ID OSB11_HUMAN Reviewed; 747 AA. AC Q9BXB4; A8K9I7; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 11-FEB-2002, sequence version 2. DT 27-MAR-2024, entry version 174. DE RecName: Full=Oxysterol-binding protein-related protein 11; DE Short=ORP-11; DE Short=OSBP-related protein 11; GN Name=OSBPL11; Synonyms=ORP11, OSBP12; 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]. RX PubMed=11735225; DOI=10.1006/geno.2001.6663; RA Jaworski C.J., Moreira E., Li A., Lee R., Rodriguez I.R.; RT "A family of 12 human genes containing oxysterol-binding domains."; RL Genomics 78:185-196(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Thymus; 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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 [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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-315. RX PubMed=11483621; RA Lehto M., Laitinen S., Chinetti G., Johansson M., Ehnholm C., Staels B., RA Ikonen E., Olkkonen V.M.; RT "The OSBP-related protein family in humans."; RL J. Lipid Res. 42:1203-1213(2001). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION BY RP 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 FUNCTION. RX PubMed=17428193; DOI=10.1042/bj20070176; RA Suchanek M., Hynynen R., Wohlfahrt G., Lehto M., Johansson M., Saarinen H., RA Radzikowska A., Thiele C., Olkkonen V.M.; RT "The mammalian oxysterol-binding protein-related proteins (ORPs) bind 25- RT hydroxycholesterol in an evolutionarily conserved pocket."; RL Biochem. J. 405:473-480(2007). RN [9] RP IDENTIFICATION BY 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 THR-27, AND IDENTIFICATION BY RP 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 THR-27; SER-181 AND SER-189, 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 [12] 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-27; TYR-62; SER-172; SER-174 RP AND SER-181, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [14] RP SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=20599956; DOI=10.1016/j.yexcr.2010.06.008; RA Zhou Y., Li S., Mayranpaa M.I., Zhong W., Back N., Yan D., Olkkonen V.M.; RT "OSBP-related protein 11 (ORP11) dimerizes with ORP9 and localizes at the RT Golgi-late endosome interface."; RL Exp. Cell Res. 316:3304-3316(2010). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-27; SER-181 AND SER-189, 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 [16] 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, AND IDENTIFICATION BY RP 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 [18] RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=23028956; DOI=10.1371/journal.pone.0045352; RA Zhou Y., Robciuc M.R., Wabitsch M., Juuti A., Leivonen M., Ehnholm C., RA Yki-Jarvinen H., Olkkonen V.M.; RT "OSBP-related proteins (ORPs) in human adipose depots and cultured RT adipocytes: evidence for impacts on the adipocyte phenotype."; RL PLoS ONE 7:E45352-E45352(2012). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; THR-27; SER-172; SER-174; RP SER-181; SER-184 AND SER-189, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-172 AND SER-181, 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). RN [21] RP STRUCTURE BY NMR OF 59-165. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the PH domain of oxysterol binding protein-related RT protein 11 from human."; RL Submitted (JUN-2006) to the PDB data bank. RN [22] RP VARIANT [LARGE SCALE ANALYSIS] LEU-184. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Plays a role in regulating ADIPOQ and FABP4 levels in CC differentiating adipocytes and is also involved in regulation of CC adipocyte triglyceride storage (PubMed:23028956). Weakly binds 25- CC hydroxycholesterol (PubMed:17428193). {ECO:0000269|PubMed:17428193, CC ECO:0000269|PubMed:23028956}. CC -!- SUBUNIT: Heterodimer with OSBPL9. {ECO:0000269|PubMed:20599956}. CC -!- INTERACTION: CC Q9BXB4; Q96SU4: OSBPL9; NbExp=7; IntAct=EBI-2514786, EBI-2511368; CC -!- SUBCELLULAR LOCATION: Late endosome membrane CC {ECO:0000269|PubMed:20599956}. Golgi apparatus, trans-Golgi network CC membrane {ECO:0000269|PubMed:20599956}. Note=Localizes at the Golgi- CC late endosome interface. CC -!- TISSUE SPECIFICITY: Present at highest levels in ovary, testis, kidney, CC liver, stomach, brain, and adipose tissue. Strong expression (at CC protein level) in epithelial cells of kidney tubules, testicular CC tubules, caecum, and skin (PubMed:20599956). Present at low levels in CC subcutaneous and visceral adipose tissue (at protein CC level)(PubMed:23028956). {ECO:0000269|PubMed:20599956, CC ECO:0000269|PubMed:23028956}. CC -!- DEVELOPMENTAL STAGE: During adipocyte differentiation, levels are CC elevated two-fold (at protein level). {ECO:0000269|PubMed:23028956}. CC -!- DOMAIN: The PH domain binds phosphoinositides. CC {ECO:0000269|PubMed:20599956}. CC -!- SIMILARITY: Belongs to the OSBP 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; AF392454; AAL40667.1; -; mRNA. DR EMBL; AK292702; BAF85391.1; -; mRNA. DR EMBL; CH471052; EAW79389.1; -; Genomic_DNA. DR EMBL; BC065213; AAH65213.1; -; mRNA. DR EMBL; AF346292; AAK31141.1; -; mRNA. DR CCDS; CCDS3033.1; -. DR RefSeq; NP_073613.2; NM_022776.4. DR PDB; 2D9X; NMR; -; A=59-165. DR PDBsum; 2D9X; -. DR AlphaFoldDB; Q9BXB4; -. DR BMRB; Q9BXB4; -. DR SMR; Q9BXB4; -. DR BioGRID; 125386; 105. DR ComplexPortal; CPX-8168; OSBPL9-OSBPL11 oxysterol-binding protein-related complex. DR IntAct; Q9BXB4; 18. DR MINT; Q9BXB4; -. DR STRING; 9606.ENSP00000296220; -. DR GlyGen; Q9BXB4; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9BXB4; -. DR PhosphoSitePlus; Q9BXB4; -. DR BioMuta; OSBPL11; -. DR DMDM; 20139127; -. DR EPD; Q9BXB4; -. DR jPOST; Q9BXB4; -. DR MassIVE; Q9BXB4; -. DR MaxQB; Q9BXB4; -. DR PaxDb; 9606-ENSP00000296220; -. DR PeptideAtlas; Q9BXB4; -. DR ProteomicsDB; 79398; -. DR Pumba; Q9BXB4; -. DR Antibodypedia; 33023; 348 antibodies from 29 providers. DR DNASU; 114885; -. DR Ensembl; ENST00000296220.6; ENSP00000296220.5; ENSG00000144909.8. DR GeneID; 114885; -. DR KEGG; hsa:114885; -. DR MANE-Select; ENST00000296220.6; ENSP00000296220.5; NM_022776.5; NP_073613.2. DR UCSC; uc003eic.4; human. DR AGR; HGNC:16397; -. DR CTD; 114885; -. DR DisGeNET; 114885; -. DR GeneCards; OSBPL11; -. DR HGNC; HGNC:16397; OSBPL11. DR HPA; ENSG00000144909; Tissue enhanced (skeletal muscle, tongue). DR MIM; 606739; gene. DR neXtProt; NX_Q9BXB4; -. DR OpenTargets; ENSG00000144909; -. DR PharmGKB; PA32825; -. DR VEuPathDB; HostDB:ENSG00000144909; -. DR eggNOG; KOG2210; Eukaryota. DR GeneTree; ENSGT00940000158398; -. DR HOGENOM; CLU_012334_3_1_1; -. DR InParanoid; Q9BXB4; -. DR OMA; CDHKEDD; -. DR OrthoDB; 1018068at2759; -. DR PhylomeDB; Q9BXB4; -. DR TreeFam; TF312807; -. DR PathwayCommons; Q9BXB4; -. DR Reactome; R-HSA-9013407; RHOH GTPase cycle. DR SignaLink; Q9BXB4; -. DR BioGRID-ORCS; 114885; 21 hits in 1155 CRISPR screens. DR ChiTaRS; OSBPL11; human. DR EvolutionaryTrace; Q9BXB4; -. DR GeneWiki; OSBPL11; -. DR GenomeRNAi; 114885; -. DR Pharos; Q9BXB4; Tbio. DR PRO; PR:Q9BXB4; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q9BXB4; Protein. DR Bgee; ENSG00000144909; Expressed in biceps brachii and 205 other cell types or tissues. DR ExpressionAtlas; Q9BXB4; baseline and differential. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central. DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0032934; F:sterol binding; IBA:GO_Central. DR GO; GO:0015248; F:sterol transporter activity; IBA:GO_Central. DR GO; GO:0045444; P:fat cell differentiation; IMP:BHF-UCL. DR GO; GO:0010890; P:positive regulation of sequestering of triglyceride; IMP:BHF-UCL. DR CDD; cd13291; PH_ORP10_ORP11; 1. DR Gene3D; 1.10.287.2720; -; 1. DR Gene3D; 2.40.160.120; -; 1. DR Gene3D; 3.30.70.3490; -; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR037239; OSBP_sf. DR InterPro; IPR000648; Oxysterol-bd. DR InterPro; IPR018494; Oxysterol-bd_CS. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR PANTHER; PTHR10972; OXYSTEROL-BINDING PROTEIN-RELATED; 1. DR PANTHER; PTHR10972:SF46; OXYSTEROL-BINDING PROTEIN-RELATED PROTEIN 11; 1. DR Pfam; PF01237; Oxysterol_BP; 2. DR Pfam; PF00169; PH; 1. DR SMART; SM00233; PH; 1. DR SUPFAM; SSF144000; Oxysterol-binding protein-like; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR PROSITE; PS01013; OSBP; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR Genevisible; Q9BXB4; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Endosome; Golgi apparatus; Lipid transport; KW Lipid-binding; Membrane; Phosphoprotein; Reference proteome; Transport. FT CHAIN 1..747 FT /note="Oxysterol-binding protein-related protein 11" FT /id="PRO_0000100381" FT DOMAIN 58..155 FT /note="PH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT REGION 1..50 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 158..188 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 689..714 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 20..50 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 15 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 27 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 62 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 172 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 174 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 177 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8CI95" FT MOD_RES 181 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 184 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 189 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT VARIANT 184 FT /note="S -> L (in a breast cancer sample; somatic mutation; FT dbSNP:rs746035150)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036100" FT STRAND 62..70 FT /evidence="ECO:0007829|PDB:2D9X" FT TURN 71..73 FT /evidence="ECO:0007829|PDB:2D9X" FT STRAND 74..82 FT /evidence="ECO:0007829|PDB:2D9X" FT TURN 84..86 FT /evidence="ECO:0007829|PDB:2D9X" FT STRAND 88..94 FT /evidence="ECO:0007829|PDB:2D9X" FT HELIX 95..97 FT /evidence="ECO:0007829|PDB:2D9X" FT STRAND 98..100 FT /evidence="ECO:0007829|PDB:2D9X" FT STRAND 103..107 FT /evidence="ECO:0007829|PDB:2D9X" FT STRAND 117..121 FT /evidence="ECO:0007829|PDB:2D9X" FT STRAND 123..125 FT /evidence="ECO:0007829|PDB:2D9X" FT STRAND 128..130 FT /evidence="ECO:0007829|PDB:2D9X" FT STRAND 133..135 FT /evidence="ECO:0007829|PDB:2D9X" FT HELIX 140..160 FT /evidence="ECO:0007829|PDB:2D9X" SQ SEQUENCE 747 AA; 83643 MW; B443D3BDE8AE5FB6 CRC64; MQGGEPVSTM KVSESEGKLE GQATAVTPNK NSSCGGGISS SSSSRGGSAK GWQYSDHMEN VYGYLMKYTN LVTGWQYRFF VLNNEAGLLE YFVNEQSRNQ KPRGTLQLAG AVISPSDEDS HTFTVNAASG EQYKLRATDA KERQHWVSRL QICTQHHTEA IGKNNPPLKS RSFSLASSSN SPISQRRPSQ NAISFFNVGH SKLQSLSKRT NLPPDHLVEV REMMSHAEGQ QRDLIRRIEC LPTSGHLSSL DQDLLMLKAT SMATMNCLND CFHILQLQHA SHQKGSLPSG TTIEWLEPKI SLSNHYKNGA DQPFATDQSK PVAVPEEQPV AESGLLAREP EEINADDEIE DTCDHKEDDL GAVEEQRSVI LHLLSQLKLG MDLTRVVLPT FILEKRSLLE MYADFMSHPD LFIAITNGAT AEDRMIRFVE YYLTSFHEGR KGAIAKKPYN PIIGETFHCS WKMPKSEVAS SVFSSSSTQG VTNHAPLSGE SLTQVGSDCY TVRFVAEQVS HHPPVSGFYA ECTERKMCVN AHVWTKSKFL GMSIGVTMVG EGILSLLEHG EEYTFSLPCA YARSILTVPW VELGGKVSVN CAKTGYSASI TFHTKPFYGG KLHRVTAEVK HNITNTVVCR VQGEWNSVLE FTYSNGETKY VDLTKLAVTK KRVRPLEKQD PFESRRLWKN VTDSLRESEI DKATEHKHTL EERQRTEERH RTETGTPWKT KYFIKEGDGW VYHKPLWKII PTTQPAE //