OSB11_HUMAN
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 03-AUG-2022, entry version 165.
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}.
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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; 93.
DR IntAct; Q9BXB4; 16.
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; Q9BXB4; -.
DR PeptideAtlas; Q9BXB4; -.
DR PRIDE; Q9BXB4; -.
DR ProteomicsDB; 79398; -.
DR Antibodypedia; 33023; 298 antibodies from 28 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 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; QGVTNHA; -.
DR OrthoDB; 949920at2759; -.
DR PhylomeDB; Q9BXB4; -.
DR TreeFam; TF312807; -.
DR PathwayCommons; Q9BXB4; -.
DR Reactome; R-HSA-9013407; RHOH GTPase cycle.
DR SignaLink; Q9BXB4; -.
DR BioGRID-ORCS; 114885; 19 hits in 1078 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 203 other tissues.
DR ExpressionAtlas; Q9BXB4; baseline and differential.
DR Genevisible; Q9BXB4; HS.
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 Gene3D; 2.30.29.30; -; 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; PTHR10972; 1.
DR Pfam; PF01237; Oxysterol_BP; 2.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF144000; SSF144000; 1.
DR PROSITE; PS01013; OSBP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
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
