DPTOR_HUMAN
ID DPTOR_HUMAN Reviewed; 409 AA.
AC Q8TB45; B2RCL9; B4DN97; E7EV87; Q96EQ1; Q9H0R7; Q9H894; Q9HA07;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=DEP domain-containing mTOR-interacting protein;
DE AltName: Full=DEP domain-containing protein 6;
GN Name=DEPTOR; Synonyms=DEPDC6;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-204.
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP SER-204 AND ASN-389.
RC TISSUE=Heart, Mammary gland, and Thyroid;
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].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS SER-204
RP AND ASN-389.
RC TISSUE=Cervix, and Colon;
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 [6]
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 [7]
RP FUNCTION, INTERACTION WITH MTOR, INDUCTION, PHOSPHORYLATION AT THR-241;
RP SER-244; SER-258; THR-259; SER-263; SER-265; SER-282; SER-283; SER-287;
RP SER-293; SER-297; SER-298 AND SER-299, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19446321; DOI=10.1016/j.cell.2009.03.046;
RA Peterson T.R., Laplante M., Thoreen C.C., Sancak Y., Kang S.A., Kuehl W.M.,
RA Gray N.S., Sabatini D.M.;
RT "DEPTOR is an mTOR inhibitor frequently overexpressed in multiple myeloma
RT cells and required for their survival.";
RL Cell 137:873-886(2009).
RN [8]
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [11]
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 [12]
RP INTERACTION WITH MINAR1, AND UBIQUITINATION.
RX PubMed=30080879; DOI=10.1371/journal.pgen.1007583;
RA Zhang H., Zhang Q., Gao G., Wang X., Wang T., Kong Z., Wang G., Zhang C.,
RA Wang Y., Peng G.;
RT "UBTOR/KIAA1024 regulates neurite outgrowth and neoplasia through mTOR
RT signaling.";
RL PLoS Genet. 14:E1007583-E1007583(2018).
RN [13]
RP INTERACTION WITH SIK3.
RX PubMed=30232230; DOI=10.1126/scitranslmed.aat9356;
RA Csukasi F., Duran I., Barad M., Barta T., Gudernova I., Trantirek L.,
RA Martin J.H., Kuo C.Y., Woods J., Lee H., Cohn D.H., Krejci P., Krakow D.;
RT "The PTH/PTHrP-SIK3 pathway affects skeletogenesis through altered mTOR
RT signaling.";
RL Sci. Transl. Med. 10:0-0(2018).
CC -!- FUNCTION: Negative regulator of the mTORC1 and mTORC2 signaling
CC pathways. Inhibits the kinase activity of both complexes.
CC {ECO:0000269|PubMed:19446321}.
CC -!- SUBUNIT: Part of the mammalian target of rapamycin complex 1 (mTORC1)
CC which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR. Part of
CC the mammalian target of rapamycin complex 2 (mTORC2) which contains
CC MTOR, MLST8, PROTOR1, RICTOR, MAPKAP1 and DEPTOR. Interacts (via PDZ
CC domain) with MTOR; interacts with MTOR within both mammalian target of
CC rapamycin complexes mTORC1 and mTORC2 (PubMed:19446321). Interacts (via
CC PDZ domain) with MINAR1 (via N-terminus) (PubMed:30080879). Interacts
CC with SIK3 (PubMed:30232230). {ECO:0000269|PubMed:19446321,
CC ECO:0000269|PubMed:30080879, ECO:0000269|PubMed:30232230}.
CC -!- INTERACTION:
CC Q8TB45; X5D778: ANKRD11; NbExp=3; IntAct=EBI-2359040, EBI-17183751;
CC Q8TB45; Q8TBZ0: CCDC110; NbExp=3; IntAct=EBI-2359040, EBI-2837012;
CC Q8TB45; P42345: MTOR; NbExp=5; IntAct=EBI-2359040, EBI-359260;
CC Q8TB45; Q13077: TRAF1; NbExp=3; IntAct=EBI-2359040, EBI-359224;
CC Q8TB45; P42346: Mtor; Xeno; NbExp=2; IntAct=EBI-2359040, EBI-1571489;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TB45-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TB45-2; Sequence=VSP_054681;
CC -!- INDUCTION: Expression is negatively regulated by both mTORC1 and mTORC2
CC (at protein level). {ECO:0000269|PubMed:19446321}.
CC -!- PTM: Phosphorylated. Phosphorylation weakens interaction with MTOR
CC within mTORC1 and mTORC2. {ECO:0000269|PubMed:19446321}.
CC -!- PTM: Ubiquitinated; ubiquitination leads to proteasomal degradation.
CC {ECO:0000269|PubMed:30080879}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14723.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL136678; CAB66613.1; -; mRNA.
DR EMBL; AK022490; BAB14054.1; -; mRNA.
DR EMBL; AK023916; BAB14723.1; ALT_INIT; mRNA.
DR EMBL; AK297822; BAG60159.1; -; mRNA.
DR EMBL; AK315175; BAG37616.1; -; mRNA.
DR EMBL; AC091563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP005717; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471060; EAW91997.1; -; Genomic_DNA.
DR EMBL; BC012040; AAH12040.1; -; mRNA.
DR EMBL; BC024746; AAH24746.1; -; mRNA.
DR CCDS; CCDS6331.1; -. [Q8TB45-1]
DR CCDS; CCDS64960.1; -. [Q8TB45-2]
DR RefSeq; NP_001269941.1; NM_001283012.1. [Q8TB45-2]
DR RefSeq; NP_073620.2; NM_022783.3. [Q8TB45-1]
DR PDB; 7DKL; X-ray; 1.50 A; A=21-235.
DR PDB; 7OWG; EM; 4.70 A; O=1-409.
DR PDB; 7PE7; EM; 3.41 A; I/J=1-409.
DR PDB; 7PE8; EM; 3.20 A; I=1-409.
DR PDB; 7PE9; EM; 3.70 A; I=1-409.
DR PDB; 7PEA; EM; 4.07 A; I/J=1-409.
DR PDB; 7PEB; EM; 3.67 A; I=1-409.
DR PDB; 7PEC; EM; 4.24 A; I=1-409.
DR PDB; 7PED; X-ray; 1.93 A; A/B=1-230.
DR PDBsum; 7DKL; -.
DR PDBsum; 7OWG; -.
DR PDBsum; 7PE7; -.
DR PDBsum; 7PE8; -.
DR PDBsum; 7PE9; -.
DR PDBsum; 7PEA; -.
DR PDBsum; 7PEB; -.
DR PDBsum; 7PEC; -.
DR PDBsum; 7PED; -.
DR AlphaFoldDB; Q8TB45; -.
DR SMR; Q8TB45; -.
DR BioGRID; 122304; 29.
DR IntAct; Q8TB45; 11.
DR MINT; Q8TB45; -.
DR STRING; 9606.ENSP00000286234; -.
DR ChEMBL; CHEMBL4105866; -.
DR GlyGen; Q8TB45; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TB45; -.
DR PhosphoSitePlus; Q8TB45; -.
DR BioMuta; DEPTOR; -.
DR DMDM; 251757257; -.
DR EPD; Q8TB45; -.
DR jPOST; Q8TB45; -.
DR MassIVE; Q8TB45; -.
DR MaxQB; Q8TB45; -.
DR PaxDb; Q8TB45; -.
DR PeptideAtlas; Q8TB45; -.
DR PRIDE; Q8TB45; -.
DR ProteomicsDB; 18583; -.
DR ProteomicsDB; 73961; -. [Q8TB45-1]
DR Antibodypedia; 13704; 281 antibodies from 32 providers.
DR DNASU; 64798; -.
DR Ensembl; ENST00000286234.6; ENSP00000286234.5; ENSG00000155792.10. [Q8TB45-1]
DR Ensembl; ENST00000523492.5; ENSP00000430457.1; ENSG00000155792.10. [Q8TB45-2]
DR GeneID; 64798; -.
DR KEGG; hsa:64798; -.
DR MANE-Select; ENST00000286234.6; ENSP00000286234.5; NM_022783.4; NP_073620.2.
DR UCSC; uc003yow.6; human. [Q8TB45-1]
DR CTD; 64798; -.
DR DisGeNET; 64798; -.
DR GeneCards; DEPTOR; -.
DR HGNC; HGNC:22953; DEPTOR.
DR HPA; ENSG00000155792; Tissue enhanced (skeletal muscle, tongue).
DR MIM; 612974; gene.
DR neXtProt; NX_Q8TB45; -.
DR OpenTargets; ENSG00000155792; -.
DR PharmGKB; PA134897957; -.
DR VEuPathDB; HostDB:ENSG00000155792; -.
DR eggNOG; ENOG502QS4Y; Eukaryota.
DR GeneTree; ENSGT00520000055667; -.
DR HOGENOM; CLU_042535_0_0_1; -.
DR InParanoid; Q8TB45; -.
DR OMA; DTHDSPF; -.
DR OrthoDB; 1289616at2759; -.
DR PhylomeDB; Q8TB45; -.
DR PathwayCommons; Q8TB45; -.
DR SignaLink; Q8TB45; -.
DR SIGNOR; Q8TB45; -.
DR BioGRID-ORCS; 64798; 9 hits in 1068 CRISPR screens.
DR ChiTaRS; DEPTOR; human.
DR GeneWiki; DEPTOR; -.
DR GenomeRNAi; 64798; -.
DR Pharos; Q8TB45; Tchem.
DR PRO; PR:Q8TB45; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q8TB45; protein.
DR Bgee; ENSG00000155792; Expressed in parotid gland and 202 other tissues.
DR Genevisible; Q8TB45; HS.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0045792; P:negative regulation of cell size; IMP:UniProtKB.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:UniProtKB.
DR GO; GO:0032007; P:negative regulation of TOR signaling; IMP:UniProtKB.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IGI:FlyBase.
DR GO; GO:1903940; P:negative regulation of TORC2 signaling; IGI:FlyBase.
DR GO; GO:2001236; P:regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR CDD; cd04442; DEP_1_DEP6; 1.
DR CDD; cd04441; DEP_2_DEP6; 1.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR037589; DEPTOR.
DR InterPro; IPR037335; DEPTOR_DEP_1.
DR InterPro; IPR037336; DEPTOR_DEP_2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR22829:SF18; PTHR22829:SF18; 1.
DR Pfam; PF00610; DEP; 2.
DR SMART; SM00049; DEP; 2.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF46785; SSF46785; 2.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50186; DEP; 2.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..409
FT /note="DEP domain-containing mTOR-interacting protein"
FT /id="PRO_0000284784"
FT DOMAIN 36..119
FT /note="DEP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 145..219
FT /note="DEP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 330..407
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
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 ECO:0007744|PubMed:22814378"
FT MOD_RES 241
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19446321"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19446321,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19446321"
FT MOD_RES 259
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19446321"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19446321"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19446321"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q570Y9"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19446321"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19446321"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19446321"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19446321"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19446321"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19446321"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19446321"
FT VAR_SEQ 42..142
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054681"
FT VARIANT 148
FT /note="N -> S (in dbSNP:rs34057546)"
FT /id="VAR_031816"
FT VARIANT 204
FT /note="N -> S (in dbSNP:rs2271900)"
FT /evidence="ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_031817"
FT VARIANT 389
FT /note="S -> N (in dbSNP:rs4871827)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_031818"
FT CONFLICT 166
FT /note="M -> V (in Ref. 2; BAB14054)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="R -> G (in Ref. 1; CAB66613)"
FT /evidence="ECO:0000305"
FT HELIX 22..46
FT /evidence="ECO:0007829|PDB:7DKL"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:7DKL"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:7DKL"
FT HELIX 66..75
FT /evidence="ECO:0007829|PDB:7DKL"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:7PED"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:7DKL"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:7DKL"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:7DKL"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:7DKL"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:7DKL"
FT HELIX 128..143
FT /evidence="ECO:0007829|PDB:7DKL"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:7DKL"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:7DKL"
FT HELIX 167..176
FT /evidence="ECO:0007829|PDB:7DKL"
FT HELIX 183..195
FT /evidence="ECO:0007829|PDB:7DKL"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:7DKL"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:7DKL"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:7DKL"
FT HELIX 227..231
FT /evidence="ECO:0007829|PDB:7DKL"
FT HELIX 316..320
FT /evidence="ECO:0007829|PDB:7PE8"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:7PE7"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:7PE8"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:7PE8"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:7PE8"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:7PE8"
FT HELIX 360..363
FT /evidence="ECO:0007829|PDB:7PE8"
FT STRAND 371..375
FT /evidence="ECO:0007829|PDB:7PE7"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:7PE8"
FT HELIX 385..394
FT /evidence="ECO:0007829|PDB:7PE8"
FT STRAND 397..403
FT /evidence="ECO:0007829|PDB:7PE8"
SQ SEQUENCE 409 AA; 46294 MW; AD132F0E9AFFB90C CRC64;
MEEGGSTGSA GSDSSTSGSG GAQQRELERM AEVLVTGEQL RLRLHEEKVI KDRRHHLKTY
PNCFVAKELI DWLIEHKEAS DRETAIKLMQ KLADRGIIHH VCDEHKEFKD VKLFYRFRKD
DGTFPLDNEV KAFMRGQRLY EKLMSPENTL LQPREEEGVK YERTFMASEF LDWLVQEGEA
TTRKEAEQLC HRLMEHGIIQ HVSNKHPFVD SNLLYQFRMN FRRRRRLMEL LNEKSPSSQE
THDSPFCLRK QSHDNRKSTS FMSVSPSKEI KIVSAVRRSS MSSCGSSGYF SSSPTLSSSP
PVLCNPKSVL KRPVTSEELL TPGAPYARKT FTIVGDAVGW GFVVRGSKPC HIQAVDPSGP
AAAAGMKVCQ FVVSVNGLNV LHVDYRTVSN LILTGPRTIV MEVMEELEC
