UBA5_HUMAN
ID UBA5_HUMAN Reviewed; 404 AA.
AC Q9GZZ9; A6NJL3; D3DNC8; Q96ST1;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme 5 {ECO:0000305};
DE Short=Ubiquitin-activating enzyme 5 {ECO:0000303|PubMed:15071506};
DE AltName: Full=ThiFP1 {ECO:0000303|PubMed:16328888};
DE AltName: Full=UFM1-activating enzyme {ECO:0000303|PubMed:15071506};
DE AltName: Full=Ubiquitin-activating enzyme E1 domain-containing protein 1 {ECO:0000303|PubMed:16328888};
GN Name=UBA5 {ECO:0000303|PubMed:15071506, ECO:0000312|HGNC:HGNC:23230};
GN Synonyms=UBE1DC1 {ECO:0000303|PubMed:16328888};
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, AND MUTAGENESIS OF
RP CYS-250.
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=16328888; DOI=10.1007/s11033-005-4822-y;
RA Dou T., Gu S., Liu J., Chen F., Zeng L., Guo L., Xie Y., Mao Y.;
RT "Isolation and characterization of ubiquitin-activating enzyme E1-domain
RT containing 1, UBE1DC1.";
RL Mol. Biol. Rep. 32:265-271(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon, and Teratocarcinoma;
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=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(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].
RC TISSUE=Lung;
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 UFC1.
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 [9]
RP FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), AND SUBCELLULAR
RP LOCATION.
RX PubMed=18442052; DOI=10.1002/jcb.21791;
RA Zheng M., Gu X., Zheng D., Yang Z., Li F., Zhao J., Xie Y., Ji C., Mao Y.;
RT "UBE1DC1, an ubiquitin-activating enzyme, activates two different
RT ubiquitin-like proteins.";
RL J. Cell. Biochem. 104:2324-2334(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP FUNCTION.
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 [16]
RP INTERACTION WITH UFC1, AND MUTAGENESIS OF CYS-250.
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 [17]
RP FUNCTION, SUBUNIT, INTERACTION WITH UFM1, AND MUTAGENESIS OF ASP-290.
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 [18]
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 [19] {ECO:0007744|PDB:3GUC, ECO:0007744|PDB:3H8V}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 57-329 IN COMPLEX WITH ATP AND
RP ZINC, FUNCTION, AND ACTIVE SITE.
RX PubMed=20368332; DOI=10.1074/jbc.m110.102921;
RA Bacik J.P., Walker J.R., Ali M., Schimmer A.D., Dhe-Paganon S.;
RT "Crystal structure of the human ubiquitin-activating enzyme 5 (UBA5) bound
RT to ATP: mechanistic insights into a minimalistic E1 enzyme.";
RL J. Biol. Chem. 285:20273-20280(2010).
RN [20] {ECO:0007744|PDB:5IAA, ECO:0007744|PDB:5L95}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 57-346 IN COMPLEX WITH UFM1; AMP
RP AND ZINC, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, INTERACTION WITH UFM1 AND
RP UFC1, AND MUTAGENESIS OF ARG-188; 215-HIS--GLN-217; 230-ALA--LEU-233;
RP CYS-250; LYS-271 AND ASP-290.
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 [21] {ECO:0007744|PDB:5HKH}
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 338-346 IN COMPLEX WITH UFM1,
RP FUNCTION, INTERACTION WITH UFM1; GABARAPL2; GABARAP AND GABARAPL1, DOMAIN,
RP AND MUTAGENESIS OF TRP-341; GLY-342; ILE-343; LEU-345 AND VAL-346.
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 [22] {ECO:0007744|PDB:5IA8}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 334-346 AND 350-350 IN COMPLEX
RP WITH UFM1, INTERACTION WITH UFM1, AND MUTAGENESIS OF HIS-336 AND
RP 343-ILE--LEU-345.
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 [23] {ECO:0007744|PDB:6H8C}
RP STRUCTURE BY NMR OF 333-348 IN COMPLEX WITH GABARAPL2, INTERACTION WITH
RP GABARAPL2, AND MUTAGENESIS OF TRP-341; ILE-343; LEU-345 AND VAL-346.
RX PubMed=30990354; DOI=10.1080/15548627.2019.1606637;
RA Huber J., Obata M., Gruber J., Akutsu M., Lohr F., Rogova N., Guntert P.,
RA Dikic I., Kirkin V., Komatsu M., Dotsch V., Rogov V.V.;
RT "An atypical LIR motif within UBA5 (ubiquitin like modifier activating
RT enzyme 5) interacts with GABARAP proteins and mediates membrane
RT localization of UBA5.";
RL Autophagy 16:256-270(2020).
RN [24] {ECO:0007744|PDB:6H77, ECO:0007744|PDB:6H78}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 36-346 IN COMPLEX WITH UFM1; AMP
RP AND ZINC, FUNCTION, AND INTERACTION WITH UFM1.
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 [25]
RP VARIANTS DEE44 VAL-57; GLU-168; MET-260; THR-371 AND TYR-389,
RP CHARACTERIZATION OF VARIANTS DEE44 VAL-57; GLU-168; MET-260; THR-371 AND
RP TYR-389, FUNCTION, AND INVOLVEMENT IN DEE44.
RX PubMed=27545681; DOI=10.1016/j.ajhg.2016.06.030;
RG FREX Consortium;
RA Colin E., Daniel J., Ziegler A., Wakim J., Scrivo A., Haack T.B.,
RA Khiati S., Denomme A.S., Amati-Bonneau P., Charif M., Procaccio V.,
RA Reynier P., Aleck K.A., Botto L.D., Herper C.L., Kaiser C.S., Nabbout R.,
RA N'Guyen S., Mora-Lorca J.A., Assmann B., Christ S., Meitinger T.,
RA Strom T.M., Prokisch H., Miranda-Vizuete A., Hoffmann G.F., Lenaers G.,
RA Bomont P., Liebau E., Bonneau D.;
RT "Biallelic variants in UBA5 reveal that disruption of the UFM1 cascade can
RT result in early-onset encephalopathy.";
RL Am. J. Hum. Genet. 99:695-703(2016).
RN [26]
RP VARIANTS SCAR24 GLU-310 AND ARG-246--MET-404, CHARACTERIZATION OF VARIANTS
RP SCAR24 GLU-310 AND ARG-246--MET-404, INTERACTION WITH UFM1, SUBCELLULAR
RP LOCATION, AND INVOLVEMENT IN SCAR24.
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 [27]
RP VARIANTS DEE44 HIS-55 AND THR-371, CHARACTERIZATION OF VARIANTS DEE44
RP HIS-55 AND THR-371, MUTAGENESIS OF CYS-250, AND FUNCTION.
RX PubMed=27545674; DOI=10.1016/j.ajhg.2016.06.020;
RG DDD Study;
RA Muona M., Ishimura R., Laari A., Ichimura Y., Linnankivi T.,
RA Keski-Filppula R., Herva R., Rantala H., Paetau A., Poeyhoenen M.,
RA Obata M., Uemura T., Karhu T., Bizen N., Takebayashi H., McKee S.,
RA Parker M.J., Akawi N., McRae J., Hurles M.E., Kuismin O., Kurki M.I.,
RA Anttonen A.K., Tanaka K., Palotie A., Waguri S., Lehesjoki A.E.,
RA Komatsu M.;
RT "Biallelic variants in UBA5 link dysfunctional UFM1 ubiquitin-like modifier
RT pathway to severe infantile-onset encephalopathy.";
RL Am. J. Hum. Genet. 99:683-694(2016).
CC -!- FUNCTION: E1-like enzyme which specifically catalyzes the first step in
CC ufmylation (PubMed:15071506, PubMed:18442052, PubMed:25219498,
CC PubMed:20368332, PubMed:27653677, PubMed:26929408, PubMed:27545674,
CC PubMed:30412706, PubMed:27545681). Activates UFM1 by first adenylating
CC its C-terminal glycine residue with ATP, and thereafter linking this
CC residue to the side chain of a cysteine residue in E1, yielding a UFM1-
CC E1 thioester and free AMP (PubMed:20368332, PubMed:27653677,
CC PubMed:26929408, PubMed:30412706). Activates UFM1 via a trans-binding
CC mechanism, in which UFM1 interacts with distinct sites in both subunits
CC of the UBA5 homodimer (PubMed:27653677). Trans-binding also promotes
CC stabilization of the UBA5 homodimer, and enhances ATP-binding
CC (PubMed:29295865). Transfer of UFM1 from UBA5 to the E2-like enzyme
CC UFC1 also takes place using a trans mechanism (PubMed:27653677).
CC Ufmylation is involved in reticulophagy (also called ER-phagy) induced
CC in response to endoplasmic reticulum stress (PubMed:32160526).
CC Ufmylation is essential for erythroid differentiation of both
CC megakaryocytes and erythrocytes (By similarity).
CC {ECO:0000250|UniProtKB:Q8VE47, ECO:0000269|PubMed:15071506,
CC ECO:0000269|PubMed:18442052, ECO:0000269|PubMed:20368332,
CC ECO:0000269|PubMed:25219498, ECO:0000269|PubMed:26929408,
CC ECO:0000269|PubMed:27545674, ECO:0000269|PubMed:27545681,
CC ECO:0000269|PubMed:27653677, ECO:0000269|PubMed:29295865,
CC ECO:0000269|PubMed:30412706, ECO:0000269|PubMed:32160526}.
CC -!- SUBUNIT: Homodimer; homodimerization is required for UFM1 activation
CC (PubMed:29295865, PubMed:27653677). Interacts (via UIS motif) with
CC UFM1; binds UFM1 via a trans-binding mechanism in which UFM1 interacts
CC with distinct sites in both subunits of the UBA5 homodimer
CC (PubMed:29295865, PubMed:27653677, PubMed:26929408, PubMed:28360427,
CC PubMed:30412706, PubMed:26872069). Interacts (via UIS motif) with
CC GABARAPL2 and, with lower affinity, with GABARAP and GABARAPL1
CC (PubMed:26929408, PubMed:30990354). Interacts (via C-terminus) with
CC UFC1 (PubMed:17825256, PubMed:29868776, PubMed:27653677).
CC {ECO:0000269|PubMed:17825256, 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 ECO:0000269|PubMed:30990354}.
CC -!- INTERACTION:
CC Q9GZZ9; O95166: GABARAP; NbExp=2; IntAct=EBI-747805, EBI-712001;
CC Q9GZZ9; Q9H0R8: GABARAPL1; NbExp=2; IntAct=EBI-747805, EBI-746969;
CC Q9GZZ9; P60520: GABARAPL2; NbExp=17; IntAct=EBI-747805, EBI-720116;
CC Q9GZZ9; Q9GZQ8: MAP1LC3B; NbExp=2; IntAct=EBI-747805, EBI-373144;
CC Q9GZZ9; Q9BXW4: MAP1LC3C; NbExp=2; IntAct=EBI-747805, EBI-2603996;
CC Q9GZZ9; P61960: UFM1; NbExp=4; IntAct=EBI-747805, EBI-1045061;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18442052,
CC ECO:0000269|PubMed:26872069}. Nucleus {ECO:0000269|PubMed:18442052}.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:30990354}. Golgi
CC apparatus {ECO:0000269|PubMed:26872069}. Note=Localizes mainly in the
CC cytoplasm, while it localizes to the nucleus in presence of SUMO2
CC (PubMed:18442052). Interaction with GABARAPL2 promotes localization to
CC the endoplasmic reticulum membrane (PubMed:30990354).
CC {ECO:0000269|PubMed:18442052, ECO:0000269|PubMed:30990354}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=UBE1DC1A {ECO:0000303|PubMed:18442052};
CC IsoId=Q9GZZ9-1; Sequence=Displayed;
CC Name=2; Synonyms=UBE1DC1B {ECO:0000303|PubMed:18442052};
CC IsoId=Q9GZZ9-2; Sequence=VSP_038528;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16328888}.
CC -!- DOMAIN: The UFM1-interacting sequence (UIS) motif mediates interaction
CC with both UFM1 and LC3/GABARAP proteins (GABARAP, GABARAPL1 and
CC GABARAPL2). {ECO:0000269|PubMed:26929408}.
CC -!- DOMAIN: [Isoform 1]: The N-terminus (1-56) contributes to the transfer
CC of UFM1 from UBA5 to UFC1. {ECO:0000269|PubMed:30412706}.
CC -!- DISEASE: Developmental and epileptic encephalopathy 44 (DEE44)
CC [MIM:617132]: A form of epileptic encephalopathy, a heterogeneous group
CC of severe early-onset epilepsies characterized by refractory seizures,
CC neurodevelopmental impairment, and poor prognosis. Development is
CC normal prior to seizure onset, after which cognitive and motor delays
CC become apparent. DEE44 transmission pattern is consistent with
CC autosomal recessive inheritance. {ECO:0000269|PubMed:27545674,
CC ECO:0000269|PubMed:27545681}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Spinocerebellar ataxia, autosomal recessive, 24 (SCAR24)
CC [MIM:617133]: A form of spinocerebellar ataxia, a clinically and
CC genetically heterogeneous group of cerebellar disorders due to
CC degeneration of the cerebellum with variable involvement of the
CC brainstem and spinal cord. SCAR24 patients manifest gait instability
CC and speech difficulties with onset in childhood. Clinical features
CC include gait and limb ataxia, dysarthria, nystagmus, cataracts, and
CC cerebellar atrophy on brain imaging. {ECO:0000269|PubMed:26872069}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA5
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Was initially reported to mediate activation of SUMO2 in
CC addition to UFM1 (PubMed:18442052). However, it was later shown that it
CC is specific for UFM1 (By similarity). {ECO:0000250|UniProtKB:Q8VE47,
CC ECO:0000269|PubMed:18442052}.
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DR EMBL; AB154406; BAD15375.1; -; mRNA.
DR EMBL; AY253672; AAP79600.1; -; mRNA.
DR EMBL; AL136757; CAB66691.1; -; mRNA.
DR EMBL; AK026904; BAB15587.1; -; mRNA.
DR EMBL; AK027563; BAB55199.1; -; mRNA.
DR EMBL; AC020632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79192.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79189.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79191.1; -; Genomic_DNA.
DR EMBL; BC009737; AAH09737.1; -; mRNA.
DR CCDS; CCDS3076.1; -. [Q9GZZ9-1]
DR CCDS; CCDS3077.1; -. [Q9GZZ9-2]
DR RefSeq; NP_001307139.1; NM_001320210.1. [Q9GZZ9-2]
DR RefSeq; NP_001308167.1; NM_001321238.1.
DR RefSeq; NP_001308168.1; NM_001321239.1.
DR RefSeq; NP_079094.1; NM_024818.4. [Q9GZZ9-1]
DR RefSeq; NP_938143.1; NM_198329.3. [Q9GZZ9-2]
DR PDB; 3GUC; X-ray; 2.25 A; A/B=57-329.
DR PDB; 3H8V; X-ray; 2.00 A; A/B=57-329.
DR PDB; 5HKH; X-ray; 2.55 A; B=338-346.
DR PDB; 5IA8; X-ray; 2.00 A; A/B=334-346, A/B=349-374.
DR PDB; 5IAA; X-ray; 1.85 A; A/B=57-346.
DR PDB; 5L95; X-ray; 2.10 A; A/B=68-346.
DR PDB; 6H77; X-ray; 2.10 A; A/B/C/D=36-346.
DR PDB; 6H78; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=36-335.
DR PDB; 6H8C; NMR; -; B=333-348.
DR PDB; 7NVK; X-ray; 2.65 A; AAA=347-404.
DR PDB; 7NW1; X-ray; 1.95 A; CCC/FFF=389-404.
DR PDB; 7OVC; NMR; -; B=381-404.
DR PDBsum; 3GUC; -.
DR PDBsum; 3H8V; -.
DR PDBsum; 5HKH; -.
DR PDBsum; 5IA8; -.
DR PDBsum; 5IAA; -.
DR PDBsum; 5L95; -.
DR PDBsum; 6H77; -.
DR PDBsum; 6H78; -.
DR PDBsum; 6H8C; -.
DR PDBsum; 7NVK; -.
DR PDBsum; 7NW1; -.
DR PDBsum; 7OVC; -.
DR AlphaFoldDB; Q9GZZ9; -.
DR SASBDB; Q9GZZ9; -.
DR SMR; Q9GZZ9; -.
DR BioGRID; 122964; 116.
DR ELM; Q9GZZ9; -.
DR IntAct; Q9GZZ9; 68.
DR MINT; Q9GZZ9; -.
DR STRING; 9606.ENSP00000348565; -.
DR ChEMBL; CHEMBL2016429; -.
DR GlyGen; Q9GZZ9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9GZZ9; -.
DR MetOSite; Q9GZZ9; -.
DR PhosphoSitePlus; Q9GZZ9; -.
DR SwissPalm; Q9GZZ9; -.
DR BioMuta; UBA5; -.
DR DMDM; 74733510; -.
DR EPD; Q9GZZ9; -.
DR jPOST; Q9GZZ9; -.
DR MassIVE; Q9GZZ9; -.
DR MaxQB; Q9GZZ9; -.
DR PaxDb; Q9GZZ9; -.
DR PeptideAtlas; Q9GZZ9; -.
DR PRIDE; Q9GZZ9; -.
DR ProteomicsDB; 80189; -. [Q9GZZ9-1]
DR ProteomicsDB; 80190; -. [Q9GZZ9-2]
DR Antibodypedia; 2258; 169 antibodies from 29 providers.
DR DNASU; 79876; -.
DR Ensembl; ENST00000264991.8; ENSP00000264991.4; ENSG00000081307.15. [Q9GZZ9-2]
DR Ensembl; ENST00000356232.10; ENSP00000348565.4; ENSG00000081307.15. [Q9GZZ9-1]
DR Ensembl; ENST00000494238.6; ENSP00000418807.2; ENSG00000081307.15. [Q9GZZ9-2]
DR GeneID; 79876; -.
DR KEGG; hsa:79876; -.
DR MANE-Select; ENST00000356232.10; ENSP00000348565.4; NM_024818.6; NP_079094.1.
DR UCSC; uc003epa.5; human. [Q9GZZ9-1]
DR CTD; 79876; -.
DR DisGeNET; 79876; -.
DR GeneCards; UBA5; -.
DR HGNC; HGNC:23230; UBA5.
DR HPA; ENSG00000081307; Low tissue specificity.
DR MalaCards; UBA5; -.
DR MIM; 610552; gene.
DR MIM; 617132; phenotype.
DR MIM; 617133; phenotype.
DR neXtProt; NX_Q9GZZ9; -.
DR OpenTargets; ENSG00000081307; -.
DR Orphanet; 442835; Non-specific early-onset epileptic encephalopathy.
DR PharmGKB; PA162407661; -.
DR VEuPathDB; HostDB:ENSG00000081307; -.
DR eggNOG; KOG2336; Eukaryota.
DR GeneTree; ENSGT00940000156177; -.
DR InParanoid; Q9GZZ9; -.
DR OMA; FTPDQAG; -.
DR OrthoDB; 1092362at2759; -.
DR PhylomeDB; Q9GZZ9; -.
DR TreeFam; TF314168; -.
DR BRENDA; 6.2.1.45; 2681.
DR PathwayCommons; Q9GZZ9; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9GZZ9; -.
DR BioGRID-ORCS; 79876; 448 hits in 1098 CRISPR screens.
DR ChiTaRS; UBA5; human.
DR EvolutionaryTrace; Q9GZZ9; -.
DR GeneWiki; UBE1DC1; -.
DR GenomeRNAi; 79876; -.
DR Pharos; Q9GZZ9; Tbio.
DR PRO; PR:Q9GZZ9; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9GZZ9; protein.
DR Bgee; ENSG00000081307; Expressed in body of pancreas and 194 other tissues.
DR ExpressionAtlas; Q9GZZ9; baseline and differential.
DR Genevisible; Q9GZZ9; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0071566; F:UFM1 activating enzyme activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0030218; P:erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0030219; P:megakaryocyte differentiation; ISS:UniProtKB.
DR GO; GO:0050905; P:neuromuscular process; IGI:UniProtKB.
DR GO; GO:1990592; P:protein K69-linked ufmylation; IDA:UniProtKB.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0071569; P:protein ufmylation; IDA:UniProtKB.
DR GO; GO:0033146; P:regulation of intracellular estrogen receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:MGI.
DR GO; GO:0061709; P:reticulophagy; IMP:UniProtKB.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cytoplasm;
KW Disease variant; Endoplasmic reticulum; Epilepsy; Golgi apparatus;
KW Intellectual disability; Membrane; Metal-binding; Neurodegeneration;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway; Zinc.
FT CHAIN 1..404
FT /note="Ubiquitin-like modifier-activating enzyme 5"
FT /id="PRO_0000194970"
FT MOTIF 334..346
FT /note="UFM1-interacting sequence (UIS)"
FT /evidence="ECO:0000269|PubMed:26929408,
FT ECO:0000269|PubMed:27653677"
FT ACT_SITE 250
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000269|PubMed:20368332,
FT ECO:0000269|PubMed:27545674, ECO:0000269|PubMed:27653677"
FT BINDING 83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:20368332,
FT ECO:0000269|PubMed:27653677, ECO:0000269|PubMed:30412706,
FT ECO:0007744|PDB:5L95, ECO:0007744|PDB:6H77,
FT ECO:0007744|PDB:6H78"
FT BINDING 104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:20368332,
FT ECO:0000269|PubMed:27653677, ECO:0000269|PubMed:30412706,
FT ECO:0007744|PDB:5L95, ECO:0007744|PDB:6H78"
FT BINDING 127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:20368332,
FT ECO:0000269|PubMed:27653677, ECO:0000269|PubMed:30412706,
FT ECO:0007744|PDB:5L95, ECO:0007744|PDB:6H77,
FT ECO:0007744|PDB:6H78"
FT BINDING 150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:20368332,
FT ECO:0000269|PubMed:27653677, ECO:0000269|PubMed:30412706,
FT ECO:0007744|PDB:5L95, ECO:0007744|PDB:6H77,
FT ECO:0007744|PDB:6H78"
FT BINDING 184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:20368332,
FT ECO:0000269|PubMed:27653677, ECO:0000269|PubMed:30412706,
FT ECO:0007744|PDB:5L95, ECO:0007744|PDB:6H77,
FT ECO:0007744|PDB:6H78"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:20368332,
FT ECO:0000269|PubMed:27653677, ECO:0000269|PubMed:30412706,
FT ECO:0007744|PDB:5IAA, ECO:0007744|PDB:5L95,
FT ECO:0007744|PDB:6H77, ECO:0007744|PDB:6H78"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:20368332,
FT ECO:0000269|PubMed:27653677, ECO:0000269|PubMed:30412706,
FT ECO:0007744|PDB:5IAA, ECO:0007744|PDB:5L95,
FT ECO:0007744|PDB:6H77, ECO:0007744|PDB:6H78"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:20368332,
FT ECO:0000269|PubMed:27653677, ECO:0000269|PubMed:30412706,
FT ECO:0007744|PDB:5IAA, ECO:0007744|PDB:5L95,
FT ECO:0007744|PDB:6H77, ECO:0007744|PDB:6H78"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:20368332,
FT ECO:0000269|PubMed:27653677, ECO:0000269|PubMed:30412706,
FT ECO:0007744|PDB:5IAA, ECO:0007744|PDB:5L95,
FT ECO:0007744|PDB:6H77, ECO:0007744|PDB:6H78"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VE47"
FT VAR_SEQ 1..56
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038528"
FT VARIANT 55
FT /note="R -> H (in DEE44; reduces UFM1 activating enzyme
FT activity; dbSNP:rs774318611)"
FT /evidence="ECO:0000269|PubMed:27545674"
FT /id="VAR_077153"
FT VARIANT 57
FT /note="M -> V (in DEE44; reduces UFM1 activating enzyme
FT activity; reduces UFM1-DDRGK1 formation;
FT dbSNP:rs532178791)"
FT /evidence="ECO:0000269|PubMed:27545681"
FT /id="VAR_077154"
FT VARIANT 168
FT /note="G -> E (in DEE44; abolishes UFM1 activating enzyme
FT activity; dbSNP:rs886039761)"
FT /evidence="ECO:0000269|PubMed:27545681"
FT /id="VAR_077155"
FT VARIANT 246..404
FT /note="Missing (in SCAR24; delocalizes protein to the
FT nucleus; activates degradation through the ubiquitin
FT proteasome pathway; decreases protein stability; disrupts
FT interaction with UFM1)"
FT /id="VAR_080409"
FT VARIANT 260
FT /note="V -> M (in DEE44; reduces UFM1 activating enzyme
FT activity; dbSNP:rs886039759)"
FT /evidence="ECO:0000269|PubMed:27545681"
FT /id="VAR_077156"
FT VARIANT 310
FT /note="K -> E (in SCAR24; does not affect cytoplasm
FT localization; decreases protein stability; does not affect
FT interaction with UFM1; dbSNP:rs886039762)"
FT /evidence="ECO:0000269|PubMed:26872069"
FT /id="VAR_077157"
FT VARIANT 371
FT /note="A -> T (in DEE44; reduces UFM1 activating enzyme
FT activity; reduces UFM1 activating enzyme activity; reduces
FT UFM1-DDRGK1 formation; dbSNP:rs114925667)"
FT /evidence="ECO:0000269|PubMed:27545674,
FT ECO:0000269|PubMed:27545681"
FT /id="VAR_077158"
FT VARIANT 389
FT /note="D -> Y (in DEE44; no effect on UFM1 activating
FT enzyme activity; dbSNP:rs886039760)"
FT /evidence="ECO:0000269|PubMed:27545681"
FT /id="VAR_077159"
FT MUTAGEN 188
FT /note="R->A: Abolished ability to activate UFM1."
FT /evidence="ECO:0000269|PubMed:27653677"
FT MUTAGEN 215..217
FT /note="HIQ->AQA: Abolished ability to activate UFM1."
FT /evidence="ECO:0000269|PubMed:27653677"
FT MUTAGEN 230..233
FT /note="APPL->RPPA,FPPA: Abolished interaction with UFM1."
FT /evidence="ECO:0000269|PubMed:27653677"
FT MUTAGEN 250
FT /note="C->A: Abolished ability to activate UFM1."
FT /evidence="ECO:0000269|PubMed:27653677"
FT MUTAGEN 250
FT /note="C->S: Forms a stable intermediate complex."
FT /evidence="ECO:0000269|PubMed:15071506,
FT ECO:0000269|PubMed:27545674, ECO:0000269|PubMed:29868776"
FT MUTAGEN 271
FT /note="K->D: Impaired ability to activate UFM1 via a trans-
FT binding mechanism."
FT /evidence="ECO:0000269|PubMed:27653677"
FT MUTAGEN 290
FT /note="D->K: Impaired homodimerization and ability to
FT activate UFM1 via a trans-binding mechanism."
FT /evidence="ECO:0000269|PubMed:27653677,
FT ECO:0000269|PubMed:29295865"
FT MUTAGEN 336
FT /note="H->A,D: Impaired ability to activate UFM1."
FT /evidence="ECO:0000269|PubMed:28360427"
FT MUTAGEN 341
FT /note="W->A: Abolished interaction with UFM1 and
FT GABARAPL2."
FT /evidence="ECO:0000269|PubMed:26929408,
FT ECO:0000269|PubMed:30990354"
FT MUTAGEN 342
FT /note="G->A: Decreased interaction with UFM1 without
FT affecting interaction with GABARAPL2."
FT /evidence="ECO:0000269|PubMed:26929408"
FT MUTAGEN 343..345
FT /note="IEL->AEA: Impaired ability to activate UFM1."
FT /evidence="ECO:0000269|PubMed:28360427"
FT MUTAGEN 343
FT /note="I->A: Abolished interaction with UFM1 and decreased
FT interaction with GABARAPL2."
FT /evidence="ECO:0000269|PubMed:26929408,
FT ECO:0000269|PubMed:30990354"
FT MUTAGEN 345
FT /note="L->A: Abolished interaction with UFM1 and decreased
FT interaction with GABARAPL2."
FT /evidence="ECO:0000269|PubMed:26929408,
FT ECO:0000269|PubMed:30990354"
FT MUTAGEN 346
FT /note="V->A: Abolished interaction with UFM1 and decreased
FT interaction with GABARAPL2."
FT /evidence="ECO:0000269|PubMed:26929408,
FT ECO:0000269|PubMed:30990354"
FT CONFLICT 403
FT /note="N -> S (in Ref. 4; BAB55199)"
FT /evidence="ECO:0000305"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:6H77"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:3H8V"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:3H8V"
FT HELIX 83..95
FT /evidence="ECO:0007829|PDB:3H8V"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:3H8V"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:6H77"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:6H77"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:6H77"
FT HELIX 127..138
FT /evidence="ECO:0007829|PDB:3H8V"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:3H8V"
FT HELIX 154..166
FT /evidence="ECO:0007829|PDB:3H8V"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:3H8V"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:3H8V"
FT HELIX 185..198
FT /evidence="ECO:0007829|PDB:3H8V"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:3H8V"
FT STRAND 211..219
FT /evidence="ECO:0007829|PDB:3H8V"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:3H8V"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:3H8V"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:6H77"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:6H77"
FT HELIX 247..274
FT /evidence="ECO:0007829|PDB:3H8V"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:3H8V"
FT TURN 287..290
FT /evidence="ECO:0007829|PDB:3H8V"
FT HELIX 306..317
FT /evidence="ECO:0007829|PDB:3H8V"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:6H8C"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:7OVC"
FT HELIX 394..404
FT /evidence="ECO:0007829|PDB:7OVC"
SQ SEQUENCE 404 AA; 44863 MW; 02F0F64FEAA1E880 CRC64;
MAESVERLQQ RVQELERELA QERSLQVPRS GDGGGGRVRI EKMSSEVVDS NPYSRLMALK
RMGIVSDYEK IRTFAVAIVG VGGVGSVTAE MLTRCGIGKL LLFDYDKVEL ANMNRLFFQP
HQAGLSKVQA AEHTLRNINP DVLFEVHNYN ITTVENFQHF MDRISNGGLE EGKPVDLVLS
CVDNFEARMT INTACNELGQ TWMESGVSEN AVSGHIQLII PGESACFACA PPLVVAANID
EKTLKREGVC AASLPTTMGV VAGILVQNVL KFLLNFGTVS FYLGYNAMQD FFPTMSMKPN
PQCDDRNCRK QQEEYKKKVA ALPKQEVIQE EEEIIHEDNE WGIELVSEVS EEELKNFSGP
VPDLPEGITV AYTIPKKQED SVTELTVEDS GESLEDLMAK MKNM
