ID   MDN1_HUMAN              Reviewed;        5596 AA.
AC   Q9NU22; O15019; Q5T794;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2002, sequence version 2.
DT   27-MAR-2024, entry version 194.
DE   RecName: Full=Midasin;
DE   AltName: Full=Dynein-related AAA-ATPase MDN1;
DE   AltName: Full=MIDAS-containing protein;
GN   Name=MDN1; Synonyms=KIAA0301;
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].
RC   TISSUE=Testis;
RX   PubMed=12102729; DOI=10.1186/1471-2164-3-18;
RA   Garbarino J.E., Gibbons I.R.;
RT   "Expression and genomic analysis of midasin, a novel and highly conserved
RT   AAA protein distantly related to dynein.";
RL   BMC Genomics 3:18-18(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2387-5596.
RC   TISSUE=Brain;
RX   PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA   Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. VII. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 4:141-150(1997).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4898, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4538 AND THR-4898, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4538 AND THR-4898, AND
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   [7]
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4538, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4538 AND SER-4752, AND
RP   IDENTIFICATION 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   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1683, 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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4538 AND THR-4898, AND
RP   IDENTIFICATION 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., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [12]
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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1177; SER-4538; SER-4752;
RP   SER-4754; SER-4889; THR-4898; SER-4937; SER-4946 AND SER-5015, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [14]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=22002106; DOI=10.1074/mcp.m111.013680;
RA   Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.;
RT   "Systematic analysis of protein pools, isoforms, and modifications
RT   affecting turnover and subcellular localization.";
RL   Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1754; THR-4212; SER-4538;
RP   SER-4752; SER-4754; THR-4898 AND SER-5015, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and 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   [16]
RP   INTERACTION WITH WDR12 AND NLE1, AND SUBCELLULAR LOCATION.
RX   PubMed=26601951; DOI=10.1074/jbc.m115.693259;
RA   Romes E.M., Sobhany M., Stanley R.E.;
RT   "The crystal structure of the ubiquitin-like domain of ribosome assembly
RT   factor Ytm1 and characterization of its interaction with the AAA-ATPase
RT   Midasin.";
RL   J. Biol. Chem. 291:882-893(2016).
RN   [17]
RP   FUNCTION, AND INTERACTION WITH PELP1 AND SUMO2.
RX   PubMed=27814492; DOI=10.1016/j.molcel.2016.09.039;
RA   Raman N., Weir E., Mueller S.;
RT   "The AAA ATPase MDN1 acts as a SUMO-targeted regulator in mammalian pre-
RT   ribosome remodeling.";
RL   Mol. Cell 64:607-615(2016).
CC   -!- FUNCTION: Nuclear chaperone required for maturation and nuclear export
CC       of pre-60S ribosome subunits (PubMed:27814492). Functions at successive
CC       maturation steps to remove ribosomal factors at critical transition
CC       points, first driving the exit of early pre-60S particles from the
CC       nucleolus and then driving late pre-60S particles from the nucleus (By
CC       similarity). At an early stage in 60S maturation, mediates the
CC       dissociation of the PeBoW complex (PES1-BOP1-WDR12) from early pre-60S
CC       particles, rendering them competent for export from the nucleolus to
CC       the nucleoplasm (By similarity). Subsequently recruited to the
CC       nucleoplasmic particles through interaction with SUMO-conjugated PELP1
CC       complex (PubMed:27814492). This binding is only possible if the 5S RNP
CC       at the central protuberance has undergone the rotation to complete its
CC       maturation (By similarity). {ECO:0000250|UniProtKB:Q12019,
CC       ECO:0000269|PubMed:27814492}.
CC   -!- SUBUNIT: Associates with pre-60S ribosomes in the nucleoplasm.
CC       Interacts (via its hexameric AAA ATPase ring) with the PELP1 complex
CC       (via PELP1); the interaction is regulated by SUMO conjugation of PELP1
CC       and is crucial for recruitment of MDN1 to the pre-ribosomal particle
CC       (PubMed:27814492). Interacts (via VWFA/MIDAS domain) with WDR12 (via
CC       UBL domain) (PubMed:26601951). Interacts (via VWFA/MIDAS domain) with
CC       NLE1 (via UBL domain) (PubMed:26601951). {ECO:0000269|PubMed:26601951,
CC       ECO:0000269|PubMed:27814492}.
CC   -!- INTERACTION:
CC       Q9NU22; Q8IZL8: PELP1; NbExp=3; IntAct=EBI-1050480, EBI-716449;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:22002106}.
CC       Nucleus, nucleoplasm {ECO:0000269|PubMed:26601951}. Cytoplasm
CC       {ECO:0000269|PubMed:26601951}.
CC   -!- SIMILARITY: Belongs to the midasin family.
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DR   EMBL; AF503925; AAM77722.1; -; mRNA.
DR   EMBL; AL096678; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL158813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL353692; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB002299; BAA20761.2; -; mRNA.
DR   CCDS; CCDS5024.1; -.
DR   RefSeq; NP_055426.1; NM_014611.2.
DR   SMR; Q9NU22; -.
DR   BioGRID; 116804; 211.
DR   ComplexPortal; CPX-8081; Rixosome RNA degradation complex.
DR   IntAct; Q9NU22; 60.
DR   MINT; Q9NU22; -.
DR   STRING; 9606.ENSP00000358400; -.
DR   ChEMBL; CHEMBL4105779; -.
DR   GlyConnect; 2010; 9 N-Linked glycans (1 site).
DR   GlyCosmos; Q9NU22; 1 site, 9 glycans.
DR   GlyGen; Q9NU22; 3 sites, 9 N-linked glycans (1 site), 1 O-linked glycan (2 sites).
DR   iPTMnet; Q9NU22; -.
DR   PhosphoSitePlus; Q9NU22; -.
DR   SwissPalm; Q9NU22; -.
DR   BioMuta; MDN1; -.
DR   DMDM; 24212017; -.
DR   EPD; Q9NU22; -.
DR   jPOST; Q9NU22; -.
DR   MassIVE; Q9NU22; -.
DR   MaxQB; Q9NU22; -.
DR   PaxDb; 9606-ENSP00000358400; -.
DR   PeptideAtlas; Q9NU22; -.
DR   ProteomicsDB; 82649; -.
DR   Pumba; Q9NU22; -.
DR   Antibodypedia; 31873; 18 antibodies from 10 providers.
DR   DNASU; 23195; -.
DR   Ensembl; ENST00000369393.8; ENSP00000358400.3; ENSG00000112159.13.
DR   GeneID; 23195; -.
DR   KEGG; hsa:23195; -.
DR   MANE-Select; ENST00000369393.8; ENSP00000358400.3; NM_014611.3; NP_055426.1.
DR   UCSC; uc003pnn.2; human.
DR   AGR; HGNC:18302; -.
DR   CTD; 23195; -.
DR   DisGeNET; 23195; -.
DR   GeneCards; MDN1; -.
DR   HGNC; HGNC:18302; MDN1.
DR   HPA; ENSG00000112159; Low tissue specificity.
DR   MIM; 618200; gene.
DR   neXtProt; NX_Q9NU22; -.
DR   OpenTargets; ENSG00000112159; -.
DR   PharmGKB; PA30720; -.
DR   VEuPathDB; HostDB:ENSG00000112159; -.
DR   eggNOG; KOG1808; Eukaryota.
DR   GeneTree; ENSGT00550000074802; -.
DR   HOGENOM; CLU_000050_0_0_1; -.
DR   InParanoid; Q9NU22; -.
DR   OMA; ILEQWHR; -.
DR   OrthoDB; 1221059at2759; -.
DR   PhylomeDB; Q9NU22; -.
DR   TreeFam; TF300488; -.
DR   PathwayCommons; Q9NU22; -.
DR   SignaLink; Q9NU22; -.
DR   SIGNOR; Q9NU22; -.
DR   BioGRID-ORCS; 23195; 822 hits in 1166 CRISPR screens.
DR   ChiTaRS; MDN1; human.
DR   GeneWiki; MDN1; -.
DR   GenomeRNAi; 23195; -.
DR   Pharos; Q9NU22; Tdark.
DR   PRO; PR:Q9NU22; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q9NU22; Protein.
DR   Bgee; ENSG00000112159; Expressed in right lobe of liver and 94 other cell types or tissues.
DR   ExpressionAtlas; Q9NU22; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0000027; P:ribosomal large subunit assembly; IDA:UniProtKB.
DR   GO; GO:0000055; P:ribosomal large subunit export from nucleus; IBA:GO_Central.
DR   CDD; cd00009; AAA; 2.
DR   CDD; cd01460; vWA_midasin; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 7.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR040848; AAA_lid_7.
DR   InterPro; IPR011704; ATPase_dyneun-rel_AAA.
DR   InterPro; IPR048617; MDN1_AAA_lid_4.
DR   InterPro; IPR012099; Midasin.
DR   InterPro; IPR041190; Midasin_AAA_lid_5.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR48103:SF2; MIDASIN; 1.
DR   PANTHER; PTHR48103; MIDASIN-RELATED; 1.
DR   Pfam; PF07728; AAA_5; 8.
DR   Pfam; PF17865; AAA_lid_5; 1.
DR   Pfam; PF17867; AAA_lid_7; 3.
DR   Pfam; PF21108; MDN1_4th; 1.
DR   PIRSF; PIRSF010340; Midasin; 1.
DR   SMART; SM00382; AAA; 6.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 6.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS50234; VWFA; 1.
DR   Genevisible; Q9NU22; HS.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..5596
FT                   /note="Midasin"
FT                   /id="PRO_0000096336"
FT   DOMAIN          5384..5583
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   REGION          307..591
FT                   /note="AAA-ATPase protomer 1"
FT                   /evidence="ECO:0000255"
FT   REGION          517..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          659..978
FT                   /note="AAA-ATPase protomer 2"
FT                   /evidence="ECO:0000255"
FT   REGION          1048..1316
FT                   /note="AAA-ATPase protomer 3"
FT                   /evidence="ECO:0000255"
FT   REGION          1362..1616
FT                   /note="AAA-ATPase protomer 4"
FT                   /evidence="ECO:0000255"
FT   REGION          1738..1995
FT                   /note="AAA-ATPase protomer 5"
FT                   /evidence="ECO:0000255"
FT   REGION          2053..2313
FT                   /note="AAA-ATPase protomer 6"
FT                   /evidence="ECO:0000255"
FT   REGION          2418..4691
FT                   /note="Linker"
FT                   /evidence="ECO:0000250|UniProtKB:Q12019"
FT   REGION          3989..4008
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          4669..4688
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          4700..5260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4701..4740
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4755..4775
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4776..4811
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4817..4893
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4907..4931
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4941..4963
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4964..4995
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        5076..5091
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        5101..5127
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        5195..5210
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        5228..5260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         329..336
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         677..684
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         1084..1091
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         1390..1397
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         1753..1760
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2066..2073
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   MOD_RES         1177
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         1683
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         1754
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         4212
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         4538
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         4752
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         4754
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         4889
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         4898
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         4937
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         4946
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         5015
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   VARIANT         440
FT                   /note="F -> V (in dbSNP:rs4707569)"
FT                   /id="VAR_024234"
FT   VARIANT         660
FT                   /note="I -> V (in dbSNP:rs12110451)"
FT                   /id="VAR_051171"
FT   VARIANT         1044
FT                   /note="A -> V (in dbSNP:rs34764513)"
FT                   /id="VAR_051172"
FT   VARIANT         1559
FT                   /note="S -> N (in dbSNP:rs4140446)"
FT                   /id="VAR_024235"
FT   VARIANT         1929
FT                   /note="H -> D (in dbSNP:rs16882099)"
FT                   /id="VAR_051173"
FT   VARIANT         2972
FT                   /note="H -> P (in dbSNP:rs34208137)"
FT                   /id="VAR_051174"
FT   VARIANT         3004
FT                   /note="E -> K (in dbSNP:rs12530146)"
FT                   /id="VAR_051175"
FT   VARIANT         3423
FT                   /note="H -> Y (in dbSNP:rs9294445)"
FT                   /id="VAR_051176"
FT   VARIANT         3794
FT                   /note="A -> G (in dbSNP:rs34766278)"
FT                   /id="VAR_051177"
FT   VARIANT         3986
FT                   /note="R -> L (in dbSNP:rs17293121)"
FT                   /id="VAR_051178"
FT   VARIANT         4044
FT                   /note="A -> S (in dbSNP:rs9353689)"
FT                   /id="VAR_024236"
FT   VARIANT         4167
FT                   /note="A -> T (in dbSNP:rs35509794)"
FT                   /id="VAR_051179"
FT   VARIANT         4720
FT                   /note="I -> T (in dbSNP:rs16882046)"
FT                   /id="VAR_051180"
FT   VARIANT         4783
FT                   /note="D -> E (in dbSNP:rs36040566)"
FT                   /id="VAR_051181"
FT   VARIANT         5251
FT                   /note="N -> K (in dbSNP:rs4707557)"
FT                   /id="VAR_051182"
SQ   SEQUENCE   5596 AA;  632820 MW;  586C62616A1F96D4 CRC64;
     MEHFLLEVAA APLRLIAAKN EKSRSELGRF LAKQVWTPQD RQCVLSTLAQ LLLDKDCTVL
     VGRQLRPLLL DLLERNAEAI KAGGQINHDL HERLCVSMSK LIGNHPDVLP FALRYFKDTS
     PVFQRLFLES SDANPVRYGR RRMKLRDLME AAFKFLQQEQ SVFRELWDWS VCVPLLRSHD
     TLVRWYTANC LALVTCMNEE HKLSFLKKIF NSDELIHFRL RLLEEAQLQD LEKALVLANP
     EVSLWRKQKE LQYLQGHLVS SDLSPRVTAV CGVVLPGQLP APGELGGNRS SSREQELALR
     SYVLVESVCK SLQTLAMAVA SQNAVLLEGP IGCGKTSLVE YLAAVTGRTK PPQLLKVQLG
     DQTDSKMLLG MYRCTDVPGE FVWQPGTLTQ AATMGHWILL EDIDYAPLDV VSVLIPLLEN
     GELLIPGRGD CLKVAPGFQF FATRRLLSCG GNWYRPLNSH ATLLDKYWTK IHLDNLDKRE
     LNEVLQSRYP SLLAVVDHLL DIYIQLTGEK HHSWSDSSVG CEQAPEEVSE ARRENKRPTL
     EGRELSLRDL LNWCNRIAHS FDSSSLSASL NIFQEALDCF TAMLSEHTSK LKMAEVIGSK
     LNISRKKAEF FCQLYKPEIV INELDLQVGR VRLLRKQSEA VHLQREKFTF AATRPSSVLI
     EQLAVCVSKG EPVLLVGETG TGKTSTIQYL AHITGHRLRV VNMNQQSDTA DLLGGYKPVD
     HKLIWLPLRE AFEELFAQTF SKKQNFTFLG HIQTCYRQKR WHDLLRLMQH VHKSAVNKDG
     KDSETGLLIK EKWEAFGLRL NHAQQQMKMT ENTLLFAFVE GTLAQAVKKG EWILLDEINL
     AAPEILECLS GLLEGSSGSL VLLDRGDTEP LVRHPDFRLF ACMNPATDVG KRNLPPGIRN
     RFTELYVEEL ESKEDLQVLI VDYLKGLSVN KNTVQGIINF YTALRKESGT KLVDGTGHRP
     HYSLRTLCRA LRFAASNPCG NIQRSLYEGF CLGFLTQLDR ASHPIVQKLI CQHIVPGNVK
     SLLKQPIPEP KGGRLIQVEG YWIAVGDKEP TIDETYILTS SVKLNLRDIV RVVSAGTYPV
     LIQGETSVGK TSLIQWLAAA TGNHCVRINN HEHTDIQEYI GCYTSDSSGK LVFKEGVLID
     AMRKGYWIIL DELNLAPTDV LEALNRLLDD NRELLVTETQ EVVKAHPRFM LFATQNPPGL
     YGGRKVLSRA FRNRFVELHF DELPSSELET ILHKRCSLPP SYCSKLVKVM LDLQSYRRSS
     SVFAGKQGFI TLRDLFRWAE RYRLAEPTEK EYDWLQHLAN DGYMLLAGRV RKQEEIDVIQ
     EVLEKHFKKK LCPQSLFSKE NVLKLLGKLS TQISTLECNF GHIVWTEGMR RLAMLVGRAL
     EFGEPVLLVG DTGCGKTTIC QVFAALANQK LYSVSCHLHM ETSDFLGGLR PVRQKPNDKE
     EIDTSRLFEW HDGPLVQAMK EDGFFLLDEI SLADDSVLER LNSVLEVEKS LVLAEKGSPE
     DKDSEIELLT AGKKFRILAT MNPGGDFGKK ELSPALRNRF TEIWCPQSTS REDLIQIISH
     NLRPGLCLGR IDPKGSDIPE VMLDFIDWLT HQEFGRKCVV SIRDILSWVN FMNKMGEEAA
     LKRPEIISTV TSFVHAACLV YIDGIGSGVT SSGFGTALLA RKECLKFLIK RLAKIVRLTE
     YQKNELKIYD RMKAKEFTGI DNLWGIHPFF IPRGPVLHRN NIADYALSAG TTAMNAQRLL
     RATKLKKPIL LEGSPGVGKT SLVGALAKAS GNTLVRINLS EQTDITDLFG ADLPVEGGKG
     GEFAWRDGPL LAALKAGHWV VLDELNLASQ SVLEGLNACF DHRGEIYVPE LGMSFQVQHE
     KTKIFGCQNP FRQGGGRKGL PRSFLNRFTQ VFVDPLTVID MEFIASTLFP AIEKNIVKKM
     VAFNNQIDHE VTVEKKWGQK GGPWEFNLRD LFRWCQLMLV DQSPGCYDPG QHVFLVYGER
     MRTEEDKKKV IAVFKDVFGS NSNPYMGTRL FRITPYDVQL GYSVLSRGSC VPHPSRHPLL
     LLHQSFQPLE SIMKCVQMSW MVILVGPASV GKTSLVQLLA HLTGHTLKIM AMNSAMDTTE
     LLGGFEQVDL IRPWRRLLEK VEGTVRALLR DSLLISADDA EVVLRAWSHF LLTYKPKCLG
     EGGKAITMEI VNKLEAVLLL MQRLNNKINS YCKAEFAKLV EEFRSFGVKL TQLASGHSHG
     TFEWVDSMLV QALKSGDWLL MDNVNFCNPS VLDRLNALLE PGGVLTISER GMIDGSTPTI
     TPNPNFRLFL SMDPVHGDIS RAMRNRGLEI YISGEGDAST PDNLDLKVLL HSLGLVGNSV
     CDILLALHTE TRSTVVGSPT SSVSTLIQTA ILIVQYLQRG LSLDRAFSEA CWEVYVCSQH
     SPANRKLVQA LLEKHVSSLR AHETWGDSIL GMGLWPDSVP SALFATEDSH LSTVRRDGQI
     LVYCLNRMSM KTSSWTRSQP FTLQDLEKIM QSPSPENLKF NAVEVNTYWI DEPDVLVMAV
     KLLIERATNQ DWMLRVKWLY HLAKNIPQGL ESIQIHLEAS AASLRNFYSH SLSGAVSNVF
     KILQPNTTDE FVIPLDPRWN MQALDMIRNL MDFDPQTDQP DQLFALLESA ANKTIIYLDR
     EKRVFTEANL VSVGSKKLRE SVLRMSFEFH QDPESYHTLP HEIVVNLAAF FELCDALVLL
     WVQSSQGMVS DASANEILGS LRWRDRFWTV ADTVKVDAPG LALLALHWHW VLKHLVHQIP
     RLLMNYEDKY YKEVQTVSEH IQNCLGSQTG GFAGIKKLQK FLGRPFPFKD KLVVECFSQL
     KVLNKVLAIR EQMSALGESG WQEDINRLQV VASQWTLKKS LLQAWGLILR ANILEDVSLD
     ELKNFVHAQC LELKAKGLSL GFLEKKHDEA SSLSHPDLTS VIHLTRSVQL WPAMEYLAML
     WRYKVTADFM AQACLRRCSK NQQPQINEEI SHLISFCLYH TPVTPQELRD LWSLLHHQKV
     SPEEITSLWS ELFNSMFMSF WSSTVTTNPE YWLMWNPLPG MQQREAPKSV LDSTLKGPGN
     LNRPIFSKCC FEVLTSSWRA SPWDVSGLPI LSSSHVTLGE WVERTQQLQD ISSMLWTNMA
     ISSVAEFRRT DSQLQGQVLF RHLAGLAELL PESRRQEYMQ NCEQLLLGSS QAFQHVGQTL
     GDMAGQEVLP KELLCQLLTS LHHFVGEGES KRSLPEPAQR GSLWVSLGLL QIQTWLPQAR
     FDPAVKREYK LNYVKEELHQ LQCEWKTRNL SSQLQTGRDL EDEVVVSYSH PHVRLLRQRM
     DRLDNLTCHL LKKQAFRPQL PAYESLVQEI HHYVTSIAKA PAVQDLLTRL LQALHIDGPR
     SAQVAQSLLK EEASWQQSHH QFRKRLSEEY TFYPDAVSPL QASILQLQHG MRLVASELHT
     SLHSSMVGAD RLGTLATALL AFPSVGPTFP TYYAHADTLC SVKSEEVLRG LGKLILKRSG
     GKELEGKGQK ACPTREQLLM NALLYLRSHV LCKGELDQRA LQLFRHVCQE IISEWDEQER
     IAQEKAEQES GLYRYRSRNS RTALSEEEEE EREFRKQFPL HEKDFADILV QPTLEENKGT
     SDGQEEEAGT NPALLSQNSM QAVMLIHQQL CLNFARSLWY QQTLPPHEAK HYLSLFLSCY
     QTGASLVTHF YPLMGVELND RLLGSQLLAC TLSHNTLFGE APSDLMVKPD GPYDFYQHPN
     VPEARQCQPV LQGFSEAVSH LLQDWPEHPA LEQLLVVMDR IRSFPLSSPI SKFLNGLEIL
     LAKAQDWEEN ASRALSLRKH LDLISQMIIR WRKLELNCWS MSLDNTMKRH TEKSTKHWFS
     IYQMLEKHMQ EQTEEQEDDK QMTLMLLVST LQAFIEGSSL GEFHVRLQML LVFHCHVLLM
     PQVEGKDSLC SVLWNLYHYY KQFFDRVQAK IVELRSPLEK ELKEFVKISK WNDVSFWSIK
     QSVEKTHRTL FKFMKKFEAV LSEPCRSSLV ESDKEEQPDF LPRPTDGAAS ELSSIQNLNR
     ALRETLLAQP AAGQATIPEW CQGAAPSGLE GELLRRLPKL RKRMRKMCLT FMKESPLPRL
     VEGLDQFTGE VISSVSELQS LKVEPSAEKE KQRSEAKHIL MQKQRALSDL FKHLAKIGLS
     YRKGLAWARS KNPQEMLHLH PLDLQSALSI VSSTQEADSR LLTEISSSWD GCQKYFYRSL
     ARHARLNAAL ATPAKEMGMG NVERCRGFSA HLMKMLVRQR RSLTTLSEQW IILRNLLSCV
     QEIHSRLMGP QAYPVAFPPQ DGVQQWTERL QHLAMQCQIL LEQLSWLLQC CPSVGPAPGH
     GNVQVLGQPP GPCLEGPELS KGQLCGVVLD LIPSNLSYPS PIPGSQLPSG CRMRKQDHLW
     QQSTTRLTEM LKTIKTVKAD VDKIRQQSCE TLFHSWKDFE VCSSALSCLS QVSVHLQGLE
     SLFILPGMEV EQRDSQMALV ESLEYVRGEI SKAMADFTTW KTHLLTSDSQ GGNQMLDEGF
     VEDFSEQMEI AIRAILCAIQ NLEERKNEKA EENTDQASPQ EDYAGFERLQ SGHLTKLLED
     DFWADVSTLH VQKIISAISE LLERLKSYGE DGTAAKHLFF SQSCSLLVRL VPVLSSYSDL
     VLFFLTMSLA THRSTAKLLS VLAQVFTELA QKGFCLPKEF MEDSAGEGAT EFHDYEGGGI
     GEGEGMKDVS DQIGNEEQVE DTFQKGQEKD KEDPDSKSDI KGEDNAIEMS EDFDGKMHDG
     ELEEQEEDDE KSDSEGGDLD KHMGDLNGEE ADKLDERLWG DDDEEEDEEE EDNKTEETGP
     GMDEEDSELV AKDDNLDSGN SNKDKSQQDK KEEKEEAEAD DGGQGEDKIN EQIDERDYDE
     NEVDPYHGNQ EKVPEPEALD LPDDLNLDSE DKNGGEDTDN EEGEEENPLE IKEKPEEAGH
     EAEERGETET DQNESQSPQE PEEGPSEDDK AEGEEEMDTG ADDQDGDAAQ HPEEHSEEQQ
     QSVEEKDKEA DEEGGENGPA DQGFQPQEEE EREDSDTEEQ VPEALERKEH ASCGQTGVEN
     MQNTQAMELA GAAPEKEQGK EEHGSGAADA NQAEGHESNF IAQLASQKHT RKNTQSFKRK
     PGQADNERSM GDHNERVHKR LRTVDTDSHA EQGPAQQPQA QVEDADAFEH IKQGSDAYDA
     QTYDVASKEQ QQSAKDSGKD QEEEEIEDTL MDTEEQEEFK AADVEQLKPE EIKSGTTAPL
     GFDEMEVEIQ TVKTEEDQDP RTDKAHKETE NEKPERSRES TIHTAHQFLM DTIFQPFLKD
     VNELRQELER QLEMWQPRES GNPEEEKVAA EMWQSYLILT APLSQRLCEE LRLILEPTQA
     AKLKGDYRTG KRLNIRKVIP YIASQFRKDK IWLRRTKPSK RQYQICLAID DSSSMVDNHT
     KQLAFESLAV IGNALTLLEV GQIAVCSFGE SVKLLHPFHE QFSDYSGSQI LRLCKFQQKK
     TKIAQFLESV ANMFAAAQQL SQNISSETAQ LLLVVSDGRG LFLEGKERVL AAVQAARNAN
     IFVIFVVLDN PSSRDSILDI KVPIFKGPGE MPEIRSYMEE FPFPYYIILR DVNALPETLS
     DALRQWFELV TASDHP
//