GenomeNet

Database: UniProt
Entry: ERG_HUMAN
LinkDB: ERG_HUMAN
Original site: ERG_HUMAN 
ID   ERG_HUMAN               Reviewed;         486 AA.
AC   P11308; B4DTW5; B4E0T4; Q16113; Q6XXX4; Q6XXX5; Q8IXK9;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   16-OCT-2019, entry version 206.
DE   RecName: Full=Transcriptional regulator ERG;
DE   AltName: Full=Transforming protein ERG;
GN   Name=ERG;
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 [MRNA] (ISOFORM ERG-2).
RX   PubMed=3299708; DOI=10.1126/science.3299708;
RA   Rao V.N., Papas T.S., Shyam E., Reddy P.;
RT   "erg, a human ets-related gene on chromosome 21: alternative splicing,
RT   polyadenylation, and translation.";
RL   Science 237:635-639(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ERG-1).
RX   PubMed=3476934; DOI=10.1073/pnas.84.17.6131;
RA   Reddy E.S.P., Rao V.N., Papas T.S.;
RT   "The erg gene: a human gene related to the ets oncogene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:6131-6135(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7).
RX   PubMed=14693372; DOI=10.1016/j.gene.2003.09.047;
RA   Owczarek C.M., Portbury K.J., Hardy M.P., O'Leary D.A., Kudoh J.,
RA   Shibuya K., Shimizu N., Kola I., Hertzog P.J.;
RT   "Detailed mapping of the ERG-ETS2 interval of human chromosome 21 and
RT   comparison with the region of conserved synteny on mouse chromosome
RT   16.";
RL   Gene 324:65-77(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND ERG-1).
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.,
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC   TISSUE=Testis;
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   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 230-259 (ISOFORM ERG-3).
RX   PubMed=8290279;
RA   Prasad D.D., Rao V.N., Lee L., Reddy E.S.;
RT   "Differentially spliced erg-3 product functions as a transcriptional
RT   activator.";
RL   Oncogene 9:669-673(1994).
RN   [7]
RP   CHROMOSOMAL TRANSLOCATION WITH EWSR1.
RX   PubMed=8076344; DOI=10.1016/0165-4608(94)90063-9;
RA   Dunn T., Praissman L., Hagag N., Viola M.V.;
RT   "ERG gene is translocated in an Ewing's sarcoma cell line.";
RL   Cancer Genet. Cytogenet. 76:19-22(1994).
RN   [8]
RP   CHROMOSOMAL TRANSLOCATION WITH FUS.
RX   PubMed=8187069;
RA   Ichikawa H., Shimizu K., Hayashi Y., Ohki M.;
RT   "An RNA-binding protein gene, TLS/FUS, is fused to ERG in human
RT   myeloid leukemia with t(16;21) chromosomal translocation.";
RL   Cancer Res. 54:2865-2868(1994).
RN   [9]
RP   CHROMOSOMAL TRANSLOCATION WITH ELF4.
RX   PubMed=16303180; DOI=10.1016/j.leukres.2005.10.014;
RA   Moore S.D., Offor O., Ferry J.A., Amrein P.C., Morton C.C.,
RA   Dal Cin P.;
RT   "ELF4 is fused to ERG in a case of acute myeloid leukemia with a
RT   t(X;21)(q25-26;q22).";
RL   Leuk. Res. 30:1037-1042(2006).
RN   [10]
RP   IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=17289661; DOI=10.1074/mcp.m600346-mcp200;
RA   Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA   Johnsen A.H., Christiansen J., Nielsen F.C.;
RT   "Molecular composition of IMP1 ribonucleoprotein granules.";
RL   Mol. Cell. Proteomics 6:798-811(2007).
RN   [11]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-289, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-
RT   modification with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [12]
RP   STRUCTURE BY NMR OF 112-208.
RX   PubMed=15351649; DOI=10.1016/j.jmb.2004.07.094;
RA   Mackereth C.D., Scharpf M., Gentile L.N., MacIntosh S.E.,
RA   Slupsky C.M., McIntosh L.P.;
RT   "Diversity in structure and function of the Ets family PNT domains.";
RL   J. Mol. Biol. 342:1249-1264(2004).
CC   -!- FUNCTION: Transcriptional regulator. May participate in
CC       transcriptional regulation through the recruitment of SETDB1
CC       histone methyltransferase and subsequent modification of local
CC       chromatin structure.
CC   -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC       containing untranslated mRNAs. Interacts with SETDB1.
CC       {ECO:0000269|PubMed:17289661}.
CC   -!- INTERACTION:
CC       P10275:AR; NbExp=4; IntAct=EBI-79704, EBI-608057;
CC       O75164:KDM4A; NbExp=2; IntAct=EBI-79704, EBI-936709;
CC       P09874:PARP1; NbExp=7; IntAct=EBI-79704, EBI-355676;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00237, ECO:0000269|PubMed:17289661}. Cytoplasm
CC       {ECO:0000269|PubMed:17289661}. Note=Localized in cytoplasmic mRNP
CC       granules containing untranslated mRNAs.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=ERG-3;
CC         IsoId=P11308-3; Sequence=Displayed;
CC       Name=ERG-2;
CC         IsoId=P11308-1; Sequence=VSP_026579;
CC       Name=ERG-1;
CC         IsoId=P11308-2; Sequence=VSP_001469, VSP_026579;
CC       Name=5;
CC         IsoId=P11308-4; Sequence=VSP_026584;
CC       Name=7;
CC         IsoId=P11308-5; Sequence=VSP_026582, VSP_026583;
CC       Name=8;
CC         IsoId=P11308-6; Sequence=VSP_026580, VSP_026581;
CC   -!- DISEASE: Ewing sarcoma (ES) [MIM:612219]: A highly malignant,
CC       metastatic, primitive small round cell tumor of bone and soft
CC       tissue that affects children and adolescents. It belongs to the
CC       Ewing sarcoma family of tumors, a group of morphologically
CC       heterogeneous neoplasms that share the same cytogenetic features.
CC       They are considered neural tumors derived from cells of the neural
CC       crest. Ewing sarcoma represents the less differentiated form of
CC       the tumors. {ECO:0000269|PubMed:8076344}. Note=The gene
CC       represented in this entry is involved in disease pathogenesis. A
CC       chromosomal aberration involving ERG has been found in patients
CC       with Erwing sarcoma. Translocation t(21;22)(q22;q12) with EWSR1.
CC       {ECO:0000269|PubMed:8076344}.
CC   -!- DISEASE: Note=Chromosomal aberrations involving ERG have been
CC       found in acute myeloid leukemia (AML). Translocation
CC       t(16;21)(p11;q22) with FUS (PubMed:8187069). Translocation
CC       t(X;21)(q25-26;q22) with ELF4 (PubMed:16303180).
CC       {ECO:0000269|PubMed:16303180, ECO:0000269|PubMed:8187069}.
CC   -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/ERGID53ch21q22.html";
DR   EMBL; M17254; AAA52398.1; -; mRNA.
DR   EMBL; M21535; AAA35811.1; -; mRNA.
DR   EMBL; AY204741; AAP41719.1; -; mRNA.
DR   EMBL; AY204742; AAP41720.1; -; mRNA.
DR   EMBL; AK300395; BAG62127.1; -; mRNA.
DR   EMBL; AK303518; BAG64546.1; -; mRNA.
DR   EMBL; BC040168; AAH40168.1; -; mRNA.
DR   EMBL; S68130; AAB29724.1; -; mRNA.
DR   CCDS; CCDS13657.1; -. [P11308-1]
DR   CCDS; CCDS13658.1; -. [P11308-4]
DR   CCDS; CCDS46648.1; -. [P11308-3]
DR   CCDS; CCDS58789.1; -. [P11308-2]
DR   PIR; A94294; TVHUEG.
DR   RefSeq; NP_001129626.1; NM_001136154.1. [P11308-3]
DR   RefSeq; NP_001129627.1; NM_001136155.1.
DR   RefSeq; NP_001230357.1; NM_001243428.1. [P11308-3]
DR   RefSeq; NP_001230358.1; NM_001243429.1. [P11308-2]
DR   RefSeq; NP_001230361.1; NM_001243432.2. [P11308-5]
DR   RefSeq; NP_001278320.1; NM_001291391.1. [P11308-6]
DR   RefSeq; NP_004440.1; NM_004449.4. [P11308-1]
DR   RefSeq; NP_891548.1; NM_182918.3. [P11308-4]
DR   PDB; 1SXE; NMR; -; A=115-208.
DR   PDB; 4IRG; X-ray; 1.70 A; A=313-412.
DR   PDB; 4IRH; X-ray; 2.10 A; A=287-412.
DR   PDB; 4IRI; X-ray; 2.77 A; A=287-412.
DR   PDB; 5YBC; X-ray; 2.50 A; A/C=317-408.
DR   PDB; 5YBD; X-ray; 2.77 A; A/X=317-406.
DR   PDBsum; 1SXE; -.
DR   PDBsum; 4IRG; -.
DR   PDBsum; 4IRH; -.
DR   PDBsum; 4IRI; -.
DR   PDBsum; 5YBC; -.
DR   PDBsum; 5YBD; -.
DR   SMR; P11308; -.
DR   BioGrid; 108389; 94.
DR   CORUM; P11308; -.
DR   DIP; DIP-31028N; -.
DR   ELM; P11308; -.
DR   IntAct; P11308; 17.
DR   MINT; P11308; -.
DR   STRING; 9606.ENSP00000414150; -.
DR   BindingDB; P11308; -.
DR   ChEMBL; CHEMBL1293191; -.
DR   iPTMnet; P11308; -.
DR   PhosphoSitePlus; P11308; -.
DR   BioMuta; ERG; -.
DR   DMDM; 152031600; -.
DR   jPOST; P11308; -.
DR   MassIVE; P11308; -.
DR   PaxDb; P11308; -.
DR   PeptideAtlas; P11308; -.
DR   PRIDE; P11308; -.
DR   ProteomicsDB; 52735; -. [P11308-3]
DR   ProteomicsDB; 52736; -. [P11308-1]
DR   ProteomicsDB; 52737; -. [P11308-2]
DR   ProteomicsDB; 52738; -. [P11308-4]
DR   ProteomicsDB; 52739; -. [P11308-5]
DR   ProteomicsDB; 52740; -. [P11308-6]
DR   TopDownProteomics; P11308-6; -. [P11308-6]
DR   DNASU; 2078; -.
DR   Ensembl; ENST00000288319; ENSP00000288319; ENSG00000157554. [P11308-4]
DR   Ensembl; ENST00000398897; ENSP00000381871; ENSG00000157554. [P11308-2]
DR   Ensembl; ENST00000398911; ENSP00000381882; ENSG00000157554. [P11308-1]
DR   Ensembl; ENST00000398919; ENSP00000381891; ENSG00000157554. [P11308-3]
DR   Ensembl; ENST00000417133; ENSP00000414150; ENSG00000157554. [P11308-3]
DR   Ensembl; ENST00000442448; ENSP00000394694; ENSG00000157554. [P11308-1]
DR   GeneID; 2078; -.
DR   KEGG; hsa:2078; -.
DR   UCSC; uc002yxa.4; human. [P11308-3]
DR   CTD; 2078; -.
DR   DisGeNET; 2078; -.
DR   GeneCards; ERG; -.
DR   HGNC; HGNC:3446; ERG.
DR   HPA; CAB018377; -.
DR   HPA; HPA046598; -.
DR   MalaCards; ERG; -.
DR   MIM; 165080; gene.
DR   MIM; 612219; phenotype.
DR   neXtProt; NX_P11308; -.
DR   OpenTargets; ENSG00000157554; -.
DR   Orphanet; 319; Ewing sarcoma.
DR   Orphanet; 370334; Extraskeletal Ewing sarcoma.
DR   PharmGKB; PA27858; -.
DR   eggNOG; KOG3806; Eukaryota.
DR   eggNOG; ENOG410Z0ZF; LUCA.
DR   GeneTree; ENSGT00940000160662; -.
DR   InParanoid; P11308; -.
DR   KO; K09435; -.
DR   OMA; ECAYGSP; -.
DR   OrthoDB; 1568974at2759; -.
DR   PhylomeDB; P11308; -.
DR   TreeFam; TF350537; -.
DR   SignaLink; P11308; -.
DR   SIGNOR; P11308; -.
DR   ChiTaRS; ERG; human.
DR   EvolutionaryTrace; P11308; -.
DR   GeneWiki; ERG_(gene); -.
DR   GenomeRNAi; 2078; -.
DR   Pharos; P11308; -.
DR   PRO; PR:P11308; -.
DR   Proteomes; UP000005640; Chromosome 21.
DR   Bgee; ENSG00000157554; Expressed in 197 organ(s), highest expression level in tendon of biceps brachii.
DR   ExpressionAtlas; P11308; baseline and differential.
DR   Genevisible; P11308; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000790; C:nuclear chromatin; ISA:NTNU_SB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IC:NTNU_SB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 1.10.150.50; -; 1.
DR   InterPro; IPR000418; Ets_dom.
DR   InterPro; IPR003118; Pointed_dom.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00178; Ets; 1.
DR   Pfam; PF02198; SAM_PNT; 1.
DR   PRINTS; PR00454; ETSDOMAIN.
DR   SMART; SM00413; ETS; 1.
DR   SMART; SM00251; SAM_PNT; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF47769; SSF47769; 1.
DR   PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR   PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR   PROSITE; PS50061; ETS_DOMAIN_3; 1.
DR   PROSITE; PS51433; PNT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Chromosomal rearrangement;
KW   Complete proteome; Cytoplasm; DNA-binding; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Proto-oncogene; Reference proteome; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN         1    486       Transcriptional regulator ERG.
FT                                /FTId=PRO_0000204103.
FT   DOMAIN      120    206       PNT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00762}.
FT   DNA_BIND    318    398       ETS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00237}.
FT   SITE        469    470       Breakpoint for translocation to form
FT                                ELF4-ERG oncogene.
FT   MOD_RES      55     55       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P81270}.
FT   MOD_RES      88     88       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P81270}.
FT   MOD_RES     103    103       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P81270}.
FT   CROSSLNK    289    289       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   VAR_SEQ       1     99       Missing (in isoform ERG-1).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:3476934}.
FT                                /FTId=VSP_001469.
FT   VAR_SEQ       1     11       MIQTVPDPAAH -> MAST (in isoform 5).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_026584.
FT   VAR_SEQ     232    255       Missing (in isoform ERG-1 and isoform
FT                                ERG-2). {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:3299708,
FT                                ECO:0000303|PubMed:3476934}.
FT                                /FTId=VSP_026579.
FT   VAR_SEQ     256    325       DLPYEPPRRSAWTGHGHPTPQSKAAQPSPSTVPKTEDQRPQ
FT                                LDPYQILGPTSSRLANPGSGQIQLWQFLL -> GTKTPLCD
FT                                LFIERHPRCPAEIRALSHVIQRELIPELKPVPDSLILPLLI
FT                                WRLNPLKPFHSKTTLKELRAD (in isoform 8).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_026580.
FT   VAR_SEQ     315    317       SGQ -> WTQ (in isoform 7).
FT                                {ECO:0000303|PubMed:14693372}.
FT                                /FTId=VSP_026582.
FT   VAR_SEQ     318    486       Missing (in isoform 7).
FT                                {ECO:0000303|PubMed:14693372}.
FT                                /FTId=VSP_026583.
FT   VAR_SEQ     326    486       Missing (in isoform 8). {ECO:0000305}.
FT                                /FTId=VSP_026581.
FT   HELIX       116    119       {ECO:0000244|PDB:1SXE}.
FT   TURN        127    130       {ECO:0000244|PDB:1SXE}.
FT   STRAND      131    134       {ECO:0000244|PDB:1SXE}.
FT   HELIX       143    157       {ECO:0000244|PDB:1SXE}.
FT   HELIX       164    166       {ECO:0000244|PDB:1SXE}.
FT   HELIX       172    175       {ECO:0000244|PDB:1SXE}.
FT   HELIX       180    183       {ECO:0000244|PDB:1SXE}.
FT   TURN        184    186       {ECO:0000244|PDB:1SXE}.
FT   HELIX       189    202       {ECO:0000244|PDB:1SXE}.
FT   HELIX       320    328       {ECO:0000244|PDB:4IRG}.
FT   HELIX       331    333       {ECO:0000244|PDB:4IRG}.
FT   TURN        334    336       {ECO:0000244|PDB:4IRG}.
FT   STRAND      338    340       {ECO:0000244|PDB:5YBC}.
FT   TURN        341    344       {ECO:0000244|PDB:5YBC}.
FT   STRAND      345    347       {ECO:0000244|PDB:4IRG}.
FT   HELIX       351    362       {ECO:0000244|PDB:4IRG}.
FT   HELIX       369    381       {ECO:0000244|PDB:4IRG}.
FT   STRAND      384    387       {ECO:0000244|PDB:4IRG}.
FT   STRAND      394    397       {ECO:0000244|PDB:4IRG}.
FT   HELIX       399    405       {ECO:0000244|PDB:4IRG}.
SQ   SEQUENCE   486 AA;  54608 MW;  A0B548DFAE25029E CRC64;
     MIQTVPDPAA HIKEALSVVS EDQSLFECAY GTPHLAKTEM TASSSSDYGQ TSKMSPRVPQ
     QDWLSQPPAR VTIKMECNPS QVNGSRNSPD ECSVAKGGKM VGSPDTVGMN YGSYMEEKHM
     PPPNMTTNER RVIVPADPTL WSTDHVRQWL EWAVKEYGLP DVNILLFQNI DGKELCKMTK
     DDFQRLTPSY NADILLSHLH YLRETPLPHL TSDDVDKALQ NSPRLMHARN TGGAAFIFPN
     TSVYPEATQR ITTRPDLPYE PPRRSAWTGH GHPTPQSKAA QPSPSTVPKT EDQRPQLDPY
     QILGPTSSRL ANPGSGQIQL WQFLLELLSD SSNSSCITWE GTNGEFKMTD PDEVARRWGE
     RKSKPNMNYD KLSRALRYYY DKNIMTKVHG KRYAYKFDFH GIAQALQPHP PESSLYKYPS
     DLPYMGSYHA HPQKMNFVAP HPPALPVTSS SFFAAPNPYW NSPTGGIYPN TRLPTSHMPS
     HLGTYY
//
DBGET integrated database retrieval system