCommons; P61960; -. DR SignaLink; P61960; -. DR Agora; ENSG00000120686; -. DR BioGRID-ORCS; 51569; 417 hits in 1167 CRISPR screens. DR ChiTaRS; UFM1; human. DR EvolutionaryTrace; P61960; -. DR GeneWiki; UFM1; -. DR GenomeRNAi; 51569; -. DR Pharos; P61960; Tbio. DR PRO; PR:P61960; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; P61960; protein. DR Bgee; ENSG00000120686; Expressed in corpus epididymis and 210 other cell types or tissues. DR ExpressionAtlas; P61960; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:ParkinsonsUK-UCL. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0007420; P:brain development; IMP:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:ParkinsonsUK-UCL. DR GO; GO:0042308; P:negative regulation of protein import into nucleus; IMP:CACAO. DR GO; GO:1990592; P:protein K69-linked ufmylation; IDA:UniProtKB. DR GO; GO:0071569; P:protein ufmylation; IDA:UniProtKB. DR GO; GO:0033146; P:regulation of intracellular estrogen receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:MGI. DR GO; GO:0061709; P:reticulophagy; IMP:UniProtKB. DR CDD; cd01766; Ubl_UFM1; 1. DR FunFam; 3.10.20.90:FF:000044; Ubiquitin-fold modifier 1; 1. DR Gene3D; 3.10.20.90; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1; 1. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR InterPro; IPR005375; UFM1. DR PANTHER; PTHR15825; UBIQUITIN-FOLD MODIFIER 1; 1. DR PANTHER; PTHR15825:SF5; UBIQUITIN-FOLD MODIFIER 1; 1. DR Pfam; PF03671; Ufm1; 1. DR PIRSF; PIRSF038027; Ubiquitin-like_Ufm1; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Disease variant; KW Isopeptide bond; Leukodystrophy; Nucleus; Proteomics identification; KW Reference proteome; Ubl conjugation; Ubl conjugation pathway. FT CHAIN 1..83 FT /note="Ubiquitin-fold modifier 1" FT /evidence="ECO:0000269|PubMed:15071506" FT /id="PRO_0000042122" FT PROPEP 84..85 FT /note="Removed in mature form" FT /evidence="ECO:0000269|PubMed:15071506" FT /id="PRO_0000042123" FT CROSSLNK 69 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in UFM1)" FT /evidence="ECO:0000269|PubMed:25219498" FT CROSSLNK 83 FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with FT K-? in acceptor proteins)" FT /evidence="ECO:0000269|PubMed:15071506, FT ECO:0000269|PubMed:25219498, ECO:0000269|PubMed:27653677" FT VAR_SEQ 1..20 FT /note="MSKVSFKITLTSDPRLPYKV -> MIRAFPTTTPRSLHLFTSSTFLARALPG FT AFPTGACEER (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16344560" FT /id="VSP_041186" FT VARIANT 81 FT /note="R -> C (in HLD14; decreased ability to form FT thioester bonds with UBA5 and UFC1; decreased protein FT ufmylation; does not affect the cellular response to FT endoplasmic reticulum stress; dbSNP:rs1033946108)" FT /evidence="ECO:0000269|PubMed:29868776" FT /id="VAR_081218" FT MUTAGEN 21 FT /note="L->A: Abolished ability to be activated by UBA5." FT /evidence="ECO:0000269|PubMed:28360427" FT MUTAGEN 38 FT /note="E->A: Abolished ability to be activated by UBA5." FT /evidence="ECO:0000269|PubMed:28360427" FT MUTAGEN 48 FT /note="A->F,Q: Abolished ability to be activated by UBA5." FT /evidence="ECO:0000269|PubMed:27653677" FT MUTAGEN 79 FT /note="R->A: Slightly reduced interaction with UBA5." FT /evidence="ECO:0000269|PubMed:27653677" FT MUTAGEN 83..85 FT /note="Missing: Abolished activity." FT /evidence="ECO:0000269|PubMed:38377992" FT MUTAGEN 83 FT /note="G->A: Confers resistance to cleavage." FT /evidence="ECO:0000269|PubMed:15071506" FT CONFLICT 12 FT /note="S -> W (in Ref. 7; CAA94181)" FT /evidence="ECO:0000305" FT CONFLICT 78..80 FT /note="PRD -> LEI (in Ref. 7; CAA94181)" FT /evidence="ECO:0000305" FT STRAND 2..10 FT /evidence="ECO:0007829|PDB:7W3N" FT STRAND 14..16 FT /evidence="ECO:0007829|PDB:1WXS" FT STRAND 18..24 FT /evidence="ECO:0007829|PDB:7W3N" FT STRAND 25..28 FT /evidence="ECO:0007829|PDB:1WXS" FT HELIX 29..40 FT /evidence="ECO:0007829|PDB:7W3N" FT HELIX 44..46 FT /evidence="ECO:0007829|PDB:7W3N" FT STRAND 47..51 FT /evidence="ECO:0007829|PDB:7W3N" FT STRAND 59..62 FT /evidence="ECO:0007829|PDB:7W3N" FT HELIX 63..70 FT /evidence="ECO:0007829|PDB:7W3N" FT STRAND 72..78 FT /evidence="ECO:0007829|PDB:7W3N" SQ SEQUENCE 85 AA; 9118 MW; EDB2412E5E5836D8 CRC64; MSKVSFKITL TSDPRLPYKV LSVPESTPFT AVLKFAAEEF KVPAATSAII TNDGIGINPA QTAGNVFLKH GSELRIIPRD RVGSC //