UBA1_MOUSE
ID UBA1_MOUSE Reviewed; 1058 AA.
AC Q02053; A6H6S6; P31253; Q542H8;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme 1;
DE EC=6.2.1.45 {ECO:0000250|UniProtKB:P22314};
DE AltName: Full=Ubiquitin-activating enzyme E1;
DE AltName: Full=Ubiquitin-activating enzyme E1 X;
DE AltName: Full=Ubiquitin-like modifier-activating enzyme 1 X;
GN Name=Uba1; Synonyms=Sbx, Ube1, Ube1ax, Ube1x;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND PATHWAY.
RX PubMed=1511901; DOI=10.1016/0378-1119(92)90200-9;
RA Imai N., Kaneda S., Nagai Y., Seno T., Ayusawa D., Hanaoka F., Yamao F.;
RT "Cloning and sequence of a functionally active cDNA encoding the mouse
RT ubiquitin-activating enzyme E1.";
RL Gene 118:279-282(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Ovary, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [5]
RP PROTEIN SEQUENCE OF 69-81; 90-97; 175-182; 227-239; 351-368; 375-384;
RP 386-411; 451-465; 471-485; 538-551; 559-581; 593-604; 636-671; 679-693;
RP 785-802; 844-851; 870-880; 890-923; 945-980 AND 1011-1021, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 615-1058.
RC STRAIN=129/Sv;
RX PubMed=1684224; DOI=10.1038/354483a0;
RA Mitchell M.J., Woods D.R., Tucker P.K., Opp J.S., Bishop C.E.;
RT "Homology of a candidate spermatogenic gene from the mouse Y chromosome to
RT the ubiquitin-activating enzyme E1.";
RL Nature 354:483-487(1991).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 655-763.
RC STRAIN=BALB/c AnCr; TISSUE=Liver;
RX PubMed=7714913; DOI=10.1007/bf00166597;
RA Chang B.H.-J., Li W.H.;
RT "Estimating the intensity of male-driven evolution in rodents by using X-
RT linked and Y-linked Ube 1 genes and pseudogenes.";
RL J. Mol. Evol. 40:70-77(1995).
RN [8]
RP REGULATION OF EXPRESSION BY THE THYROID HORMONE RECEPTOR.
RX PubMed=7937138; DOI=10.1093/nar/22.20.4132;
RA Caubin J., Iglesias T., Bernal J., Munoz A., Marquez G., Barbero J.L.,
RA Zaballos A.;
RT "Isolation of genomic DNA fragments corresponding to genes modulated in
RT vivo by a transcription factor.";
RL Nucleic Acids Res. 22:4132-4138(1994).
RN [9]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=8948595; DOI=10.1006/dbio.1996.0305;
RA Odorisio T., Mahadevaiah S.K., McCarrey J.R., Burgoyne P.S.;
RT "Transcriptional analysis of the candidate spermatogenesis gene Ube1y and
RT of the closely related Ube1x shows that they are coexpressed in
RT spermatogonia and spermatids but are repressed in pachytene
RT spermatocytes.";
RL Dev. Biol. 180:336-343(1996).
RN [10]
RP ISGYLATION.
RX PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT human cells.";
RL Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-55, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-816 AND SER-820, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-21; SER-24; SER-46;
RP SER-810; SER-816; SER-820 AND SER-835, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-671, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-528, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 626-891.
RX PubMed=15774460; DOI=10.1074/jbc.m502583200;
RA Szczepanowski R.H., Filipek R., Bochtler M.;
RT "Crystal structure of a fragment of mouse ubiquitin-activating enzyme.";
RL J. Biol. Chem. 280:22006-22011(2005).
CC -!- FUNCTION: Catalyzes the first step in ubiquitin conjugation to mark
CC cellular proteins for degradation through the ubiquitin-proteasome
CC system (PubMed:1511901). Activates ubiquitin by first adenylating its
CC C-terminal glycine residue with ATP, and thereafter linking this
CC residue to the side chain of a cysteine residue in E1, yielding a
CC ubiquitin-E1 thioester and free AMP. Essential for the formation of
CC radiation-induced foci, timely DNA repair and for response to
CC replication stress. Promotes the recruitment of TP53BP1 and BRCA1 at
CC DNA damage sites. {ECO:0000250|UniProtKB:P22314,
CC ECO:0000305|PubMed:1511901}.
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:0000305|PubMed:1511901}.
CC -!- SUBUNIT: Monomer. Interacts with GAN (via BTB domain).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P22314}.
CC Mitochondrion {ECO:0000250|UniProtKB:P22314}. Nucleus
CC {ECO:0000250|UniProtKB:P22314}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. In testis, expressed in A
CC spermatogonia and spermatids but at very low levels in pachytene
CC spermatocytes. {ECO:0000269|PubMed:8948595}.
CC -!- DEVELOPMENTAL STAGE: In testis, highly expressed from 14.5 days post
CC coitum (dpc) until the day of birth, with levels falling after 10 days
CC post partum (dpp) but peaking again at 28 dpp.
CC {ECO:0000269|PubMed:8948595}.
CC -!- INDUCTION: May be modulated by the thyroid hormone receptor.
CC -!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
CC -!- MISCELLANEOUS: There are two active sites within the E1 molecule,
CC allowing it to accommodate two ubiquitin moieties at a time, with a new
CC ubiquitin forming an adenylate intermediate as the previous one is
CC transferred to the thiol site. {ECO:0000250|UniProtKB:P22515}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA44465.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D10576; BAA01433.1; -; mRNA.
DR EMBL; AK088057; BAC40121.1; -; mRNA.
DR EMBL; AK088528; BAC40405.1; -; mRNA.
DR EMBL; AK143416; BAE25369.1; -; mRNA.
DR EMBL; AK171667; BAE42599.1; -; mRNA.
DR EMBL; AL807240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC058630; AAH58630.1; -; mRNA.
DR EMBL; BC145984; AAI45985.1; -; mRNA.
DR EMBL; X62580; CAA44465.1; ALT_FRAME; mRNA.
DR EMBL; U09051; AAC52169.1; -; Genomic_DNA.
DR EMBL; U09055; AAC52171.1; -; Genomic_DNA.
DR CCDS; CCDS30044.1; -.
DR PIR; I48756; I48756.
DR PIR; I63168; I63168.
DR PIR; JC1254; JC1254.
DR RefSeq; NP_001129557.1; NM_001136085.2.
DR RefSeq; NP_001263245.1; NM_001276316.1.
DR RefSeq; NP_001263246.1; NM_001276317.1.
DR RefSeq; NP_033483.2; NM_009457.4.
DR PDB; 1Z7L; X-ray; 2.80 A; A/B/C=626-891.
DR PDB; 2LZJ; NMR; -; A=202-312.
DR PDB; 2V31; NMR; -; A=202-312.
DR PDBsum; 1Z7L; -.
DR PDBsum; 2LZJ; -.
DR PDBsum; 2V31; -.
DR AlphaFoldDB; Q02053; -.
DR BMRB; Q02053; -.
DR SMR; Q02053; -.
DR BioGRID; 204410; 57.
DR ELM; Q02053; -.
DR IntAct; Q02053; 9.
DR MINT; Q02053; -.
DR STRING; 10090.ENSMUSP00000001989; -.
DR iPTMnet; Q02053; -.
DR PhosphoSitePlus; Q02053; -.
DR SwissPalm; Q02053; -.
DR EPD; Q02053; -.
DR jPOST; Q02053; -.
DR MaxQB; Q02053; -.
DR PaxDb; Q02053; -.
DR PRIDE; Q02053; -.
DR ProteomicsDB; 298351; -.
DR Antibodypedia; 345; 428 antibodies from 40 providers.
DR DNASU; 22201; -.
DR Ensembl; ENSMUST00000001989; ENSMUSP00000001989; ENSMUSG00000001924.
DR Ensembl; ENSMUST00000089217; ENSMUSP00000086626; ENSMUSG00000001924.
DR GeneID; 22201; -.
DR KEGG; mmu:22201; -.
DR UCSC; uc009stl.2; mouse.
DR CTD; 7317; -.
DR MGI; MGI:98890; Uba1.
DR VEuPathDB; HostDB:ENSMUSG00000001924; -.
DR eggNOG; KOG2012; Eukaryota.
DR GeneTree; ENSGT00940000158975; -.
DR HOGENOM; CLU_002556_0_0_1; -.
DR InParanoid; Q02053; -.
DR OMA; GANLHAF; -.
DR OrthoDB; 91748at2759; -.
DR PhylomeDB; Q02053; -.
DR TreeFam; TF300586; -.
DR BRENDA; 6.2.1.45; 3474.
DR Reactome; R-MMU-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 22201; 31 hits in 72 CRISPR screens.
DR ChiTaRS; Uba1; mouse.
DR EvolutionaryTrace; Q02053; -.
DR PRO; PR:Q02053; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q02053; protein.
DR Bgee; ENSMUSG00000001924; Expressed in cortical plate and 267 other tissues.
DR ExpressionAtlas; Q02053; baseline and differential.
DR Genevisible; Q02053; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030057; C:desmosome; ISO:MGI.
DR GO; GO:0010008; C:endosome membrane; ISO:MGI.
DR GO; GO:0000792; C:heterochromatin; ISO:MGI.
DR GO; GO:0005765; C:lysosomal membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004839; F:ubiquitin activating enzyme activity; IDA:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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; IPR018074; UBQ-activ_enz_E1_CS.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
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.
DR PROSITE; PS00536; UBIQUITIN_ACTIVAT_1; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Ligase; Mitochondrion; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P22314"
FT CHAIN 2..1058
FT /note="Ubiquitin-like modifier-activating enzyme 1"
FT /id="PRO_0000194935"
FT REPEAT 63..199
FT /note="1-1"
FT REPEAT 459..611
FT /note="1-2"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..611
FT /note="2 approximate repeats"
FT COMPBIAS 20..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 632
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10132"
FT BINDING 478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 504
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 515
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 528
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT BINDING 576..577
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22515"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P22314"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22314"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 55
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 528
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 671
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 800
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P22314"
FT MOD_RES 810
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 816
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 835
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 980
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P22314"
FT CONFLICT 963
FT /note="L -> V (in Ref. 6; CAA44465)"
FT /evidence="ECO:0000305"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:2LZJ"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:2LZJ"
FT STRAND 227..234
FT /evidence="ECO:0007829|PDB:2LZJ"
FT STRAND 246..255
FT /evidence="ECO:0007829|PDB:2LZJ"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:2LZJ"
FT STRAND 265..278
FT /evidence="ECO:0007829|PDB:2LZJ"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:2LZJ"
FT STRAND 288..294
FT /evidence="ECO:0007829|PDB:2LZJ"
FT HELIX 631..635
FT /evidence="ECO:0007829|PDB:1Z7L"
FT HELIX 641..656
FT /evidence="ECO:0007829|PDB:1Z7L"
FT HELIX 658..666
FT /evidence="ECO:0007829|PDB:1Z7L"
FT HELIX 671..677
FT /evidence="ECO:0007829|PDB:1Z7L"
FT HELIX 683..695
FT /evidence="ECO:0007829|PDB:1Z7L"
FT TURN 696..698
FT /evidence="ECO:0007829|PDB:1Z7L"
FT HELIX 703..718
FT /evidence="ECO:0007829|PDB:1Z7L"
FT HELIX 720..728
FT /evidence="ECO:0007829|PDB:1Z7L"
FT STRAND 740..742
FT /evidence="ECO:0007829|PDB:1Z7L"
FT HELIX 759..775
FT /evidence="ECO:0007829|PDB:1Z7L"
FT HELIX 784..792
FT /evidence="ECO:0007829|PDB:1Z7L"
FT STRAND 809..811
FT /evidence="ECO:0007829|PDB:1Z7L"
FT HELIX 824..832
FT /evidence="ECO:0007829|PDB:1Z7L"
FT HELIX 836..838
FT /evidence="ECO:0007829|PDB:1Z7L"
FT HELIX 858..872
FT /evidence="ECO:0007829|PDB:1Z7L"
FT HELIX 880..886
FT /evidence="ECO:0007829|PDB:1Z7L"
SQ SEQUENCE 1058 AA; 117809 MW; 95D8152ED5C8E037 CRC64;
MSSSPLSKKR RVSGPDPKPG SNCSPAQSAL SEVSSVPTNG MAKNGSEADI DESLYSRQLY
VLGHEAMKML QTSSVLVSGL RGLGVEIAKN IILGGVKAVT LHDQGTTQWA DLSSQFYLRE
EDIGKNRAEV SQPRLAELNS YVPVTAYTGP LVEDFLSSFQ VVVLTNSPLE AQLRVGEFCH
SRGIKLVVAD TRGLFGQLFC DFGEEMVLTD SNGEQPLSAM VSMVTKDNPG VVTCLDEARH
GFETGDFVSF SEVQGMIQLN GCQPMEIKVL GPYTFSICDT SNFSDYIRGG IVSQVKVPKK
ISFKSLPASL VEPDFVMTDF AKYSRPAQLH IGFQALHQFC ALHNQPPRPR NEEDATELVG
LAQAVNARSP PSVKQNSLDE DLIRKLAYVA AGDLAPINAF IGGLAAQEVM KACSGKFMPI
MQWLYFDALE CLPEDKEALT EEKCLPRQNR YDGQVAVFGS DFQEKLSKQK YFLVGAGAIG
CELLKNFAMI GLGCGEGGEV VVTDMDTIEK SNLNRQFLFR PWDVTKLKSD TAAAAVRQMN
PYIQVTSHQN RVGPDTERIY DDDFFQNLDG VANALDNIDA RMYMDRRCVY YRKPLLESGT
LGTKGNVQVV IPFLTESYSS SQDPPEKSIP ICTLKNFPNA IEHTLQWARD EFEGLFKQPA
ENVNQYLTDS KFVERTLRLA GTQPLEVLEA VQRSLVLQRP QTWGDCVTWA CHHWHTQYCN
NIRQLLHNFP PDQLTSSGAP FWSGPKRCPH PLTFDVNNTL HLDYVMAAAN LFAQTYGLTG
SQDRAAVASL LQSVQVPEFT PKSGVKIHVS DQELQSANAS VDDSRLEELK ATLPSPDKLP
GFKMYPIDFE KDDDSNFHMD FIVAASNLRA ENYDISPADR HKSKLIAGKI IPAIATTTAA
VVGLVCLELY KVVQGHQQLD SYKNGFLNLA LPFFGFSEPL AAPRHQYYNQ EWTLWDRFEV
QGLQPNGEEM TLKQFLDYFK TEHKLEITML SQGVSMLYSF FMPAAKLKER LDQPMTEIVS
RVSKRKLGRH VRALVLELCC NDESGEDVEV PYVRYTIR
