KMT5C_HUMAN
ID KMT5C_HUMAN Reviewed; 462 AA.
AC Q86Y97; Q8WZ10; Q9BRZ6;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Histone-lysine N-methyltransferase KMT5C {ECO:0000305};
DE AltName: Full=Lysine N-methyltransferase 5C;
DE AltName: Full=Lysine-specific methyltransferase 5C {ECO:0000312|HGNC:HGNC:28405};
DE AltName: Full=Suppressor of variegation 4-20 homolog 2;
DE Short=Su(var)4-20 homolog 2;
DE Short=Suv4-20h2;
DE AltName: Full=[histone H4]-N-methyl-L-lysine20 N-methyltransferase KMT5B {ECO:0000305};
DE EC=2.1.1.362 {ECO:0000269|PubMed:24396869, ECO:0000269|PubMed:28114273};
DE AltName: Full=[histone H4]-lysine20 N-methyltransferase KMT5B {ECO:0000305};
DE EC=2.1.1.361 {ECO:0000269|PubMed:24396869};
GN Name=KMT5C {ECO:0000312|HGNC:HGNC:28405}; Synonyms=SUV420H2;
GN ORFNames=PP7130;
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 GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cervix;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-129 (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-416, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-416 AND THR-422, 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 [6]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND FUNCTION.
RX PubMed=28114273; DOI=10.1038/nchembio.2282;
RA Bromberg K.D., Mitchell T.R., Upadhyay A.K., Jakob C.G., Jhala M.A.,
RA Comess K.M., Lasko L.M., Li C., Tuzon C.T., Dai Y., Li F., Eram M.S.,
RA Nuber A., Soni N.B., Manaves V., Algire M.A., Sweis R.F., Torrent M.,
RA Schotta G., Sun C., Michaelides M.R., Shoemaker A.R., Arrowsmith C.H.,
RA Brown P.J., Santhakumar V., Martin A., Rice J.C., Chiang G.G., Vedadi M.,
RA Barsyte-Lovejoy D., Pappano W.N.;
RT "The SUV4-20 inhibitor A-196 verifies a role for epigenetics in genomic
RT integrity.";
RL Nat. Chem. Biol. 13:317-324(2017).
RN [7] {ECO:0007744|PDB:3RQ4}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-248 IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE AND ZINC, CATALYTIC ACTIVITY, FUNCTION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=24396869; DOI=10.1016/j.febslet.2013.10.020;
RA Wu H., Siarheyeva A., Zeng H., Lam R., Dong A., Wu X.H., Li Y.,
RA Schapira M., Vedadi M., Min J.;
RT "Crystal structures of the human histone H4K20 methyltransferases SUV420H1
RT and SUV420H2.";
RL FEBS Lett. 587:3859-3868(2013).
CC -!- FUNCTION: Histone methyltransferase that specifically methylates
CC monomethylated 'Lys-20' (H4K20me1) and dimethylated 'Lys-20' (H4K20me2)
CC of histone H4 to produce respectively dimethylated 'Lys-20' (H4K20me2)
CC and trimethylated 'Lys-20' (H4K20me3) and thus regulates transcription
CC and maintenance of genome integrity (PubMed:24396869, PubMed:28114273).
CC In vitro also methylates unmodified 'Lys-20' (H4K20me0) of histone H4
CC and nucleosomes (PubMed:24396869). H4 'Lys-20' trimethylation
CC represents a specific tag for epigenetic transcriptional repression.
CC Mainly functions in pericentric heterochromatin regions, thereby
CC playing a central role in the establishment of constitutive
CC heterochromatin in these regions. KMT5C is targeted to histone H3 via
CC its interaction with RB1 family proteins (RB1, RBL1 and RBL2) (By
CC similarity). Facilitates TP53BP1 foci formation upon DNA damage and
CC proficient non-homologous end-joining (NHEJ)-directed DNA repair by
CC catalyzing the di- and trimethylation of 'Lys-20' of histone H4
CC (PubMed:28114273). May play a role in class switch reconbination by
CC catalyzing the di- and trimethylation of 'Lys-20' of histone H4 (By
CC similarity). {ECO:0000250|UniProtKB:Q6Q783,
CC ECO:0000269|PubMed:24396869, ECO:0000269|PubMed:28114273}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine
CC = H(+) + N(6),N(6)-dimethyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60348, Rhea:RHEA-COMP:15555, Rhea:RHEA-
CC COMP:15556, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; EC=2.1.1.362;
CC Evidence={ECO:0000269|PubMed:24396869, ECO:0000269|PubMed:28114273};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60349;
CC Evidence={ECO:0000269|PubMed:28114273};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6),N(6)-dimethyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-
CC methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(20)-[histone H4]
CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:61992, Rhea:RHEA-
CC COMP:15556, Rhea:RHEA-COMP:15998, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961,
CC ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:28114273};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61993;
CC Evidence={ECO:0000269|PubMed:28114273};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60344, Rhea:RHEA-COMP:15554, Rhea:RHEA-COMP:15555,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.361;
CC Evidence={ECO:0000269|PubMed:24396869};
CC -!- ACTIVITY REGULATION: Inhibited by 6,7-Dichloro-N-cyclopentyl-4-
CC (pyridin-4-yl)phthalazin-1-amine (A-196) with an IC(50) of 144 nM.
CC {ECO:0000269|PubMed:28114273}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21 uM for H4K20me0 {ECO:0000269|PubMed:24396869};
CC KM=16 uM for H4K20me1 {ECO:0000269|PubMed:24396869};
CC KM=0.5 uM for nucleosome {ECO:0000269|PubMed:24396869};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:24396869};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with HP1 proteins CBX1,
CC CBX3 and CBX5. Interacts with RB1 family proteins RB1, RBL1 and RBL2
CC (By similarity). {ECO:0000250|UniProtKB:Q6Q783}.
CC -!- INTERACTION:
CC Q86Y97; Q13185: CBX3; NbExp=3; IntAct=EBI-7960569, EBI-78176;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000250}.
CC Note=Associated with pericentric heterochromatin. CBX1 and CBX5 are
CC required for the localization to pericentric heterochromatin (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86Y97-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86Y97-2; Sequence=VSP_043947, VSP_043948;
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. Suvar4-20
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00903}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH05842.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC Sequence=AAL55766.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AC020922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005842; AAH05842.1; ALT_SEQ; mRNA.
DR EMBL; BC019313; AAH19313.1; -; mRNA.
DR EMBL; BC044889; AAH44889.1; -; mRNA.
DR EMBL; AF289582; AAL55766.1; ALT_SEQ; mRNA.
DR CCDS; CCDS12922.1; -. [Q86Y97-1]
DR RefSeq; NP_116090.2; NM_032701.3. [Q86Y97-1]
DR RefSeq; XP_005259395.1; XM_005259338.3.
DR RefSeq; XP_006723505.1; XM_006723442.3.
DR RefSeq; XP_011525717.1; XM_011527415.2. [Q86Y97-1]
DR PDB; 3RQ4; X-ray; 1.80 A; A=2-248.
DR PDBsum; 3RQ4; -.
DR AlphaFoldDB; Q86Y97; -.
DR SMR; Q86Y97; -.
DR BioGRID; 124257; 38.
DR IntAct; Q86Y97; 30.
DR MINT; Q86Y97; -.
DR STRING; 9606.ENSP00000255613; -.
DR BindingDB; Q86Y97; -.
DR ChEMBL; CHEMBL2321644; -.
DR GuidetoPHARMACOLOGY; 2718; -.
DR iPTMnet; Q86Y97; -.
DR PhosphoSitePlus; Q86Y97; -.
DR BioMuta; KMT5C; -.
DR DMDM; 74727906; -.
DR EPD; Q86Y97; -.
DR jPOST; Q86Y97; -.
DR MassIVE; Q86Y97; -.
DR MaxQB; Q86Y97; -.
DR PaxDb; Q86Y97; -.
DR PeptideAtlas; Q86Y97; -.
DR PRIDE; Q86Y97; -.
DR ProteomicsDB; 70387; -. [Q86Y97-1]
DR ProteomicsDB; 70388; -. [Q86Y97-2]
DR ABCD; Q86Y97; 1 sequenced antibody.
DR Antibodypedia; 46420; 80 antibodies from 20 providers.
DR DNASU; 84787; -.
DR Ensembl; ENST00000255613.8; ENSP00000255613.3; ENSG00000133247.14. [Q86Y97-1]
DR Ensembl; ENST00000445196.5; ENSP00000397296.1; ENSG00000133247.14. [Q86Y97-2]
DR Ensembl; ENST00000592631.5; ENSP00000467499.1; ENSG00000133247.14. [Q86Y97-2]
DR GeneID; 84787; -.
DR KEGG; hsa:84787; -.
DR MANE-Select; ENST00000255613.8; ENSP00000255613.3; NM_032701.4; NP_116090.2.
DR UCSC; uc002qkj.5; human. [Q86Y97-1]
DR CTD; 84787; -.
DR DisGeNET; 84787; -.
DR GeneCards; KMT5C; -.
DR HGNC; HGNC:28405; KMT5C.
DR HPA; ENSG00000133247; Low tissue specificity.
DR MIM; 613198; gene.
DR neXtProt; NX_Q86Y97; -.
DR OpenTargets; ENSG00000133247; -.
DR PharmGKB; PA134934307; -.
DR VEuPathDB; HostDB:ENSG00000133247; -.
DR eggNOG; KOG2589; Eukaryota.
DR GeneTree; ENSGT00940000161700; -.
DR HOGENOM; CLU_040002_0_0_1; -.
DR InParanoid; Q86Y97; -.
DR OMA; GGWTAHY; -.
DR OrthoDB; 236983at2759; -.
DR PhylomeDB; Q86Y97; -.
DR TreeFam; TF106433; -.
DR BioCyc; MetaCyc:HS13469-MON; -.
DR BRENDA; 2.1.1.361; 2681.
DR PathwayCommons; Q86Y97; -.
DR Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR SignaLink; Q86Y97; -.
DR SIGNOR; Q86Y97; -.
DR BioGRID-ORCS; 84787; 11 hits in 1090 CRISPR screens.
DR ChiTaRS; KMT5C; human.
DR GenomeRNAi; 84787; -.
DR Pharos; Q86Y97; Tchem.
DR PRO; PR:Q86Y97; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q86Y97; protein.
DR Bgee; ENSG00000133247; Expressed in pancreatic ductal cell and 178 other tissues.
DR ExpressionAtlas; Q86Y97; baseline and differential.
DR Genevisible; Q86Y97; HS.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IEA:Ensembl.
DR GO; GO:0000792; C:heterochromatin; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IEA:Ensembl.
DR GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); IDA:UniProtKB.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
DR GO; GO:0034772; P:histone H4-K20 dimethylation; IEA:InterPro.
DR GO; GO:0034773; P:histone H4-K20 trimethylation; IBA:GO_Central.
DR GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; IMP:UniProtKB.
DR GO; GO:0045830; P:positive regulation of isotype switching; ISS:UniProtKB.
DR CDD; cd19185; SET_KMT5C; 1.
DR Gene3D; 1.10.10.1700; -; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR041938; Hist-Lys_N-MTase_N.
DR InterPro; IPR044425; KMT5C_SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR039977; Suv4-20/Set9.
DR InterPro; IPR025790; Suv4-20_animal.
DR PANTHER; PTHR12977; PTHR12977; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51570; SAM_MT43_SUVAR420_2; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromatin regulator; Chromosome;
KW Metal-binding; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase; Zinc.
FT CHAIN 1..462
FT /note="Histone-lysine N-methyltransferase KMT5C"
FT /id="PRO_0000281793"
FT DOMAIN 104..218
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 325..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..435
FT /note="Required for heterochromatin localization"
FT /evidence="ECO:0000250"
FT COMPBIAS 329..346
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24396869,
FT ECO:0007744|PDB:3RQ4"
FT BINDING 114..117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24396869,
FT ECO:0007744|PDB:3RQ4"
FT BINDING 121
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24396869,
FT ECO:0007744|PDB:3RQ4"
FT BINDING 160
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24396869,
FT ECO:0007744|PDB:3RQ4"
FT BINDING 169
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24396869,
FT ECO:0007744|PDB:3RQ4"
FT BINDING 182..183
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24396869,
FT ECO:0007744|PDB:3RQ4"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24396869,
FT ECO:0007744|PDB:3RQ4"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24396869,
FT ECO:0007744|PDB:3RQ4"
FT BINDING 230
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24396869,
FT ECO:0007744|PDB:3RQ4"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24396869,
FT ECO:0007744|PDB:3RQ4"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24396869,
FT ECO:0007744|PDB:3RQ4"
FT MOD_RES 416
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 422
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 37..97
FT /note="SPVPPLRRQQHLRSALETFLRQRDLEAAYRALTLGGWTARYFQSRGPRQEAA
FT LKTHVYRYL -> RSIATSVPSCRKVALPSCPARATPWRPTGPRSCPLVLGKRMRSWSC
FT WWAALQSCGRQMRGC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043947"
FT VAR_SEQ 98..462
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043948"
FT HELIX 8..27
FT /evidence="ECO:0007829|PDB:3RQ4"
FT HELIX 45..58
FT /evidence="ECO:0007829|PDB:3RQ4"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:3RQ4"
FT TURN 70..78
FT /evidence="ECO:0007829|PDB:3RQ4"
FT HELIX 83..99
FT /evidence="ECO:0007829|PDB:3RQ4"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:3RQ4"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:3RQ4"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:3RQ4"
FT STRAND 134..144
FT /evidence="ECO:0007829|PDB:3RQ4"
FT HELIX 147..152
FT /evidence="ECO:0007829|PDB:3RQ4"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:3RQ4"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:3RQ4"
FT TURN 166..169
FT /evidence="ECO:0007829|PDB:3RQ4"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:3RQ4"
FT HELIX 177..180
FT /evidence="ECO:0007829|PDB:3RQ4"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:3RQ4"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:3RQ4"
FT STRAND 198..205
FT /evidence="ECO:0007829|PDB:3RQ4"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:3RQ4"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:3RQ4"
FT HELIX 232..237
FT /evidence="ECO:0007829|PDB:3RQ4"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:3RQ4"
SQ SEQUENCE 462 AA; 52113 MW; 6814F7BDFA109070 CRC64;
MGPDRVTARE LCENDDLATS LVLDPYLGFR THKMNVSPVP PLRRQQHLRS ALETFLRQRD
LEAAYRALTL GGWTARYFQS RGPRQEAALK THVYRYLRAF LPESGFTILP CTRYSMETNG
AKIVSTRAWK KNEKLELLVG CIAELREADE GLLRAGENDF SIMYSTRKRS AQLWLGPAAF
INHDCKPNCK FVPADGNAAC VKVLRDIEPG DEVTCFYGEG FFGEKNEHCE CHTCERKGEG
AFRTRPREPA LPPRPLDKYQ LRETKRRLQQ GLDSGSRQGL LGPRACVHPS PLRRDPFCAA
CQPLRLPACS ARPDTSPLWL QWLPQPQPRV RPRKRRRPRP RRAPVLSTHH AARVSLHRWG
GCGPHCRLRG EALVALGQPP HARWAPQQDW HWARRYGLPY VVRVDLRRLA PAPPATPAPA
GTPGPILIPK QALAFAPFSP PKRLRLVVSH GSIDLDVGGE EL
