UFM1_HUMAN
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 03-AUG-2022, entry version 163.
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=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 [17] {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 [18] {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 [19] {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 [20] {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 [21] {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).
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:29868776, PubMed:27653677). The so-called ufmylation, requires
CC the UFM1-activating E1 enzyme UBA5, the UFM1-conjugating E2 enzyme
CC UFC1, and the UFM1-ligase E3 enzyme UFL1 (PubMed:15071506,
CC PubMed:20018847, PubMed:29868776, PubMed:27653677). Ufmylation is
CC involved in reticulophagy (also called ER-phagy) induced in response to
CC endoplasmic reticulum stress (PubMed:32160526). Ufmylation of TRIP4
CC regulates nuclear receptors-mediated transcription (PubMed:25219498).
CC {ECO:0000269|PubMed:15071506, ECO:0000269|PubMed:20018847,
CC ECO:0000269|PubMed:25219498, ECO:0000269|PubMed:27653677,
CC ECO:0000269|PubMed:29868776, ECO:0000269|PubMed:32160526}.
CC -!- SUBUNIT: Interacts with UBA5 (PubMed:26872069, PubMed:29295865,
CC PubMed:27653677, PubMed:26929408, PubMed:28360427, 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; Q0VD86: INCA1; NbExp=3; IntAct=EBI-1045061, EBI-6509505;
CC P61960; Q4G0X4: KCTD21; NbExp=3; IntAct=EBI-1045061, EBI-11976683;
CC P61960; Q9GZZ9: UBA5; NbExp=4; 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 -!- 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}.
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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_001286704.1. [P61960-2]
DR RefSeq; NP_001273634.1; NM_001286705.1.
DR RefSeq; NP_001273635.1; NM_001286706.1.
DR RefSeq; NP_057701.1; NM_016617.3. [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 PDBsum; 1WXS; -.
DR PDBsum; 5HKH; -.
DR PDBsum; 5IA7; -.
DR PDBsum; 5IA8; -.
DR PDBsum; 5IAA; -.
DR PDBsum; 5L95; -.
DR PDBsum; 6H77; -.
DR AlphaFoldDB; P61960; -.
DR SASBDB; P61960; -.
DR SMR; P61960; -.
DR BioGRID; 119616; 95.
DR IntAct; P61960; 16.
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 EPD; P61960; -.
DR jPOST; P61960; -.
DR MassIVE; P61960; -.
DR MaxQB; P61960; -.
DR PaxDb; P61960; -.
DR PeptideAtlas; P61960; -.
DR PRIDE; P61960; -.
DR ProteomicsDB; 57344; -. [P61960-1]
DR ProteomicsDB; 57345; -. [P61960-2]
DR TopDownProteomics; P61960-1; -. [P61960-1]
DR TopDownProteomics; P61960-2; -. [P61960-2]
DR Antibodypedia; 42138; 73 antibodies from 20 providers.
DR DNASU; 51569; -.
DR Ensembl; ENST00000239878.9; ENSP00000239878.4; ENSG00000120686.12. [P61960-1]
DR Ensembl; ENST00000379649.5; ENSP00000368970.1; ENSG00000120686.12. [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 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 neXtProt; NX_P61960; -.
DR OpenTargets; ENSG00000120686; -.
DR Orphanet; 139441; Hypomyelination with atrophy of basal ganglia and cerebellum.
DR PharmGKB; PA134863405; -.
DR VEuPathDB; HostDB:ENSG00000120686; -.
DR eggNOG; KOG3483; Eukaryota.
DR GeneTree; ENSGT00390000010391; -.
DR HOGENOM; CLU_175114_2_0_1; -.
DR InParanoid; P61960; -.
DR OMA; INPAQNA; -.
DR OrthoDB; 1575050at2759; -.
DR PhylomeDB; P61960; -.
DR TreeFam; TF312934; -.
DR PathwayCommons; P61960; -.
DR SignaLink; P61960; -.
DR BioGRID-ORCS; 51569; 411 hits in 1089 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 208 other tissues.
DR ExpressionAtlas; P61960; baseline and differential.
DR Genevisible; P61960; HS.
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 InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR005375; UFM1.
DR PANTHER; PTHR15825; PTHR15825; 1.
DR Pfam; PF03671; Ufm1; 1.
DR PIRSF; PIRSF038027; Ubiquitin-like_Ufm1; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Disease variant;
KW Isopeptide bond; Leukodystrophy; Nucleus; Reference proteome;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..83
FT /note="Ubiquitin-fold modifier 1"
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 UFM1."
FT /evidence="ECO:0000269|PubMed:27653677"
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 5..13
FT /evidence="ECO:0007829|PDB:5IA7"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:1WXS"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:5IA7"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1WXS"
FT HELIX 29..40
FT /evidence="ECO:0007829|PDB:5IA7"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:5IA7"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:5IA7"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:5IA7"
FT HELIX 63..70
FT /evidence="ECO:0007829|PDB:5IA7"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:5IA7"
SQ SEQUENCE 85 AA; 9118 MW; EDB2412E5E5836D8 CRC64;
MSKVSFKITL TSDPRLPYKV LSVPESTPFT AVLKFAAEEF KVPAATSAII TNDGIGINPA
QTAGNVFLKH GSELRIIPRD RVGSC
