UBA6_HUMAN
ID UBA6_HUMAN Reviewed; 1052 AA.
AC A0AVT1; A6N8M7; B2RAV3; Q4W5K0; Q6UV21; Q86T78; Q86TC7; Q8N5T3; Q8N9E4;
AC Q9H3T7; Q9NVC9;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme 6;
DE Short=Ubiquitin-activating enzyme 6;
DE EC=6.2.1.45 {ECO:0000250|UniProtKB:P22314};
DE AltName: Full=Monocyte protein 4;
DE Short=MOP-4;
DE AltName: Full=Ubiquitin-activating enzyme E1-like protein 2;
DE Short=E1-L2;
GN Name=UBA6; Synonyms=MOP4, UBE1L2;
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 2), TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=15202508; DOI=10.1093/abbs/36.3.227;
RA Zhu H., Zhou Z.-M., Huo R., Huang X.-Y., Lu L., Lin M., Wang L.-R.,
RA Zhou Y.-D., Li J.-M., Sha J.-H.;
RT "Identification and characteristics of a novel E1 like gene nUBE1L in human
RT testis.";
RL Acta Biochim. Biophys. Sin. 36:227-234(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-224, FUNCTION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF CYS-625.
RX PubMed=17597759; DOI=10.1038/nature05902;
RA Jin J., Li X., Gygi S.P., Harper J.W.;
RT "Dual E1 activation systems for ubiquitin differentially regulate E2 enzyme
RT charging.";
RL Nature 447:1135-1138(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Blood;
RA Takayama K., Fujii Y., Ukai Y., Yoshimoto M.;
RT "Molecular and biological characterization of a new ubiquitin-activating
RT enzyme E1 like protein, MOP-4 which is highly expressed in human
RT monocytes.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT
RP THR-224.
RC TISSUE=Hippocampus;
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 MRNA] (ISOFORM 1), AND VARIANT THR-224.
RC TISSUE=Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain;
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 FUNCTION, INTERACTION WITH UBD, THIOESTER FORMATION, AND MUTAGENESIS OF
RP CYS-625.
RX PubMed=17889673; DOI=10.1016/j.molcel.2007.08.020;
RA Chiu Y.-H., Sun Q., Chen Z.J.;
RT "E1-L2 activates both ubiquitin and FAT10.";
RL Mol. Cell 27:1014-1023(2007).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-544, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54; SER-301 AND SER-737, AND
RP IDENTIFICATION 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP INTERACTION WITH UBD.
RX PubMed=25422469; DOI=10.1073/pnas.1403383111;
RA Theng S.S., Wang W., Mah W.C., Chan C., Zhuo J., Gao Y., Qin H., Lim L.,
RA Chong S.S., Song J., Lee C.G.;
RT "Disruption of FAT10-MAD2 binding inhibits tumor progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E5282-E5291(2014).
CC -!- FUNCTION: Activates ubiquitin by first adenylating its C-terminal
CC glycine residue with ATP, and thereafter linking this residue to the
CC side chain of a cysteine residue in E1, yielding a ubiquitin-E1
CC thioester and free AMP. Specific for ubiquitin, does not activate
CC ubiquitin-like peptides. Differs from UBE1 in its specificity for
CC substrate E2 charging. Does not charge cell cycle E2s, such as CDC34.
CC Essential for embryonic development. Required for UBD/FAT10
CC conjugation. Isoform 2 may play a key role in ubiquitin system and may
CC influence spermatogenesis and male fertility.
CC {ECO:0000269|PubMed:15202508, ECO:0000269|PubMed:17597759,
CC ECO:0000269|PubMed:17889673}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
CC = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-
CC L-cysteine.; EC=6.2.1.45; Evidence={ECO:0000250|UniProtKB:P22314};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:P22314}.
CC -!- SUBUNIT: Forms a thioester with UBD in cells stimulated with tumor
CC necrosis factor-alpha (TNFa) and interferon-gamma (IFNg)
CC (PubMed:17889673, PubMed:25422469). {ECO:0000269|PubMed:17889673,
CC ECO:0000269|PubMed:25422469}.
CC -!- INTERACTION:
CC A0AVT1; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-5282516, EBI-2549423;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=A0AVT1-1; Sequence=Displayed;
CC Name=2; Synonyms=nUBE1L;
CC IsoId=A0AVT1-2; Sequence=VSP_023083;
CC Name=3;
CC IsoId=A0AVT1-3; Sequence=VSP_023086, VSP_023087;
CC Name=4;
CC IsoId=A0AVT1-4; Sequence=VSP_023084, VSP_023085;
CC -!- TISSUE SPECIFICITY: Widely expressed. Isoform 2 is predominantly
CC expressed in testis with higher expression in adult testis than in
CC fetal testis. {ECO:0000269|PubMed:15202508,
CC ECO:0000269|PubMed:17597759}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91824.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY359880; AAQ63403.1; -; mRNA.
DR EMBL; EF623993; ABR25253.1; -; mRNA.
DR EMBL; AB014773; BAB19785.1; -; mRNA.
DR EMBL; AK001670; BAA91824.1; ALT_INIT; mRNA.
DR EMBL; AK094969; BAC04463.1; -; mRNA.
DR EMBL; AK314371; BAG37000.1; -; mRNA.
DR EMBL; AL832015; CAD89908.1; -; mRNA.
DR EMBL; AL832458; CAD89959.1; -; mRNA.
DR EMBL; AC079880; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC096720; AAY40999.1; -; Genomic_DNA.
DR EMBL; BC031637; AAH31637.1; -; mRNA.
DR EMBL; BC126484; AAI26485.1; -; mRNA.
DR EMBL; BC126486; AAI26487.1; -; mRNA.
DR CCDS; CCDS3516.1; -. [A0AVT1-1]
DR RefSeq; NP_060697.4; NM_018227.5. [A0AVT1-1]
DR AlphaFoldDB; A0AVT1; -.
DR SMR; A0AVT1; -.
DR BioGRID; 120529; 151.
DR DIP; DIP-57633N; -.
DR IntAct; A0AVT1; 16.
DR MINT; A0AVT1; -.
DR STRING; 9606.ENSP00000313454; -.
DR BindingDB; A0AVT1; -.
DR ChEMBL; CHEMBL2321622; -.
DR GlyGen; A0AVT1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; A0AVT1; -.
DR MetOSite; A0AVT1; -.
DR PhosphoSitePlus; A0AVT1; -.
DR SwissPalm; A0AVT1; -.
DR BioMuta; UBA6; -.
DR EPD; A0AVT1; -.
DR jPOST; A0AVT1; -.
DR MassIVE; A0AVT1; -.
DR MaxQB; A0AVT1; -.
DR PaxDb; A0AVT1; -.
DR PeptideAtlas; A0AVT1; -.
DR PRIDE; A0AVT1; -.
DR ProteomicsDB; 26; -. [A0AVT1-1]
DR ProteomicsDB; 27; -. [A0AVT1-2]
DR ProteomicsDB; 28; -. [A0AVT1-3]
DR ProteomicsDB; 29; -. [A0AVT1-4]
DR Antibodypedia; 24140; 305 antibodies from 32 providers.
DR DNASU; 55236; -.
DR Ensembl; ENST00000322244.10; ENSP00000313454.4; ENSG00000033178.13. [A0AVT1-1]
DR Ensembl; ENST00000420827.2; ENSP00000399234.2; ENSG00000033178.13. [A0AVT1-3]
DR GeneID; 55236; -.
DR KEGG; hsa:55236; -.
DR MANE-Select; ENST00000322244.10; ENSP00000313454.4; NM_018227.6; NP_060697.4.
DR UCSC; uc003hdg.5; human. [A0AVT1-1]
DR CTD; 55236; -.
DR DisGeNET; 55236; -.
DR GeneCards; UBA6; -.
DR HGNC; HGNC:25581; UBA6.
DR HPA; ENSG00000033178; Low tissue specificity.
DR MIM; 611361; gene.
DR neXtProt; NX_A0AVT1; -.
DR OpenTargets; ENSG00000033178; -.
DR PharmGKB; PA162407690; -.
DR VEuPathDB; HostDB:ENSG00000033178; -.
DR eggNOG; KOG2012; Eukaryota.
DR GeneTree; ENSGT00940000158826; -.
DR HOGENOM; CLU_002556_0_0_1; -.
DR InParanoid; A0AVT1; -.
DR OMA; WSHCVEL; -.
DR PhylomeDB; A0AVT1; -.
DR TreeFam; TF300586; -.
DR BRENDA; 6.2.1.45; 2681.
DR PathwayCommons; A0AVT1; -.
DR Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; A0AVT1; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 55236; 242 hits in 1079 CRISPR screens.
DR ChiTaRS; UBA6; human.
DR GeneWiki; UBE1L2; -.
DR GenomeRNAi; 55236; -.
DR Pharos; A0AVT1; Tchem.
DR PRO; PR:A0AVT1; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; A0AVT1; protein.
DR Bgee; ENSG00000033178; Expressed in adrenal tissue and 191 other tissues.
DR ExpressionAtlas; A0AVT1; baseline and differential.
DR Genevisible; A0AVT1; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019780; F:FAT10 activating enzyme activity; IMP:UniProtKB.
DR GO; GO:0004839; F:ubiquitin activating enzyme activity; IBA:GO_Central.
DR GO; GO:0021764; P:amygdala development; IEA:Ensembl.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0060996; P:dendritic spine development; IEA:Ensembl.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0007612; P:learning; IEA:Ensembl.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR Gene3D; 1.10.10.2660; -; 1.
DR Gene3D; 2.40.30.180; -; 1.
DR Gene3D; 3.10.290.60; -; 1.
DR Gene3D; 3.50.50.80; -; 1.
DR InterPro; IPR032420; E1_4HB.
DR InterPro; IPR032418; E1_FCCH.
DR InterPro; IPR042302; E1_FCCH_sf.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR018965; Ub-activating_enz_E1_C.
DR InterPro; IPR042449; Ub-E1_IAD_1.
DR InterPro; IPR038252; UBA_E1_C_sf.
DR InterPro; IPR019572; UBA_E1_SCCH.
DR InterPro; IPR042063; Ubi_acti_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR018075; UBQ-activ_enz_E1.
DR InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR Pfam; PF16191; E1_4HB; 1.
DR Pfam; PF16190; E1_FCCH; 1.
DR Pfam; PF09358; E1_UFD; 1.
DR Pfam; PF00899; ThiF; 2.
DR Pfam; PF10585; UBA_e1_thiolCys; 1.
DR PRINTS; PR01849; UBIQUITINACT.
DR SMART; SM00985; UBA_e1_C; 1.
DR SUPFAM; SSF69572; SSF69572; 2.
DR TIGRFAMs; TIGR01408; Ube1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Ligase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..1052
FT /note="Ubiquitin-like modifier-activating enzyme 6"
FT /id="PRO_0000277797"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 625
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10132"
FT BINDING 470
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 497
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 508
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 521
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 569..570
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 54
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 544
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 729
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8C7R4"
FT MOD_RES 737
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..474
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15202508"
FT /id="VSP_023083"
FT VAR_SEQ 321..340
FT /note="APLEIHTAMLALDQFQEKYS -> VNKHFAGLREAAESEMRISE (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023084"
FT VAR_SEQ 341..1052
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023085"
FT VAR_SEQ 369..389
FT /note="PDVNADIVHWLSWTAQGFLSP -> VTIEIYGCPNICLLIHKCSVY (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023086"
FT VAR_SEQ 390..1052
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023087"
FT VARIANT 224
FT /note="A -> T (in dbSNP:rs10010188)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:17597759, ECO:0000269|PubMed:17974005"
FT /id="VAR_030594"
FT MUTAGEN 625
FT /note="C->A,S: Impairs ubiquitin activation."
FT /evidence="ECO:0000269|PubMed:17597759,
FT ECO:0000269|PubMed:17889673"
FT CONFLICT 14
FT /note="E -> K (in Ref. 5; CAD89908)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="V -> A (in Ref. 5; CAD89908)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="C -> Y (in Ref. 4; BAC04463)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="N -> D (in Ref. 5; CAD89959)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="V -> A (in Ref. 4; BAC04463)"
FT /evidence="ECO:0000305"
FT CONFLICT 645
FT /note="F -> V (in Ref. 1; AAQ63403)"
FT /evidence="ECO:0000305"
FT CONFLICT 803
FT /note="Q -> H (in Ref. 4; BAA91824)"
FT /evidence="ECO:0000305"
FT CONFLICT 821
FT /note="E -> G (in Ref. 5; CAD89959)"
FT /evidence="ECO:0000305"
FT CONFLICT 868
FT /note="L -> P (in Ref. 5; CAD89908)"
FT /evidence="ECO:0000305"
FT CONFLICT 905
FT /note="V -> G (in Ref. 1; AAQ63403)"
FT /evidence="ECO:0000305"
FT CONFLICT 909
FT /note="M -> K (in Ref. 5; CAD89959)"
FT /evidence="ECO:0000305"
FT CONFLICT 920
FT /note="A -> V (in Ref. 3; BAB19785)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1052 AA; 117970 MW; 9F9C70EABA750A71 CRC64;
MEGSEPVAAH QGEEASCSSW GTGSTNKNLP IMSTASVEID DALYSRQRYV LGDTAMQKMA
KSHVFLSGMG GLGLEIAKNL VLAGIKAVTI HDTEKCQAWD LGTNFFLSED DVVNKRNRAE
AVLKHIAELN PYVHVTSSSV PFNETTDLSF LDKYQCVVLT EMKLPLQKKI NDFCRSQCPP
IKFISADVHG IWSRLFCDFG DEFEVLDTTG EEPKEIFISN ITQANPGIVT CLENHPHKLE
TGQFLTFREI NGMTGLNGSI QQITVISPFS FSIGDTTELE PYLHGGIAVQ VKTPKTVFFE
SLERQLKHPK CLIVDFSNPE APLEIHTAML ALDQFQEKYS RKPNVGCQQD SEELLKLATS
ISETLEEKPD VNADIVHWLS WTAQGFLSPL AAAVGGVASQ EVLKAVTGKF SPLCQWLYLE
AADIVESLGK PECEEFLPRG DRYDALRACI GDTLCQKLQN LNIFLVGCGA IGCEMLKNFA
LLGVGTSKEK GMITVTDPDL IEKSNLNRQF LFRPHHIQKP KSYTAADATL KINSQIKIDA
HLNKVCPTTE TIYNDEFYTK QDVIITALDN VEARRYVDSR CLANLRPLLD SGTMGTKGHT
EVIVPHLTES YNSHRDPPEE EIPFCTLKSF PAAIEHTIQW ARDKFESSFS HKPSLFNKFW
QTYSSAEEVL QKIQSGHSLE GCFQVIKLLS RRPRNWSQCV ELARLKFEKY FNHKALQLLH
CFPLDIRLKD GSLFWQSPKR PPSPIKFDLN EPLHLSFLQN AAKLYATVYC IPFAEEDLSA
DALLNILSEV KIQEFKPSNK VVQTDETARK PDHVPISSED ERNAIFQLEK AILSNEATKS
DLQMAVLSFE KDDDHNGHID FITAASNLRA KMYSIEPADR FKTKRIAGKI IPAIATTTAT
VSGLVALEMI KVTGGYPFEA YKNCFLNLAI PIVVFTETTE VRKTKIRNGI SFTIWDRWTV
HGKEDFTLLD FINAVKEKYG IEPTMVVQGV KMLYVPVMPG HAKRLKLTMH KLVKPTTEKK
YVDLTVSFAP DIDGDEDLPG PPVRYYFSHD TD
