LBR_MOUSE
ID LBR_MOUSE Reviewed; 626 AA.
AC Q3U9G9; Q3TSW2; Q811V8; Q811V9; Q8BST3; Q8K2Y8; Q8VDM0; Q91YS5; Q91Z27;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Delta(14)-sterol reductase LBR;
DE Short=Delta-14-SR;
DE EC=1.3.1.70 {ECO:0000250|UniProtKB:Q14739};
DE AltName: Full=3-beta-hydroxysterol Delta (14)-reductase {ECO:0000303|PubMed:18785926};
DE AltName: Full=C-14 sterol reductase;
DE Short=C14SR;
DE AltName: Full=Integral nuclear envelope inner membrane protein {ECO:0000250|UniProtKB:Q14739};
DE AltName: Full=Lamin-B receptor {ECO:0000250|UniProtKB:Q14739};
DE AltName: Full=Sterol C14-reductase;
GN Name=Lbr;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Colon, Liver, Pituitary, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-308 AND 324-584.
RX PubMed=12490533; DOI=10.1093/hmg/ddg003;
RA Shultz L.D., Lyons B.L., Burzenski L.M., Gott B., Samuels R.,
RA Schweitzer P.A., Dreger C., Herrmann H., Kalscheuer V., Olins A.L.,
RA Olins D.E., Sperling K., Hoffmann K.;
RT "Mutations at the mouse ichthyosis locus are within the lamin B receptor
RT gene: a single gene model for human Pelger-Huet anomaly.";
RL Hum. Mol. Genet. 12:61-69(2003).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ;
RX PubMed=18785926; DOI=10.1111/j.1742-4658.2008.06637.x;
RA Bennati A.M., Schiavoni G., Franken S., Piobbico D., Della Fazia M.A.,
RA Caruso D., De Fabiani E., Benedetti L., Cusella De Angelis M.G.,
RA Gieselmann V., Servillo G., Beccari T., Roberti R.;
RT "Disruption of the gene encoding 3beta-hydroxysterol Delta14-reductase
RT (Tm7sf2) in mice does not impair cholesterol biosynthesis.";
RL FEBS J. 275:5034-5047(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-71 AND SER-103, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67 AND THR-128, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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 DEVELOPMENTAL STAGE.
RX PubMed=21327084; DOI=10.4161/nucl.1.4.12435;
RA Clayton P., Fischer B., Mann A., Mansour S., Rossier E., Veen M., Lang C.,
RA Baasanjav S., Kieslich M., Brossuleit K., Gravemann S., Schnipper N.,
RA Karbasyian M., Demuth I., Zwerger M., Vaya A., Utermann G., Mundlos S.,
RA Stricker S., Sperling K., Hoffmann K.;
RT "Mutations causing Greenberg dysplasia but not Pelger anomaly uncouple
RT enzymatic from structural functions of a nuclear membrane protein.";
RL Nucleus 1:354-366(2010).
RN [8]
RP FUNCTION.
RX PubMed=22140257; DOI=10.4049/jimmunol.1003804;
RA Subramanian G., Chaudhury P., Malu K., Fowler S., Manmode R., Gotur D.,
RA Zwerger M., Ryan D., Roberti R., Gaines P.;
RT "Lamin B receptor regulates the growth and maturation of myeloid
RT progenitors via its sterol reductase domain: implications for cholesterol
RT biosynthesis in regulating myelopoiesis.";
RL J. Immunol. 188:85-102(2012).
RN [9]
RP INTERACTION WITH CLNK.
RX PubMed=26009488; DOI=10.1016/j.bbrc.2015.05.046;
RA Xu M., Cai C., Sun X., Chen W., Li Q., Zhou H.;
RT "Clnk plays a role in TNF-alpha-induced cell death in murine fibrosarcoma
RT cell line L929.";
RL Biochem. Biophys. Res. Commun. 463:275-279(2015).
CC -!- FUNCTION: Catalyzes the reduction of the C14-unsaturated bond of
CC lanosterol, as part of the metabolic pathway leading to cholesterol
CC biosynthesis (PubMed:18785926). Plays a critical role in myeloid cell
CC cholesterol biosynthesis which is essential to both myeloid cell growth
CC and functional maturation (PubMed:22140257). Mediates the activation of
CC NADPH oxidases, perhaps by maintaining critical levels of cholesterol
CC required for membrane lipid raft formation during neutrophil
CC differentiation (PubMed:22140257). Anchors the lamina and the
CC heterochromatin to the inner nuclear membrane (By similarity).
CC {ECO:0000250|UniProtKB:Q14739, ECO:0000269|PubMed:18785926,
CC ECO:0000269|PubMed:22140257}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5alpha-cholest-8,14-dien-3beta-ol + H(+) + NADPH = 5alpha-
CC cholest-8-en-3beta-ol + NADP(+); Xref=Rhea:RHEA:46456,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16608, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:86131;
CC Evidence={ECO:0000269|PubMed:18785926};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP(+) =
CC 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + H(+) + NADPH;
CC Xref=Rhea:RHEA:18561, ChEBI:CHEBI:15378, ChEBI:CHEBI:17813,
CC ChEBI:CHEBI:18364, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.70;
CC Evidence={ECO:0000250|UniProtKB:Q14739};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4,4-dimethyl-8,14-cholestadien-3beta-ol + H(+) + NADPH = 4,4-
CC dimethyl-5alpha-cholest-8-en-3beta-ol + NADP(+);
CC Xref=Rhea:RHEA:46812, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:78904, ChEBI:CHEBI:87044;
CC Evidence={ECO:0000250|UniProtKB:Q14739};
CC -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis.
CC -!- SUBUNIT: Interacts with CBX5 (By similarity). Interacts with DNA (By
CC similarity). Interaction with DNA is sequence independent with higher
CC affinity for supercoiled and relaxed circular DNA than linear DNA (By
CC similarity). Interacts with lamin B (By similarity). Interacts with
CC CLNK (PubMed:26009488). {ECO:0000250|UniProtKB:Q14739,
CC ECO:0000269|PubMed:26009488}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:18785926}; Multi-pass membrane protein
CC {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:Q14739}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q14739}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q14739}. Note=Nucleus; nuclear rim.
CC {ECO:0000250|UniProtKB:Q14739}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the testis and lung. Also
CC expressed in the heart, ovary, kidney and liver.
CC {ECO:0000269|PubMed:18785926}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed in liver, skin, brain as well
CC as in specific regions of the developing cartilage and bone in embryos.
CC {ECO:0000269|PubMed:21327084}.
CC -!- DOMAIN: The Tudor domain may not recognize methylation marks, but
CC rather bind unassembled free histone H3.
CC {ECO:0000250|UniProtKB:P23913}.
CC -!- PTM: Phosphorylated by CDK1 in mitosis when the inner nuclear membrane
CC breaks down into vesicles that dissociate from the lamina and the
CC chromatin (By similarity). It is phosphorylated by different protein
CC kinases in interphase when the membrane is associated with these
CC structures (By similarity). Phosphorylation of LBR and HP1 proteins may
CC be responsible for some of the alterations in chromatin organization
CC and nuclear structure which occur at various times during the cell
CC cycle (By similarity). Phosphorylated by SRPK1 (By similarity). In late
CC anaphase LBR is dephosphorylated, probably by PP1 and/or PP2A, allowing
CC reassociation with chromatin (By similarity).
CC {ECO:0000250|UniProtKB:Q14739}.
CC -!- SIMILARITY: Belongs to the ERG4/ERG24 family. {ECO:0000305}.
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DR EMBL; AK030606; BAC27042.1; -; mRNA.
DR EMBL; AK028426; BAE20442.1; -; mRNA.
DR EMBL; AK033459; BAE20487.1; -; mRNA.
DR EMBL; AK151798; BAE30698.1; -; mRNA.
DR EMBL; AK161762; BAE36563.1; -; mRNA.
DR EMBL; AK166850; BAE39069.1; -; mRNA.
DR EMBL; AK167157; BAE39298.1; -; mRNA.
DR EMBL; BC010261; AAH10261.1; -; mRNA.
DR EMBL; BC014835; AAH14835.1; -; mRNA.
DR EMBL; BC021516; AAH21516.1; -; mRNA.
DR EMBL; BC029171; AAH29171.1; -; mRNA.
DR EMBL; BC042522; AAH42522.1; -; mRNA.
DR EMBL; AY148158; AAN76314.1; -; Genomic_DNA.
DR EMBL; AY148158; AAN76315.1; -; Genomic_DNA.
DR CCDS; CCDS15584.1; -.
DR RefSeq; NP_598576.2; NM_133815.2.
DR RefSeq; XP_006497133.1; XM_006497070.3.
DR RefSeq; XP_006497134.1; XM_006497071.3.
DR RefSeq; XP_017168530.1; XM_017313041.1.
DR AlphaFoldDB; Q3U9G9; -.
DR SMR; Q3U9G9; -.
DR BioGRID; 221046; 15.
DR IntAct; Q3U9G9; 1.
DR MINT; Q3U9G9; -.
DR STRING; 10090.ENSMUSP00000005003; -.
DR GlyGen; Q3U9G9; 1 site.
DR iPTMnet; Q3U9G9; -.
DR PhosphoSitePlus; Q3U9G9; -.
DR SwissPalm; Q3U9G9; -.
DR EPD; Q3U9G9; -.
DR jPOST; Q3U9G9; -.
DR MaxQB; Q3U9G9; -.
DR PaxDb; Q3U9G9; -.
DR PeptideAtlas; Q3U9G9; -.
DR PRIDE; Q3U9G9; -.
DR ProteomicsDB; 290012; -.
DR Antibodypedia; 34642; 245 antibodies from 31 providers.
DR DNASU; 98386; -.
DR Ensembl; ENSMUST00000005003; ENSMUSP00000005003; ENSMUSG00000004880.
DR GeneID; 98386; -.
DR KEGG; mmu:98386; -.
DR UCSC; uc007dxo.2; mouse.
DR CTD; 3930; -.
DR MGI; MGI:2138281; Lbr.
DR VEuPathDB; HostDB:ENSMUSG00000004880; -.
DR eggNOG; KOG1435; Eukaryota.
DR GeneTree; ENSGT00390000000417; -.
DR HOGENOM; CLU_015631_0_2_1; -.
DR InParanoid; Q3U9G9; -.
DR OMA; SYWRVDT; -.
DR OrthoDB; 532774at2759; -.
DR PhylomeDB; Q3U9G9; -.
DR TreeFam; TF101179; -.
DR Reactome; R-MMU-191273; Cholesterol biosynthesis.
DR Reactome; R-MMU-2995383; Initiation of Nuclear Envelope (NE) Reformation.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR Reactome; R-MMU-9022692; Regulation of MECP2 expression and activity.
DR UniPathway; UPA00063; -.
DR BioGRID-ORCS; 98386; 1 hit in 79 CRISPR screens.
DR ChiTaRS; Lbr; mouse.
DR PRO; PR:Q3U9G9; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q3U9G9; protein.
DR Bgee; ENSMUSG00000004880; Expressed in femorotibial joint and 261 other tissues.
DR ExpressionAtlas; Q3U9G9; baseline and differential.
DR Genevisible; Q3U9G9; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR GO; GO:0005637; C:nuclear inner membrane; IBA:GO_Central.
DR GO; GO:0005652; C:nuclear lamina; TAS:MGI.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR GO; GO:0070087; F:chromo shadow domain binding; ISO:MGI.
DR GO; GO:0050613; F:delta14-sterol reductase activity; IMP:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0070402; F:NADPH binding; ISS:UniProtKB.
DR GO; GO:0008139; F:nuclear localization sequence binding; ISO:MGI.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IBA:GO_Central.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IDA:UniProtKB.
DR GO; GO:0030223; P:neutrophil differentiation; IMP:UniProtKB.
DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
DR CDD; cd04508; TUDOR; 1.
DR InterPro; IPR001171; ERG24_DHCR-like.
DR InterPro; IPR019023; Lamin-B_rcpt_of_tudor.
DR InterPro; IPR018083; Sterol_reductase_CS.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF01222; ERG4_ERG24; 1.
DR Pfam; PF09465; LBR_tudor; 1.
DR SMART; SM00333; TUDOR; 1.
DR PROSITE; PS01017; STEROL_REDUCT_1; 1.
DR PROSITE; PS01018; STEROL_REDUCT_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cholesterol biosynthesis; Cholesterol metabolism; Cytoplasm;
KW DNA-binding; Endoplasmic reticulum; Glycoprotein; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Nucleus; Oxidoreductase; Phosphoprotein;
KW Receptor; Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..626
FT /note="Delta(14)-sterol reductase LBR"
FT /id="PRO_0000227909"
FT TOPO_DOM 1..221
FT /note="Nuclear"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 572..592
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1..62
FT /note="Tudor"
FT REGION 52..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..94
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 55
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14739"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14739"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 86
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14739"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14739"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 128
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14739"
FT MOD_RES 211
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14739"
FT MOD_RES 605
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14739"
FT MOD_RES 612
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14739"
FT CARBOHYD 98
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CONFLICT 174
FT /note="T -> A (in Ref. 2; AAH42522/AAH21516)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="E -> G (in Ref. 1; BAE30698)"
FT /evidence="ECO:0000305"
FT CONFLICT 525
FT /note="N -> S (in Ref. 1; BAE30698)"
FT /evidence="ECO:0000305"
FT CONFLICT 585
FT /note="I -> T (in Ref. 2; AAH14835)"
FT /evidence="ECO:0000305"
FT CONFLICT 600
FT /note="H -> N (in Ref. 1; BAE36563)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 626 AA; 71440 MW; 559CAAFFF73836F4 CRC64;
MPSRKFVEGE VVRGRWPGSS LYYEVEILSH DNKSQLYTVK YKDGTELELK ESDIKPLKSF
KQRKSGSISS SPSRRRGSRS RSRSRSRSRS PGRAPKGSRR SVSASHEGDV KEKKEKEMRR
EILQVKLTPL VLKPFGNSVS VYNGEPEHME KNATPYKDKQ ERIILSTEDR YIVTQYSLRP
RREEVKAKEI ESEEQNLVTK GPAPLGTFQV TTPQRKDLEF GGVPGAVLIM LGLPACVLLL
LLQCRQKDPG LLHFPPPLPA LHELWEPRVC GVYLLWFFVQ ALFHLLPVGK VAEGTPLVDG
RRLQYRLNGL YAFILTSAAL GAAVFWGVEL CYLYTHFLQL ALAATGFSVL LSAYLYVRSL
RAPREELSPA SSGNAVYDFF IGRELNPRLG AFDLKFFCEL RPGLIGWVVI NLVMLLMEMK
IQERAAPSLA MILVNSFQLL YVVDALWNEE ALLTSMDIMH DGFGFMLAFG DLVWVPFTYS
LQAFYLVSHP HDLSWPLASV IIALKLCGYV IFRCANSQKN AFRKNPTDPK LAHLKTIHTS
TGKSLLVSGW WGFVRHPNYL GDLIMALAWS LPCGFNHLLP YFYIIYFTAL LIHREARDEH
QCRRKYGLAW EKYCQRVPYR IFPYIY
