GenomeNet

Database: UniProt
Entry: Q9GZZ9
LinkDB: Q9GZZ9
Original site: Q9GZZ9 
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   13-FEB-2019, entry version 168.
DE   RecName: Full=Ubiquitin-like modifier-activating enzyme 5;
DE            Short=Ubiquitin-activating enzyme 5;
DE   AltName: Full=ThiFP1;
DE   AltName: Full=UFM1-activating enzyme;
DE   AltName: Full=Ubiquitin-activating enzyme E1 domain-containing protein 1;
GN   Name=UBA5; Synonyms=UBE1DC1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAD15375.1}
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
RT   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-
RT   domain containing 1, UBE1DC1.";
RL   Mol. Biol. Rep. 32:265-271(2005).
RN   [3] {ECO:0000312|EMBL:CAB66691.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Testis {ECO:0000312|EMBL:CAB66691.1};
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.,
RA   Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA   Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA   Wambutt R., Korn B., Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and
RT   analysis of 500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [4] {ECO:0000312|EMBL:BAB15587.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon {ECO:0000312|EMBL:BAB15587.1}, and
RC   Teratocarcinoma {ECO:0000312|EMBL:BAB55199.1};
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA   Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA   Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA   Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA   Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA   Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA   Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA   Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA   Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA   Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA   Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA   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.,
RA   Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA   Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA   Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [6] {ECO:0000312|EMBL:AAP79600.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000312|EMBL:AAH09737.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung {ECO:0000312|EMBL:AAH09737.1};
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
RT   project: 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.,
RA   Ogasahara K., 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.,
RA   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
RP   BY 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
RP   BY 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.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation 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.,
RA   Buerckstuemmer T., 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
RP   BY 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   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 57-329 IN COMPLEX WITH ATP
RP   AND 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)
RT   bound to ATP: mechanistic insights into a minimalistic E1 enzyme.";
RL   J. Biol. Chem. 285:20273-20280(2010).
RN   [16]
RP   INVOLVEMENT IN EIEE44, VARIANTS EIEE44 VAL-57; GLU-168; MET-260;
RP   THR-371 AND TYR-389, CHARACTERIZATION OF VARIANTS EIEE44 VAL-57;
RP   GLU-168; MET-260; THR-371 AND TYR-389, AND FUNCTION.
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.,
RA   Nabbout R., N'Guyen S., Mora-Lorca J.A., Assmann B., Christ S.,
RA   Meitinger T., Strom T.M., Prokisch H., Miranda-Vizuete A.,
RA   Hoffmann G.F., Lenaers G., Bomont P., Liebau E., Bonneau D.;
RT   "Biallelic variants in UBA5 reveal that disruption of the UFM1 cascade
RT   can result in early-onset encephalopathy.";
RL   Am. J. Hum. Genet. 99:695-703(2016).
RN   [17]
RP   INTERACTION WITH UFM1, SUBCELLULAR LOCATION, INVOLVEMENT IN SCAR24,
RP   VARIANTS SCAR24 GLU-310 AND ARG-246--MET-404, AND CHARACTERIZATION OF
RP   VARIANTS SCAR24 GLU-310 AND ARG-246--MET-404.
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.,
RA   Shen L., 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   [18]
RP   INVOLVEMENT IN EIEE44, VARIANTS EIEE44 HIS-55 AND THR-371,
RP   CHARACTERIZATION OF VARIANTS EIEE44 HIS-55 AND THR-371, MUTAGENESIS OF
RP   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
RT   modifier pathway to severe infantile-onset encephalopathy.";
RL   Am. J. Hum. Genet. 99:683-694(2016).
RN   [19]
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.,
RA   Monies D., Abouelhoda M., Meyer B.F., Alfadhel M., Eyaid W.,
RA   Zweier M., Steindl K., Rauch A., Arold S.T., Woods C.G., Komatsu M.,
RA   Alkuraya F.S.;
RT   "Biallelic UFM1 and UFC1 mutations expand the essential role of
RT   ufmylation in brain development.";
RL   Brain 141:1934-1945(2018).
CC   -!- FUNCTION: E1-like enzyme which activates UFM1 and SUMO2.
CC       {ECO:0000269|PubMed:15071506, ECO:0000269|PubMed:18442052,
CC       ECO:0000269|PubMed:20368332, ECO:0000269|PubMed:27545674,
CC       ECO:0000269|PubMed:27545681}.
CC   -!- SUBUNIT: Interacts (via C-terminus) with UFC1 (PubMed:17825256,
CC       PubMed:29868776). Interacts with UFM1.
CC       {ECO:0000269|PubMed:17825256, ECO:0000269|PubMed:26872069,
CC       ECO:0000269|PubMed:29868776}.
CC   -!- INTERACTION:
CC       O95166:GABARAP; NbExp=2; IntAct=EBI-747805, EBI-712001;
CC       Q9H0R8:GABARAPL1; NbExp=2; IntAct=EBI-747805, EBI-746969;
CC       P60520:GABARAPL2; NbExp=15; IntAct=EBI-747805, EBI-720116;
CC       Q9GZQ8:MAP1LC3B; NbExp=2; IntAct=EBI-747805, EBI-373144;
CC       Q9BXW4:MAP1LC3C; NbExp=2; IntAct=EBI-747805, EBI-2603996;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18442052,
CC       ECO:0000269|PubMed:26872069}. Nucleus
CC       {ECO:0000269|PubMed:18442052}. Golgi apparatus
CC       {ECO:0000269|PubMed:26872069}. Note=Localizes mainly in the
CC       cytoplasm, while it localizes to the nucleus in presence of SUMO2
CC       (PubMed:18442052).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=UBE1DC1A;
CC         IsoId=Q9GZZ9-1; Sequence=Displayed;
CC       Name=2; Synonyms=UBE1DC1B;
CC         IsoId=Q9GZZ9-2; Sequence=VSP_038528;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC       {ECO:0000269|PubMed:16328888}.
CC   -!- DISEASE: Epileptic encephalopathy, early infantile, 44 (EIEE44)
CC       [MIM:617132]: A form of epileptic encephalopathy, a heterogeneous
CC       group of severe childhood onset epilepsies characterized by
CC       refractory seizures, neurodevelopmental impairment, and poor
CC       prognosis. Development is normal prior to seizure onset, after
CC       which cognitive and motor delays become apparent. EIEE44
CC       transmission pattern is consistent with autosomal recessive
CC       inheritance. {ECO:0000269|PubMed:27545674,
CC       ECO:0000269|PubMed:27545681}. Note=The disease is caused by
CC       mutations 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
CC       instability and speech difficulties with onset in childhood.
CC       Clinical features include gait and limb ataxia, dysarthria,
CC       nystagmus, cataracts, and cerebellar atrophy on brain imaging.
CC       {ECO:0000269|PubMed:26872069}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA5
CC       subfamily. {ECO:0000255}.
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   UniGene; Hs.170737; -.
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   PDBsum; 3GUC; -.
DR   PDBsum; 3H8V; -.
DR   PDBsum; 5HKH; -.
DR   PDBsum; 5IA8; -.
DR   PDBsum; 5IAA; -.
DR   PDBsum; 5L95; -.
DR   PDBsum; 6H77; -.
DR   PDBsum; 6H78; -.
DR   ProteinModelPortal; Q9GZZ9; -.
DR   SMR; Q9GZZ9; -.
DR   BioGrid; 122964; 87.
DR   ELM; Q9GZZ9; -.
DR   IntAct; Q9GZZ9; 54.
DR   MINT; Q9GZZ9; -.
DR   STRING; 9606.ENSP00000348565; -.
DR   ChEMBL; CHEMBL2016429; -.
DR   iPTMnet; Q9GZZ9; -.
DR   PhosphoSitePlus; Q9GZZ9; -.
DR   SwissPalm; Q9GZZ9; -.
DR   BioMuta; UBA5; -.
DR   DMDM; 74733510; -.
DR   EPD; Q9GZZ9; -.
DR   jPOST; Q9GZZ9; -.
DR   MaxQB; Q9GZZ9; -.
DR   PaxDb; Q9GZZ9; -.
DR   PeptideAtlas; Q9GZZ9; -.
DR   PRIDE; Q9GZZ9; -.
DR   ProteomicsDB; 80189; -.
DR   ProteomicsDB; 80190; -. [Q9GZZ9-2]
DR   DNASU; 79876; -.
DR   Ensembl; ENST00000264991; ENSP00000264991; ENSG00000081307. [Q9GZZ9-2]
DR   Ensembl; ENST00000356232; ENSP00000348565; ENSG00000081307. [Q9GZZ9-1]
DR   Ensembl; ENST00000494238; ENSP00000418807; ENSG00000081307. [Q9GZZ9-2]
DR   GeneID; 79876; -.
DR   KEGG; hsa:79876; -.
DR   UCSC; uc003epa.5; human. [Q9GZZ9-1]
DR   CTD; 79876; -.
DR   DisGeNET; 79876; -.
DR   EuPathDB; HostDB:ENSG00000081307.12; -.
DR   GeneCards; UBA5; -.
DR   HGNC; HGNC:23230; UBA5.
DR   HPA; HPA017235; -.
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; Undetermined early-onset epileptic encephalopathy.
DR   PharmGKB; PA162407661; -.
DR   eggNOG; KOG2336; Eukaryota.
DR   eggNOG; COG0476; LUCA.
DR   GeneTree; ENSGT00940000156177; -.
DR   HOGENOM; HOG000256352; -.
DR   HOVERGEN; HBG056496; -.
DR   InParanoid; Q9GZZ9; -.
DR   KO; K12164; -.
DR   OMA; ETHNYNI; -.
DR   OrthoDB; 1092362at2759; -.
DR   PhylomeDB; Q9GZZ9; -.
DR   TreeFam; TF314168; -.
DR   BRENDA; 6.2.1.B9; 2681.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   EvolutionaryTrace; Q9GZZ9; -.
DR   GeneWiki; UBE1DC1; -.
DR   GenomeRNAi; 79876; -.
DR   PRO; PR:Q9GZZ9; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   Bgee; ENSG00000081307; Expressed in 220 organ(s), highest expression level in body of pancreas.
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: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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0071566; F:UFM1 activating enzyme activity; IDA: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   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   Pfam; PF00899; ThiF; 1.
DR   SUPFAM; SSF69572; SSF69572; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Complete proteome;
KW   Cytoplasm; Disease mutation; Epilepsy; Golgi apparatus;
KW   Mental retardation; Metal-binding; Neurodegeneration;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome; Ubl conjugation pathway; Zinc.
FT   CHAIN         1    404       Ubiquitin-like modifier-activating enzyme
FT                                5.
FT                                /FTId=PRO_0000194970.
FT   ACT_SITE    250    250       Glycyl thioester intermediate.
FT                                {ECO:0000269|PubMed:20368332,
FT                                ECO:0000269|PubMed:27545674}.
FT   METAL       226    226       Zinc. {ECO:0000269|PubMed:20368332}.
FT   METAL       229    229       Zinc. {ECO:0000269|PubMed:20368332}.
FT   METAL       303    303       Zinc. {ECO:0000269|PubMed:20368332}.
FT   METAL       308    308       Zinc. {ECO:0000269|PubMed:20368332}.
FT   BINDING      83     83       ATP; via amide nitrogen.
FT                                {ECO:0000269|PubMed:20368332}.
FT   BINDING     104    104       ATP. {ECO:0000269|PubMed:20368332}.
FT   BINDING     127    127       ATP. {ECO:0000269|PubMed:20368332}.
FT   BINDING     150    150       ATP. {ECO:0000269|PubMed:20368332}.
FT   BINDING     184    184       ATP. {ECO:0000269|PubMed:20368332}.
FT   MOD_RES      45     45       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     358    358       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES     393    393       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8VE47}.
FT   VAR_SEQ       1     56       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_038528.
FT   VARIANT      55     55       R -> H (in EIEE44; reduces UFM1
FT                                activating enzyme activity;
FT                                dbSNP:rs774318611).
FT                                {ECO:0000269|PubMed:27545674}.
FT                                /FTId=VAR_077153.
FT   VARIANT      57     57       M -> V (in EIEE44; reduces UFM1
FT                                activating enzyme activity; reduces UFM1-
FT                                DDRGK1 formation; dbSNP:rs532178791).
FT                                {ECO:0000269|PubMed:27545681}.
FT                                /FTId=VAR_077154.
FT   VARIANT     168    168       G -> E (in EIEE44; abolishes UFM1
FT                                activating enzyme activity;
FT                                dbSNP:rs886039761).
FT                                {ECO:0000269|PubMed:27545681}.
FT                                /FTId=VAR_077155.
FT   VARIANT     246    404       Missing (in SCAR24; delocalizes protein
FT                                to the nucleus; activates degradation
FT                                through the ubiquitin proteasome pathway;
FT                                decreases protein stability; disrupts
FT                                interaction with UFM1).
FT                                /FTId=VAR_080409.
FT   VARIANT     260    260       V -> M (in EIEE44; reduces UFM1
FT                                activating enzyme activity;
FT                                dbSNP:rs886039759).
FT                                {ECO:0000269|PubMed:27545681}.
FT                                /FTId=VAR_077156.
FT   VARIANT     310    310       K -> E (in SCAR24; does not affect
FT                                cytoplasm localization; decreases protein
FT                                stability; does not affect interaction
FT                                with UFM1; dbSNP:rs886039762).
FT                                {ECO:0000269|PubMed:26872069}.
FT                                /FTId=VAR_077157.
FT   VARIANT     371    371       A -> T (in EIEE44; reduces UFM1
FT                                activating enzyme activity; reduces UFM1
FT                                activating enzyme activity; reduces UFM1-
FT                                DDRGK1 formation; dbSNP:rs114925667).
FT                                {ECO:0000269|PubMed:27545674,
FT                                ECO:0000269|PubMed:27545681}.
FT                                /FTId=VAR_077158.
FT   VARIANT     389    389       D -> Y (in EIEE44; no effect on UFM1
FT                                activating enzyme activity;
FT                                dbSNP:rs886039760).
FT                                {ECO:0000269|PubMed:27545681}.
FT                                /FTId=VAR_077159.
FT   MUTAGEN     250    250       C->S: Forms a stable intermediate
FT                                complex. {ECO:0000269|PubMed:15071506,
FT                                ECO:0000269|PubMed:27545674,
FT                                ECO:0000269|PubMed:29868776}.
FT   CONFLICT    403    403       N -> S (in Ref. 4; BAB55199).
FT                                {ECO:0000305}.
FT   HELIX        54     61       {ECO:0000244|PDB:6H77}.
FT   HELIX        70     73       {ECO:0000244|PDB:3H8V}.
FT   STRAND       75     79       {ECO:0000244|PDB:3H8V}.
FT   HELIX        83     95       {ECO:0000244|PDB:3H8V}.
FT   STRAND       98    103       {ECO:0000244|PDB:3H8V}.
FT   HELIX       110    112       {ECO:0000244|PDB:6H77}.
FT   STRAND      115    117       {ECO:0000244|PDB:6H77}.
FT   HELIX       120    122       {ECO:0000244|PDB:6H77}.
FT   HELIX       127    138       {ECO:0000244|PDB:3H8V}.
FT   STRAND      142    147       {ECO:0000244|PDB:3H8V}.
FT   HELIX       154    166       {ECO:0000244|PDB:3H8V}.
FT   STRAND      167    170       {ECO:0000244|PDB:3H8V}.
FT   STRAND      176    180       {ECO:0000244|PDB:3H8V}.
FT   HELIX       185    198       {ECO:0000244|PDB:3H8V}.
FT   STRAND      202    207       {ECO:0000244|PDB:3H8V}.
FT   STRAND      211    219       {ECO:0000244|PDB:3H8V}.
FT   TURN        221    223       {ECO:0000244|PDB:3H8V}.
FT   STRAND      229    231       {ECO:0000244|PDB:3H8V}.
FT   HELIX       233    236       {ECO:0000244|PDB:6H77}.
FT   HELIX       241    244       {ECO:0000244|PDB:6H77}.
FT   HELIX       247    274       {ECO:0000244|PDB:3H8V}.
FT   STRAND      281    286       {ECO:0000244|PDB:3H8V}.
FT   TURN        287    290       {ECO:0000244|PDB:3H8V}.
FT   HELIX       306    317       {ECO:0000244|PDB:3H8V}.
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
//
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