GenomeNet

Database: UniProt
Entry: P11308
LinkDB: P11308
Original site: P11308 
ID   ERG_HUMAN               Reviewed;         479 AA.
AC   P11308; B4DTW5; B4E0T4; Q16113; Q6XXX4; Q6XXX5; Q8IXK9;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   12-AUG-2020, sequence version 3.
DT   07-OCT-2020, entry version 212.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
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 4).
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] (ISOFORMS 5 AND 6).
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 16.";
RL   Gene 324:65-77(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 230-259 (ISOFORM 2).
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 myeloid
RT   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., 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-282, AND IDENTIFICATION BY MASS
RP   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-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [12]
RP   STRUCTURE BY NMR OF 105-201.
RX   PubMed=15351649; DOI=10.1016/j.jmb.2004.07.094;
RA   Mackereth C.D., Scharpf M., Gentile L.N., MacIntosh S.E., Slupsky C.M.,
RA   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 transcriptional
CC       regulation through the recruitment of SETDB1 histone methyltransferase
CC       and subsequent modification of local 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       P11308; P10275: AR; NbExp=4; IntAct=EBI-79704, EBI-608057;
CC       P11308; O75164: KDM4A; NbExp=2; IntAct=EBI-79704, EBI-936709;
CC       P11308; P09874: PARP1; NbExp=7; IntAct=EBI-79704, EBI-355676;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237,
CC       ECO:0000269|PubMed:17289661}. Cytoplasm {ECO:0000269|PubMed:17289661}.
CC       Note=Localized in cytoplasmic mRNP granules containing untranslated
CC       mRNAs.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=P11308-4; Sequence=Displayed;
CC       Name=2; Synonyms=ERG-3;
CC         IsoId=P11308-3; Sequence=VSP_060678;
CC       Name=3; Synonyms=ERG-2;
CC         IsoId=P11308-1; Sequence=VSP_060678, VSP_060679;
CC       Name=4; Synonyms=ERG-1;
CC         IsoId=P11308-2; Sequence=VSP_060677, VSP_060679;
CC       Name=5;
CC         IsoId=P11308-5; Sequence=VSP_060678, VSP_060681, VSP_060682;
CC       Name=6;
CC         IsoId=P11308-6; Sequence=VSP_060678, VSP_060680, VSP_060683;
CC   -!- DISEASE: Ewing sarcoma (ES) [MIM:612219]: A highly malignant,
CC       metastatic, primitive small round cell tumor of bone and soft tissue
CC       that affects children and adolescents. It belongs to the Ewing sarcoma
CC       family of tumors, a group of morphologically heterogeneous neoplasms
CC       that share the same cytogenetic features. They are considered neural
CC       tumors derived from cells of the neural crest. Ewing sarcoma represents
CC       the less differentiated form of the tumors.
CC       {ECO:0000269|PubMed:8076344}. Note=The gene represented in this entry
CC       is involved in disease pathogenesis. A chromosomal aberration involving
CC       ERG has been found in patients with Erwing sarcoma. Translocation
CC       t(21;22)(q22;q12) with EWSR1. {ECO:0000269|PubMed:8076344}.
CC   -!- DISEASE: Note=Chromosomal aberrations involving ERG have been found in
CC       acute myeloid leukemia (AML). Translocation t(16;21)(p11;q22) with FUS
CC       (PubMed:8187069). Translocation t(X;21)(q25-26;q22) with ELF4
CC       (PubMed:16303180). {ECO:0000269|PubMed:16303180,
CC       ECO:0000269|PubMed:8187069}.
CC   -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       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=108-201.
DR   PDB; 4IRG; X-ray; 1.70 A; A=306-405.
DR   PDB; 4IRH; X-ray; 2.10 A; A=280-405.
DR   PDB; 4IRI; X-ray; 2.77 A; A=280-405.
DR   PDB; 5YBC; X-ray; 2.50 A; A/C=310-401.
DR   PDB; 5YBD; X-ray; 2.77 A; A/X=310-399.
DR   PDBsum; 1SXE; -.
DR   PDBsum; 4IRG; -.
DR   PDBsum; 4IRH; -.
DR   PDBsum; 4IRI; -.
DR   PDBsum; 5YBC; -.
DR   PDBsum; 5YBD; -.
DR   BMRB; P11308; -.
DR   SMR; P11308; -.
DR   BioGRID; 108389; 95.
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   ABCD; P11308; 1 sequenced antibody.
DR   Antibodypedia; 4338; 568 antibodies.
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. [P11308-4]
DR   CTD; 2078; -.
DR   DisGeNET; 2078; -.
DR   EuPathDB; HostDB:ENSG00000157554.18; -.
DR   GeneCards; ERG; -.
DR   HGNC; HGNC:3446; ERG.
DR   HPA; ENSG00000157554; Low tissue specificity.
DR   MalaCards; ERG; -.
DR   MIM; 165080; gene.
DR   MIM; 612219; phenotype.
DR   neXtProt; NX_P11308; -.
DR   OpenTargets; ENSG00000157554; -.
DR   Orphanet; 370334; Extraskeletal Ewing sarcoma.
DR   Orphanet; 319; Skeletal Ewing sarcoma.
DR   PharmGKB; PA27858; -.
DR   eggNOG; KOG3806; Eukaryota.
DR   GeneTree; ENSGT00940000160662; -.
DR   HOGENOM; CLU_045216_0_0_1; -.
DR   InParanoid; P11308; -.
DR   KO; K09435; -.
DR   OMA; TWTSHSH; -.
DR   PhylomeDB; P11308; -.
DR   TreeFam; TF350537; -.
DR   PathwayCommons; P11308; -.
DR   SignaLink; P11308; -.
DR   SIGNOR; P11308; -.
DR   BioGRID-ORCS; 2078; 10 hits in 894 CRISPR screens.
DR   ChiTaRS; ERG; human.
DR   EvolutionaryTrace; P11308; -.
DR   GeneWiki; ERG_(gene); -.
DR   GenomeRNAi; 2078; -.
DR   Pharos; P11308; Tchem.
DR   PRO; PR:P11308; -.
DR   Proteomes; UP000005640; Chromosome 21.
DR   RNAct; P11308; protein.
DR   Bgee; ENSG00000157554; Expressed in tendon of biceps brachii and 208 other tissues.
DR   ExpressionAtlas; P11308; baseline and differential.
DR   Genevisible; P11308; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:InterPro.
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; IMP: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 cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
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; Cytoplasm;
KW   DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Proto-oncogene;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..479
FT                   /note="Transcriptional regulator ERG"
FT                   /id="PRO_0000204103"
FT   DOMAIN          113..199
FT                   /note="PNT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00762"
FT   DNA_BIND        311..391
FT                   /note="ETS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT   SITE            462..463
FT                   /note="Breakpoint for translocation to form ELF4-ERG
FT                   oncogene"
FT   MOD_RES         48
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P81270"
FT   MOD_RES         81
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P81270"
FT   MOD_RES         96
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P81270"
FT   CROSSLNK        282
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:28112733"
FT   VAR_SEQ         1..92
FT                   /note="Missing (in isoform 4)"
FT                   /id="VSP_060677"
FT   VAR_SEQ         1..4
FT                   /note="MAST -> MIQTVPDPAAH (in isoform 2, isoform 3,
FT                   isoform 5 and isoform 6)"
FT                   /id="VSP_060678"
FT   VAR_SEQ         225..248
FT                   /note="Missing (in isoform 3 and isoform 4)"
FT                   /id="VSP_060679"
FT   VAR_SEQ         249..318
FT                   /note="DLPYEPPRRSAWTGHGHPTPQSKAAQPSPSTVPKTEDQRPQLDPYQILGPTS
FT                   SRLANPGSGQIQLWQFLL -> GTKTPLCDLFIERHPRCPAEIRALSHVIQRELIPELK
FT                   PVPDSLILPLLIWRLNPLKPFHSKTTLKELRAD (in isoform 6)"
FT                   /id="VSP_060680"
FT   VAR_SEQ         308..310
FT                   /note="SGQ -> WTQ (in isoform 5)"
FT                   /id="VSP_060681"
FT   VAR_SEQ         311..479
FT                   /note="Missing (in isoform 5)"
FT                   /id="VSP_060682"
FT   VAR_SEQ         319..479
FT                   /note="Missing (in isoform 6)"
FT                   /id="VSP_060683"
FT   HELIX           116..119
FT                   /evidence="ECO:0000244|PDB:1SXE"
FT   TURN            127..130
FT                   /evidence="ECO:0000244|PDB:1SXE"
FT   STRAND          131..134
FT                   /evidence="ECO:0000244|PDB:1SXE"
FT   HELIX           143..157
FT                   /evidence="ECO:0000244|PDB:1SXE"
FT   HELIX           164..166
FT                   /evidence="ECO:0000244|PDB:1SXE"
FT   HELIX           172..175
FT                   /evidence="ECO:0000244|PDB:1SXE"
FT   HELIX           180..183
FT                   /evidence="ECO:0000244|PDB:1SXE"
FT   TURN            184..186
FT                   /evidence="ECO:0000244|PDB:1SXE"
FT   HELIX           189..202
FT                   /evidence="ECO:0000244|PDB:1SXE"
FT   HELIX           320..328
FT                   /evidence="ECO:0000244|PDB:4IRG"
FT   HELIX           331..333
FT                   /evidence="ECO:0000244|PDB:4IRG"
FT   TURN            334..336
FT                   /evidence="ECO:0000244|PDB:4IRG"
FT   STRAND          338..340
FT                   /evidence="ECO:0000244|PDB:5YBC"
FT   TURN            341..344
FT                   /evidence="ECO:0000244|PDB:5YBC"
FT   STRAND          345..347
FT                   /evidence="ECO:0000244|PDB:4IRG"
FT   HELIX           351..362
FT                   /evidence="ECO:0000244|PDB:4IRG"
FT   HELIX           369..381
FT                   /evidence="ECO:0000244|PDB:4IRG"
FT   STRAND          384..387
FT                   /evidence="ECO:0000244|PDB:4IRG"
FT   STRAND          394..397
FT                   /evidence="ECO:0000244|PDB:4IRG"
FT   HELIX           399..405
FT                   /evidence="ECO:0000244|PDB:4IRG"
SQ   SEQUENCE   479 AA;  53838 MW;  A5069C393E409483 CRC64;
     MASTIKEALS VVSEDQSLFE CAYGTPHLAK TEMTASSSSD YGQTSKMSPR VPQQDWLSQP
     PARVTIKMEC NPSQVNGSRN SPDECSVAKG GKMVGSPDTV GMNYGSYMEE KHMPPPNMTT
     NERRVIVPAD PTLWSTDHVR QWLEWAVKEY GLPDVNILLF QNIDGKELCK MTKDDFQRLT
     PSYNADILLS HLHYLRETPL PHLTSDDVDK ALQNSPRLMH ARNTGGAAFI FPNTSVYPEA
     TQRITTRPDL PYEPPRRSAW TGHGHPTPQS KAAQPSPSTV PKTEDQRPQL DPYQILGPTS
     SRLANPGSGQ IQLWQFLLEL LSDSSNSSCI TWEGTNGEFK MTDPDEVARR WGERKSKPNM
     NYDKLSRALR YYYDKNIMTK VHGKRYAYKF DFHGIAQALQ PHPPESSLYK YPSDLPYMGS
     YHAHPQKMNF VAPHPPALPV TSSSFFAAPN PYWNSPTGGI YPNTRLPTSH MPSHLGTYY
//
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