DC1L1_HUMAN
ID DC1L1_HUMAN Reviewed; 523 AA.
AC Q9Y6G9; A2RRG7; Q53HC8; Q53HK7;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Cytoplasmic dynein 1 light intermediate chain 1;
DE Short=LIC1;
DE AltName: Full=Dynein light chain A;
DE Short=DLC-A;
DE AltName: Full=Dynein light intermediate chain 1, cytosolic;
GN Name=DYNC1LI1; Synonyms=DNCLI1;
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], AND VARIANT ARG-277.
RC TISSUE=Pituitary;
RA Dai M., Peng Y., Song H., Huang Q., Mao Y., Zhang Q., Mao M., Fu G.,
RA Luo M., Chen J., Hu R.;
RT "Human dynein light chain-A mRNA, complete cds.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-277.
RC TISSUE=Cerebellum, and Coronary artery;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-398 AND SER-487, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; THR-213; SER-419;
RP SER-421; SER-510; THR-512; THR-513; THR-515 AND SER-516, AND IDENTIFICATION
RP 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 [12]
RP IDENTIFICATION BY MASS 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 [13]
RP FUNCTION IN THE SPINDLE ASSEMBLY CHECKPOINT, SUBUNIT, PHOSPHORYLATION AT
RP SER-207; SER-398; SER-405 AND THR-408, AND SUBCELLULAR LOCATION.
RX PubMed=19229290; DOI=10.1038/emboj.2009.38;
RA Sivaram M.V., Wadzinski T.L., Redick S.D., Manna T., Doxsey S.J.;
RT "Dynein light intermediate chain 1 is required for progress through the
RT spindle assembly checkpoint.";
RL EMBO J. 28:902-914(2009).
RN [14]
RP INTERACTION WITH HUMAN ADENOVIRUS HEXON PROTEIN (MICROBIAL INFECTION).
RX PubMed=20006841; DOI=10.1016/j.chom.2009.11.006;
RA Bremner K.H., Scherer J., Yi J., Vershinin M., Gross S.P., Vallee R.B.;
RT "Adenovirus transport via direct interaction of cytoplasmic dynein with the
RT viral capsid hexon subunit.";
RL Cell Host Microbe 6:523-535(2009).
RN [15]
RP IDENTIFICATION BY 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-510; THR-512;
RP THR-513; THR-515 AND SER-516, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-398; SER-419;
RP SER-421; SER-487 AND SER-516, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND SER-516, 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-398; SER-405;
RP THR-408; SER-412; SER-421; SER-427; SER-487; SER-510 AND SER-516, AND
RP IDENTIFICATION BY MASS 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND SER-510, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Acts as one of several non-catalytic accessory components of
CC the cytoplasmic dynein 1 complex that are thought to be involved in
CC linking dynein to cargos and to adapter proteins that regulate dynein
CC function. Cytoplasmic dynein 1 acts as a motor for the intracellular
CC retrograde motility of vesicles and organelles along microtubules. May
CC play a role in binding dynein to membranous organelles or chromosomes.
CC Probably involved in the microtubule-dependent transport of
CC pericentrin. Is required for progress through the spindle assembly
CC checkpoint. The phosphorylated form appears to be involved in the
CC selective removal of MAD1L1 and MAD1L2 but not BUB1B from kinetochores.
CC {ECO:0000269|PubMed:19229290}.
CC -!- SUBUNIT: Homodimer (By similarity). The cytoplasmic dynein 1 complex
CC consists of two catalytic heavy chains (HCs) and a number of non-
CC catalytic subunits presented by intermediate chains (ICs), light
CC intermediate chains (LICs) and light chains (LCs); the composition
CC seems to vary in respect to the IC, LIC and LC composition. The heavy
CC chain homodimer serves as a scaffold for the probable homodimeric
CC assembly of the respective non-catalytic subunits. The ICs and LICs
CC bind directly to the HC dimer and the LCs assemble on the IC dimer.
CC Self-associates. Interacts with DYNC1H1; DYNC1LI1 and DYNC1LI2 bind
CC mutually exclusive to DYNC1H1. Interacts with PCNT (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:19229290}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human adenovirus 5 hexon
CC protein; this interaction probably allows virus intracellular
CC transport. {ECO:0000269|PubMed:20006841}.
CC -!- INTERACTION:
CC Q9Y6G9; P15259: PGAM2; NbExp=3; IntAct=EBI-2556107, EBI-2511669;
CC Q9Y6G9; Q04864: REL; NbExp=4; IntAct=EBI-2556107, EBI-307352;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Chromosome, centromere,
CC kinetochore {ECO:0000269|PubMed:19229290}. Cytoplasm, cytoskeleton,
CC spindle pole {ECO:0000269|PubMed:19229290}.
CC -!- PTM: Phosphorylated during mitosis but not in interphase.
CC {ECO:0000269|PubMed:19229290}.
CC -!- SIMILARITY: Belongs to the dynein light intermediate chain family.
CC {ECO:0000305}.
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DR EMBL; AF078849; AAD44481.1; -; mRNA.
DR EMBL; AK222573; BAD96293.1; -; mRNA.
DR EMBL; AK222653; BAD96373.1; -; mRNA.
DR EMBL; CH471055; EAW64433.1; -; Genomic_DNA.
DR EMBL; BC131620; AAI31621.1; -; mRNA.
DR CCDS; CCDS2654.1; -.
DR RefSeq; NP_057225.2; NM_016141.3.
DR PDB; 6B9H; X-ray; 1.50 A; B=433-458.
DR PDB; 6PSD; X-ray; 2.66 A; B/D/F/H/J/L/N/P=433-457.
DR PDB; 6PSE; X-ray; 2.40 A; C=433-458.
DR PDBsum; 6B9H; -.
DR PDBsum; 6PSD; -.
DR PDBsum; 6PSE; -.
DR AlphaFoldDB; Q9Y6G9; -.
DR SMR; Q9Y6G9; -.
DR BioGRID; 119327; 153.
DR CORUM; Q9Y6G9; -.
DR IntAct; Q9Y6G9; 38.
DR MINT; Q9Y6G9; -.
DR STRING; 9606.ENSP00000273130; -.
DR GlyGen; Q9Y6G9; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q9Y6G9; -.
DR MetOSite; Q9Y6G9; -.
DR PhosphoSitePlus; Q9Y6G9; -.
DR SwissPalm; Q9Y6G9; -.
DR BioMuta; DYNC1LI1; -.
DR DMDM; 134047749; -.
DR CPTAC; CPTAC-965; -.
DR EPD; Q9Y6G9; -.
DR jPOST; Q9Y6G9; -.
DR MassIVE; Q9Y6G9; -.
DR MaxQB; Q9Y6G9; -.
DR PaxDb; Q9Y6G9; -.
DR PeptideAtlas; Q9Y6G9; -.
DR PRIDE; Q9Y6G9; -.
DR ProteomicsDB; 86677; -.
DR Antibodypedia; 27761; 243 antibodies from 24 providers.
DR DNASU; 51143; -.
DR Ensembl; ENST00000273130.9; ENSP00000273130.4; ENSG00000144635.9.
DR GeneID; 51143; -.
DR KEGG; hsa:51143; -.
DR MANE-Select; ENST00000273130.9; ENSP00000273130.4; NM_016141.4; NP_057225.2.
DR UCSC; uc003cfb.4; human.
DR CTD; 51143; -.
DR DisGeNET; 51143; -.
DR GeneCards; DYNC1LI1; -.
DR HGNC; HGNC:18745; DYNC1LI1.
DR HPA; ENSG00000144635; Low tissue specificity.
DR MIM; 615890; gene.
DR neXtProt; NX_Q9Y6G9; -.
DR OpenTargets; ENSG00000144635; -.
DR PharmGKB; PA38670; -.
DR VEuPathDB; HostDB:ENSG00000144635; -.
DR eggNOG; KOG3905; Eukaryota.
DR GeneTree; ENSGT00390000008295; -.
DR HOGENOM; CLU_021937_2_1_1; -.
DR InParanoid; Q9Y6G9; -.
DR OMA; RCNIWIL; -.
DR OrthoDB; 1299592at2759; -.
DR PhylomeDB; Q9Y6G9; -.
DR TreeFam; TF352602; -.
DR PathwayCommons; Q9Y6G9; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9646399; Aggrephagy.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; Q9Y6G9; -.
DR SIGNOR; Q9Y6G9; -.
DR BioGRID-ORCS; 51143; 33 hits in 1081 CRISPR screens.
DR ChiTaRS; DYNC1LI1; human.
DR GeneWiki; DYNC1LI1; -.
DR GenomeRNAi; 51143; -.
DR Pharos; Q9Y6G9; Tbio.
DR PRO; PR:Q9Y6G9; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9Y6G9; protein.
DR Bgee; ENSG00000144635; Expressed in cortical plate and 206 other tissues.
DR ExpressionAtlas; Q9Y6G9; baseline and differential.
DR Genevisible; Q9Y6G9; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0045504; F:dynein heavy chain binding; IPI:FlyBase.
DR GO; GO:0019003; F:GDP binding; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; IMP:UniProtKB.
DR DisProt; DP02547; -.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR008467; Dynein1_light_intermed_chain.
DR InterPro; IPR022780; Dynein_light_int_chain.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12688; PTHR12688; 1.
DR Pfam; PF05783; DLIC; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; Centromere;
KW Chromosome; Cytoplasm; Cytoskeleton; Dynein; Host-virus interaction;
KW Kinetochore; Microtubule; Mitosis; Motor protein; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..523
FT /note="Cytoplasmic dynein 1 light intermediate chain 1"
FT /id="PRO_0000114666"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 74..81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19229290,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 213
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19229290,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19229290,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 408
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19229290,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 512
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 513
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 515
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VARIANT 147
FT /note="M -> T (in dbSNP:rs34181332)"
FT /id="VAR_061141"
FT VARIANT 277
FT /note="Q -> R (in dbSNP:rs2303857)"
FT /evidence="ECO:0000269|Ref.1, ECO:0000269|Ref.2"
FT /id="VAR_023325"
FT CONFLICT 186
FT /note="M -> I (in Ref. 2; BAD96293)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="R -> G (in Ref. 2; BAD96293)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="L -> V (in Ref. 1; AAD44481)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="I -> F (in Ref. 1; AAD44481)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="D -> G (in Ref. 2; BAD96293)"
FT /evidence="ECO:0000305"
FT HELIX 443..453
FT /evidence="ECO:0007829|PDB:6B9H"
SQ SEQUENCE 523 AA; 56579 MW; 29159F560E382095 CRC64;
MAAVGRVGSF GSSPPGLSST YTGGPLGNEI ASGNGGAAAG DDEDGQNLWS CILSEVSTRS
RSKLPAGKNV LLLGEDGAGK TSLIRKIQGI EEYKKGRGLE YLYLNVHDED RDDQTRCNVW
ILDGDLYHKG LLKFSLDAVS LKDTLVMLVV DMSKPWTALD SLQKWASVVR EHVDKLKIPP
EEMKQMEQKL IRDFQEYVEP GEDFPASPQR RNTASQEDKD DSVVLPLGAD TLTHNLGIPV
LVVCTKCDAI SVLEKEHDYR DEHFDFIQSH IRKFCLQYGA ALIYTSVKEN KNIDLVYKYI
VQKLYGFPYK IPAVVVEKDA VFIPAGWDND KKIGILHENF QTLKAEDNFE DIITKPPVRK
FVHEKEIMAE DDQVFLMKLQ SLLAKQPPTA AGRPVDASPR VPGGSPRTPN RSVSSNVASV
SPIPAGSKKI DPNMKAGATS EGVLANFFNS LLSKKTGSPG GPGVSGGSPA GGAGGGSSGL
PPSTKKSGQK PVLDVHAELD RITRKPVTVS PTTPTSPTEG EAS
