ID LTOR1_HUMAN Reviewed; 161 AA. AC Q6IAA8; Q8WZ09; Q9NWT0; DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 2. DT 05-JUL-2017, entry version 112. DE RecName: Full=Ragulator complex protein LAMTOR1; DE AltName: Full=Late endosomal/lysosomal adaptor and MAPK and MTOR activator 1; DE AltName: Full=Lipid raft adaptor protein p18; DE AltName: Full=Protein associated with DRMs and endosomes; DE AltName: Full=p27Kip1-releasing factor from RhoA; DE Short=p27RF-Rho; GN Name=LAMTOR1; Synonyms=C11orf59, PDRO; ORFNames=PP7157; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15498874; DOI=10.1073/pnas.0404089101; RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., RA Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., RA Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., RA Gu J.; RT "Large-scale cDNA transfection screening for genes related to cancer RT development and progression."; RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PROTEIN SEQUENCE OF 48-60 AND 135-147, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Submitted (JUN-2005) to UniProtKB. RN [6] 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 RT phosphorylation analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [7] 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 [8] 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., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [9] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MMP14 AND CDKN1B. RX PubMed=19654316; DOI=10.1074/jbc.M109.041400; RA Hoshino D., Tomari T., Nagano M., Koshikawa N., Seiki M.; RT "A novel protein associated with membrane-type 1 matrix RT metalloproteinase binds p27(kip1) and regulates RhoA activation, actin RT remodeling, and matrigel invasion."; RL J. Biol. Chem. 284:27315-27326(2009). RN [10] 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 [11] RP FUNCTION, IDENTIFICATION IN RAGULATOR COMPLEX, AND INTERACTION WITH RP RRAGB AND RRAGD. RX PubMed=20381137; DOI=10.1016/j.cell.2010.02.024; RA Sancak Y., Bar-Peled L., Zoncu R., Markhard A.L., Nada S., RA Sabatini D.M.; RT "Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is RT necessary for its activation by amino acids."; RL Cell 141:290-303(2010). RN [12] RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION BY CHOLESTEROL. RX PubMed=20544018; DOI=10.1371/journal.pone.0010977; RA Guillaumot P., Luquain C., Malek M., Huber A.L., Brugiere S., RA Garin J., Grunwald D., Regnier D., Petrilli V., Lefai E., Manie S.N.; RT "Pdro, a protein associated with late endosomes and lysosomes and RT implicated in cellular cholesterol homeostasis."; RL PLoS ONE 5:E10977-E10977(2010). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION RP 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [14] 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., RA Buerckstuemmer T., 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 [15] RP FUNCTION IN MTORC1 SIGNALING, IDENTIFICATION IN RAGULATOR COMPLEX, AND RP INTERACTION WITH MTORC1 COMPLEX AND RAG GTPASES. RX PubMed=22980980; DOI=10.1016/j.cell.2012.07.032; RA Bar-Peled L., Schweitzer L.D., Zoncu R., Sabatini D.M.; RT "Ragulator is a GEF for the Rag GTPases that signal amino acid levels RT to mTORC1."; RL Cell 150:1196-1208(2012). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-42; SER-56; RP SER-98 AND SER-141, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP 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 [17] 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [18] RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=25255805; DOI=10.1038/ncomms5919; RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., RA Wright M.H., Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.; RT "Global profiling of co- and post-translationally N-myristoylated RT proteomes in human cells."; RL Nat. Commun. 5:4919-4919(2014). RN [19] RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=25807930; DOI=10.1002/anie.201500342; RA Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J., RA Magee A.I., Tate E.W.; RT "Multifunctional reagents for quantitative proteome-wide analysis of RT protein modification in human cells and dynamic profiling of protein RT lipidation during vertebrate development."; RL Angew. Chem. Int. Ed. 54:5948-5951(2015). RN [20] RP INTERACTION WITH SLC38A9. RX PubMed=25561175; DOI=10.1038/nature14107; RA Rebsamen M., Pochini L., Stasyk T., de Araujo M.E., Galluccio M., RA Kandasamy R.K., Snijder B., Fauster A., Rudashevskaya E.L., RA Bruckner M., Scorzoni S., Filipek P.A., Huber K.V., Bigenzahn J.W., RA Heinz L.X., Kraft C., Bennett K.L., Indiveri C., Huber L.A., RA Superti-Furga G.; RT "SLC38A9 is a component of the lysosomal amino acid sensing machinery RT that controls mTORC1."; RL Nature 519:477-481(2015). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [22] RP INTERACTION WITH SLC38A9. RX PubMed=25567906; DOI=10.1126/science.1257132; RA Wang S., Tsun Z.Y., Wolfson R.L., Shen K., Wyant G.A., Plovanich M.E., RA Yuan E.D., Jones T.D., Chantranupong L., Comb W., Wang T., RA Bar-Peled L., Zoncu R., Straub C., Kim C., Park J., Sabatini B.L., RA Sabatini D.M.; RT "Metabolism. Lysosomal amino acid transporter SLC38A9 signals arginine RT sufficiency to mTORC1."; RL Science 347:188-194(2015). CC -!- FUNCTION: As part of the Ragulator complex it is involved in amino CC acid sensing and activation of mTORC1, a signaling complex CC promoting cell growth in response to growth factors, energy CC levels, and amino acids. Activated by amino acids through a CC mechanism involving the lysosomal V-ATPase, the Ragulator CC functions as a guanine nucleotide exchange factor activating the CC small GTPases Rag. Activated Ragulator and Rag GTPases function as CC a scaffold recruiting mTORC1 to lysosomes where it is in turn CC activated. LAMTOR1 is directly responsible for anchoring the CC Ragulator complex to membranes. Also required for late CC endosomes/lysosomes biogenesis it may regulate both the recycling CC of receptors through endosomes and the MAPK signaling pathway CC through recruitment of some of its components to late endosomes. CC May be involved in cholesterol homeostasis regulating LDL uptake CC and cholesterol release from late endosomes/lysosomes. May also CC play a role in RHOA activation. {ECO:0000269|PubMed:19654316, CC ECO:0000269|PubMed:20381137, ECO:0000269|PubMed:20544018, CC ECO:0000269|PubMed:22980980}. CC -!- SUBUNIT: Part of the Ragulator complex composed of LAMTOR1, CC LAMTOR2, LAMTOR3, LAMTOR4 and LAMTOR5. LAMTOR4 and LAMTOR5 form a CC heterodimer that interacts, through LAMTOR1, with a LAMTOR2, CC LAMTOR3 heterodimer. The Ragulator complex interacts with both the CC mTORC1 complex and heterodimers constituted of the Rag GTPases CC RRAGA, RRAGB, RRAGC and RRAGD; regulated by amino acid CC availability (PubMed:20381137, PubMed:22980980). The Ragulator CC complex interacts with SLC38A9; the probable amino acid sensor CC (PubMed:25561175, PubMed:25567906). Interacts with LAMTOR2 and CC LAMTOR3; the interaction is direct. Interacts with RRAGB and CC RRAGD; the interaction is direct indicating that it probably CC constitutes the main RAG-interacting subunit of the Ragulator CC complex (PubMed:22980980). Interacts with MMP14 (PubMed:19654316). CC Interacts with CDKN1B; prevents the interaction of CDKN1B with CC RHOA leaving RHOA in a form accessible to activation by ARHGEF2 CC (PubMed:19654316). {ECO:0000269|PubMed:19654316, CC ECO:0000269|PubMed:20381137, ECO:0000269|PubMed:22980980, CC ECO:0000269|PubMed:25561175, ECO:0000269|PubMed:25567906}. CC -!- INTERACTION: CC Q7L523:RRAGA; NbExp=10; IntAct=EBI-715385, EBI-752376; CC Q8NBW4:SLC38A9; NbExp=9; IntAct=EBI-715385, EBI-9978316; CC -!- SUBCELLULAR LOCATION: Late endosome membrane; Lipid-anchor; CC Cytoplasmic side. Lysosome membrane; Lipid-anchor; Cytoplasmic CC side. Cell membrane. CC -!- INDUCTION: Down-regulated by cholesterol (at protein level). CC {ECO:0000269|PubMed:20544018}. CC -!- SIMILARITY: Belongs to the LAMTOR1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF289583; AAL55767.1; -; mRNA. DR EMBL; CR457247; CAG33528.1; -; mRNA. DR EMBL; AK000632; BAA91297.1; -; mRNA. DR EMBL; BC001706; AAH01706.1; -; mRNA. DR CCDS; CCDS8209.1; -. DR RefSeq; NP_060377.1; NM_017907.2. DR UniGene; Hs.731528; -. DR ProteinModelPortal; Q6IAA8; -. DR SMR; Q6IAA8; -. DR BioGrid; 120336; 30. DR DIP; DIP-39650N; -. DR IntAct; Q6IAA8; 34. DR MINT; MINT-1372069; -. DR STRING; 9606.ENSP00000278671; -. DR iPTMnet; Q6IAA8; -. DR PhosphoSitePlus; Q6IAA8; -. DR SwissPalm; Q6IAA8; -. DR BioMuta; LAMTOR1; -. DR DMDM; 125863645; -. DR EPD; Q6IAA8; -. DR MaxQB; Q6IAA8; -. DR PaxDb; Q6IAA8; -. DR PeptideAtlas; Q6IAA8; -. DR PRIDE; Q6IAA8; -. DR TopDownProteomics; Q6IAA8; -. DR Ensembl; ENST00000278671; ENSP00000278671; ENSG00000149357. DR GeneID; 55004; -. DR KEGG; hsa:55004; -. DR UCSC; uc001ort.3; human. DR CTD; 55004; -. DR DisGeNET; 55004; -. DR GeneCards; LAMTOR1; -. DR H-InvDB; HIX0009905; -. DR HGNC; HGNC:26068; LAMTOR1. DR HPA; HPA002997; -. DR MIM; 613510; gene. DR neXtProt; NX_Q6IAA8; -. DR OpenTargets; ENSG00000149357; -. DR PharmGKB; PA143485354; -. DR eggNOG; ENOG410IH39; Eukaryota. DR eggNOG; ENOG4112AMJ; LUCA. DR GeneTree; ENSGT00390000016789; -. DR HOVERGEN; HBG081218; -. DR InParanoid; Q6IAA8; -. DR KO; K20397; -. DR OMA; HNLEQHE; -. DR OrthoDB; EOG091G0XGD; -. DR PhylomeDB; Q6IAA8; -. DR TreeFam; TF323788; -. DR Reactome; R-HSA-1632852; Macroautophagy. DR Reactome; R-HSA-165159; mTOR signalling. DR Reactome; R-HSA-166208; mTORC1-mediated signalling. DR Reactome; R-HSA-380972; Energy dependent regulation of mTOR by LKB1-AMPK. DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR SIGNOR; Q6IAA8; -. DR GenomeRNAi; 55004; -. DR PRO; PR:Q6IAA8; -. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; ENSG00000149357; -. DR CleanEx; HS_C11orf59; -. DR ExpressionAtlas; Q6IAA8; baseline and differential. DR Genevisible; Q6IAA8; HS. DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome. DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome. DR GO; GO:0005764; C:lysosome; IDA:UniProtKB. DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0071986; C:Ragulator complex; IDA:UniProtKB. DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome. DR GO; GO:0051020; F:GTPase binding; IPI:CAFA. DR GO; GO:0007050; P:cell cycle arrest; TAS:Reactome. DR GO; GO:0016049; P:cell growth; IMP:UniProtKB. DR GO; GO:0034613; P:cellular protein localization; IMP:UniProtKB. DR GO; GO:0071230; P:cellular response to amino acid stimulus; IMP:UniProtKB. DR GO; GO:0042632; P:cholesterol homeostasis; IMP:UniProtKB. DR GO; GO:0032439; P:endosome localization; ISS:UniProtKB. DR GO; GO:0007032; P:endosome organization; ISS:UniProtKB. DR GO; GO:0032418; P:lysosome localization; ISS:UniProtKB. DR GO; GO:0007040; P:lysosome organization; ISS:UniProtKB. DR GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome. DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:GOC. DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB. DR GO; GO:0032008; P:positive regulation of TOR signaling; IMP:UniProtKB. DR GO; GO:0010874; P:regulation of cholesterol efflux; IMP:UniProtKB. DR GO; GO:0010872; P:regulation of cholesterol esterification; IMP:UniProtKB. DR GO; GO:0060620; P:regulation of cholesterol import; IMP:UniProtKB. DR GO; GO:0016241; P:regulation of macroautophagy; TAS:Reactome. DR GO; GO:0001919; P:regulation of receptor recycling; ISS:UniProtKB. DR InterPro; IPR026310; LAMTOR1-like. DR InterPro; IPR028209; LAMTOR1/MEH1. DR PANTHER; PTHR13401; PTHR13401; 1. DR Pfam; PF15454; LAMTOR; 1. DR SMART; SM01262; LAMTOR; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Direct protein sequencing; Endosome; KW Lipoprotein; Lysosome; Membrane; Myristate; Phosphoprotein; KW Polymorphism; Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:25255805, FT ECO:0000269|PubMed:25807930}. FT CHAIN 2 161 Ragulator complex protein LAMTOR1. FT /FTId=PRO_0000274292. FT REGION 121 161 Interaction with LAMTOR2 and LAMTOR3. FT {ECO:0000250}. FT MOD_RES 27 27 Phosphoserine. FT {ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 42 42 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 56 56 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 98 98 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 141 141 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT LIPID 2 2 N-myristoyl glycine. FT {ECO:0000269|PubMed:25255805, FT ECO:0000269|PubMed:25807930}. FT VARIANT 73 73 S -> L (in dbSNP:rs1053443). FT /FTId=VAR_030250. FT CONFLICT 50 50 E -> V (in Ref. 2; CAG33528). FT {ECO:0000305}. FT CONFLICT 60 60 K -> R (in Ref. 1; AAL55767). FT {ECO:0000305}. FT CONFLICT 69 69 S -> P (in Ref. 2; CAG33528). FT {ECO:0000305}. SQ SEQUENCE 161 AA; 17745 MW; 610CC6C548356051 CRC64; MGCCYSSENE DSDQDREERK LLLDPSSPPT KALNGAEPNY HSLPSARTDE QALLSSILAK TASNIIDVSA ADSQGMEQHE YMDRARQYST RLAVLSSSLT HWKKLPPLPS LTSQPHQVLA SEPIPFSDLQ QVSRIAAYAY SALSQIRVDA KEELVVQFGI P //