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Histone-lysine N-methyltransferase, H3 lysine-79 specific (EC 2.1.1.43) (DOT1-like protein) (Histone H3-K79 methyltransferase) (H3-K79-HMTase) (Lysine N-methyltransferase 4)

 DOT1L_HUMAN             Reviewed;        1739 AA.
Q8TEK3; O60379; Q96JL1;
15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
15-NOV-2002, sequence version 2.
23-MAY-2018, entry version 162.
RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-79 specific;
EC=2.1.1.43;
AltName: Full=DOT1-like protein;
AltName: Full=Histone H3-K79 methyltransferase;
Short=H3-K79-HMTase;
AltName: Full=Lysine N-methyltransferase 4;
Name=DOT1L; Synonyms=KIAA1814, KMT4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, AND
MUTAGENESIS OF 163-GLY--GLY-165.
PubMed=12123582; DOI=10.1016/S0960-9822(02)00901-6;
Feng Q., Wang H., Ng H.H., Erdjument-Bromage H., Tempst P., Struhl K.,
Zhang Y.;
"Methylation of H3-lysine 79 is mediated by a new family of HMTases
without a SET domain.";
Curr. Biol. 12:1052-1058(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 454-1739 (ISOFORM 2).
TISSUE=Brain;
PubMed=11347906; DOI=10.1093/dnares/8.2.85;
Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 8:85-95(2001).
[4]
PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Spleen;
PubMed=12693554; DOI=10.1093/dnares/10.1.49;
Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N.,
Ohara O.;
"Characterization of long cDNA clones from human adult spleen. II. The
complete sequences of 81 cDNA clones.";
DNA Res. 10:49-57(2003).
[5]
INTERACTION WITH MLLT10, AND SUBCELLULAR LOCATION.
PubMed=15851025; DOI=10.1016/j.cell.2005.02.020;
Okada Y., Feng Q., Lin Y., Jiang Q., Li Y., Coffield V.M., Su L.,
Xu G., Zhang Y.;
"hDOT1L links histone methylation to leukemogenesis.";
Cell 121:167-178(2005).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1001, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-775; SER-1001
AND SER-1009, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; THR-900; SER-902
AND SER-1001, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-471; THR-480;
SER-775; SER-834; SER-902; SER-1001; SER-1035 AND SER-1213, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374 AND SER-902, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297; SER-374; SER-448;
SER-775; SER-786; SER-826; SER-834; THR-900; SER-902; THR-984;
SER-997; SER-1001; SER-1009; SER-1035; SER-1093; SER-1104; SER-1213
AND SER-1246, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-416 IN COMPLEX WITH
S-ADENOSINE-L-METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY,
MUTAGENESIS OF ASN-241 AND TYR-312, NUCLEOSOME BINDING, AND
INTERACTION WITH DNA.
PubMed=12628190; DOI=10.1016/S0092-8674(03)00114-4;
Min J., Feng Q., Li Z., Zhang Y., Xu R.-M.;
"Structure of the catalytic domain of human DOT1L, a non-SET domain
nucleosomal histone methyltransferase.";
Cell 112:711-723(2003).
-!- FUNCTION: Histone methyltransferase. Methylates 'Lys-79' of
histone H3. Nucleosomes are preferred as substrate compared to
free histones. Binds to DNA.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000255|PROSITE-ProRule:PRU00902,
ECO:0000269|PubMed:12123582}.
-!- SUBUNIT: Interacts with MLLT10. {ECO:0000269|PubMed:12628190,
ECO:0000269|PubMed:15851025}.
-!- INTERACTION:
Q03111:MLLT1; NbExp=6; IntAct=EBI-2619253, EBI-1384215;
P42568:MLLT3; NbExp=6; IntAct=EBI-2619253, EBI-716132;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15851025}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=2;
IsoId=Q8TEK3-1; Sequence=Displayed;
Name=1;
IsoId=Q8TEK3-2; Sequence=VSP_002228, VSP_002229;
Note=No experimental confirmation available.;
-!- MISCELLANEOUS: In contrast to other lysine histone
methyltransferases, it does not contain a SET domain, suggesting
the existence of another mechanism for methylation of lysine
residues of histones.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. DOT1 family. {ECO:0000255|PROSITE-
ProRule:PRU00902}.
-!- SEQUENCE CAUTION:
Sequence=AAC08316.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AF509504; AAM88322.1; -; mRNA.
EMBL; AC004490; AAC08316.1; ALT_SEQ; Genomic_DNA.
EMBL; AB058717; BAB47443.1; -; mRNA.
EMBL; AK074120; BAB84946.1; -; mRNA.
CCDS; CCDS42460.1; -. [Q8TEK3-2]
RefSeq; NP_115871.1; NM_032482.2. [Q8TEK3-2]
UniGene; Hs.713641; -.
PDB; 1NW3; X-ray; 2.50 A; A=1-416.
PDB; 2MV7; NMR; -; B=877-900.
PDB; 3QOW; X-ray; 2.10 A; A=1-416.
PDB; 3QOX; X-ray; 2.30 A; A=1-416.
PDB; 3SR4; X-ray; 2.50 A; A=1-351.
PDB; 3SX0; X-ray; 2.28 A; A=1-420.
PDB; 3UWP; X-ray; 2.05 A; A=1-420.
PDB; 4EK9; X-ray; 2.50 A; A=1-416.
PDB; 4EKG; X-ray; 2.80 A; A=1-416.
PDB; 4EKI; X-ray; 2.85 A; A=1-416.
PDB; 4EQZ; X-ray; 2.15 A; A=1-420.
PDB; 4ER0; X-ray; 2.50 A; A=1-420.
PDB; 4ER3; X-ray; 2.40 A; A=1-351.
PDB; 4ER5; X-ray; 2.57 A; A=1-412.
PDB; 4ER6; X-ray; 2.30 A; A=1-412.
PDB; 4ER7; X-ray; 2.20 A; A=1-420.
PDB; 4HRA; X-ray; 3.15 A; A=1-416.
PDB; 4WVL; X-ray; 2.41 A; A=1-347.
PDB; 5DRT; X-ray; 2.69 A; A/B=2-333.
PDB; 5DRY; X-ray; 2.41 A; A/B=2-333.
PDB; 5DSX; X-ray; 2.41 A; A/B=2-332.
PDB; 5DT2; X-ray; 2.30 A; A/B=2-332.
PDB; 5DTM; X-ray; 2.20 A; A/B=2-332.
PDB; 5DTQ; X-ray; 2.61 A; A/B=2-332.
PDB; 5DTR; X-ray; 2.34 A; A/B=2-332.
PDB; 5JUW; X-ray; 2.28 A; A=1-420.
PDB; 5MVS; X-ray; 2.18 A; A/B=2-332.
PDB; 5MW3; X-ray; 2.09 A; A/B=2-332.
PDB; 5MW4; X-ray; 2.19 A; A/B=2-332.
PDBsum; 1NW3; -.
PDBsum; 2MV7; -.
PDBsum; 3QOW; -.
PDBsum; 3QOX; -.
PDBsum; 3SR4; -.
PDBsum; 3SX0; -.
PDBsum; 3UWP; -.
PDBsum; 4EK9; -.
PDBsum; 4EKG; -.
PDBsum; 4EKI; -.
PDBsum; 4EQZ; -.
PDBsum; 4ER0; -.
PDBsum; 4ER3; -.
PDBsum; 4ER5; -.
PDBsum; 4ER6; -.
PDBsum; 4ER7; -.
PDBsum; 4HRA; -.
PDBsum; 4WVL; -.
PDBsum; 5DRT; -.
PDBsum; 5DRY; -.
PDBsum; 5DSX; -.
PDBsum; 5DT2; -.
PDBsum; 5DTM; -.
PDBsum; 5DTQ; -.
PDBsum; 5DTR; -.
PDBsum; 5JUW; -.
PDBsum; 5MVS; -.
PDBsum; 5MW3; -.
PDBsum; 5MW4; -.
ProteinModelPortal; Q8TEK3; -.
SMR; Q8TEK3; -.
BioGrid; 124082; 45.
DIP; DIP-56410N; -.
IntAct; Q8TEK3; 28.
MINT; Q8TEK3; -.
STRING; 9606.ENSP00000381657; -.
BindingDB; Q8TEK3; -.
ChEMBL; CHEMBL1795117; -.
GuidetoPHARMACOLOGY; 2650; -.
iPTMnet; Q8TEK3; -.
PhosphoSitePlus; Q8TEK3; -.
BioMuta; DOT1L; -.
DMDM; 25090171; -.
EPD; Q8TEK3; -.
MaxQB; Q8TEK3; -.
PaxDb; Q8TEK3; -.
PeptideAtlas; Q8TEK3; -.
PRIDE; Q8TEK3; -.
Ensembl; ENST00000398665; ENSP00000381657; ENSG00000104885. [Q8TEK3-2]
GeneID; 84444; -.
KEGG; hsa:84444; -.
UCSC; uc002lvb.4; human. [Q8TEK3-1]
CTD; 84444; -.
DisGeNET; 84444; -.
EuPathDB; HostDB:ENSG00000104885.17; -.
GeneCards; DOT1L; -.
HGNC; HGNC:24948; DOT1L.
HPA; HPA011875; -.
HPA; HPA071217; -.
MIM; 607375; gene.
neXtProt; NX_Q8TEK3; -.
OpenTargets; ENSG00000104885; -.
PharmGKB; PA134993717; -.
eggNOG; KOG3924; Eukaryota.
eggNOG; ENOG410XSYC; LUCA.
GeneTree; ENSGT00390000013515; -.
HOGENOM; HOG000143530; -.
HOVERGEN; HBG051393; -.
InParanoid; Q8TEK3; -.
KO; K11427; -.
OMA; SMNGHAT; -.
OrthoDB; EOG091G00FV; -.
PhylomeDB; Q8TEK3; -.
TreeFam; TF106393; -.
Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
SIGNOR; Q8TEK3; -.
ChiTaRS; DOT1L; human.
EvolutionaryTrace; Q8TEK3; -.
GeneWiki; DOT1L; -.
GenomeRNAi; 84444; -.
PRO; PR:Q8TEK3; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000104885; -.
CleanEx; HS_DOT1L; -.
ExpressionAtlas; Q8TEK3; baseline and differential.
Genevisible; Q8TEK3; HS.
GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0032991; C:protein-containing complex; IDA:MGI.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0042054; F:histone methyltransferase activity; IDA:MGI.
GO; GO:0031151; F:histone methyltransferase activity (H3-K79 specific); IBA:GO_Central.
GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0006348; P:chromatin silencing at telomere; IBA:GO_Central.
GO; GO:0000077; P:DNA damage checkpoint; IBA:GO_Central.
GO; GO:0006281; P:DNA repair; IBA:GO_Central.
GO; GO:0034729; P:histone H3-K79 methylation; IDA:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0046425; P:regulation of JAK-STAT cascade; IDA:UniProtKB.
GO; GO:2000677; P:regulation of transcription regulatory region DNA binding; IMP:UniProtKB.
GO; GO:0032200; P:telomere organization; TAS:BHF-UCL.
InterPro; IPR025789; DOT1_dom.
InterPro; IPR021169; DOT1L/grappa.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF08123; DOT1; 1.
PIRSF; PIRSF037123; Histone_H3-K79_MeTrfase_met; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51569; DOT1; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromatin regulator;
Complete proteome; DNA-binding; Methyltransferase; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
S-adenosyl-L-methionine; Transferase.
CHAIN 1 1739 Histone-lysine N-methyltransferase, H3
lysine-79 specific.
/FTId=PRO_0000186089.
DOMAIN 16 330 DOT1. {ECO:0000255|PROSITE-
ProRule:PRU00902}.
REGION 136 139 S-adenosyl-L-methionine binding.
REGION 159 168 S-adenosyl-L-methionine binding.
REGION 222 223 S-adenosyl-L-methionine binding.
REGION 391 416 Required for interaction with nucleosomes
and DNA. {ECO:0000269|PubMed:12628190}.
BINDING 186 186 S-adenosyl-L-methionine.
MOD_RES 297 297 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 374 374 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 448 448 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 471 471 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 480 480 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 775 775 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 786 786 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 826 826 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 834 834 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 900 900 Phosphothreonine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 902 902 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 984 984 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 997 997 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1001 1001 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1009 1009 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1035 1035 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1093 1093 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1104 1104 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1213 1213 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1246 1246 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1537 1537 V -> N (in isoform 1).
{ECO:0000303|PubMed:12123582}.
/FTId=VSP_002228.
VAR_SEQ 1538 1739 Missing (in isoform 1).
{ECO:0000303|PubMed:12123582}.
/FTId=VSP_002229.
VARIANT 726 726 L -> M (in dbSNP:rs880525).
/FTId=VAR_014287.
VARIANT 1386 1386 G -> S (in dbSNP:rs3815308).
/FTId=VAR_014288.
VARIANT 1418 1418 V -> L (in dbSNP:rs2302061).
/FTId=VAR_014289.
MUTAGEN 163 165 GSG->RCR: Abolishes methyltransferase
activity. {ECO:0000269|PubMed:12123582}.
MUTAGEN 241 241 N->A,D: Loss of activity.
{ECO:0000269|PubMed:12628190}.
MUTAGEN 312 312 Y->A: Loss of activity.
{ECO:0000269|PubMed:12628190}.
MUTAGEN 312 312 Y->F: No effect.
{ECO:0000269|PubMed:12628190}.
CONFLICT 210 210 G -> E (in Ref. 4; BAB84946).
{ECO:0000305}.
CONFLICT 454 467 RSPHSPFYQLPPSV -> TLRTPSGSPRRTKL (in Ref.
3). {ECO:0000305}.
CONFLICT 464 464 P -> L (in Ref. 4; BAB84946).
{ECO:0000305}.
STRAND 6 9 {ECO:0000244|PDB:3UWP}.
STRAND 18 23 {ECO:0000244|PDB:3UWP}.
STRAND 26 28 {ECO:0000244|PDB:3UWP}.
HELIX 33 47 {ECO:0000244|PDB:3UWP}.
HELIX 49 54 {ECO:0000244|PDB:3UWP}.
HELIX 57 62 {ECO:0000244|PDB:3UWP}.
HELIX 68 90 {ECO:0000244|PDB:3UWP}.
STRAND 91 93 {ECO:0000244|PDB:3UWP}.
STRAND 98 100 {ECO:0000244|PDB:4ER7}.
HELIX 104 118 {ECO:0000244|PDB:3UWP}.
HELIX 122 124 {ECO:0000244|PDB:3UWP}.
HELIX 126 128 {ECO:0000244|PDB:4EQZ}.
STRAND 129 131 {ECO:0000244|PDB:3UWP}.
HELIX 133 138 {ECO:0000244|PDB:3UWP}.
HELIX 140 151 {ECO:0000244|PDB:3UWP}.
STRAND 158 163 {ECO:0000244|PDB:3UWP}.
HELIX 168 176 {ECO:0000244|PDB:3UWP}.
STRAND 180 186 {ECO:0000244|PDB:3UWP}.
HELIX 189 209 {ECO:0000244|PDB:3UWP}.
STRAND 215 220 {ECO:0000244|PDB:3UWP}.
HELIX 226 233 {ECO:0000244|PDB:3UWP}.
STRAND 236 240 {ECO:0000244|PDB:3UWP}.
TURN 243 245 {ECO:0000244|PDB:3QOW}.
HELIX 247 257 {ECO:0000244|PDB:3UWP}.
STRAND 265 270 {ECO:0000244|PDB:3UWP}.
STRAND 281 283 {ECO:0000244|PDB:3UWP}.
HELIX 287 289 {ECO:0000244|PDB:3UWP}.
STRAND 290 295 {ECO:0000244|PDB:3UWP}.
TURN 298 300 {ECO:0000244|PDB:5DTM}.
STRAND 301 303 {ECO:0000244|PDB:5MW4}.
STRAND 307 309 {ECO:0000244|PDB:4ER7}.
STRAND 313 317 {ECO:0000244|PDB:3UWP}.
HELIX 320 330 {ECO:0000244|PDB:3UWP}.
HELIX 332 342 {ECO:0000244|PDB:3UWP}.
STRAND 880 882 {ECO:0000244|PDB:2MV7}.
TURN 885 887 {ECO:0000244|PDB:2MV7}.
SEQUENCE 1739 AA; 184853 MW; EBA575CE3C090CAC CRC64;
MGEKLELRLK SPVGAEPAVY PWPLPVYDKH HDAAHEIIET IRWVCEEIPD LKLAMENYVL
IDYDTKSFES MQRLCDKYNR AIDSIHQLWK GTTQPMKLNT RPSTGLLRHI LQQVYNHSVT
DPEKLNNYEP FSPEVYGETS FDLVAQMIDE IKMTDDDLFV DLGSGVGQVV LQVAAATNCK
HHYGVEKADI PAKYAETMDR EFRKWMKWYG KKHAEYTLER GDFLSEEWRE RIANTSVIFV
NNFAFGPEVD HQLKERFANM KEGGRIVSSK PFAPLNFRIN SRNLSDIGTI MRVVELSPLK
GSVSWTGKPV SYYLHTIDRT ILENYFSSLK NPKLREEQEA ARRRQQRESK SNAATPTKGP
EGKVAGPADA PMDSGAEEEK AGAATVKKPS PSKARKKKLN KKGRKMAGRK RGRPKKMNTA
NPERKPKKNQ TALDALHAQT VSQTAASSPQ DAYRSPHSPF YQLPPSVQRH SPNPLLVAPT
PPALQKLLES FKIQYLQFLA YTKTPQYKAS LQELLGQEKE KNAQLLGAAQ QLLSHCQAQK
EEIRRLFQQK LDELGVKALT YNDLIQAQKE ISAHNQQLRE QSEQLEQDNR ALRGQSLQLL
KARCEELQLD WATLSLEKLL KEKQALKSQI SEKQRHCLEL QISIVELEKS QRQQELLQLK
SCVPPDDALS LHLRGKGALG RELEPDASRL HLELDCTKFS LPHLSSMSPE LSMNGQAAGY
ELCGVLSRPS SKQNTPQYLA SPLDQEVVPC TPSHVGRPRL EKLSGLAAPD YTRLSPAKIV
LRRHLSQDHT VPGRPAASEL HSRAEHTKEN GLPYQSPSVP GSMKLSPQDP RPLSPGALQL
AGEKSSEKGL RERAYGSSGE LITSLPISIP LSTVQPNKLP VSIPLASVVL PSRAERARST
PSPVLQPRDP SSTLEKQIGA NAHGAGSRSL ALAPAGFSYA GSVAISGALA GSPASLTPGA
EPATLDESSS SGSLFATVGS RSSTPQHPLL LAQPRNSLPA SPAHQLSSSP RLGGAAQGPL
PEASKGDLPS DSGFSDPESE AKRRIVFTIT TGAGSAKQSP SSKHSPLTAS ARGDCVPSHG
QDSRRRGRRK RASAGTPSLS AGVSPKRRAL PSVAGLFTQP SGSPLNLNSM VSNINQPLEI
TAISSPETSL KSSPVPYQDH DQPPVLKKER PLSQTNGAHY SPLTSDEEPG SEDEPSSARI
ERKIATISLE SKSPPKTLEN GGGLAGRKPA PAGEPVNSSK WKSTFSPISD IGLAKSADSP
LQASSALSQN SLFTFRPALE EPSADAKLAA HPRKGFPGSL SGADGLSPGT NPANGCTFGG
GLAADLSLHS FSDGASLPHK GPEAAGLSSP LSFPSQRGKE GSDANPFLSK RQLDGLAGLK
GEGSRGKEAG EGGLPLCGPT DKTPLLSGKA AKARDREVDL KNGHNLFISA AAVPPGSLLS
GPGLAPAASS AGGAASSAQT HRSFLGPFPP GPQFALGPMS LQANLGSVAG SSVLQSLFSS
VPAAAGLVHV SSAATRLTNS HAMGSFSGVA GGTVGGVVFN HAVPSASAHP FGARVGRGAA
CGSATLGPSP LQAAASASAS SFQAPASVET RPPPPPPPPP PPLPPPAHLG RSPAGPPVLH
APPPPNAALP PPPTLLASNP EPALLQSLAS LPPNQAFLPP TSAASLPPAN ASLSIKLTSL
PHKGARPSFT VHHQPLPRLA LAQAAPGIPQ ASATGPSAVW VSLGMPPPYA AHLSGVKPR


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