MDN1_HUMAN
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 03-AUG-2022, entry version 185.
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; 178.
DR IntAct; Q9NU22; 46.
DR MINT; Q9NU22; -.
DR STRING; 9606.ENSP00000358400; -.
DR ChEMBL; CHEMBL4105779; -.
DR GlyConnect; 2010; 9 N-Linked glycans (1 site).
DR GlyGen; Q9NU22; 2 sites, 9 N-linked glycans (1 site), 1 O-linked glycan (1 site).
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; Q9NU22; -.
DR PeptideAtlas; Q9NU22; -.
DR PRIDE; Q9NU22; -.
DR ProteomicsDB; 82649; -.
DR Antibodypedia; 31873; 16 antibodies from 9 providers.
DR DNASU; 23195; -.
DR Ensembl; ENST00000369393.8; ENSP00000358400.3; ENSG00000112159.12.
DR Ensembl; ENST00000629399.2; ENSP00000486270.1; ENSG00000112159.12.
DR Ensembl; ENST00000672983.1; ENSP00000499895.1; ENSG00000288121.1.
DR Ensembl; ENST00000673332.1; ENSP00000499843.1; ENSG00000288121.1.
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 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; ELGPPNI; -.
DR OrthoDB; 138219at2759; -.
DR PhylomeDB; Q9NU22; -.
DR TreeFam; TF300488; -.
DR PathwayCommons; Q9NU22; -.
DR SignaLink; Q9NU22; -.
DR SIGNOR; Q9NU22; -.
DR BioGRID-ORCS; 23195; 788 hits in 1089 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 92 other tissues.
DR ExpressionAtlas; Q9NU22; baseline and differential.
DR Genevisible; Q9NU22; HS.
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:2000200; P:regulation of ribosomal subunit export from nucleus; IBA:GO_Central.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IDA:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 7.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR040848; AAA_lid_7.
DR InterPro; IPR011704; ATPase_dyneun-rel_AAA.
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 Pfam; PF07728; AAA_5; 8.
DR Pfam; PF17865; AAA_lid_5; 1.
DR Pfam; PF17867; AAA_lid_7; 3.
DR PIRSF; PIRSF010340; Midasin; 1.
DR SMART; SM00382; AAA; 6.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF52540; SSF52540; 6.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50234; VWFA; 1.
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
