ID   DYHC1_MOUSE             Reviewed;        4644 AA.
AC   Q9JHU4; E9QM71;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 197.
DE   RecName: Full=Cytoplasmic dynein 1 heavy chain 1;
DE   AltName: Full=Cytoplasmic dynein heavy chain 1;
DE   AltName: Full=Dynein heavy chain, cytosolic;
GN   Name=Dync1h1; Synonyms=Dhc1, Dnch1, Dnchc1, Dyhc;
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].
RC   STRAIN=FVB/NJ;
RA   Sasaki S., Shionoya A., Hirotsune S.;
RT   "Complete cDNA sequence of murine cytoplasmic dynein heavy chain.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
RP   INVOLVEMENT IN MOTOR NEURON DEGENERATION, VARIANT LOA TYR-580, AND VARIANT
RP   CRA1 CYS-1055.
RX   PubMed=12730604; DOI=10.1126/science.1083129;
RA   Hafezparast M., Klocke R., Ruhrberg C., Marquardt A., Ahmad-Annuar A.,
RA   Bowen S., Lalli G., Witherden A.S., Hummerich H., Nicholson S.,
RA   Morgan P.J., Oozageer R., Priestley J.V., Averill S., King V.R., Ball S.,
RA   Peters J., Toda T., Yamamoto A., Hiraoka Y., Augustin M., Korthaus D.,
RA   Wattler S., Wabnitz P., Dickneite C., Lampel S., Boehme F., Peraus G.,
RA   Popp A., Rudelius M., Schlegel J., Fuchs H., de Angelis M.H., Schiavo G.,
RA   Shima D.T., Russ A.P., Stumm G., Martin J.E., Fisher E.M.C.;
RT   "Mutations in dynein link motor neuron degeneration to defects in
RT   retrograde transport.";
RL   Science 300:808-812(2003).
RN   [4]
RP   INTERACTION WITH DNALI1.
RX   PubMed=16496424; DOI=10.1002/mrd.20475;
RA   Rashid S., Breckle R., Hupe M., Geisler S., Doerwald N., Neesen J.;
RT   "The murine Dnali1 gene encodes a flagellar protein that interacts with the
RT   cytoplasmic dynein heavy chain 1.";
RL   Mol. Reprod. Dev. 73:784-794(2006).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1228, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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   [7]
RP   INTERACTION WITH BICD2.
RX   PubMed=22956769; DOI=10.1091/mbc.e12-03-0210;
RA   Splinter D., Razafsky D.S., Schlager M.A., Serra-Marques A., Grigoriev I.,
RA   Demmers J., Keijzer N., Jiang K., Poser I., Hyman A.A., Hoogenraad C.C.,
RA   King S.J., Akhmanova A.;
RT   "BICD2, dynactin, and LIS1 cooperate in regulating dynein recruitment to
RT   cellular structures.";
RL   Mol. Biol. Cell 23:4226-4241(2012).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-4281, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE 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).
CC   -!- FUNCTION: Cytoplasmic dynein 1 acts as a motor for the intracellular
CC       retrograde motility of vesicles and organelles along microtubules.
CC       Dynein has ATPase activity; the force-producing power stroke is thought
CC       to occur on release of ADP. Plays a role in mitotic spindle assembly
CC       and metaphase plate congression. {ECO:0000250|UniProtKB:Q14204}.
CC   -!- SUBUNIT: Homodimer. The cytoplasmic dynein 1 complex consists of two
CC       catalytic heavy chains (HCs) and a number of non-catalytic subunits
CC       presented by intermediate chains (ICs), light intermediate chains
CC       (LICs) and light chains (LCs); the composition seems to vary in respect
CC       to the IC, LIC and LC composition. The heavy chain homodimer serves as
CC       a scaffold for the probable homodimeric assembly of the respective non-
CC       catalytic subunits. The ICs and LICs bind directly to the HC dimer and
CC       dynein LCs assemble on the IC dimer. Interacts with DYNC1LI1; DYNC1LI1
CC       and DYNC1LI2 bind mutually exclusive to DYNC1H1. Interacts with
CC       DYNC1LI2; DYNC1LI1 and DYNC1LI2 bind mutually exclusive to DYNC1H1.
CC       Interacts with DYNC1I2 (By similarity). Interacts with BICD2
CC       (PubMed:22956769). Interacts with DNALI1 (PubMed:16496424).
CC       {ECO:0000250|UniProtKB:P38650, ECO:0000269|PubMed:16496424,
CC       ECO:0000269|PubMed:22956769}.
CC   -!- INTERACTION:
CC       Q9JHU4; P07141: Csf1; NbExp=2; IntAct=EBI-645061, EBI-777188;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- DOMAIN: Dynein heavy chains probably consist of an N-terminal stem
CC       (which binds cargo and interacts with other dynein components), and the
CC       head or motor domain. The motor contains six tandemly-linked AAA
CC       domains in the head, which form a ring. A stalk-like structure (formed
CC       by two of the coiled coil domains) protrudes between AAA 4 and AAA 5
CC       and terminates in a microtubule-binding site. A seventh domain may also
CC       contribute to this ring; it is not clear whether the N-terminus or the
CC       C-terminus forms this extra domain. There are four well-conserved and
CC       two non-conserved ATPase sites, one per AAA domain. Probably only one
CC       of these (within AAA 1) actually hydrolyzes ATP, the others may serve a
CC       regulatory function.
CC   -!- DISEASE: Note=Defects in Dync1h1 are the cause of the 'Legs at odd
CC       angles' (LOA) phenotype, an autosomal dominant trait where affected
CC       animals display unusual twisting of the body and clenching of the
CC       hindlimbs when suspended by the tail. Heterozygotes suffer age-related
CC       progressive loss of muscle tone and locomotor ability without major
CC       reduction in life-span while homozygotes show a more severe phenotype
CC       with an inability to move or feed, and die within 24 hours of birth.
CC       LOA mutants display defects in migration of facial motor neuron cell
CC       bodies and impaired retrograde transport in spinal cord motor neurons.
CC       {ECO:0000269|PubMed:12730604}.
CC   -!- DISEASE: Note=Defects in Dync1h1 are the cause of the Cramping 1 (Cra1)
CC       phenotype, an autosomal dominant trait where affected animals display
CC       unusual twisting of the body and clenching of the hindlimbs when
CC       suspended by the tail. Heterozygotes suffer age-related progressive
CC       loss of muscle tone and locomotor ability without major reduction in
CC       life-span while homozygotes show a more severe phenotype with an
CC       inability to move or feed, and die within 24 hours of birth.
CC       {ECO:0000269|PubMed:12730604}.
CC   -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}.
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DR   EMBL; AY004877; AAF91078.1; -; mRNA.
DR   EMBL; AC152827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS36559.1; -.
DR   RefSeq; NP_084514.2; NM_030238.2.
DR   PDB; 3ERR; X-ray; 2.27 A; A/B=3260-3427.
DR   PDB; 3J1T; EM; 9.70 A; A=3264-3427.
DR   PDB; 3J1U; EM; 9.70 A; A=3264-3427.
DR   PDB; 3WUQ; X-ray; 3.50 A; A=3207-3483.
DR   PDB; 5AYH; X-ray; 3.01 A; A=3207-3475.
DR   PDB; 6RZA; EM; 5.40 A; X=3270-3285, X=3410-3418.
DR   PDB; 6RZB; EM; 5.00 A; C=3270-3418.
DR   PDBsum; 3ERR; -.
DR   PDBsum; 3J1T; -.
DR   PDBsum; 3J1U; -.
DR   PDBsum; 3WUQ; -.
DR   PDBsum; 5AYH; -.
DR   PDBsum; 6RZA; -.
DR   PDBsum; 6RZB; -.
DR   BMRB; Q9JHU4; -.
DR   EMDB; EMD-10060; -.
DR   EMDB; EMD-10061; -.
DR   SMR; Q9JHU4; -.
DR   BioGRID; 199254; 75.
DR   ComplexPortal; CPX-5699; Cytoplasmic dynein complex, variant 1.
DR   IntAct; Q9JHU4; 39.
DR   MINT; Q9JHU4; -.
DR   STRING; 10090.ENSMUSP00000018851; -.
DR   GlyGen; Q9JHU4; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9JHU4; -.
DR   MetOSite; Q9JHU4; -.
DR   PhosphoSitePlus; Q9JHU4; -.
DR   SwissPalm; Q9JHU4; -.
DR   EPD; Q9JHU4; -.
DR   jPOST; Q9JHU4; -.
DR   MaxQB; Q9JHU4; -.
DR   PaxDb; 10090-ENSMUSP00000018851; -.
DR   PeptideAtlas; Q9JHU4; -.
DR   ProteomicsDB; 277422; -.
DR   Pumba; Q9JHU4; -.
DR   Antibodypedia; 122; 168 antibodies from 28 providers.
DR   DNASU; 13424; -.
DR   Ensembl; ENSMUST00000018851.14; ENSMUSP00000018851.8; ENSMUSG00000018707.14.
DR   GeneID; 13424; -.
DR   KEGG; mmu:13424; -.
DR   UCSC; uc007pbo.1; mouse.
DR   AGR; MGI:103147; -.
DR   CTD; 1778; -.
DR   MGI; MGI:103147; Dync1h1.
DR   VEuPathDB; HostDB:ENSMUSG00000018707; -.
DR   eggNOG; KOG3595; Eukaryota.
DR   GeneTree; ENSGT00940000156103; -.
DR   HOGENOM; CLU_000038_7_0_1; -.
DR   InParanoid; Q9JHU4; -.
DR   OMA; NERQMTR; -.
DR   OrthoDB; 312195at2759; -.
DR   PhylomeDB; Q9JHU4; -.
DR   TreeFam; TF101165; -.
DR   Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR   Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR   Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR   Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR   Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR   Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR   Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR   Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR   Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR   Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR   Reactome; R-MMU-68877; Mitotic Prometaphase.
DR   Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR   Reactome; R-MMU-9646399; Aggrephagy.
DR   Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR   BioGRID-ORCS; 13424; 26 hits in 77 CRISPR screens.
DR   ChiTaRS; Dync1h1; mouse.
DR   EvolutionaryTrace; Q9JHU4; -.
DR   PRO; PR:Q9JHU4; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q9JHU4; Protein.
DR   Bgee; ENSMUSG00000018707; Expressed in cortical plate and 269 other cell types or tissues.
DR   ExpressionAtlas; Q9JHU4; baseline and differential.
DR   GO; GO:0030424; C:axon; ISO:MGI.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005868; C:cytoplasmic dynein complex; ISO:MGI.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR   GO; GO:0030286; C:dynein complex; ISO:MGI.
DR   GO; GO:0030175; C:filopodium; IDA:MGI.
DR   GO; GO:0002177; C:manchette; ISO:MGI.
DR   GO; GO:0005874; C:microtubule; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0045505; F:dynein intermediate chain binding; IEA:InterPro.
DR   GO; GO:0051959; F:dynein light intermediate chain binding; IPI:MGI.
DR   GO; GO:0008569; F:minus-end-directed microtubule motor activity; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0003341; P:cilium movement; IC:MGI.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR   GO; GO:0051293; P:establishment of spindle localization; ISO:MGI.
DR   GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR   GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR   GO; GO:0033962; P:P-body assembly; IMP:BHF-UCL.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR   GO; GO:0032388; P:positive regulation of intracellular transport; ISS:UniProtKB.
DR   GO; GO:1905832; P:positive regulation of spindle assembly; ISS:UniProtKB.
DR   GO; GO:0090235; P:regulation of metaphase plate congression; ISS:UniProtKB.
DR   GO; GO:0060236; P:regulation of mitotic spindle organization; ISS:UniProtKB.
DR   GO; GO:0008090; P:retrograde axonal transport; IBA:GO_Central.
DR   GO; GO:0034063; P:stress granule assembly; IMP:BHF-UCL.
DR   CDD; cd00009; AAA; 2.
DR   Gene3D; 1.10.287.2620; -; 1.
DR   Gene3D; 1.10.472.130; -; 1.
DR   Gene3D; 1.10.8.1220; -; 1.
DR   Gene3D; 1.10.8.710; -; 1.
DR   Gene3D; 1.20.1270.280; -; 1.
DR   Gene3D; 1.20.58.1120; -; 1.
DR   Gene3D; 1.20.920.20; -; 2.
DR   Gene3D; 1.20.920.30; -; 1.
DR   Gene3D; 1.20.920.60; -; 1.
DR   Gene3D; 3.10.490.20; -; 1.
DR   Gene3D; 6.10.140.1060; -; 1.
DR   Gene3D; 1.20.140.100; Dynein heavy chain, N-terminal domain 2; 1.
DR   Gene3D; 3.20.180.20; Dynein heavy chain, N-terminal domain 2; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 5.
DR   Gene3D; 1.10.8.720; Region D6 of dynein motor; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR035699; AAA_6.
DR   InterPro; IPR035706; AAA_9.
DR   InterPro; IPR041658; AAA_lid_11.
DR   InterPro; IPR042219; AAA_lid_11_sf.
DR   InterPro; IPR026983; DHC_fam.
DR   InterPro; IPR042222; Dynein_2_N.
DR   InterPro; IPR043157; Dynein_AAA1S.
DR   InterPro; IPR041466; Dynein_AAA5_ext.
DR   InterPro; IPR041228; Dynein_C.
DR   InterPro; IPR043160; Dynein_C_barrel.
DR   InterPro; IPR024743; Dynein_HC_stalk.
DR   InterPro; IPR024317; Dynein_heavy_chain_D4_dom.
DR   InterPro; IPR004273; Dynein_heavy_D6_P-loop.
DR   InterPro; IPR013602; Dynein_heavy_linker.
DR   InterPro; IPR013594; Dynein_heavy_tail.
DR   InterPro; IPR042228; Dynein_linker_3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR46532:SF13; DYNEIN CYTOPLASMIC 1 HEAVY CHAIN 1; 1.
DR   PANTHER; PTHR46532; MALE FERTILITY FACTOR KL5; 1.
DR   Pfam; PF12774; AAA_6; 1.
DR   Pfam; PF12775; AAA_7; 1.
DR   Pfam; PF12780; AAA_8; 1.
DR   Pfam; PF12781; AAA_9; 1.
DR   Pfam; PF18198; AAA_lid_11; 1.
DR   Pfam; PF08385; DHC_N1; 1.
DR   Pfam; PF08393; DHC_N2; 1.
DR   Pfam; PF17852; Dynein_AAA_lid; 1.
DR   Pfam; PF18199; Dynein_C; 1.
DR   Pfam; PF03028; Dynein_heavy; 1.
DR   Pfam; PF12777; MT; 1.
DR   SMART; SM00382; AAA; 4.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR   Genevisible; Q9JHU4; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Disease variant; Dynein; Microtubule;
KW   Mitosis; Motor protein; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Repeat; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q14204"
FT   CHAIN           2..4644
FT                   /note="Cytoplasmic dynein 1 heavy chain 1"
FT                   /id="PRO_0000114628"
FT   REGION          2..1865
FT                   /note="Stem"
FT                   /evidence="ECO:0000250"
FT   REGION          446..701
FT                   /note="Interaction with DYNC1I2"
FT                   /evidence="ECO:0000250"
FT   REGION          649..800
FT                   /note="Interaction with DYNC1LI2"
FT                   /evidence="ECO:0000250"
FT   REGION          1866..2097
FT                   /note="AAA 1"
FT                   /evidence="ECO:0000250"
FT   REGION          2178..2450
FT                   /note="AAA 2"
FT                   /evidence="ECO:0000250"
FT   REGION          2388..2408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2554..2803
FT                   /note="AAA 3"
FT                   /evidence="ECO:0000250"
FT   REGION          2897..3166
FT                   /note="AAA 4"
FT                   /evidence="ECO:0000250"
FT   REGION          3187..3498
FT                   /note="Stalk"
FT                   /evidence="ECO:0000250"
FT   REGION          3551..3780
FT                   /note="AAA 5"
FT                   /evidence="ECO:0000250"
FT   REGION          4003..4219
FT                   /note="AAA 6"
FT                   /evidence="ECO:0000250"
FT   COILED          48..69
FT                   /evidence="ECO:0000255"
FT   COILED          179..200
FT                   /evidence="ECO:0000255"
FT   COILED          453..476
FT                   /evidence="ECO:0000255"
FT   COILED          541..564
FT                   /evidence="ECO:0000255"
FT   COILED          1169..1201
FT                   /evidence="ECO:0000255"
FT   COILED          1229..1250
FT                   /evidence="ECO:0000255"
FT   COILED          1355..1371
FT                   /evidence="ECO:0000255"
FT   COILED          3187..3273
FT                   /evidence="ECO:0000255"
FT   COILED          3394..3498
FT                   /evidence="ECO:0000255"
FT   COILED          3735..3798
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        2388..2406
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1904..1911
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2222..2229
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2593..2600
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2935..2942
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14204"
FT   MOD_RES         68
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14204"
FT   MOD_RES         1123
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14204"
FT   MOD_RES         1228
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         3478
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14204"
FT   MOD_RES         4160
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14204"
FT   MOD_RES         4281
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         4364
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14204"
FT   MOD_RES         4366
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14204"
FT   VARIANT         580
FT                   /note="F -> Y (in LOA)"
FT                   /evidence="ECO:0000269|PubMed:12730604"
FT   VARIANT         1055
FT                   /note="Y -> C (in CRA1)"
FT                   /evidence="ECO:0000269|PubMed:12730604"
FT   CONFLICT        517
FT                   /note="A -> T (in Ref. 1; AAF91078)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2373
FT                   /note="F -> L (in Ref. 1; AAF91078)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2689
FT                   /note="G -> A (in Ref. 1; AAF91078)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3760
FT                   /note="D -> V (in Ref. 1; AAF91078)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3856
FT                   /note="I -> V (in Ref. 1; AAF91078)"
FT                   /evidence="ECO:0000305"
FT   HELIX           3260..3295
FT                   /evidence="ECO:0007829|PDB:3ERR"
FT   HELIX           3299..3306
FT                   /evidence="ECO:0007829|PDB:3ERR"
FT   HELIX           3313..3325
FT                   /evidence="ECO:0007829|PDB:3ERR"
FT   HELIX           3333..3336
FT                   /evidence="ECO:0007829|PDB:3ERR"
FT   HELIX           3339..3341
FT                   /evidence="ECO:0007829|PDB:3ERR"
FT   HELIX           3345..3351
FT                   /evidence="ECO:0007829|PDB:3ERR"
FT   HELIX           3354..3356
FT                   /evidence="ECO:0007829|PDB:3ERR"
FT   HELIX           3359..3368
FT                   /evidence="ECO:0007829|PDB:3ERR"
FT   TURN            3369..3371
FT                   /evidence="ECO:0007829|PDB:3ERR"
FT   HELIX           3377..3383
FT                   /evidence="ECO:0007829|PDB:3ERR"
FT   HELIX           3387..3427
FT                   /evidence="ECO:0007829|PDB:3ERR"
FT   TURN            3455..3457
FT                   /evidence="ECO:0007829|PDB:5AYH"
FT   HELIX           3458..3471
FT                   /evidence="ECO:0007829|PDB:5AYH"
SQ   SEQUENCE   4644 AA;  532045 MW;  C88C9FC21D41DD56 CRC64;
     MSEPGGGEDG SAGLEVSAVQ NVADVAVLQK HLRKLVPLLL EDGGDAPAAL EAALEEKSAL
     EQMRKFLSDP QVHTVLVERS TLKEDVGDEG EEEKEFISYN INIDIHYGVK SNSLAFIKRA
     PVIDADKPVS SQLRVLTLSE DSPYETLHSF ISNAVAPFFK SYIRESGKAD RDGDKMAPSV
     EKKIAELEMG LLHLQQNIEI PEISLPIHPI ITNVAKQCYE RGEKPKVTDF GDKVEDPTFL
     NQLQSGVNRW IREIQKVTKL DRDPASGTAL QEISFWLNLE RALYRIQEKR ESPEVLLTLD
     ILKHGKRFHA TVSFDTDTGL KQALETVNDY NPLMKDFPLN DLLSATELDK IRQALVAIFT
     HLRKIRNTKY PIQRALRLVE AISRDLSSQL LKVLGTRKLM HVAYEEFEKV MVACFEVFQT
     WDDEYEKLQV LLRDIVKRKR EENLKMVWRI NPAHRKLQAR LDQMRKFRRQ HEQLRAVIVR
     VLRPQVTAVA QQNQGEAPEP QDMKVAEVLF DAADANAIEE VNLAYENVKE VDGLDVSKEG
     TEAWEAAMKR YDERIDRVET RITARLRDQL GTAKNANEMF RIFSRFNALF VRPHIRGAIR
     EYQTQLIQRV KDDIESLHDK FKVQYPQSQA CKMSHVRDLP PVSGSIIWAK QIDRQLTAYM
     KRVEDVLGKG WENHVEGQKL KQDGDSFRMK LNTQEIFDDW ARKVQQRNLG VSGRIFTIES
     ARVRGRTGNV LKLKVNFLPE IITLSKEVRN LKWLGFRVPL AIVNKAHQAN QLYPFAISLI
     ESVRTYERTC EKVEERNTIS LLVAGLKKEV QALIAEGIAL VWESYKLDPY VQRLAETVFN
     FQEKVDDLLI IEEKIDLEVR SLETCMYDHK TFSEILNRVQ KAVDDLNLHS YSNLPIWVNK
     LDMEIERILG VRLQAGLRAW TQVLLGQAED KAEVDMDTDA PQVSHKPGGE PKIKNVVHEL
     RITNQVIYLN PPIEECRYKL YQEMFAWKMV VLSLPRIQSQ RYQVGVHYEL TEEEKFYRNA
     LTRMPDGPVA LEESYSAVMG IVTEVEQYVK VWLQYQCLWD MQAENIYNRL GEDLNKWQAL
     LVQIRKARGT FDNAETKKEF GPVVIDYGKV QSKVNLKYDS WHKEVLSKFG QMLGSNMTEF
     HSQISKSRQE LEQHSVDTAS TSDAVTFITY VQSLKRKIKQ FEKQVELYRN GQRLLEKQRF
     QFPPSWLYID NIEGEWGAFN DIMRRKDSAI QQQVANLQMK IVQEDRAVES RTTDLLTDWE
     KTKPVTGNLR PEEALQALTI YEGKFGRLKD DREKCAKAKE ALELTDTGLL SGSEERVQVA
     LEELQDLKGV WSELSKVWEQ IDQMKEQPWV SVQPRKLRQN LDGLLNQLKN FPARLRQYAS
     YEFVQRLLKG YMKINMLVIE LKSEALKDRH WKQLMKRLHV NWVVSELTLG QIWDVDLQKN
     EAVVKDVLLV AQGEMALEEF LKQIREVWNT YELDLVNYQN KCRLIRGWDD LFNKVKEHIN
     SVSAMKLSPY YKVFEEDALS WEDKLNRIMA LFDVWIDVQR RWVYLEGIFT GSADIKHLLP
     VETQRFQSIS TEFLALMKKV SKSPLVMDVL NIQGVQRSLE RLADLLGKIQ KALGEYLERE
     RSSFPRFYFV GDEDLLEIIG NSKNVAKLQK HFKKMFAGVS SIILNEDNSV VLGISSREGE
     EVMFKTPVSI TEHPKINEWL TLVEKEMRVT LAKLLAESVT EVEIFGKATS IDPNTYITWI
     DKYQAQLVVL SAQIAWSENV ENALSNVGGG GDVGPLQSVL SNVEVTLNVL ADSVLMEQPP
     LRRRKLEHLI TELVHQRDVT RSLIKSKIDN AKSFEWLSQM RFYFDPKQTD VLQQLSIQMA
     NAKFNYGFEY LGVQDKLVQT PLTDRCYLTM TQALEARLGG SPFGPAGTGK TESVKALGHQ
     LGRFVLVFNC DETFDFQAMG RIFVGLCQVG AWGCFDEFNR LEERMLSAVS QQVQCIQEAL
     REHSNPNYDK TSAPITCELL NKQVKVSPDM AIFITMNPGY AGRSNLPDNL KKLFRSLAMT
     KPDRQLIAQV MLYSQGFRTA EVLANKIVPF FKLCDEQLSS QSHYDFGLRA LKSVLVSAGN
     VKRERIQKIK REKEERGEAV DEGEIAENLP EQEILIQSVC ETMVPKLVAE DIPLLFSLLS
     DVFPGVQYHR GEMTALREEL KKVCQEMYLT YGDGEEVGGM WVEKVLQLYQ ITQINHGLMM
     VGPSGSGKSM AWRVLLKALE RLEGVEGVAH IIDPKAISKD HLYGTLDPNT REWTDGLFTH
     VLRKIIDNVR GELQKRQWIV FDGDVDPEWV ENLNSVLDDN KLLTLPNGER LSLPPNVRIM
     FEVQDLKYAT LATVSRCGMV WFSEDVLSTD MIFNNFLARL RSIPLDEGED EAQRRRKGKE
     DEGEEAASPM LQIQRDAATI MQPYFTSNGL VTKALEHAFK LEHIMDLTRL RCLGSLFSML
     HQACRNVAQY NANHPDFPMQ IEQLERYIQR YLVYAILWSL SGDSRLKMRA ELGEYIRRIT
     TVPLPTAPNV PIIDYEVSIS GEWSPWQAKV PQIEVETHKV AAPDVVVPTL DTVRHEALLY
     TWLAEHKPLV LCGPPGSGKT MTLFSALRAL PDMEVVGLNF SSATTPELLL KTFDHYCEYR
     RTPNGVVLAP VQLGKWLVLF CDEINLPDMD KYGTQRVISF IRQMVEHGGF YRTSDQTWVK
     LERIQFVGAC NPPTDPGRKP LSHRFLRHVP VVYVDYPGPA SLTQIYGTFN RAMLRLIPSL
     RTYAEPLTAA MVEFYTMSQE RFTQDTQPHY IYSPREMTRW VRGIFEALRP LETLPVEGLI
     RIWAHEALRL FQDRLVEDEE RRWTDENIDM VALKHFPNID KEKAMSRPIL YSNWLSKDYI
     PVDQEELRDY VKARLKVFYE EELDVPLVLF NEVLDHVLRI DRIFRQPQGH LLLIGVSGAG
     KTTLSRFVAW MNGLSVYQIK VHRKYTGEDF DEDLRTVLRR SGCKNEKIAF IMDESNVLDS
     GFLERMNTLL ANGEVPGLFE GDEYATLMTQ CKEGAQKEGL MLDSHEELYK WFTSQVIRNL
     HVVFTMNPSS EGLKDRAATS PALFNRCVLN WFGDWSTEAL YQVGKEFTSK MDLEKPNYIV
     PDYMPVVYDK LPQPPTHREA IVNSCVFVHQ TLHQANARLA KRGGRTMAIT PRHYLDFINH
     YANLFHEKRS ELEEQQMHLN VGLRKIKETV DQVEELRRDL RIKSQELEVK NAAANDKLKK
     MVKDQQEAEK KKVMSQEIQE QLHKQQEVIA DKQMSVKEDL DKVEPAVIEA QNAVKSIKKQ
     HLVEVRSMAN PPAAVKLALE SICLLLGEST TDWKQIRSII MRENFIPTIV NFSAEEISDA
     IREKMKKNYM SNPSYNYEIV NRASLACGPM VKWAIAQLNY ADMLKRVEPL RNELQKLEDD
     AKDNQQKANE VEQMIRDLEA SIARYKEEYA VLISEAQAIK ADLAAVEAKV NRSTALLKSL
     SAERERWEKT SETFKNQMST IAGDCLLSAA FIAYAGYFDQ QMRQNLFTTW SHHLQQANIQ
     FRTDIARTEY LSNADERLRW QASSLPADDL CTENAIMLKR FNRYPLIIDP SGQATEFIMN
     EYKDRKITRT SFLDDAFRKN LESALRFGNP LLVQDVESYD PVLNPVLNRE VRRTGGRVLI
     TLGDQDIDLS PSFVIFLSTR DPTVEFPPDL CSRVTFVNFT VTRSSLQSQC LNEVLKAERP
     DVDEKRSDLL KLQGEFQLRL RQLEKSLLQA LNEVKGRILD DDTIITTLEN LKREAAEVTR
     KVEETDIVMQ EVETVSQQYL PLSTACSSIY FTMESLKQVH FLYQYSLQFF LDIYHNVLYE
     NPNLKGATDH TQRLSIITKD LFQVAFNRVA RGMLHQDHIT FAMLLARIKL KGTVGEPTYD
     AEFQHFLRGK EIVLSAGSTP KIQGLTVEQA EAVVRLSCLP AFKDLIAKVQ ADEQFGIWLD
     SSSPEQTVPY LWSEETPTTP IGQAIHRLLL IQAFRPDRLL AMAHMFVSTN LGESFMSIME
     QPLDLTHIVG TEVKPNTPVL MCSVPGYDAS GHVEDLAAEQ NTQITSIAIG SAEGFNQADK
     AINTAVKSGR WVMLKNVHLA PGWLMQLEKK LHSLQPHACF RLFLTMEINP KVPVNLLRAG
     RIFVFEPPPG VKANMLRTFS SIPVSRICKS PNERARLYFL LAWFHAIIQE RLRYAPLGWS
     KKYEFGESDL RSACDTVDTW LDDTAKGRQN ISPDKIPWSA LKTLMAQSIY GGRVDNEFDQ
     RLLNTFLERL FTTRSFDSEF KLACKVDGHK DIQMPDGIRR EEFVQWVELL PDAQTPSWLG
     LPNNAERVLL TTQGVDMISK MLKMQMLEDE DDLAYAETEK KARTDSTSDG RPAWMRTLHT
     TASNWLHLIP QTLSPLKRTV ENIKDPLFRF FEREVKMGAK LLQDVRQDLA DVVQVCEGKK
     KQTNYLRTLI NELVKGILPR SWSHYTVPAG MTVIQWVSDF SERIKQLQNI SQAAASGGAK
     ELKNIHVCLG GLFVPEAYIT ATRQYVAQAN SWSLEELCLE VNVTASQSAT LDACSFGVTG
     LKLQGATCSN NKLSLSNAIS TVLPLTQLRW VKQTSAEKKA SVVTLPVYLN FTRADLIFTV
     DFEIATKEDP RSFYERGVAV LCTE
//