UFC1_HUMAN
ID UFC1_HUMAN Reviewed; 167 AA.
AC Q9Y3C8; A8K9R1; D3DVF9; Q549X0; Q5VTX1; Q9BS96; Q9P009;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Ubiquitin-fold modifier-conjugating enzyme 1 {ECO:0000305};
DE Short=Ufm1-conjugating enzyme 1 {ECO:0000303|PubMed:15071506};
GN Name=UFC1 {ECO:0000303|PubMed:15071506, ECO:0000312|HGNC:HGNC:26941};
GN ORFNames=CGI-126 {ECO:0000303|PubMed:10810093},
GN HSPC155 {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], FUNCTION, MUTAGENESIS OF CYS-116, AND ACTIVE
RP SITE.
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].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
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=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
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], AND VARIANT CYS-90.
RC TISSUE=Urinary bladder;
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 INTERACTION WITH UFL1.
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 INTERACTION WITH KIRREL3.
RX PubMed=25902260; DOI=10.1371/journal.pone.0123106;
RA Liu Y.F., Sowell S.M., Luo Y., Chaubey A., Cameron R.S., Kim H.G.,
RA Srivastava A.K.;
RT "Autism and intellectual disability-associated KIRREL3 interacts with
RT neuronal proteins MAP1B and MYO16 with potential roles in
RT neurodevelopment.";
RL PLoS ONE 10:E0123106-E0123106(2015).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP INTERACTION WITH UBA5.
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 [13]
RP FUNCTION, INTERACTION WITH UFM1, INTERACTION WITH UBA5, MUTAGENESIS OF
RP CYS-116, ACTIVE SITE, INVOLVEMENT IN NEDSG, VARIANTS NEDSG GLN-23 AND
RP ILE-106, AND CHARACTERIZATION OF VARIANTS NEDSG GLN-23 AND ILE-106.
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 [14]
RP INTERACTION WITH UFL1.
RX PubMed=30886146; DOI=10.1038/s41467-019-09175-0;
RA Qin B., Yu J., Nowsheen S., Wang M., Tu X., Liu T., Li H., Wang L., Lou Z.;
RT "UFL1 promotes histone H4 ufmylation and ATM activation.";
RL Nat. Commun. 10:1242-1242(2019).
RN [15]
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 [16]
RP PRELIMINARY STRUCTURE BY NMR.
RX PubMed=16132835; DOI=10.1007/s10858-005-7941-9;
RA Liu G., Aramini J., Atreya H.S., Eletsky A., Xiao R., Acton T., Ma L.,
RA Montelione G.T., Szyperski T.;
RT "GFT NMR based resonance assignment for the 21 kDa human protein UFC1.";
RL J. Biomol. NMR 32:261-261(2005).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), INTERACTION WITH UBA5, AND
RP MUTAGENESIS OF GLN-30 AND LYS-33.
RX PubMed=17825256; DOI=10.1016/j.bbrc.2007.08.129;
RA Mizushima T., Tatsumi K., Ozaki Y., Kawakami T., Suzuki A., Ogasahara K.,
RA Komatsu M., Kominami E., Tanaka K., Yamane T.;
RT "Crystal structure of Ufc1, the Ufm1-conjugating enzyme.";
RL Biochem. Biophys. Res. Commun. 362:1079-1084(2007).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS), AND STRUCTURE BY NMR.
RX PubMed=19101823; DOI=10.1007/s10969-008-9054-7;
RA Liu G., Forouhar F., Eletsky A., Atreya H.S., Aramini J.M., Xiao R.,
RA Huang Y.J., Abashidze M., Seetharaman J., Liu J., Rost B., Acton T.,
RA Montelione G.T., Hunt J.F., Szyperski T.;
RT "NMR and X-RAY structures of human E2-like ubiquitin-fold modifier
RT conjugating enzyme 1 (UFC1) reveal structural and functional conservation
RT in the metazoan UFM1-UBA5-UFC1 ubiquination pathway.";
RL J. Struct. Funct. Genomics 10:127-136(2009).
CC -!- FUNCTION: E1-like enzyme which specifically catalyzes the second step
CC in ufmylation (PubMed:15071506, PubMed:29868776). Accepts the
CC ubiquitin-like modifier UFM1 from the E1 enzyme UBA5 and forms an
CC intermediate with UFM1 via a thioester linkage (PubMed:15071506,
CC PubMed:29868776). Ufmylation is involved in reticulophagy (also called
CC ER-phagy) induced in response to endoplasmic reticulum stress
CC (PubMed:32160526). {ECO:0000269|PubMed:15071506,
CC ECO:0000269|PubMed:29868776, ECO:0000269|PubMed:32160526}.
CC -!- SUBUNIT: Interacts with UBA5 (via C-terminus) (PubMed:17825256,
CC PubMed:27653677, PubMed:29868776). Interacts with UFL1
CC (PubMed:20018847, PubMed:30886146). Interacts with KIRREL3
CC (PubMed:25902260). Interacts with UFM1 (PubMed:29868776).
CC {ECO:0000269|PubMed:17825256, ECO:0000269|PubMed:20018847,
CC ECO:0000269|PubMed:25902260, ECO:0000269|PubMed:27653677,
CC ECO:0000269|PubMed:29868776, ECO:0000269|PubMed:30886146}.
CC -!- INTERACTION:
CC Q9Y3C8; X5D778: ANKRD11; NbExp=3; IntAct=EBI-1045733, EBI-17183751;
CC Q9Y3C8; P57678: GEMIN4; NbExp=3; IntAct=EBI-1045733, EBI-356700;
CC Q9Y3C8; Q8IZU9: KIRREL3; NbExp=4; IntAct=EBI-1045733, EBI-16427312;
CC Q9Y3C8; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-1045733, EBI-741158;
CC Q9Y3C8; O60260-5: PRKN; NbExp=3; IntAct=EBI-1045733, EBI-21251460;
CC -!- DISEASE: Neurodevelopmental disorder with spasticity and poor growth
CC (NEDSG) [MIM:618076]: An autosomal recessive disorder apparent soon
CC after birth or in early infancy. NEDSG is characterized by axial
CC hypotonia, delayed psychomotor development, poor feeding, failure to
CC thrive, peripheral spasticity with hyperreflexia, poor overall growth,
CC and microcephaly in most patients. Additional variable features include
CC contractures, facial dysmorphisms, and ocular movement abnormalities.
CC {ECO:0000269|PubMed:29868776}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. UFC1
CC subfamily. {ECO:0000305}.
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DR EMBL; AB154405; BAD15374.1; -; mRNA.
DR EMBL; AF151884; AAD34121.1; -; mRNA.
DR EMBL; AF161504; AAF29119.1; -; mRNA.
DR EMBL; AK292776; BAF85465.1; -; mRNA.
DR EMBL; AL590714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52646.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52647.1; -; Genomic_DNA.
DR EMBL; BC005187; AAH05187.1; -; mRNA.
DR CCDS; CCDS1220.1; -.
DR RefSeq; NP_057490.2; NM_016406.3.
DR RefSeq; XP_016856939.1; XM_017001450.1.
DR RefSeq; XP_016856940.1; XM_017001451.1.
DR PDB; 2K07; NMR; -; A=1-167.
DR PDB; 2Z6O; X-ray; 1.60 A; A=1-167.
DR PDB; 2Z6P; X-ray; 1.80 A; A=1-167.
DR PDB; 3EVX; X-ray; 2.54 A; A/B/C/D=1-167.
DR PDB; 7NVJ; X-ray; 2.20 A; AAA=1-167.
DR PDB; 7NVK; X-ray; 2.65 A; AAA=1-167.
DR PDB; 7NW1; X-ray; 1.95 A; AAA/BBB=1-167.
DR PDB; 7OVC; NMR; -; A=1-167.
DR PDBsum; 2K07; -.
DR PDBsum; 2Z6O; -.
DR PDBsum; 2Z6P; -.
DR PDBsum; 3EVX; -.
DR PDBsum; 7NVJ; -.
DR PDBsum; 7NVK; -.
DR PDBsum; 7NW1; -.
DR PDBsum; 7OVC; -.
DR AlphaFoldDB; Q9Y3C8; -.
DR BMRB; Q9Y3C8; -.
DR SMR; Q9Y3C8; -.
DR BioGRID; 119577; 54.
DR IntAct; Q9Y3C8; 9.
DR STRING; 9606.ENSP00000356982; -.
DR GlyGen; Q9Y3C8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y3C8; -.
DR PhosphoSitePlus; Q9Y3C8; -.
DR SwissPalm; Q9Y3C8; -.
DR BioMuta; UFC1; -.
DR DMDM; 116242840; -.
DR EPD; Q9Y3C8; -.
DR jPOST; Q9Y3C8; -.
DR MassIVE; Q9Y3C8; -.
DR MaxQB; Q9Y3C8; -.
DR PaxDb; Q9Y3C8; -.
DR PeptideAtlas; Q9Y3C8; -.
DR PRIDE; Q9Y3C8; -.
DR ProteomicsDB; 86017; -.
DR Antibodypedia; 34296; 221 antibodies from 26 providers.
DR DNASU; 51506; -.
DR Ensembl; ENST00000368003.6; ENSP00000356982.5; ENSG00000143222.12.
DR GeneID; 51506; -.
DR KEGG; hsa:51506; -.
DR MANE-Select; ENST00000368003.6; ENSP00000356982.5; NM_016406.4; NP_057490.2.
DR UCSC; uc001fyd.5; human.
DR CTD; 51506; -.
DR DisGeNET; 51506; -.
DR GeneCards; UFC1; -.
DR HGNC; HGNC:26941; UFC1.
DR HPA; ENSG00000143222; Low tissue specificity.
DR MalaCards; UFC1; -.
DR MIM; 610554; gene.
DR MIM; 618076; phenotype.
DR neXtProt; NX_Q9Y3C8; -.
DR OpenTargets; ENSG00000143222; -.
DR PharmGKB; PA142670644; -.
DR VEuPathDB; HostDB:ENSG00000143222; -.
DR eggNOG; KOG3357; Eukaryota.
DR GeneTree; ENSGT00390000008196; -.
DR HOGENOM; CLU_101170_0_0_1; -.
DR InParanoid; Q9Y3C8; -.
DR OMA; IKYVQNN; -.
DR OrthoDB; 1339876at2759; -.
DR PhylomeDB; Q9Y3C8; -.
DR TreeFam; TF313587; -.
DR PathwayCommons; Q9Y3C8; -.
DR SignaLink; Q9Y3C8; -.
DR BioGRID-ORCS; 51506; 224 hits in 1091 CRISPR screens.
DR ChiTaRS; UFC1; human.
DR EvolutionaryTrace; Q9Y3C8; -.
DR GenomeRNAi; 51506; -.
DR Pharos; Q9Y3C8; Tbio.
DR PRO; PR:Q9Y3C8; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y3C8; protein.
DR Bgee; ENSG00000143222; Expressed in bronchial epithelial cell and 206 other tissues.
DR Genevisible; Q9Y3C8; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0061657; F:UFM1 conjugating enzyme activity; IDA:UniProtKB.
DR GO; GO:0071568; F:UFM1 transferase activity; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR GO; GO:1990592; P:protein K69-linked ufmylation; IDA:UniProtKB.
DR GO; GO:0071569; P:protein ufmylation; IDA:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:MGI.
DR GO; GO:0061709; P:reticulophagy; IMP:UniProtKB.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR014806; Ufc1.
DR PANTHER; PTHR12921; PTHR12921; 1.
DR Pfam; PF08694; UFC1; 1.
DR PIRSF; PIRSF008716; DUF1782; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disease variant; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..167
FT /note="Ubiquitin-fold modifier-conjugating enzyme 1"
FT /id="PRO_0000082613"
FT ACT_SITE 116
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000269|PubMed:15071506,
FT ECO:0000269|PubMed:29868776"
FT VARIANT 23
FT /note="R -> Q (in NEDSG; decreased ability to form
FT thioester bond with UFM1; decreased protein ufmylation;
FT dbSNP:rs1181612302)"
FT /evidence="ECO:0000269|PubMed:29868776"
FT /id="VAR_081216"
FT VARIANT 90
FT /note="Y -> C (in dbSNP:rs17849932)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_028312"
FT VARIANT 106
FT /note="T -> I (in NEDSG; decreased ability to form
FT thioester bond with UFM1; decreased protein ufmylation;
FT dbSNP:rs1553232770)"
FT /evidence="ECO:0000269|PubMed:29868776"
FT /id="VAR_081217"
FT MUTAGEN 30
FT /note="Q->A: Does not affect neither UBA5-binding nor
FT thioester formation with UFM1."
FT /evidence="ECO:0000269|PubMed:17825256"
FT MUTAGEN 33
FT /note="K->A: Impairs binding to UBA5 and thioester
FT formation with UFM1."
FT /evidence="ECO:0000269|PubMed:17825256"
FT MUTAGEN 116
FT /note="C->S: Instead of the formation of an intermediate
FT complex with a thiol ester bond between UFC1 (E2-like
FT enzyme) and UFM1 (substrate), a stable complex with an O-
FT ester bond is formed."
FT /evidence="ECO:0000269|PubMed:15071506,
FT ECO:0000269|PubMed:29868776"
FT CONFLICT 159
FT /note="I -> N (in Ref. 4; BAF85465)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="Q -> H (in Ref. 1; BAD15374 and 3; AAF29119)"
FT /evidence="ECO:0000305"
FT HELIX 2..10
FT /evidence="ECO:0007829|PDB:2Z6O"
FT HELIX 26..48
FT /evidence="ECO:0007829|PDB:2Z6O"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:2Z6O"
FT STRAND 64..73
FT /evidence="ECO:0007829|PDB:2Z6O"
FT STRAND 76..85
FT /evidence="ECO:0007829|PDB:2Z6O"
FT TURN 88..92
FT /evidence="ECO:0007829|PDB:2Z6O"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:2Z6O"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:2Z6O"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:2Z6O"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:2Z6O"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:2Z6O"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:2Z6O"
FT HELIX 142..156
FT /evidence="ECO:0007829|PDB:2Z6O"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:2Z6O"
SQ SEQUENCE 167 AA; 19458 MW; 1675D9187DC43E14 CRC64;
MADEATRRVV SEIPVLKTNA GPRDRELWVQ RLKEEYQSLI RYVENNKNAD NDWFRLESNK
EGTRWFGKCW YIHDLLKYEF DIEFDIPITY PTTAPEIAVP ELDGKTAKMY RGGKICLTDH
FKPLWARNVP KFGLAHLMAL GLGPWLAVEI PDLIQKGVIQ HKEKCNQ
